protein_name
stringlengths 6
11
| species
stringclasses 299
values | sequence
stringlengths 5
4.97k
| annotation
stringlengths 5
2.1k
⌀ |
|---|---|---|---|
C85A3_SOLLC | Solanum lycopersicum | MAIFLIIFVVFFGFCILSTPLFRWIDIVYNKKNLPPGTMGWPIFGETREFLNQGPNFMKNQRARYGNFFKSHILGCPTVVSMDAGLNVYILNNEAKGLIPGYPQSMLDILGKCNIAAVHGATHKYIRGALLSLINPTMIKDHILPKIDKFMRSHLSGWDNCNVIDIQQMTKEMAFFSSLDQIGGFATSSSIAQEFRAGFLNIALGTISLPINFPTTNYYRGLQGRKTIVKLLRKIIEDRRGSKKIQQDMLGLMMNEEAKNRYTLSDEELIDQIITIMYSGFETVSTTSMMAVKYLHDHPKALEEIRKEHFAIREKKSLEDPIDYNDFKAMRFTRAVIYETLRLATIVNGVLRKTTQDMELNGYMIPKGWRIYVYTRELNYDPLIYPDPYTFNPWRWLENNLDHQSSFLMFGGGTRLCPGKELGVAEISTFLHYFVTRYRWEEVGGNKLMKFPRVEALNGLWIKVSAY | Catalyzes the C6-oxidation step in brassinosteroids biosynthesis . Converts 6-deoxocastasterone (6-deoxoCS) to castasterone (CS), and castasterone (CS) to brassinolide (BL) .
Subcellular locations: Membrane
Expressed in fruits. |
C85A_PHAVU | Phaseolus vulgaris | MALFMAILGVLVLLLCLCSALLKWNEVRFRRKGLPPGAMGWPVFGETTEFLKQGPNFMKNKRARYGSFFKSHILGCPTIVSMDPELNRFILMNEAKGLVPGYPQSMLDILGTRNIAAVHGSTHKYMRGALLSIISPTLIRDQLLPKIDEFMRTHLMDWDNKVINIQEKTKEMAFLSSLKQIAGMESSSIAQPFMTEFFKLVLGTLSLPINLPRTNYRGGLQARKSIISILSRLLEERKASQDVHVDMLGCLMKKDENRYKLNDEEIIDLVITIMYSGYETVSTTSMMAVKYLHDHPKVLEEIRKEHFAIRERKKPEDPIDCNDLKSMRFTRAVIFETSRLATIVNGVLRKTTHDMELNGYLIPKGWRIYVYTREINYDPFLYHDPLTFNPWRWLGNSLESQSHFLIFGGGTRQCPGKELGIAEISTFLHYFVTRYRWEEVGGDKLMKFPRVVAPNGLHIRVSSFSN | Catalyzes the C6-oxidation step in brassinosteroids biosynthesis.
Subcellular locations: Membrane |
CALM_WHEAT | Triticum aestivum | MADQLTDEQIAEFKEAFSLFDKDGDGCITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLNLMARKMKDTDSEEELKEAFRVFDKDQDGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKVMMAK | Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. |
CAMT_MEDSA | Medicago sativa | MATNEDQKQTESGRHQEVGHKSLLQSDALYQYILETSVFPREHEAMKELREVTAKHPWNIMTTSADEGQFLSMLLKLINAKNTMEIGVYTGYSLLATALAIPEDGKILAMDINKENYELGLPVIKKAGVDHKIDFREGPALPVLDEMIKDEKNHGSYDFIFVDADKDNYLNYHKRLIDLVKVGGVIGYDNTLWNGSVVAPPDAPLRKYVRYYRDFVLELNKALAVDPRIEICMLPVGDGITICRRIK | Methylates caffeoyl-CoA to feruloyl-CoA and 5-hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers. |
CAMT_SOLTU | Solanum tuberosum | MASNGENGRHQEVGHKSLLQSDALYQYILETSVYPREPEAMKELREITAKHPWNLMTTSADEGQFLNMLLKLINAKNTMEIGVFTGYSLLATAMALPDDGKILAMDINRENYEIGLPVIEKAGLAHKIDFREGPALPVLDQMIEDGKYHGSYDFIFVDADKDNYLNYHKRLIDLVKVGGLIGYDNTLWNGSVVAPPDAPLRKYVRYYRDFVLELNKALAADPRIEICQLPVGDGITLCRRIS | Methylates caffeoyl-CoA to feruloyl-CoA and 5-hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers. |
CAS1_GLYGL | Glycyrrhiza glabra | MWKLKIAEGGSPWLRTVNNHVGRQVWEFDPKLGSPEDLLEIEKARQNFHDNRFTHKHSADLLMRIHFAKENPMNEVLPKVRVKDIEDVTEETVKTTLRRAINFHSTLQSHDGHWPGDYGGPMFLMPGLVITLSITGALNAVLTEEHRKEICRYLYNHQNKDGGWGLHIEGPSTMFGSVLNYVALRLLGEGPNDRQGEMEKGRDWILGHGGATFITSWGKMWLSVLGVYEWSGNNPLPPEIWLLPYVLPIHPGRMWCHCRMVYLPMSYLYGKRFVGPITPTILSLRKELYTIPYHDIDWNQARNLCAKEDLYYPHPLVQDILWASLHKFLEPILMHWPGKKLREMAIKTAIEHIHYEDDNTRYLCIGPVNKVLNMLCCWVEDPNSEAFKLHLPRIYDYLWIAEDGMKMQGYNGSQLWDTAFTAQAIISSNLIEEYGPTLRKAHTYIKNSQVLEDCPGDLSKWYRHISKGAWPFSTADHGWPISDCTAEGLKAVLLLSKIAPEIVGEPLDAKRLYDAVNVILSLQNEDGGFATYELTRSYTWLELINPAETFGDIVIDYPYVECTSAAIQALTSFKKLYPGHRREEIQCCIEKAASFIEKTQASDGSWYGSWGVCFTYGTWFGVKGLIAAGKSFNNCSSIRKACEFLLSKQLPSGGWGESYLSCQNKVYSNVESNRSHVVNTGWAMLALIDAEQAKRDPTPLHRAAVYLINSQMENGDFPQQEIMGVFNKNCMITYAAYRNVFPIWALGEYRHRVLQSQ | Oxidosqualene cyclase converting oxidosqualene to cycloartenol. Required for the production of sterols.
Expressed in thickened roots and root nodules. |
CAS2_SOLTU | Solanum tuberosum | MATLSRFLKKRSLASNRLFSTQLPHTNIKSEVSQLIGKTPMVYLKKVTEGCGAYIAVKQEMFQPTSSIKDRPALAMINDAEKKGLISPEKTTLIEPTSGNMGISMAFMAAMKGYKMVLTMPSYTSMERRVTMRAFGADLILTDPTKGMGGTVKKAYELLESTPNAFMLQQFSNPANTQVHFDTTGPEIWEETLGNVDIFVMGIGSGGTVTGVGLYLKSKNPNVKIYGLEPTESNILNGGKPGPHHITGNGVGSKPDIVDMDLMEEVLMVSSEDAVNMARELAVKEGLMVGISSGANTVAALRLAQKPENKGKLIVTVHASFGERYLSSVLYQDLRKEAENMQPVSVD | Has very low cyanoalanine synthase and cysteine synthase activities.
Subcellular locations: Mitochondrion
Expressed in tubers, buds and leaves. |
CATA1_CUCPE | Cucurbita pepo | MDPYRHRPSSAFNAPFWTTNSGAPVWNNNSSMTVGPRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDITNLSCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDLVGNNFPVFFIRDGMKFTRHVHPLKPNPKSHIQENWRILDFFSHHPESLNMFSFLFDDIGIPQDYRHMDGSGVNTYTLINKAGKAHYVKFHWRPTCGVKSLLEEDAIRVGGSNHSHATQDLYDSIAAGNYPEWKLFIQTIDPDHEDKYDFDPLDVTKTWPEDILPLQPVGRMVLNKNIDNFFAENEQLAFCPAIIVPGVYYSDDKLLQTRIFSYADTQRHRLGPNYLQLPANAPKCAHHNNHHEGFMNFMHRDEEVNYFPSRFDPSRHAERYPHPPAVCSGKRERCIIEKENNFKEPGERYRSWTPDRQERFVRRWVDALSDTRVTHEIRSIWISYWSQADRSLGQKLASHLNVRPSI | Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Subcellular locations: Glyoxysome
High expression in seeds and early seedlings. |
CATA1_HORVU | Hordeum vulgare | MDPYKHRPTSGANSAYWTTNSGAPVWNNNNALTVGHRGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDVSQLTCADFLRAPGVQTPVIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPSPKTNMQENWRVVDFFSHHPESLHMFTFLFDDVGIPLNYRHMDGFGVNTYTLISRDGKAHLVKFHWKPTCGVKCLLDDEAVTVGGTCHTHATKDLTDSIAAGNYPEWKLFIQTIDADHEDRFDFDPLDVTKTWPEDIIPLQPVGRMVLNKNIDNFFAENEQLAFCPAVTVPGIHYSDDKLLQTRIFSYADTQRHRLGPNYLMLPVNAPKCAHHNNHHDGLMNFIHRDEEVNYFPSRFDPTRHAEKYPMPPRVLSGCREKCIIDKENNFKQAGERYRSFDPARQDRFLQRWVDALTDARVTHEIQSIWVSYWSQCDASLGQKLASRLKIKPNM | Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Subcellular locations: Peroxisome, Glyoxysome
In whole endosperms (aleurones plus starchy endosperm), in isolated aleurones and in developing seeds. |
CATA1_MAIZE | Zea mays | MDPYKHRPSSGSNSSFWTTNSGAPVWNNNSALTVGQRGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDVSHLTCADFLRAPGVQTPVIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPNPKTNLQENWRIVDFFSHHPESLHMFTFLFDDVGIPLNYRHMEGFGVNTYSLINRDGKPHLVKFHWKPTCGVKCLLDNEAVTVGGTCHSHATKDLYDSIAAGNYPEWKLYIQTIDLDHEDKFDFDPLDVTKTWPEDIIPLQPVGRMVLNKNVDNFFAENEQIAFCPAISVPAIHYSDDKLLQTRIFSYADTQRHRLGPNYLMLPVNAPKCAHHNNHHDGFMNFMHRDEEVNYFPSRFDPARHAEKVPIPPRVLTRCREKCIIQKENNFKQAGERYRSFDPARQDRFIQRWVDALTHPRVTHEHRTIWISYWSQCDAALGQKLPSRLNLKPSM | Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Subcellular locations: Peroxisome
Scutella, milky endosperm of immature kernels, leaves and epicotyls. |
CATA1_ORYSI | Oryza sativa subsp. indica | MDPCKFRPSSSFDTKTTTTNAGAPVWNDNEALTVGPRGPILLEDYHLIEKVAHFARERIPERVVHARGASAKGFFECTHDVTDITCADFLRSPGAQTPVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRVFDFLSHHPESLHTFFFLFDDVGIPTDYRHMDGFGVNTYTFVTRDAKARYVKFHWKPTCGVSCLMDDEATLVGGKNHSHATQDLYDSIAAGNFPEWKLFVQVIDPEEEERFDFDPLDDTKTWPEDEVPLRPVGRLVLNRNVDNFFNENEQLAFGPGLVVPGIYYSDDKMLQCRVFAYADTQRYRLGPNYLMLPVNAPKCAHHNNHYDGAMNFMHRDEEVDYYPSRHAPLRHAPPTPITPRPVVGRRQKATIHKQNDFKQPGERYRSWAPDRQERFIRRFAGELAHPKVSPELRAIWVNYLSQCDESLGVKIANRLNVKPSM | Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Subcellular locations: Peroxisome, Glyoxysome |
CATA1_ORYSJ | Oryza sativa subsp. japonica | MDPCKFRPSSSFDTKTTTTNAGAPVWNDNEALTVGPRGPILLEDYHLIEKVAHFARERIPERVVHARGASAKGFFECTHDVTDITCADFLRSPGAQTPVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRVFDFLSHHPESLHTFFFLFDDVGIPTDYRHMDGFGVNTYTFVTRDAKARYVKFHWKPTCGVSCLMDDEATLVGGKNHSHATQDLYDSIAAGNFPEWKLFVQVIDPEEEERFDFDPLDDTKTWPEDEVPLRPVGRLVLNRNVDNFFNENEQLAFGPGLVVPGIYYSDDKMLQCRVFAYADTQRYRLGPNYLMLPVNAPKCAHHNNHYDGAMNFMHRDEEVDYYPSRHAPLRHAPPTPITPRPVVGRRQKATIHKQNDFKQPGERYRSWAPDRQERFIRRFAGELAHPKVSPELRAIWVNYLSQCDESLGVKIANRLNVKPSM | Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide (By similarity). Involved in environmental stress response. Promotes drought stress tolerance and recovery (Ref.10).
Subcellular locations: Cytoplasm, Cell membrane
Mostly expressed in young leaves (blades and sheaths) and seeds (Ref.10 ). Abundant in leaf sheath and moderately expressed in leaf blade and root ( ). Also present at a high levels in panicles, but barely in culms (, Ref.10). Observed in stems and anthers . |
CATA1_SOLLC | Solanum lycopersicum | MDPSKYRPSSAYDTPFLTTNAGGPVYNNVSSLTVGPRGPVLLEDYYLIEKLATFDREKIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGAQTPVICRFSTVVHERGSPESIRDIRGFAVKFYTREGNFDLVGNNVPVFFNRDAKSFPDTIRALKPNPKSHIQENWRILDFFSFLPESLHTFAFFYDDVCLPTDYRHMEGFGVHAYQLINKEGKAHYVKFHWKPTCGVKCMSEEEAIRVGGTNHSHATKDLYDSIAAGNYPEWKLFIQTMDPEDVDKFDFDPLDVTKTWPEDLLPLIPVGRLVLNRNIDNFFAENEQLAFNPGHIVPGIYYSEDKLLQTRIFAYADTQRHRIGPNYMQLPVNAPKCGHHNNHRDGAMNMTHRDEEVDYLPSRFDPCRPAEQYPIPSCVLNGRRTNCVIPKENNFKQAGERYRSWEPDRQDRYINKWVESLSDPRVTHEIRSIWISYLSQADKSCGQKVASRLTVKPTM | Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Subcellular locations: Peroxisome |
CATA1_SOLTU | Solanum tuberosum | MDPSKYRPSSAYDTPFLTTNAGGPVYNNVSSLTVGPRGPVLLEDYYLIEKLATFDREKIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGAQTPVICRFSTVVHERGSPESIRDIRGFGVKFYNRGGNFDLVGNNVPVFFNRDAKSFPDTIRALKPNPKSHIQEDWRTLDFFSFLPESLHTFAFFYDDVCLPTDYRHMEGFGVHAYQLINKEGKAHYVKFHWKPTCGVKCMSEEEAIRVGGTNHSHATKDLYDSIAAGNYPEWKLFIQTMDPEDVDKFDFDPLDVTKTWPEDLLPLIPVGRLVLNRNIDNFFAENEQLAFNPGHIVPGIYYSEDKLLQTRIFAYADTQRHRIGPNYMQLPVNAPKCGHHNNHRDGAMNMTHRDEEVDYFPSRFDPCRPAEQYPIPACVLNGRRTNCVIPKENNSKQAGERYRSWESDRQDRYINKWVESLSDPRVTHEIRSIWISYLSQADKSCGQKVASRLTVKPTM | Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Subcellular locations: Peroxisome, Glyoxysome |
CATA1_SOYBN | Glycine max | MDPYKNRPSSAFNSPFWTTNSGAPIWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPLIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDLVGNNFPVFFVRDGLKFPDMVHALKPNPKSHIQENWRILDFFSHHPESLHMFSFLFDDVGIPQDYRHMDGFGVNTYTLINKAGKALYVKFHWKTTSGEKSLLDDEAIRVGGSNHSHATQDLYDSIAAGNYPEWKLYIQTLDPENEDRLDFDPLDVTKTWPEDVLPLQPVGRMVLNKNIDNFFAENEQLAFCPAIIVPGVYYSDDKLLQTRVFSYADTQRHRLGPNYLQLPANAPKCAHHNNHHDGFMNFMHRDEEVNYFPSRYDPVRHAEKVPVPPRILGGKREKCMIEKENNFKQPGERYRSWPSDRQERFVRRWVDALSDPRVTHEIRSIWISYWSQADRSLGQKIASHLNLKPSI | Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Subcellular locations: Peroxisome, Glyoxysome |
CATB_MEDTR | Medicago truncatula | MAQWTLLIVFFCVATAAAGLSFHDSNPIRMVSDMEEQLLQVIGESRHAVSFARFANRYGKRYDTVDEMKRRFKIFSENLQLIKSTNKKRLGYTLGVNHFADWTWEEFRSHRLGAAQNCSATLKGNHRITDVVLPAEKDWRKEGIVSEVKDQGHCGSCWTFSTTGALESAYAQAFGKNISLSEQQLVDCAGAYNNFGCNGGLPSQAFEYIKYNGGLETEEAYPYTGQNGLCKFTSENVAVQVLGSVNITLGAEDELKHAVAFARPVSVAFQVVDDFRLYKKGVYTSTTCGSTPMDVNHAVLAVGYGIEDGVPYWLIKNSWGGEWGDHGYFKMEMGKNMCGVATCSSYPVVA | May play a role in proteolysis leading to mobilization of nitrogen during senescence and starvation.
Subcellular locations: Vacuole, Lysosome |
CBPX_ORYSJ | Oryza sativa subsp. japonica | MATGKSGGSSAEDLGHHAGYYRLPNTHDARLFYFFFESRGSKGEDDPVVIWLTGGPGCSSELALFYENGPFHIADNMSLVWNDFGWDQESNLIYVDQPTGTGFSYSSNPRDTRHDEAGVSNDLYAFLQAFFTEHPNFAKNDFYITGESYAGHYIPAFASRVYKGNKNSEGIHINLKGFAIGNGLTDPAIQYKAYTDYSLDMGLITKSQFNRINKIVPTCELAIKLCGTSGTISCLGAYVVCNLIFSSIETIIGKKNYYDIRKPCVGSLCYDLSNMEKFLQLKSVRESLGVGDIQFVSCSPTVYQAMLLDWMRNLEVGIPELLENDIKVLIYAGEYDLICNWLGNSRWVNSMEWSGKEAFVSSSEEPFTVDGKEAGILKSYGPLSFLKVHDAGHMVPMDQPKVALEMLMRWTSGNLSNASSSFQRLDFTM | Abundant in germinated embryos composed of leaf, root, and scutellum. |
CBPX_PEA | Pisum sativum | TGESYAGHYIPALASRIHQGNQANEGIHINLKGLAIGNGLTNPAIQYKGYPDYALDMGIITQTTHDLLGKVLVPACELAIKLCGTNGKVSCLTANVACNLIFSDIMLHAGGVNYYDIRKKCEGSLCYDFSNMEKFLNQESVRDSLGVGKIRFVSCSTEVYMAMLVDWMRNLEVGIPLLLEDGINLLIYAGEYDLICNWLGNSRWVHAMKWSGQKEFVASSDVPFVVNGSQAGLLKSYGPLSFLKVHDAGHMVPMDQPKAALEMVKQWTRGTLAESIDGEEKLVADM | Involved in degradation of small peptides. |
CCB11_ORYSJ | Oryza sativa subsp. japonica | MATRSQNVAAAPQPPQNRGNVAALGKQKAVVAGRPDAKNRRALGEIGNVMNVRLPEGKPLQQAPAGRTANFGAQLLKNAQANAAANKQNAVAPAAVARPAQRQARKAPVKPAPPPPEHVIEISSDSDQSMRQQSEGSASSVRKCSRKKVINTLTSVLTARSKVACGITDKPREVIEDIDKLDGDNELAVVDYIEDIYKFYKVAENECRPCDYIDTQVEINSKMRAILADWIIEVHHKFELMPETLYLSMYVIDRYLSMQQVQRRELQLVGVSAMLIACKYEEIWAPEVNDFILISDSAYTREQILAMEKGILNKLQWNLTVPTAYVFIMRYLKAGASADNKSDKEMEHMAFFFAELALMQYGLVASLPSKVAASAVYAARLTLKKSPLWTDTLKHHTGFTESQLLDSAKLLVTSHSTAPESKLRVVYKKYSSEQLGGVALRSPAVELCK | null |
CCB12_ORYSJ | Oryza sativa subsp. japonica | MASGGVVKKEIGGNHDVVRFGVNDSVKGDLAPPHPLQASVHKEAKFWADKKRFGAEAIYGSAFNIRKDLDAQILSKFQRPPGALPSSMLGYEALTGSLDDFGFEDYLNYAAASEDGWVLGRGALELLLGGTAYTQATSAPQISLSMQQVQRRELQLVAVSAMLIDCKYEEIWAPEVNDFIFISDSAYTREQILAMEKGILNKLQWNLTIPTPYVFIMMLSASADNKSDKENAEALKFKRLSQSRQQLIDWSVKIKVSKEHGGFMRFIQVSCLGASASSSRMLRAKAAGEESVLKEFPEPLRLLISHRQSMGTCILNFHSRIQPVYVVDVAAAIVNSLKDDGTSMGKSYGLGGPEIYTVHDLAELMYETICEWPRYIDVPLPIARAIASPES | null |
CH61_CUCMA | Cucurbita maxima | MHRFATGLASKARLARNGANQIASRSNWRRNYAAKDVKFGVEARGLMLKGVEDLADAVKVTMGPKGRTVVIEQSFGAPKVTKDGVTVAKSIEFKDKVKNVGASLVKQVANATNDVAGDGTTCATILTKAIFTEGCKSVASGMNAMDLRRGISMAVDSVVTNLKSRARMISTSEEIAQVGTISANGEREIGELIAKAMEKVGKEGVITISDGKTMDNELEVVEGMKLDRGYISPYFITNQKNQKCELDDPLIIIYEKKISSINAVVKVLELALKKQRPLLIVSEDVESEALATLILNKLRAGIKVCAIKAPGFGENRKAGLQDLAVLTGGQVITEELGMNLEKVDLDMLGSCKKITISKDDTVILDGAGDKKAIEERCDQIRSGIEASTSDYDKEKLQERLAKLSGGVAVLKIGGASEAEVGEKKDRVTDALNATKAAVEEGIVPGGGVALLYASKELDKLPTANFDQKIGVQIIQNALKTPVHTIASNAGVEGAVVVGKLLEQDDPDLGYDAAKGEYVDMVKAGIIDPLKVIRTALVDAASVSSLMTTTEVVVVELPKDENEVPAMGGGMGGMDY | Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix.
Subcellular locations: Mitochondrion |
CH61_MAIZE | Zea mays | MYRAAASLASKARQAGNSLATRQVGSRLAWSRNYAAKDIKFGVEARALMLRGVEELADAVKVTMGPKGRNVVIEQSFGAPKVTKDGVTVAKSIEFKDRVKNVGASLVKQVANATNDTAGDGTTCATVLTKAIFTEGCKSVAAGMNAMDLRRGISMAVDAVVTNLKGMARMISTSEEIAQVGTISANGEREIGELIAKAMEKVGKEGVITIADGNTLYNELEVVEGMKLDRGYISPYFITNSKTQKCELEDPLILIHDKKVTNMHAVVKVLEMALKKQKPLLIVAEDVESEALGTLIINKLRAGIKVCAVKAPGFGENRKANLQDLAILTGGEVITEELGMNLENFEPHMLGTCKKVTVSKDDTVILDGAGDKKSIEERAEQIRSAIENSTSDYDKEKLQERLAKLSGGVAVLKIGGASEAEVGEKKDRVTDALNATKAAVEEGIVPGGGVALLYASKELDKLQTANFDQKIGVQIIQNALKTPVHTIASNAGVEGAVVVGKLLEQENTDLGYDAAKGEYVDMVKTGIIDPLKVIRTALVDAASVSSLMTTTESIIVEIPKEEAPAPAMGGGMGGMDY | Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix.
Subcellular locations: Mitochondrion |
CH62_CUCMA | Cucurbita maxima | MHRFASGLASKARLARKGANQIASRSSWSRNYAAKDVKFGVEARGLMLKGVEDLADAVKVTMGPKGRNVVIEQSYGAPKVTKDGVTVAKSIEFKDKVKNVGASLVKQVANATNDVAGDGTTCATILTRAIFTEGCKSVAAGMNAMDLRRGISMAVDSVVTNLKSRARMISTSEEIAQVGTISANGEREIGELIAKAMEKVGKEGVITISDGKTLFNELEVVEGMKLDRGYISPYFITNQKNQKCELDDPLILIHEKKISSINSVVKVLELALKRQRPLLIVSEDVESDALATLILNKLRAGIKVCAIKAPGFGENRKAGLHDLAVLTGGQLITEELGMNLEKVDLDMLGSCKKITISKDDTVILDGAGDKKSIEERCEQIRSAIELSTSDYDKEKLQERLAKLSGGVAVLKIGGASEAEVGEKKDRVTDALNATKAAVEEGIVPGGGVALLYASKELDKLSTANFDQKIGVQIIQNALKTPVHTIASNAGVEGAVVVGKLLEQDNPDLGYDAAKGEYVDMIKAGIIDPLKVIRTALVDAASVSSLMTTTEAIVVELPKDEKEVPAMGGGMGGMDY | Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix.
Subcellular locations: Mitochondrion |
CH62_MAIZE | Zea mays | MYRAAASLASKARQAGSSSAARQVGSRLAWSRNYAAKDIKFGVEARALMLRGVEELADAVKVTMGPKGRNVVIEQSFGAPKVTKDGVTVAKSIEFKDRVKNVGASLVKQVANATNDTAGDGTTCATVLTKAIFTEGCKSVAAGMNAMDLRRGISMAVDAVVTNLKGMARMISTSEEIAQVGTISANGEREIGELIAKAMEKVGKEGVITIADGNTLYNELEVVEGMKLDRGYISPYFITNSKAQKCELEDPLILIHDKKVTNMHAVVKVLEMALKKQRPLLIVAEDVESEALGTLIINKLRAGIKVCAVKAPGFGENRKANLQDLAILTGGEVITEELGMNLENVEPHMLGSCKKVTVSKDDTVILDGAGDKKSIEERADQIRSAVENSTSDYDKEKLQERLAKLSGGVAVLKIGGASEAEVGEKKDRVTDALNATKAAVEEGIVPGGGVALLYASKELDKLQTANFDQKIGVQIIQNALKTPVHTIASNAGVEGAVVVGKLLEQGNTDLGYDAAKDEYVDMVKAGIIDPLKVIRTALVDAASVSSLMTTTESIIVEIPKEEAPAPAMGGMGGMDY | Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix.
Subcellular locations: Mitochondrion |
CHI3_ARAHY | Arachis hypogaea | MTPQGNKPSSHDVITGRWTPSDADRAAGRVSGFGVITNIINGGLDC | Defense against chitin-containing fungal and bacterial pathogens. |
CHI3_ORYSJ | Oryza sativa subsp. japonica | MRALALAVVAMAVVAVRGEQCGSQAGGALCPNCLCCSQYGWCGSTSDYCGAGCQSQCSGGCGGGPTPPSSGGGSGVASIISPSLFDQMLLHRNDQACAAKGFYTYDAFVAAANAYPDFATTGDADTCKREVAAFLAQTSHETTGGWPTAPDGPYSWGYCFKEENNGNAPTYCEPKPEWPCAAGKKYYGRGPIQITYNYNYGPAGQAIGSDLLNNPDLVASDATVSFKTAFWFWMTPQSPKPSCHAVITGQWTPSADDQAAGRVPGYGEITNIINGGVECGHGADDKVADRIGFYKRYCDMLGVSYGDNLDCYNQRPYPPS | Hydrolyzes chitin and plays a role in defense against fungal pathogens containing chitin. Inhibits the growth of T.reesei fungus on plate assay.
Expressed at low levels in roots, leaves, sheaths and meristems. |
CHI3_SOLTU | Solanum tuberosum | EFTIFSLLFSLLLLNASAEQCGSQAGGALCAPGLCCSKFGWCGNTNDYCGPGNCQSQCPGGPGPSGDLGGVISNSMFDQMLNHRNDNACQGKNNFYSYNAFISAAGSFPGFGTTGDITARKREIAAFLAQTSHETTGGWPSAPDGPYAWGYCFLREQGSPGDYCTPSSQWPCAPGRKYFGRGPIQISHNYNYGPCGRAIGVDLLNNPDLVATDSVISFKSAIWFWMTPQSPKPSCHDVITGRWQPSGADQAANRVPGFGVITNIINGGLECGHGSDSRVQDRIGFYRRYCGILGVSPGDNLDCGNQRSFGNGLLVDTV | Defense against chitin-containing fungal pathogens.
Subcellular locations: Vacuole
Vacuolar and protoplast. |
CHI4_ARAHY | Arachis hypogaea | MTPQGNKPSCHDVITNAWRPTATDSAAGRAPGYGVITNIINGGLDC | Defense against chitin-containing fungal and bacterial pathogens. |
CHLG_ORYSJ | Oryza sativa subsp. japonica | MATSHLLAAASSTAASSATFRPPLLSLRSPPPSSLRLNRRRHFQVVRAAETDKETKANAPEKAPAGGSSFNQLLGIKGAKQENDIWKIRLQLTKPVTWPPLVWGVLCGAAASGNFHWTVEDVAKSIVCMIMSGPCLTGYTQTINDWYDRDIDAINEPYRPIPSGAISENEVITQIWALLLAGLGLGALLDVWAGHDFPIIFYLAVGGSLLSYIYSAPPLKLKQNGWIGNFALGASYIGLPWWAGQALFGTLTPDIVVLTSLYSIAGLGIAIVNDFKSVEGDRALGLQSLPVAFGMETAKWICVGAIDITQLSVAGYLFSSGKPYYALALLGLTIPQVVFQFQYFLKDPVKYDVKYQASAQPFFVLGLLVTALATSH | Involved in one of the last steps of the biosynthesis of chlorophyll a.
Subcellular locations: Plastid, Chloroplast membrane |
CHLH_ORYSI | Oryza sativa subsp. indica | MSSLVSTPFTTATGVQKKLGAPVPLHSFLLSRRQPAAGAGRGRAAAAAIRCAVAGNGLFTQTKPEVRRVVPPEGDASRRGVPRVKVVYVVLEAQYQSSVTAAVRELNADPRRAAGFEVVGYLVEELRDEETYKTFCADLADANVFIGSLIFVEELALKVKDAVEKERDRMDAVLVFPSMPEVMRLNKLGSFSMSQLGQSKSPFFQLFKRKKNSGGFADSMLKLVRTLPKVLKYLPSDKAQDARLYILSLQFWLGGSPDNLQNFLKMIAVSYVPALKGADIKYDDPVLFLDAGIWHPLAPTMYDDVKEYLNWYGTRRDTNDKLKDPNAPVIGLVLQRSHIVTGDDGHYVAVIMELEAKGAKVIPIFAGGLDFSGPTQRYLVDPITGKPFVNAVVSLTGFALVGGPARQDHPKAIAALQKLDVPYIVALPLVFQTTEEWLNSTLGLHPIQVALQVALPELDGGMEPIVFAGRDPRTGKSHALHKRVEQLCTRAIRWAELKRKTKEEKKLAITVFSFPPDKGNVGTAAYLNVFNSIYSVLQDLKKDGYNVEGLPDTAEALIEEVIHDKEAQFNSPNLNVAYRMNVREYQSLTSYASLLEENWGKPPGNLNSDGENLLVYGKQYGNVFIGVQPTFGYEGDPMRLLFSKSASPHHGFAAYYTFVEKIFQADAVLHFGTHGSLEFMPGKQVGMSDACYPDSLIGNIPNIYYYAANNPSEATVAKRRSYANTISYLTPPAENAGLYKGLKQLSELISSYQSLKDTGRGPQIVSSIISTAKQCNLDKDVPLPEEGVELPPNERDLIVGKVYAKIMEIESRLLPCGLHVIGEPPSAIEAVATLVNIASLDRPEDEIYSLPNILAQTVGRNIEDVYRGSDKGILADVELLRQITEASRGAITAFVERTTNNKGQVVDVTNKLSTMLGFGLSEPWVQHLSKTKFIRADREKLRTLFTFLGECLKLIVADNELGSLKLALEGSYVEPGPGGDPIRNPKVLPTGKNIHALDPQAIPTTAALKSAKIVVDRLLERQKVDNGGKYPETIALVLWGTDNIKTYGESLAQVLWMIGVRPVADTFGRVNRVEPVSLEELGRPRIDVVVNCSGVFRDLFINQMNLLDRAVKMVAELDEPEEMNYVRKHAQEQARELGVSLREAATRVFSNASGSYSSNVNLAVENASWTDEKQLQDMYLSRKSFAFDCDAPGAGMREQRKTFELALATADATFQNLDSSEISLTDVSHYFDSDPTKLVQGLRKDGRAPSSYIADTTTANAQVRTLSETVRLDARTKLLNPKWYEGMMKSGYEGVREIEKRLTNTVGWSATSGQVDNWVYEEANATFIEDEAMRKRLMDTNPNSFRKLVQTFLEASGRGYWETSEENLEKLRELYSEVEDKIEGIDR | Involved in chlorophyll biosynthesis. Catalyzes the insertion of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. The reaction takes place in two steps, with an ATP-dependent activation followed by an ATP-dependent chelation step. May be involved in the plastid-to-nucleus retrograde signaling (By similarity).
Subcellular locations: Plastid, Chloroplast stroma, Plastid, Chloroplast membrane, Plastid, Chloroplast membrane
Predominantly associated with the chloroplast envelope. Spans the chloroplast envelope and its N- and C-termini are exposed to the cytosol (By similarity). |
CHLH_ORYSJ | Oryza sativa subsp. japonica | MSSLVSTPFTTATGVQKKLGAPVPLHSFLLSRRQPAAGAGRGRAAAAAIRCAVAGNGLFTQTKPEVRRVVPPEGDASRRGVPRVKVVYVVLEAQYQSSVTAAVRELNADPRRAAGFEVVGYLVEELRDEETYKTFCADLADANVFIGSLIFVEELALKVKDAVEKERDRMDAVLVFPSMPEVMRLNKLGSFSMSQLGQSKSPFFQLFKRKKNSGGFADSMLKLVRTLPKVLKYLPSDKAQDARLYILSLQFWLGGSPDNLQNFLKMIAVSYVPALKGADIKYDDPVLFLDAGIWHPLAPTMYDDVKEYLNWYGTRRDTNDKLKDPNAPVIGLVLQRSHIVTGDDGHYVAVIMELEAKGAKVIPIFAGGLDFSGPTQRYLVDPITGKPFVNAVVSLTGFALVGGPARQDHPKAIAALQKLDVPYIVALPLVFQTTEEWLNSTLGLHPIQVALQVALPELDGGMEPIVFAGRDPRTGKSHALHKRVEQLCTRAIRWAELKRKTKEEKKLAITVFSFPPDKGNVGTAAYLNVFNSIYSVLQDLKKDGYNVEGLPDTAEALIEEVIHDKEAQFNSPNLNVAYRMNVREYQSLTSYASLLEENWGKPPGNLNSDGENLLVYGKQYGNVFIGVQPTFGYEGDPMRLLFSKSASPHHGFAAYYTFVEKIFQADAVLHFGTHGSLEFMPGKQVGMSDACYPDSLIGNIPNIYYYAANNPSEATVAKRRSYANTISYLTPPAENAGLYKGLKQLSELISSYQSLKDTGRGPQIVSSIISTAKQCNLDKDVPLPEEGVELPPNERDLIVGKVYAKIMEIESRLLPCGLHVIGEPPSAIEAVATLVNIASLDRPEDEIYSLPNILAQTVGRNIEDVYRGSDKGILADVELLRQITEASRGAITTFVERTTNNKGQVVDVTNKLSTMLGFGLSEPWVQHLSKTKFIRADREKLRTLFTFLGECLKLIVADNELGSLKLALEGSYVEPGPGGDPIRNPKVLPTGKNIHALDPQAIPTTAALKSAKIIVDRLLERQKVDNGGKYPETIALVLWGTDNIKTYGESLAQVLWMIGVRPVADTFGRVNRVEPVSLEELGRPRIDVVINCSGVFRDLFINQMNLLDRAVKMVAELDEPEEMNYVRKHAQEQARELGVSLREAATRVFSNASGSYSSNVNLAVENASWTDEKQLQDMYLSRKSFAFDCDAPGAGMREQRKTFELALATADATFQNLDSSEISLTDVSHYFDSDPTKLVQGLRKDGRAPSSYIADTTTANAQVRTLSETVRLDARTKLLNPKWYEGMMKSGYEGVREIEKRLTNTVGWSATSGQVDNWVYEEANATFIEDEAMRKRLMDTNPNSFRKLVQTFLEASGRGYWETSEENLEKLRELYSEVEDKIEGIDR | Involved in chlorophyll biosynthesis. Catalyzes the insertion of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. The reaction takes place in two steps, with an ATP-dependent activation followed by an ATP-dependent chelation step. May be involved in the plastid-to-nucleus retrograde signaling.
Subcellular locations: Plastid, Chloroplast stroma, Plastid, Chloroplast membrane, Plastid, Chloroplast membrane
Predominantly associated with the chloroplast envelope. Spans the chloroplast envelope and its N- and C-termini are exposed to the cytosol (By similarity). |
CHOMT_MEDSA | Medicago sativa | MGNSYITKEDNQISATSEQTEDSACLSAMVLTTNLVYPAVLNAAIDLNLFEIIAKATPPGAFMSPSEIASKLPASTQHSDLPNRLDRMLRLLASYSVLTSTTRTIEDGGAERVYGLSMVGKYLVPDESRGYLASFTTFLCYPALLQVWMNFKEAVVDEDIDLFKNVHGVTKYEFMGKDKKMNQIFNKSMVDVCATEMKRMLEIYTGFEGISTLVDVGGGSGRNLELIISKYPLIKGINFDLPQVIENAPPLSGIEHVGGDMFASVPQGDAMILKAVCHNWSDEKCIEFLSNCHKALSPNGKVIIVEFILPEEPNTSEESKLVSTLDNLMFITVGGRERTEKQYEKLSKLSGFSKFQVACRAFNSLGVMEFYK | Methylates the 2'-hydroxyl of isoliquiritigenin and licodione. Does not methylate narigenin chalcone, caffeic acid or daidzein. Involved in the root nodulation initiation by promoting the biosynthesis of nod-inducing molecules.
Roots (at protein level). Expressed mainly in roots, and to a lesser extent in root nodules. In the roots, expression is not detected in the root tip or the cells immediately behind the tip, but is detected in tissues starting 1.5-2.0 mm distal to the root tip. Detected in the epidermal and cortical cells of 2 day old roots, with lower levels in vascular tissue. |
CHS2_TRISU | Trifolium subterraneum | MVSVSEIRKAQRAEGPATILAIGTANPANRVEQATYPDFYFKITNSEHKVELKEKFQRMCDKSMIKSRYMYLTEEILKENPSVCEYMAPSLDARQDMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSEVTAVTFRGPSDTHLDSLVGQALFGDGAAALIVGSDPVPEIEKPIFEMVWTAQTIAPDSEGAIDGHLREAGLTFHLLKDVPGIVSKNIDKALVEAFQPLNISDYNSIFWIAHPGGPAILDQVEQKLALKPEKMKATREVLSEYGNMSSACVLFILDEMRKKSAQNGLKTTGEGLEWGVLFGFGPGLTIETVVLHSVAI | The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin. |
CHS3_MEDSA | Medicago sativa | MVSVSEIRQAQRAEGPATIMAIGTANPSNCVEQSTYPDFYFKITNSEHKVELKEKFQRMCDKSMIKRRYMYLTEEILKENPSVCEYMAPSLDARQDMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSEVTAVTFRGPSDTHLDSLVGQALFGDGAAALIVGSDPIPEIEKPIFEMVWTAQTIAPDSEGAIDGHLVEAGLTFHLLKDVPGIVSKNIDKALIEAFQPLNISDYNSIFWIAHPGGPAILDQVEEKLGLKPEKMKATREVLSEYGNMSSACVLFILDEMRKKSAQAGLKTTGEGLDWGVLFGFGPGLTIETVVLHSVAI | The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin. |
CHS3_PEA | Pisum sativum | MVSVSEIRKAQRAEGPATILAIGTANPANCVEQSTYPDFYFRITNSEHKTELKQKFQRMCDKSMINRRYMYLTEEILKENPSVCEYMAPSLDARQDMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSEVTAVTFRGPSDTHLDSLVGQALFGDGAAALIVGSDPLPEIENPIFEMVWTAQTIAPDSEGAIDGHLREAGLTFHLLKDVPAIVSKNIDKALVEAFQPLGISDYNSIFWIAHPGGPAILDQVEQKLALKPEKMKATREVLSEYGNMSSACVLFILDEMRRKSIQNGLKTTGEGLEWGVLFGFGPGLTIETVVLHSVAI | The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin. |
CHS3_SORBI | Sorghum bicolor | MAAATVTVEEVRKAQRATGPATVLAIGTATPANCVHQADYPDYYFRITKSEHMTDLKEKFKRMCDKSQIRKRYMHLTEEYLAENPNMCAYMAPSLDARQDIVVVEVPKLGKAAAQKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKMLGLRPSVNRLMMYQQGCFAGGTVLRVAKDLAENNRGARVLVVCSEITAVTFRGPSESHLDSMVGQALFGDGAAAVIVGADPDERVERPLFQLVSASQTILPDSEGAIDGHLREVGLTFHLLKDVPGLISKNIERSLEEAFKPLGITDYNSIFWVAHPGGPAILDQVEAKVGLEKERLRATRHVLSEYGNMSSACVLFILDEMRKRSAEDGQATTGEGFDWGVLFGFGPGLTVETVVLHSVPITTGAAITA | The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin. |
CHS3_SOYBN | Glycine max | MVSVEEIRNAQRAEGPATVMAIGTATPPNCVDQSTYPDYYFRITNSEHMTELKEKFKRMCDKSMIKKRYMYLNEEILKENPSVCAYMAPSLDARQDMVVVEVPKLGKEAATKAIKEWGQPKSKITHLIFCTTSGVDMPGADYQLTKLLGLRPSVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPTDTHLDSLVGQALFGDGAAAVIVGSDPLPVEKPLFQLVWTAQTILPDSEGAIDGHLGEVGLTFHLLKDVPGLISKNIEKALVEAFQPLGISDYNSIFWIAHPGGPAILDQVEAKLGLKPEKMEATRHVLSEYGNMSSACVLFILDQMRKKSIENGLGTTGEGLDWGVLFGFGPGLTVETVVLRSVTV | The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin. |
CIPKL_ORYSJ | Oryza sativa subsp. japonica | MQKTSMNPVTDPVAAATGRVAIRQLPIKTQPNSQSLTPFLQLPPKPPPNLLFSSPLASVELRHRARARRRRRPSHPRRAPAMRMGKYEMGRALGEGHFGKVKLARHADTGAAFAIKILDRQRILAMKIDEQIKREIATLKLLKHPNVVRLHEVSASKTKIYMVLEYVNGGELFDKIALKGKLSEKEGRKLFQQLMDAVSYCHEKGVYHRDLKPENVLVDAKGNIKVSDFGLSALPQNQRKDGLLHTTCGSPNYIAPEVLLNRGYDGSLSDIWSCGVILYVMLTGNLPFDDQNTVVLYQKILKGDARIPKWLSPGAQDILRKILDPNPITRLDITGIRAHEWFRQDYTPAMPFDDDDDNNISDGNLHMTENQDIETSPAISQINAFQLIGMSSCLDLSGFFEKEDVSERKIRFVSNYSPTSLFEKIESTVTEKGFQVQKNSGKLKVIQVCKEPANPRGHGNLLISAEVFEINESLYVVELKRSSGDCSLYRQLCASLSEDLGICKRQQLLKKDSMRQDLCRYNSSF | CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity). |
CIPKM_ORYSJ | Oryza sativa subsp. japonica | MPPAGDDESPAATGDGYSKKVLQGRYELGRVLGQGASSKVYRARDARTGAHVAVKAIRKQQQPHHHPSCRSPEAAAAARRCVEVEREVAALRRVRGHPHVVALLDVLATRSTVYLVLELASGGSVLSALDSRGGGHYDEPAARRLFAQLASAVAHAHSLGVFHRDIKPENLLLDERGDLRLTDFGLSAFADADQHLGATDGLAATHCGSPAYVAPEILLKRRYDASKADVWSCGVVLFVLTAGYLPFNDGNLMAMYRKICAAKFRCPKWCSQELRSLIGRMLDPEPDTRIKIGEIFDHPWLQQDGSSSSFGMIQAASSHSKPEVEKWEAELEQAMELNAFDIIGFASGCDLSGLIGPLPDRVRFVLPGGDSKSVLDKVEKLGREEGLVVRRKEEEWCGGVHVEATSGKFTAYVRVNLLPKKILMIEAERVIGSEIPKFWHQLQIGNLLVRK | CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity). |
CIPKN_ORYSJ | Oryza sativa subsp. japonica | MSVSGGRTRVGRYELGRTLGEGTFAKVKFARNADSGENVAIKILDKDKVLKHKMIAQIKREISTMKLIRHPNVIRMHEVMASKTKIYIVMELVTGGELFDKIASRGRLKEDDARKYFQQLINAVDYCHSRGVYHRDLKPENLLLDASGTLKVSDFGLSALSQQVREDGLLHTTCGTPNYVAPEVINNKGYDGAKADLWSCGVILFVLMAGYLPFEDSNLMSLYKKIFKADFSCPSWFSTSAKKLIKKILDPNPSTRITIAELINNEWFKKGYQPPRFETADVNLDDINSIFNESGDQTQLVVERREERPSVMNAFELISTSQGLNLGTLFEKQSQGSVKRETRFASRLPANEILSKIEAAAGPMGFNVQKRNYKLKLQGENPGRKGQLAIATEVFEVTPSLYMVELRKSNGDTLEFHKFYHNISNGLKDVMWKPESSIIAGDEIQHRRSP | CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity). |
CIPKO_ORYSJ | Oryza sativa subsp. japonica | MGGEEGMAAGRKKRVGRYEVGRTIGQGTFAKVKFAVDADTGAAVAMKVLDKDTILNHRMLHQIKREISIMKIVRHPNIVRLNEVLAGKTKIYIILELITGGELFDKIARQGKLRENEARKYFQQLIDAINYCHSKGVYHRDLKPENLLLDSRGNLKVSDFGLSTLAQKGVGLLHTTCGTPNYVAPEVLSNNGYDGSAADVWSCGVILYVLMAGYLPFEEDDLPTLYDKITAGQFSCPYWFSPGATSLIHRILDPNPKTRITIEQIREDTWFKKTYVAIKRGEDENVDLDDVQAVFDNIEDKYVSEQVTHNDGGPLVMNAFEMITLSQGLDLSALFDRQQEFVKRQTRFVSRKPAKTIVATIEVVAETMGLKVHSQNYKLRLEGVSSNRMSPFAVVLQVFEVAPSLFMVDVRKVAGDTLEYHRFYKNLCNKMESIIWRPIEVSAKSALLRTATC | Involved in the regulatory pathway for the control of intracellular Na(+) and K(+) homeostasis and salt tolerance. Operates in synergy with CBL4 to activate the plasma membrane Na(+)/H(+) antiporter SOS1. CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. |
CIPKP_ORYSJ | Oryza sativa subsp. japonica | MFRSMGTGTGTKPPAMTTERYEFGPLVGEGNFAKVYLGRHRATGEEVAIKVMDKEKLVRLGATELIKREIAVMQRLRHPNVVRIHEVMANKRRICVVMEYVRGGALYRYFRRGPSGGAAGLREHEARRFFQQLVSAVAYCHSRGVFHRDIKLDNLLVDEQGNLKVADFGLSALADMERREAHLQTVCGTPLFLAPEVFKRRGYDGAKADVWACGVVLYVLLTGRKPFPDEHVSRLYRLIGQNQFQCPPSFSPDLARLVRRLLQPDPDRRITIPEIMEMRWFKRGFKEVTYYIDSNDRLRSLDGLDGEPELYDSDTDTIESSSSSESPTPVAGTPRGMHTSVSAPALSELDRMEDSASLPLPLPLPPRPRMPRPKSLNAFDIIASSPSFDLSGLFEERGERMRFVSGAPVADIIAKLQEIAGMVSFTARTKDCQVSIEATRNGQKGALAISAKVFELTRELVMVQVCKKAGDTAEYRRFCDNELKAGLRGLVVDALPPPVEGGGHGGAAAAAEAE | CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity). |
CIPKQ_ORYSJ | Oryza sativa subsp. japonica | MDDRRTILMDRYEIGRQLGQGNFAKVYYARNLTSGQAVAIKMIDKEKVTRVGLMVQIKREISIMRLVKHPNILQLFEVMASKSKIYFVLEYAKGGELFKKISKGKFSEDVARRYFHQLISGIDYCHSRGVYHRDLKPENLLLDENESLKVSDFGLSALSESKRHDGLLHTTCGTPAYVAPEVLSRRGYDGAKADIWSCGVILFVLVSGYLPFHDTNLIEMYRKIAKAEYKCPRSFSAELKDLLYKILDPDPSTRISIPKIKRSAWYRKSSDVNALKSKHETGDKVYKGEATTSDTTECSIFEGNRASSRDKVYTNGEATTSDSPECSNSDGKQASLSLPNLNAFDIISLSTGFDLSNLFEERYGRREERFTTRQPAAAIFAKLNELARRFKLKIKKKENGVLRLVAPKEGIKGLLELDAEVFELAPSFHLVEFKKSNGDTIEYQKLMKEDIRPALKDIVWAWQGGQHQQPEQSMQGMQGEQQPSRLPSQQPQG | CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity). |
CIPKR_ORYSJ | Oryza sativa subsp. japonica | MEGKGVLEGRYEMGRVLGHGNFGRVHAARDVRTGRAVAMKVVSKDKVERAGMAEQIKREIAVMKMVSHPSVVELHEVMATRTKVYLALELVRGGELFDRIARHGRVGEGVARRYFRQLVSAVDFCHGRGVYHRDLKPENLLLDEAGNLKVADFGLSALACHARPDGLLHTACGTPAYVAPEVLAGNGYDGAKADLWSCGVILYVLLAGALPFQDDNLVCMYRKMRRGDFCCPPWVTTDARKLIKSLLDPNPGTRITVAGLLETPWFRKTAPVPRPIIADPAAAPVDTRGNAGDDKDEPPEVLNAFHLISLSEGFDLSPLFEHDPAASPGRATARAGGTRFATREAASGVVARLEALAMGGARVAPSLLMVDVKKDGGDAMEYRPFFSEELRPALKDIVWSPAAT | CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity). |
CIPKS_ORYSJ | Oryza sativa subsp. japonica | MEERSVLMERYVIGRQLGQGTFGKVYYARNLSSGQSVAIKMIDKEKILKVGLMEQIKREISIMRLVRHPNVLQLFEVMATKSNIYFALEYAKGGELFHKMARAKLNEESARNYFQQLISAMDYCHSRGVYHRDLKPENLLLDENETLKVSDFGLSALAESRRQDGLLHTACGTPAYVAPEVLSRKGYSGSKADVWSCGVILFVLVANYLPFHDRNIIQMYRKIAKAEYRCPRHFSAELKELLYGILDPDPSTRMSISRIKRSAWYRKPIAISALNNETGKKSCTSEAPFSGPTICISSERNQEPPNLHNLNAFDIISLSTGFDLSGLFGERYGRRESLFTSRKPAAAVLVKLKELAKALNLKVTKTDNGVLKLATTKEGRKGRLELDAEVSEVAPFLLVELKKTNGDTLEYQRMMKEDIRPSLKDIIWTWQGDQQ | CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity). |
CIPKT_ORYSJ | Oryza sativa subsp. japonica | MPPSTGSVPPAASTPAAGDEATAAGRVLLGRYELGGLLGRGASAKVYLARDLLTGRDVAIKSFPNPRHGGGLRGGEEDVLLRPAPIEREAAILPRLRHRHVMRLREILATRKKVHFVLDLAAGGELFSLLDASGRMTEDLARHYFRQLISAVRYCHSRGVYHRDIKPENLLLDDAGDLKVADFGLGAVADGALHHTLCGTPAYVAPEILSRKGYNPAKVDIWSCGVVLFVLAAGYLPFNDASLVNMYRKIYAGKFRCPAWFSPELRCLVRRILDPNPATRIDTEEIITHPWFRQDASHFAMAQLMQHGHDEEAKFKTEFKEDDMARDMTAFDILACSPGSDLSGLFGAEPGKERVFVGEPAAAVLSRVEEAGKKEGYMVTREGKKGTGPVYVKGENGGIVAKVCVFKIADAVSVVEVVKGYGAEAARFWKARLEPAMKPPAAI | CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity). |
CIPKU_ORYSJ | Oryza sativa subsp. japonica | MAMETTSQDSQVIMGRYKLGRLLGRGTFAKVYKAYKLATGEAVAIKVFDKEAVQRSGTVEQVKREVDVMRRVHHRHVIRLHEVMATRSRIYFVMEYASGGELFTRLSRSPRFPEPVARRYFQQLITAVEFCHSRGVYHRDLKPENLLLDARGDLKVTDFGLSALDGGLRGDGLLHTTCGTPAYVAPEVLLKRGYDGAKADIWSCGVILFVLLAGYLPFNETNLVILYRNITESNYRCPPWFSVEARKLLARLLDPNPKTRITISKIMDRPWFQQATCPLGDMSLVASAPSVLLARKEASQQHDDEEDDGFAREKKKRSNVIMSSPVIDVRPSSMNAFDIISRSRGLDLSKMFDAEERRSEARFSTRETTTAIVSKLEEIAEAGRFSFKLKEKGRVELEGSQDGRKGALAIEAEIFKVAPEVHVVEVRKTGGDSPDFRDFYKQELKPSLGDMVWAWQGGDSPPLVPAAGRRPITKRS | CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity). |
CIPKV_ORYSJ | Oryza sativa subsp. japonica | MYRAKRAALSPKVKRRVGKYELGRTIGEGTFAKVRFAKNTENDEPVAIKILDKEKVQKHRLVEQIRREICTMKLVKHPNVVRLFEVMGSKARIFIVLEYVTGGELFEIIATNGRLKEEEARKYFQQLINAVDYCHSRGVYHRDLKLENLLLDASGNLKVSDFGLSALTEQVKADGLLHTTCGTPNYVAPEVIEDRGYDGAAADIWSCGVILYVLLAGFLPFEDDNIIALYKKISEAQFTCPSWFSTGAKKLITRILDPNPTTRITISQILEDPWFKKGYKPPVFDEKYETSFDDVDAAFGDSEDRHVKEETEDQPTSMNAFELISLNQALNLDNLFEAKKEYKRETRFTSQCPPKEIITKIEEAAKPLGFDIQKKNYKMRMENLKAGRKGNLNVATEVFQVAPSLHVVELKKAKGDTLEFQKFYRTLSTQLKDVVWKCDGEVEGNGAAA | Involved in cold stress tolerance. CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner.
Highly expressed in leaf blade and leaf sheath, but not in other tissues. |
CIPKW_ORYSJ | Oryza sativa subsp. japonica | MSTTKVKRRVGKYELGRTIGEGTFAKVKFARDTETGDPVAIKILDKEKVLKHKMVEQIKREISTMKLIKHPNVVRIYEVMGSKTKIYIVLEYVTGGELFDTIVNHGRMREDEARRYFQQLINAVDYCHSRGVYHRDLKPENLLLDSYGNLKVSDFGLSALSQQIKDDGLLHTTCGTPNYVAPEVLEDQGYDGAMADLWSCGVILFVLLAGYLPFEDSNLMTLYKKISNAEFTFPPWTSFPAKRLLTRILDPNPMTRVTIPEILEDEWFKKGYKRPEFDEKYDTTLDDVYAVFNDSEEHHVTEKKEEPEALNAFELISMSAGLNLGNLFDSEQEFKRETRFTSKCPPKEIVRKIEEAAKPLGFDVQKKNYKLRLEKVKAGRKGNLNVATEILQVAPSLHMVEVRKAKGDTLEFHKFYKNLSRTLKDVVWKSDDLQNQLS | CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity). |
CIPKX_ORYSJ | Oryza sativa subsp. japonica | MSTTKVKRRVGKYELGRTIGEGTFAKVKFARDTETGDPVAIKILDKEKVLKHKMVEQIKREISTMKLIKHPNVVRIYEVMGSKTNIYIVLEYVTGGELFDTIVNHGRMREDEARRYFQQLINAVDYCHSRGVYHRDLKPENLLLDSYGNLKVSDFGLSALSQQIKDDGLLHTTCGTPNYVAPEVLEDQGYDGAMADLWSCGVILFVLLAGYLPFEDSNLMTLYKKISNAEFTFPPWTSFPAKRLLTRILDPNPMTRITIPEILEDEWFKKGYKRPEFDEKYDTTLDDVDAVFNDSEEHHVTEKKEEPEALNAFELISMSAGLNLGNLFDSEQEFKRETRFTSKCPPKEIVRKIEEAAKPLGFDVQKKNYKICSPCLTTICMNIPFKLRLEKVKAGRKGNLNVATEILQVAPSLHMVEVRKAKGDTLEFHKFYKNLSRTLKDVVWKSDDLQNQLS | CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity). |
CLV1A_SOYBN | Glycine max | MRSCVCYTLLLFVFFIWLHVATCSSFSDMDALLKLKESMKGDRAKDDALHDWKFSTSLSAHCFFSGVSCDQELRVVAINVSFVPLFGHVPPEIGELDKLENLTISQNNLTGELPKELAALTSLKHLNISHNVFSGYFPGKIILPMTELEVLDVYDNNFTGSLPEEFVKLEKLKYLKLDGNYFSGSIPESYSEFKSLEFLSLSTNSLSGNIPKSLSKLKTLRILKLGYNNAYEGGIPPEFGTMESLKYLDLSSCNLSGEIPPSLANMRNLDTLFLQMNNLTGTIPSELSDMVSLMSLDLSFNGLTGEIPTRFSQLKNLTLMNFFHNNLRGSVPSFVGELPNLETLQLWENNFSSELPQNLGQNGKFKFFDVTKNHFSGLIPRDLCKSGRLQTFLITDNFFHGPIPNEIANCKSLTKIRASNNYLNGAVPSGIFKLPSVTIIELANNRFNGELPPEISGDSLGILTLSNNLFTGKIPPALKNLRALQTLSLDTNEFLGEIPGEVFDLPMLTVVNISGNNLTGPIPTTFTRCVSLAAVDLSRNMLDGEIPKGMKNLTDLSIFNVSINQISGSVPDEIRFMLSLTTLDLSYNNFIGKVPTGGQFLVFSDKSFAGNPNLCSSHSCPNSSLKKRRGPWSLKSTRVIVMVIALATAAILVAGTEYMRRRRKLKLAMTWKLTGFQRLNLKAEEVVECLKEENIIGKGGAGIVYRGSMRNGSDVAIKRLVGAGSGRNDYGFKAEIETVGKIRHRNIMRLLGYVSNKETNLLLYEYMPNGSLGEWLHGAKGGHLKWEMRYKIAVEAAKGLCYLHHDCSPLIIHRDVKSNNILLDAHFEAHVADFGLAKFLYDLGSSQSMSSIAGSYGYIAPEYAYTLKVDEKSDVYSFGVVLLELIIGRKPVGEFGDGVDIVGWVNKTRLELSQPSDAAVVLAVVDPRLSGYPLISVIYMFNIAMMCVKEVGPTRPTMREVVHMLSNPPHSTTHTHNLINL | LRR receptor kinase involved in the regulation of plant growth.
Subcellular locations: Cell membrane
Expressed in roots, leaves, vegetative shoot apex, and reproductive floral apex. |
CLV1B_SOYBN | Glycine max | MRSCVCYTLLLFIFFIWLRVATCSSFTDMESLLKLKDSMKGDKAKDDALHDWKFFPSLSAHCFFSGVKCDRELRVVAINVSFVPLFGHLPPEIGQLDKLENLTVSQNNLTGVLPKELAALTSLKHLNISHNVFSGHFPGQIILPMTKLEVLDVYDNNFTGPLPVELVKLEKLKYLKLDGNYFSGSIPESYSEFKSLEFLSLSTNSLSGKIPKSLSKLKTLRYLKLGYNNAYEGGIPPEFGSMKSLRYLDLSSCNLSGEIPPSLANLTNLDTLFLQINNLTGTIPSELSAMVSLMSLDLSINDLTGEIPMSFSQLRNLTLMNFFQNNLRGSVPSFVGELPNLETLQLWDNNFSFVLPPNLGQNGKLKFFDVIKNHFTGLIPRDLCKSGRLQTIMITDNFFRGPIPNEIGNCKSLTKIRASNNYLNGVVPSGIFKLPSVTIIELANNRFNGELPPEISGESLGILTLSNNLFSGKIPPALKNLRALQTLSLDANEFVGEIPGEVFDLPMLTVVNISGNNLTGPIPTTLTRCVSLTAVDLSRNMLEGKIPKGIKNLTDLSIFNVSINQISGPVPEEIRFMLSLTTLDLSNNNFIGKVPTGGQFAVFSEKSFAGNPNLCTSHSCPNSSLYPDDALKKRRGPWSLKSTRVIVIVIALGTAALLVAVTVYMMRRRKMNLAKTWKLTAFQRLNFKAEDVVECLKEENIIGKGGAGIVYRGSMPNGTDVAIKRLVGAGSGRNDYGFKAEIETLGKIRHRNIMRLLGYVSNKETNLLLYEYMPNGSLGEWLHGAKGGHLKWEMRYKIAVEAAKGLCYLHHDCSPLIIHRDVKSNNILLDGDLEAHVADFGLAKFLYDPGASQSMSSIAGSYGYIAPEYAYTLKVDEKSDVYSFGVVLLELIIGRKPVGEFGDGVDIVGWVNKTRLELAQPSDAALVLAVVDPRLSGYPLTSVIYMFNIAMMCVKEMGPARPTMREVVHMLSEPPHSATHTHNLINL | LRR receptor kinase involved in the regulation of root and shoot growth, and root nodule organogenesis . Involved in long distance nodulation signaling events . Involved in the autoregulation of nodulation (AON), a long distance systemic signaling from root to shoot and back again, which allows legumes to limit the number of root nodules formed based on available nitrogen and previous rhizobial colonization . Acts from shoot to root to control AON .
Subcellular locations: Cell membrane
Expressed in roots, leaves, vegetative shoot apex, and reproductive floral apex. |
CNIH1_ORYSJ | Oryza sativa subsp. japonica | MVFVWLTAFFLVVALIVLVIYQLMCLADLEFDYINPFDSSSRINKVVIPEFVLQAALSVLFLLSGHWAMFLLSAPMVYYNYTLYQRRQHLVDVTEIFNHLGREKKRRLFKIVGLIILLFLSLFWMIWTVLLEEDE | Acts as a cargo receptor necessary for the transportation of the cation transporter HKT1;3 and possibly other secretory proteins from the endoplasmic reticulum (ER) in COPII-coated vesicles targeted to the Golgi apparatus.
Subcellular locations: Endoplasmic reticulum membrane, Golgi apparatus membrane
Located primarily in the endoplasmic reticulum (ER); may cycle between the ER and the Golgi apparatus. |
CNIH2_ORYSJ | Oryza sativa subsp. japonica | MSIELILWLFSFASIMVLIGLTAYQLICLSDLEFDYINPYDSSSRINSVVLIEYALQGALCASFLLTLHWFPFLVMAPVAYYHGKLYMDRKHLVDVTEIFRQLNWEKKYRMIKLAFYFSLFIITIYRLVMTAVTLFIDEDANLVDTRTI | Acts as a cargo receptor necessary for the transportation of secretory proteins from the endoplasmic reticulum (ER) in COPII-coated vesicles targeted to the Golgi apparatus.
Subcellular locations: Endoplasmic reticulum membrane, Golgi apparatus membrane
Located primarily in the endoplasmic reticulum (ER); may cycle between the ER and the Golgi apparatus. |
COB21_ORYSJ | Oryza sativa subsp. japonica | MPLRLEIKRKFAQRSERVKSVDLHPTEPWILSSLYSGSVCIWDYQSQTMVKSFEVSELPVRSAKFISRKQWVVAGADDMFIRVYNYNTMDKVKVFEAHTDYIRCVAVHPTLPYVLSSSDDMLIKLWDWDKGWMCTQIFEGHSHYVMQVTFNPKDTNTFASASLDRTTKIWSLGSPDPNFTLDGHQKGVNCVDYFTGGDRPYLITGSDDSTAKVWDYQTKSCVQTLEGHTHNISAVCFHPELPIIITGSEDGTVRIWHSTTYRLENTLNYGLERVWAVGYMKGSRRMVIGYDEGTIMIKMGREVPVASMDTSGKIIWAKHNEIQTVNIKTVGAGFEVTDGERLPLAVKELGSCDLYPQSLKHNPNGRFVVVCGDGEFIIYTALAWRNRSFGSALEFVWSSEGEYAIRESTSRIKIFSKSFQEKKTIRPTFSAERIFGGILLAMCSSDFICFYDWADCRLIRRIDVNVKNLYWADSGDLVAIASDTSFYILKYNRDVVASYLESGKPVDEEGVEDAFELLHEVNERVRTGIWVGDCFIYNNSSWRLNYCVGGEVTTMYHLDRPMYLLGYLANQSRVYLIDKEFNVMGYTLLLSLIEYKTLVMRGDIERANDILPSIPKAQYNNVAHFLESRGMLEEALEIATDADYRFDLAVQLGKLEVAKAIAMEAQSESKWKQLGELAMSTGKLDMAEECLVQAKDLSGLLLLYSSLGDAEGIEKLASQAKEHGKNNVAFLCLFMLGKLEDCIQLLIDSNRIPEAALMARSYLPSKVSEIVAIWRNDLSKVNPKAAESLADPSEYPNLFEDWQVALTVEKNVASRRVHYPPADEYLNHAEKSDMTLVEAFKRMQVIEDEETEDALDENGEPDEEVLEENKVEESTDEAVEVDADEPEETVLVNGKEGEEQWVLTEHE | The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular locations: Cytoplasm, Golgi apparatus membrane, Cytoplasmic vesicle, COPI-coated vesicle membrane
The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. |
COB22_ORYSJ | Oryza sativa subsp. japonica | MPLRLDIKRKLAQRSERVKSVDLHPTEPWILSSLYSGSVCIWNYQTQTMVKSFEVTELPVRSSKFIARKQWIVAGADDMFIRVYNYNTMDKVKVFEAHTDYIRCVAVHPTQPFVLSSSDDMLIKLWDWDKGWMCTQIFEGHSHYVMQVTFNPKDTNTFASASLDRTVKVWSLGSPDPNFTLDGHSKGVNCVDYFTGGDRPYLITGSDDQTAKVWDYQTKSCVQTLEGHAHNVSAVCFHPELPITLTGSEDGTVRLWHSTTYRLENTLNYGLERVWALGYMKGSRRVVIGYDEGTIMIKIGREVPVASMDSSGKIIWSKHNEIQTVNIKTIGADNEIADGERLPLAVKELGTCDLYPQSLRHNPNGRFVVVCGDGEYIIYTALAWRNRSFGSALEFVWSVDGEYAVRESTSRIKIYSKNFQERKSIRPPFSAERIFGGVLLAMCTNDFICFHDWAEGRMIRRIDVNVKNLYWADSGDLVTIASDTSFYILKYNRDVVSSHLDGGGSVGEEGVEDAFELLHEINERIRTGLWVGDCFIYNNSSSRLNYCVGGEVTTLFHLDRQMYLLGYLANQSRVYLIDKQFNVVGYTLLLTMIEYKTLVMRGDFDRANALLPSIPKEQHDSVARFLESQGMLEEALEIATDSNYRFDLAVQLGRLEVAKAIAIEAQSESKWRQLGELAMSTGKLDMAEECLLHAMDLSGLLLLYSSLGDAEGLTKLTSMAKEQGKNNVAFLCFFMLGKLEECLQLLIESNRIPEAALMSRSYLPSKVPEIVTLWKKDLQKVNPKAAESLADPDEYPNLFEDWQIALNVEANVAPKRGIYPPAEEYIIHAERPNETLVEAFKSMHIHLEEVLPDENGDDTHEAIEENGVEESQEDAVEVDVEADGSTDGAVLVNGNDTEEQWGTNNEESSA | The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular locations: Cytoplasm, Golgi apparatus membrane, Cytoplasmic vesicle, COPI-coated vesicle membrane
The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. |
COB23_ORYSJ | Oryza sativa subsp. japonica | MPLRLDIKRKLAQRSERAKSVDLHPTEPWILSSLYSGSVCIWNYQTQTMVKSFEVTELPVRSSKFITRKQWVVAGADDMFIRVYNYNTMDKVKVFEAHTDYIRCVAVHPTQPFVLSSSDDMLIKLWDWDKGWMCTQIFEGHSHYVMQVTFNPKDTNTFASASLDRTVKVWSLGSPDPNFTLDGHSKGVNCVDYFTGGDRPYLITGSDDQTAKVWDYQTKSCVQTLEGHAHNVSAVCFHPELPIILTGSEDGTVRLWHSTTYRLENTLNYGLERVWALGYMKGSRRVVIGYDEGTIMIKIGREVPVASMDSSGKIIWSKHNEIQTVNIKTIGADNEIADGERLPLVVKELGTCDLYPQSLRHNPNGRFVVVCGDGEYIIYTALAWRNRSFGSALEFVWSLDGEYAVRESTSRIKIYSKNFQERKSIRPPFSAERIFGGVLLAMCTNDFICFHDWAEGRMIRRIDVNVKNLYWADSGDLVTIASDTSFYILKYNRDVVSSHLDGGGSVGEEGVEDAFELLHEINERIRTGLWVGDCFIYNNSSSRLNYCVGGEVTTLFHLDRQMYLLGYLANQSRVYLIDKQFNVVGYTLLLTMIEYKTLVMRGDFDRANALLPSIPKEQHDSVARFLESRGMLEEALEIATDSNYRFDLAVQLGRLEVAKAIAIEAQSESKWRQLGELAMSTGKLDMAEECLLHAMDLSGLLLLYSSLGDAEGLTKLTSMAKEQGKNNVAFLCFFMLGKLEECLQLLIESNRIPEAALMSRSYLPSKVPEIVTLWKKDLQKVNPKAAESLADPNEYPNLFEDWQIALNVEANVAPKRGIYAPAKEYIIHAERPNETLVEAFKNMRIHQEEVLPDENGDDTHEAIEENGVEESQEDAVEVDVEADGSTDGTVLVNGNDTEEQWGTNNEESLA | The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular locations: Cytoplasm, Golgi apparatus membrane, Cytoplasmic vesicle, COPI-coated vesicle membrane
The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. |
COLD1_ORYSI | Oryza sativa subsp. indica | MGWGAVVYEGGVVGASLVGLGWAGLWFLNRRLYKEYEERRALVQILFGLVFAFSCNLFQLVLFEILPVLSKHARFLNWHLDLFCLILLLVFVLPYYHCYLLLRNSGVRRERALLVAALFLLVFLYGFWRMGIHFPMPSPEKGFFTMPQLVSRIGVIGVSVMAVLSGFGAVNLPYSYLSLFIREIDEMDIKTLERQLMQSMETCIAKKKKIVLSKMEMERIQGSEEKLKARSFLKRIVGTVVRSVQEDQTEQDIKSLDAEVQALEELSKQLFLEIYELRQAKIAAAFSRTWRGHAQNLLGYALSVYCVYKMLKSLQSVVFKEAGSVDPVTMTITIFLRHFDIGIDVTLLSQYISLIFIGMLVVISVRGFLANVMKFFFAVSRVGSGSTTNVVLFLSEIMGMYFISSILLIRKSLANEYRVIITDVLGGDIQFDFYHRWFDAIFVASAFLSLLLISAQYTSRQTDKHPID | Involved in chilling tolerance.
Subcellular locations: Cell membrane, Endoplasmic reticulum membrane |
COLD1_ORYSJ | Oryza sativa subsp. japonica | MGWGAVVYGGGVVGASLVGLGWAGLWFLNRRLYKEYEERRALVQILFGLVFAFSCNLFQLVLFEILPVLSKHARFLNWHLDLFCLILLLVFVLPYYHCYLLLRNSGVRRERALLVAALFLLVFLYGFWRMGIHFPMPSPEKGFFTMPQLVSRIGVIGVSVMAVLSGFGAVNLPYSYLSLFIREIDEKDIKTLERQLMQSMETCIAKKKKIVLSKMEMERIQGSEEKLKARSFLKRIVGTVVRSVQEDQTEQDIKSLDAEVQALEELSKQLFLEIYELRQAKIAAAFSRTWRGHAQNLLGYALSVYCVYKMLKSLQSVVFKEAGSVDPVTMTITIFLRHFDIGIDVTLLSQYISLIFIGMLVVISVRGFLANVMKFFFAVSRVGSGSTTNVVLFLSEIMGMYFISSILLIRKSLANEYRVIITDVLGGDIQFDFYHRWFDAIFVASAFLSLLLISAQYTSRQTDKHPID | Involved in chilling tolerance. Interacts with the G-protein alpha subunit GPA1 to activate the calcium channel for sensing low temperature and to accelerate G-protein GTPase activity.
Subcellular locations: Cell membrane, Endoplasmic reticulum membrane |
CONV_CANCT | Canavalia cathartica | ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVGKRLSAVVSYPNGDSATVSYDVDLDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNSTHETNALHFVFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFDATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN | D-mannose/D-glucose-binding lectin which binds alpha-methyl-D-mannoside, D-mannose and D-glucose in that order (, ). Also binds to serum fetuin and ovalbumin . Has hemagglutinating activity towards rabbit erythrocytes . Is not toxic towards larvae of the brine shrimp Artemia . Induces relaxation in rat endothelized aorta . Shows a transient edematogenic effect in rat . |
COPG1_ORYSJ | Oryza sativa subsp. japonica | MAQPYMKKDDDDEDVEYSPFYGIEKGAVLQEARAFHDPQLDARKCSQVITKLLYLLNQGETFTKVEATEVFFAVTKLFQSKDAGLRRLVYLMIKELSPSSDEVIIVTSSLMKDMNSKTDMYRANAIRVLCRIIDGTLLTQIERYLKQAIVDKNPVVASAALVSGIHLLQANPEIVKRWSNEVQEAVQSRFALVQFHGLALLHQIRQNDRLAISKMVSGLTRGSVRSPLAQCLLIRYTSQVIRESSMNTQTSDRPFFDYLESCLRHKSEMVILEAARKIAEMDVTSRELAPAITVLQLFLSSSKPVLRFAAVRTLNKVAMTRPLAVTNCNVDLESLMSDQNRSIATLAITTLLKTGNESSVDRLMKQITNFMSDIADEFKIVVVEAIRSLCLKFPLKYRSMMNFLSNSLREEGGFEYKKAIVDSIVTLISEIPDAKEIGLLYLCEFIEDCEFTYLSSQILHLLGNEGPRTSDPSRYIRYIYNRVILENATVRASAVSTLAKFGALVDALKPRIFVLLRRCLFDTDDEVRDRATLYLQTLDGEVAVGSTEKDVKEFLFGSFDVPLANLEASLKTYEPSEEPFDISLVSREVKSQPLQEKKAPGKKPPAGAPAPAPVPAVDAYQKILSSIPEFSGFGRLFKSSEPVELTEAETEYAINVVKHIYSSHVVLQYNCTNTIPEQLLENVTVYVDATDAEEFSEVCSKPLRSLPYDSPGQIFVAFEKPEHVPATGKFSNVLKFIVKEVDTSTGEVDEDGVEDEYQIEDLEIVSADYMLRVAVSNFRNAWENMDPESERVDEYGLGVRESLAEAVSAVISILGMQPCEGTEVVPKNARSHTCLLSGVFIGDAKVLVRLSFGLSGPKEVAMKLAVRSDDPEVSDKIHEIVASG | The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular locations: Cytoplasm, Golgi apparatus membrane, Cytoplasmic vesicle, COPI-coated vesicle membrane
The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. |
COPG2_ORYSJ | Oryza sativa subsp. japonica | MAQPLVVKKDDDLDEEEYYSPFLGIEKGAVLQEARVFHDPQLDARRCCQVITKLLYLLNQGDTFTKVEATEVFFATTKLFQSKDAGLRRMVYLMIKELSPSADEVIIVTSSLMKDMNSKTDMYRANAIRVLCRIIDSTLLTQIERYLKQAIVDKNPVVASAALVSGIYLLQTSPEVVKRWSNEVQEAVQSRAALVQFHALALLHQIRQNDRLAVSKLVTSLTRGSVRSPLAQCLLIRYTSQVIRESSMNSQGGDRPFFDFLESCLRNKAEMVILEAARAITELNGVTSRELTPAITVLQLFLSSSKPVLRFAAVRTLNKVASTHPLAVTNCNIDMESLISDQNRSIATLAITTLLKTGNESSVDRLMKQMTNFMSDIADEFKIVVVEAIRSLCLKFPLKYRSLMNFLSNILREEGGFEYKKAIVDSIIILIRDIPDAKESGLFHLCEFIEDCEFTYMSTQILHFLGNEGPKTSDPSKYIRYIYNRVILENATVRASAVSTLAKFGALVDSLKPRIFVLLRRCLFDGDDEVRDRATLYLKLLGGEATVGETEKDVNEFLFGSFDIPLVNLETSLQNYEPSEAPFDISSVSLETKSQPLAEKKTTGKKPTGPASALSGPVPTVDASYEKLLSSIPEFAGFGKLFKSSAPVELTEAETEYSVNVVKHIYDGHVVLQYNCTNTIPEQLLEEVVVFVDASEADEFSEVATKSLRSLPYDSPGQTFVAFEKLEGVLATGKFSNILKFIVKEVDPSTGEADDDGVEDEYQLEDLEITSADYMLKVGVSNFRNAWESMDPESERVDEYGLGARESLAEAVSAVIGILGMQPCEGTDVVPSNSRSHTCLLSGVFIGNVKVLVRLSFGLSGPKEVAMKLAVRSDDPEISDKIHEIVANG | The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular locations: Cytoplasm, Golgi apparatus membrane, Cytoplasmic vesicle, COPI-coated vesicle membrane
The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. |
COQ5_ORYSJ | Oryza sativa subsp. japonica | MALRSAAGRLASSSRRRLLSPPTSIHTAFLHSHATSFGYKQVAEEDKSKLVGNVFSSVASSYDLMNDLMSVGLHRLWKDRLISKLNPFPGMKHLDVAGGTGDVAFRALERINSVSHRAMQGTLTDIEEETQIYVCDINPNMLNVGKKRASERGYKEGHCLSWIQGDAEALSFEDGSMDGYTIAFGIRNVTHIEKALSEAYRVLKRGGRFLCLELSHVDVPLFKEIYDVYSFSVIPAVGELVAGDRQSYQYLVESIRRFPNQEKFAQMIQEAGFERVEYENLVGGVVAIHSGLKL | Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Subcellular locations: Mitochondrion inner membrane |
COX2_ORYSJ | Oryza sativa subsp. japonica | MILRSLECRFLTIALCDAAEPWQLGSQDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALWHFNEQTNPIPQRIVHGTTIEIIRTIFPSVIPLFIAIPSFALLYSMDGVLVDPAITIKAIGHQWYRSYEYSDYNSSDEQSLTFDSYTIPEDDPELGQSRLLEVDNRVVVPAKTHLRMIVTPADVLHSWAVPSSGVKCDAVPGRSNLTSISVQREGVYYGQCSEICGTNHAFTPIVVEAVTLKDYADWVSNQLILQTN | Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular locations: Mitochondrion inner membrane |
COX2_PEA | Pisum sativum | MKLEWLFLTIAPCDAAEPWQLGFQDAATPMMQGIIDLHHDIFFFLILILVFVSRILVRALWHFHYKKNPIPQRIVHGTTIEILRTIFPSIIPMFIAIPSFALLYSMDGVLVDPAMTIKAIGHQWYRTYEYSDYNSSDEQSLTFDSYTIPEDDLELGQSGLLEVDNRVVVPAKTHLRIIVTPADVPHSWAVPSLGVKCDAVPGRLNQISISVQREGVYYGQCSEICGTNHAFPIVVEAVPSKDYGSRVSNQLIPQTGEA | Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular locations: Mitochondrion inner membrane |
COX3_MAIZE | Zea mays | MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHSFQGGATLLSLGLIFLLYTMFVWWRDVLRESTLEGHHTKAVQLGPRYGSILFIVSEVMSFFLFFWASSHSSLAPTVEIGGIWPPKGIGVLDPWEIPLLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVSTGFQGMEYYQAPSTISDSIYGSTFLLATGFHGFHVIIGTLFLIVCGIRQYLGHLTKKHHVGFEAAAWYWHFVDVVRLFPFVSIYWWGGT | Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular locations: Mitochondrion inner membrane |
COX5C_HORVU | Hordeum vulgare | MAGGRVAHATLKGPSVVKEIFIGLTLGLVAGGMWKMHHWNEQRKTRSFYDMLEKGQISVVVEE | This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Subcellular locations: Mitochondrion inner membrane |
COX5C_ORYSJ | Oryza sativa subsp. japonica | MAGGRIAHATLKGPSVVKEICIGLTLGLVAGGLWKMHHWNEQRKTRSFYDMLEKGQISVVVEE | This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Subcellular locations: Mitochondrion inner membrane |
COX5C_SOLTU | Solanum tuberosum | AGXXXAHXXYKGPSVVKELVIXXXLGLXAG | This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Subcellular locations: Mitochondrion inner membrane |
CPI10_SOLTU | Solanum tuberosum | TCHDDDNLVLPEVYDQDGNPLRIGERYIIKNPLLGAGAVYLDNIGNLQCPNAVLQHMSIPQFLGKGTPVVFIRKSESDYGDVVRLMTAVYIKFFVKTTKLCVDETVWKVNNEQLVVTGGNVGNENDIFKIKKTDLVIRGMKNVYKLLHCPSHLECKNIGSNFKNGYPRLVTVNDEKDFIPFVFIKA | Probable inhibitor of cysteine proteases. May protect the plant by inhibiting proteases of invading organisms.
Subcellular locations: Vacuole |
CPS11_ORYSJ | Oryza sativa subsp. japonica | MAAARRAAGLLPLLLSSPSRARLPHRQALALTPPLLRPHRLYSHSPKPSSSAAFSAFASASNGAPAGRARELHLYNTKSRRKELFQPRVPGGEVGMYVCGVTPYDDSHIGHARAYVAFDVLYRYLRYLDHKVRYVRNFTDIDDKIIARANQLGEDPFSLSKRYSDDFLSDMANLHCLPPSVEPRVSDHIDQIINMIKQIIDNDCAYAIGGDVYFSVENFPEYGDLSGRKLDDNRAGERVAVDERKKNPADFALWKAAKDGEPSWDSPWGPGRPGWHIECSAMSAHYLGHSFDIHGGGEDLIFPHHENEIAQSRAACCDSSINYWIHNGFVNVNSQKMSKSLGNFVTIRKVTELYHPLALRMFLLGTHYRSPINYTIEQLNVASDRLYYTYQTLQDCEESCQQHQSKAGDPLPVNTTNCIQKLHDEFETSMSDDLHTSVALAAISEPLKVMNDLLHTRKGKKQEKRLESLSAMEEKIRMVLSVLGLLPSSYYEALQQLREKALRRASMTEEQVLQKIEERTSARKAKQYEKSDEIRKELAAVGIALMDGPDGTTWRPSVPLSEQGVVAST | Nuclear genome-encoded factor required for normal assembly of chloroplast polysomes.
Subcellular locations: Plastid, Chloroplast, Mitochondrion |
CPSF2_ORYSJ | Oryza sativa subsp. japonica | MGTSVQVTPLSGAYGEGPLCYLLAVDGFRFLLDCGWTDLCDPSHLQPLAKVAPTIDAVLLSHADTMHLGALPYAMKHLGLSAPVYATEPVFRLGILTLYDYFISRRQVSDFDLFTLDDIDAAFQNVVRLKYSQNHLLNDKGEGIVIAPHVAGHDLGGTVWKITKDGEDVVYAVDFNHRKERHLNGTALGSFVRPAVLITDAYNALNNHVYKRQQDQDFIDALVKVLTGGGSVLLPIDTAGRVLEILLILEQYWAQRHLIYPIYFLTNVSTSTVDYVKSFLEWMNDSISKSFEHTRDNAFLLKCVTQIINKDELEKLGDAPKVVLASMASLEVGFSHDIFVDMANEAKNLVLFTEKGQFGTLARMLQVDPPPKAVKVTMSKRIPLVGDELKAYEEEQERIKKEEALKASLNKEEEKKASLGSNAKASDPMVIDASTSRKPSNAGSKFGGNVDILIDGFVPPSSSVAPMFPFFENTSEWDDFGEVINPEDYLMKQEEMDNTLMPGAGDGMDSMLDEGSARLLLDSTPSKVISNEMTVQVKCSLAYMDFEGRSDGRSVKSVIAHVAPLKLVLVHGSAEATEHLKMHCSKNSDLHVYAPQIEETIDVTSDLCAYKVQLSEKLMSNVISKKLGEHEIAWVDAEVGKTDDKLTLLPPSSTPAAHKSVLVGDLKLADFKQFLANKGLQVEFAGGALRCGEYITLRKIGDAGQKGSTGSQQIVIEGPLCEDYYKIRELLYSQFYLL | CPSF plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A)polymerase and other factors to bring about cleavage and poly(A) addition.
Subcellular locations: Nucleus |
CRP1_MAIZE | Zea mays | MPASLLPPTFLPHHLRRLAPAGCTTSSVTSSSVSIPASRYDFEPLLAYLSSPSVSASLTSPSPPASVPAPEHRLAASYSAVPSHEWHALLRDLAASDASLPLAFALLPFLHRHRLCFPLDLLLSSLLHSLSVSGRLLPHSLLLSFPPSLSDPPSPLLLNSLLAASAAASRPAVALRLLSLLREHDFLPDLASYSHLLASLLNTRDPPDAALLERLLGDLRESRLEPDAPLFSDLISAFARAALPDAALELLASAQAIGLTPRSNAVTALISALGTAGRVAEAEALFLEFFLAGEIKPRTRAYNALLKGYVRIASLKNAEQVLDEMSQCGVAPDEATYSLLVDAYTRAGRWESARILLKEMEADGVKPSSYVFSRILAGFRDRGDWQKAFAVLREMQASGVRPDRHFYNVMIDTFGKYNCLGHAMDAFNKMREEGIEPDVVTWNTLIDAHCKGGRHDRAAELFEEMRESNCPPGTTTYNIMINLLGEQEHWEGVEAMLSEMKEQGLVPNIITYTTLVDVYGRSGRYKEAIDCIEAMKADGLKPSPTMYHALVNAYAQRGLADHALNVVKAMKADGLEVSILVLNSLINAFGEDRRVVEAFSVLQFMRENGLRPDVITYTTLMKALIRVEQFDKVPVIYEEMITSGCAPDRKARAMLRSGLKYIKHMRVA | Required for the translation of the chloroplast petA and petD mRNAs. Required for the processing of the petD mRNA from a polycistronic precursor . Binds with high affinity to the 5'-UTR of the chloroplastic petA transcript . Activates psaC and petA translation by binding their 5'-UTRs (, ).
Subcellular locations: Plastid, Chloroplast stroma |
CSPLC_ORYSJ | Oryza sativa subsp. japonica | MGSIGNGRNGSEVGIQIPAMGNKEVLERPAIPRWPRLGVVMVATRAVALVMAVLSMALMISAKQRGSLKIFGIEIPLYANWSFSDSLEYLVGMSAVSAAYCLAQLLLTAHKAVKNAPVVQSRNYAWLLFTGDQIFAYAMMSAGSAAAAVANLNRTGIRHTALPNFCKPLPRFCDLSAASIACAFLSCIFLAASAVIDVIWLSNM | Subcellular locations: Cell membrane |
CSPLC_SORBI | Sorghum bicolor | MASRTVLLPSAVLILRLLSLGLLAASLALIAADKLNVDSDPPQRYTFRDVYAYRYVLAVAVIGCAYTLLQLPLAAVSIIASGNNKRGIGAGGGSVAVALLVLVLLADVVFALLLATGAAAGFAFTYDVKRYLDGQFDDDSIGTPEVDKLHRDMDKFFDLAYAAAGLMLAAAACMALVIMLSVYSLARQVRSDYI | Subcellular locations: Cell membrane |
CSPLC_SOYBN | Glycine max | MPEMVDSNSTPSSSTGSRTVLLLLRVLTFVFLLIALILIAIVKQTDDETGVEIKFNDIYAYRYMISTIIIGFAYNLLQMALSIFTVVSGNRVLSGDGGYLFDFFGDKIISYLLISGSAAGFGVTVELGRGVPSNSFMDKANASASLLLIAFLFTAVASTFTSFALPKKD | Subcellular locations: Cell membrane |
CSPLD_MAIZE | Zea mays | MVAAARVVSGVKAEGLLRGACAALAAAAALLLGLSTQTETVLLVRKKGTVKDVQALWVLAMAAASAAGYHLLQLLKCLYLGRGGGRALAWTCLLLDKACAYATFATTVAAAQACVVALDGAHALQWTKLCNIYTRFCEQVAGSLVLGMLAAVGTAVLSAASARNVFRHYYCSSHSPPAPPPETCDAH | Subcellular locations: Cell membrane |
CSPLD_ORYSJ | Oryza sativa subsp. japonica | MSSYMEAAAAARAAEAKTEGLLRGACALLAAAAALLVGLNTQTETVLFIRKKATVKDVQALWVLAMAAAAAAGYHLLQLLRCFYLSRFADGKPCRHRRAIAWLCFLLDKGCAYITFATTVAAAQACVVALYGTHALQWTKLCNIYTRFCEQVAGSLVCAMLAAVGTALLSVVSARNLFRLYPSMLSPPPSSFVG | Subcellular locations: Cell membrane |
CSPLD_SORBI | Sorghum bicolor | MAEEVWKALSLLFRIAALGLSLAAAIVMATASQLVIGGGGGHESSSYSVSFGQYNALRYFVAAGAISAVCSAAALYLFAVRADFTVVVVSLPLVPVLDAAAQGFLFSAAGAAFATRDVVGGGTSAGRGSSVCDAAGAFCGRVTVAAAVCAFAAVSVATAALASRDAGGGSSEGRRFEW | Subcellular locations: Cell membrane |
CURE1_SOLLC | Solanum lycopersicum | MGNIKFLLLVFFLIVVVVNGCWEEERNALLELQTNIMSSNGELLVDWAGYNAAHFVDCCFWDRVKCSLETGRVIKLDLEADFGTGDGWLFNASLFLPFKSLQVLLLSSQNIIGWTKNEGFSKLRQLPNLKEVDLQYNPIDPKVLLSSLCWISSLEVLKLGVDVDTSFSIPMTYNTNMMSKKCGGLSNLRELWFEGYEINDINILSALGELRNLEKLILDDNNFNSTIFSSLKIFPSLKHLNLAANEINGNVEMNDIIDLSNLEYLDLSDNNIHSFATTKGNKKMTSLRSLLLGSSYSNSSRVIRSLKSFSSLKSLSYKNSNLTSPSIIYALRNLSTVEYLYFKGSSLNDNFLPNIGQMTSLKVLNMPSGGNNGTLPNQGWCELKYIEELDFLNNNFVGTLPLCLGNLTSLRWLSLAGNNLHGNIASHSIWRRLTSLEYLDIADNQFDVPLSFSQFSDHKKLIYLNVGYNTIITDTEYQNWIPNFQLEFFAIQRCIALQKLPSFLHYQYDLRILAIEGNQLQGKFPTWLLENNTRLAAIYGRDNAFSGPLKLPSSVHLHLEAVDVSNNKLNGHIPQNMSLAFPKLLSLNMSHNHLEGPIPSKISGIYLTILDLSVNFLSGEVPGDLAVVDSPQLFYLRLSNNKLKGKIFSEEFRPHVLSFLYLNDNNFEGALPSNVFLSSLITLDASRNNFSGEIPGCTRDNRRLLQLDLSKNHLQGLIPVEICNLKIINVLAISENKISGSIPSCVSSLPLKHIHLQKNQLGGELGHVIFNFSSLITLDLRYNNFAGNIPYTIGSLSNLNYLLLSNNKLEGDIPTQICMLNNLSIVDLSFNKLYGPLPPCLGYLTQTKKDAEISWTYFAENYRGSWLNFVIWMRSKRHYHDSHGLLSDLFLMDVETQVQFSTKKNSYTYKGNILKYMSGIDLSSNRLTGEIPVELGNMSNIHALNLSHNHLNGRIPNTFSNLQEIESLDLSCNRLNGSIPVGLLELNSLAVFSVAYNNLSGAVPDFKAQFGTFNKSSYEGNPFLCGYPLDNKCGMSPKLSNTSNINGDEESSELEDIQCFYIGFVVSFGAILLGLAAALCLNRHWRRAWFRMIEALMFYCYYFVLDNIVTPIKSRWYKNVG | Involved in plant defense. Contributes to resistance against parasitic plant C.reflexa (, ). Acts as a receptor for the 11 kDa glycine-rich protein (GRP) of C.reflexa inducing immune responses such as emission of stress-related phytohormone ethylene, reactive oxygen species (ROS) release, and hypersensitive cell death (, ). Recognizes a specific pathogen-associated molecular pattern (PAMP), a cysteine-rich peptide 21 (crip21), from GRP located on the cell wall of C.reflexa .
Subcellular locations: Cell membrane, Cell surface |
CVCA_PEA | Pisum sativum | MATTVKSRFPLLLFLGIIFLASVCVTYANYDEGSETRVPGQRERGRQEGEKEEKRHGEWRPSYEKEEHEEEKQKYRYQREKKEQKEVQPGRERWEREEDEEQVEEEWRGSQRREDPEERARLRHREERTKRDRRHQREGEEEERSSESQEHRNPFLFKSNKFLTLFENENGHIRRLQRFDKRSDLFENLQNYRLVEYRAKPHTIFLPQHIDADLILVVLNGKAILTVLSPNDRNSYNLERGDTIKIPAGTTSYLVNQDDEEDLRVVDFVIPVNRPGKFEAFGLSENKNQYLRGFSKNILEASLNTKYETIEKVLLEEQEKKPQQLRDRKRTQQGEERDAIIKVSREQIEELRKLAKSSSKKSLPSEFEPFNLRSHKPEYSNKFGKLFEITPEKKYPQLQDLDILVSCVEINKGALMLPHYNSRAIVVLLVNEGKGNLELLGLKNEQQEREDRKERNNEVQRYEARLSPGDVVIIPAGHPVAISASSNLNLLGFGINAKNNQRNFLSGSDDNVISQIENPVKELTFPGSSQEVNRLIKNQKQSHFASAEPEQKEEESQRKRSPLSSVLDSFY | Seed storage protein.
Subcellular locations: Vacuole, Aleurone grain, Vacuole
Cotyledonary membrane-bound vacuolar protein bodies. |
CVCB_PEA | Pisum sativum | MATTIKSRFPLLLLLGIIFLASVVSVTYANYDEGSEPRVPAQRERGRQEGEKEEKRHGEWRPSYEKEEDEEEGQRERGRQEGEKEEKRHGEWGPSYEKQEDEEEKQKYRYQREKEDEEEKQKYQYQREKKEQKEVQPGRERWEREEDEEQVDEEWRGSQRREDPEERARLRHREERTKRDRRHQREGEEEERSSESQERRNPFLFKSNKFLTLFENENGHIRLLQRFDKRSDLFENLQNYRLVEYRAKPHTIFLPQHIDADLILVVLSGKAILTVLSPNDRNSYNLERGDTIKLPAGTTSYLVNQDDEEDLRLVDLVIPVNGPGKFEAFDLAKNKNQYLRGFSKNILEASYNTRYETIEKVLLEEQEKDRKRRQQGEETDAIVKVS | Seed storage protein.
Subcellular locations: Vacuole, Aleurone grain, Vacuole
Cotyledonary membrane-bound vacuolar protein bodies. |
CYB6_SOLBU | Solanum bulbocastanum | MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRPTVTEAFASVQYIMTEANFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVTGVVLAVLTASFGVTGYSLPWDQIGYWAVKIVTGVPDAIPVIGSPLVELLRGSASVGQSTLTRFYSLHTFVLPLLTAVFMLMHFPMIRKQGISGPL | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
CYB6_SOLLC | Solanum lycopersicum | MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRPTVTEAFASVQYIMTEANFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVTGVVLAVLTASFGVTGYSLPWDQIGYWAVKIVTGVPDAIPVIGSPLVELLRGSASVGQSTLTRFYSLHTFVLPLLTAVFMLMHFPMIRKQGISGPL | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
CYB6_SOLTU | Solanum tuberosum | MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRPTVTEAFASVQYIMTEANFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVTGVVLAVLTASFGVTGYSLPWDQIGYWAVKIVTGVPDAIPVIGSPLVELLRGSASVGQSTLTRFYSLHTFVLPLLTAVFMLMHFPMIRKQGISGPL | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
CYB6_SORBI | Sorghum bicolor | MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRPTVTEAFSSVQYIMTEANFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVTGVVLAVLTASFGVTGYSLPWDQIGYWAVKIVTGVPEAIPVIGSPLVELLRGSASVGQSTLTRFYSLHTFVLPLLTAVFMLMHFPMIRKQGISGPL | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
CYB6_SOYBN | Glycine max | MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRPTVTEAFASVQYIMTEANFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVTGVVLAVLTASFGVTGYSLPWDQIGYWAVKIVTGVPDAIPVIGSSLVELLRGSSSVGQSTLTRFYSLHTFVLPLLTAVFMLMHFSMIRKQGISGPL | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
CYB6_SPIOL | Spinacia oleracea | MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRPTVTDAFASVQYIMTEVNFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVTGVVLGVLTASFGVTGYSLPWDQIGYWAVKIVTGVPDAIPVIGSPLVELLRGSASVGQSTLTRFYSLHTFVLPLLTAVFMLMHFLMIRKQGISGPL | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
CYC10_CLITE | Clitoria ternatea | GIPCGESCVYIPCTVTALLGCSCKDKVCYKN | Probably participates in a plant defense mechanism.
Expressed in seed, root and nodule but not in flower, stem, shoot, leaf and pod (at protein level). |
CYC11_CLITE | Clitoria ternatea | GIPCGESCVFIPCTITALLGCSCKDKVCYKN | Probably participates in a plant defense mechanism.
Expressed in seed but not in root, nodule, flower, stem, shoot, leaf and pod (at protein level). |
CYC12_CLITE | Clitoria ternatea | MASLRIAPLALFFFLAASVMFTVEKTEAGIPCGESCVFIPCITGAIGCSCKSKVCYRDHVIAAEAKTMDDHHLLCQSHEDCITKGTGNFCASFPEQDIKYGWCFRAESEGFMLKDHLKMSVPN | Probably participates in a plant defense mechanism. |
CYC13_CLITE | Clitoria ternatea | DTTPCGESCVWIPCVSSIVGCSCQNKVCYQN | Probably participates in a plant defense mechanism. Not active against Gram-negative bacterium E.coli ATCC 700926 or Gram-positive bacterium S.aureus ATCC 12600 up to a concentration of 100 uM under low-salt conditions .
Expressed in seed but not in root nodules. |
CYC14_CLITE | Clitoria ternatea | DTIPCGESCVWIPCISSILGCSCKDKVCYHN | Probably participates in a plant defense mechanism. Not active against Gram-negative bacterium E.coli ATCC 700926 or Gram-positive bacterium S.aureus ATCC 12600 up to a concentration of 100 uM under low-salt conditions .
Expressed in seed but not in root nodules. |
CYC15_CLITE | Clitoria ternatea | GLPICGETCFKTKCYTKGCSCSYPVCKRN | Probably participates in a plant defense mechanism. Active against Gram-negative bacterium E.coli ATCC 700926 (MIC=0.5 uM) under low-salt conditions . Not active against Gram-positive bacterium S.aureus ATCC 12600 up to a concentration of 100 uM under low-salt conditions .
Expressed in root nodules but not in seed. |
CYC16_CLITE | Clitoria ternatea | GSVIGCGETCLRGRCYTPGCTCDHGICKKN | Probably participates in a plant defense mechanism. Active against Gram-negative bacterium E.coli ATCC 700926 (MIC=2.4 uM) under low-salt conditions . Not active against Gram-positive bacterium S.aureus ATCC 12600 up to a concentration of 100 uM under low-salt conditions .
Expressed in root nodules but not in seed. |
CYC17_CLITE | Clitoria ternatea | GTVPCGESCVFIPCITGIAGCSCKNKVCYLN | Probably participates in a plant defense mechanism.
Expressed in root nodules but not in seed. |
CYC7_CLITE | Clitoria ternatea | MAFARLALIFFLAASVMFAVKETEAGIPCGESCVFIPCTVTALLGCSCKDKVCYKNHVIAAEANTVNDHHLLCQSHEDCFKKGTGNFCAPSLKHDVKYGWCFRAESEGFLLKDFLKTPVDILKMSNVIGN | Probably participates in a plant defense mechanism.
Expressed in root, seed and nodule but not in flower, stem, shoot, leaf and pod (at protein level). |
CYC_ORYSI | Oryza sativa subsp. indica | MASFSEAPPGNPKAGEKIFKTKCAQCHTVDKGAGHKQGPNLNGLFGRQSGTTPGYSYSTANKNMAVIWEENTLYDYLLNPKKYIPGTKMVFPGLKKPQERADLISYLKEATS | Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Subcellular locations: Mitochondrion intermembrane space
Loosely associated with the inner membrane. |
CYC_ORYSJ | Oryza sativa subsp. japonica | MASFSEAPPGNPKAGEKIFKTKCAQCHTVDKGAGHKQGPNLNGLFGRQSGTTPGYSYSTANKNMAVIWEENTLYDYLLNPKKYIPGTKMVFPGLKKPQERADLISYLKEATS | Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Subcellular locations: Mitochondrion intermembrane space
Loosely associated with the inner membrane. |
CYF_PEA | Pisum sativum | MQTRNAFSWIKKEITRSISVLLMIYIITRAPISNAYPIFAQQGYENPREATGRIVCANCHLANKPVDIEVPQAVLPDTVFEAVVRIPYDMQVKQVLANGKKGALNVGAVLILPEGFELAPPHRLSPQIKEKIGNLSFQSYRPTKKNILVIGPVPGKKYSEITFPILSPDPATKRDVYFLKYPLYVGGNRGRGQIYPDGSKSNNNVSNATATGVVKQIIRKEKGGYEITIVDASDGSEVIDIIPPGPELLVSEGESIKLDQPLTSNPNVGGFGQGDAEIVLQDPLRVQGLLLFLASIILAQILLVLKKKQFEKVQLSEMNF | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |