lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. To a lesser extent, is also active with xylose as substrate, but mannose, arabinose, galactose, fructose 6-phosphate, glucose 6-phosphate, glycerinaldehyde 3-phosphate, ribose, sorbitol, ethanol, erythritol, or lactose are not oxidized by the enzyme. Can utilize both NAD(+) and NADP(+) as electron acceptor, with a marked preference for NADP(+). Is involved in the degradation of glucose through a non-phosphorylative variant of the Entner-Doudoroff pathway.
Sequence:
MRAVTVTPGVPESLRLREVPEPKPGPGQVLLKPLLVGVCGTDKEIIEGRYGKAPEGSDYLILGHEALAEVAALGKGVDNVSEGDLVVPTVRRPLDCQLPVDYCPPGKYLEHGIWGLHGHAAELSITDAAYLVKVPKELRDIAVLTEPLSVVEKGVELGVESYKARLGSPPKTALVLGAGPVGLLASMVLRLMGVSITAVATRPHDSLKARLVEELGGRYIDAVHERLEGEFDLVIEATGAPSLAVQGLERLAPGGVEVLLGVYPPTGELKGLGSLLTDAVLKNKLVVGSVNAGLRHFERALAHLKEANDSLNGFPKRLITKVVPLERYQEAYVWTHDDIKVVLQVQT
The following text describes a protein:
Function:
Together with EX2, enables higher plants to perceive singlet oxygen as a stress signal in plastid that activates a genetically determined nuclear stress response program which triggers a programmed cell death (PCD). This transfer of singlet oxygen-induced stress-related signals from the plastid to the nucleus that triggers genetically controlled PCD pathway is unique to photosynthetic eukaryotes and operates under mild stress conditions, impeding photosystem II (PSII) without causing photooxidative damage of the plant.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MAAAVSTAPRAPLPAGAVSSSCCSSSSSSASMSRRWDPSPNPSSGSGSRLFLAARRGERLRVRRLAGAAPAPAPRRRVSSVVRCGGGGGGVRSPDDADAGSGERRRGWDALFHDAFQGAVRRWSEYVGSHWPLAPAGKDAGLGKRVESRREEQVRGEVEEEEGKWSWERWKQHFALIEESERLVDELQLQLRTAVYREDFRSAHKLKLAIAATSKNDTVGRAISDLNSAIEEERYMDATYIRDHAGAGLLGWWSGISGNLSDPYGLIIRISAEHGRYVAKSYDTRQLNSDGPGFPIFEIYFAEANGGYNLQAVHLKPDDSDSQQLSNTLREKLGMDSINISSSSFGAKHEDHNEGVNMDDQNSDDSDISAGPAGFKNLPSDSTPVPRVKILKVVPMENVNQDYIIKIFDQMSDEDDENDNPEDEIESSEDIGDGDNVEEAEAASAEDNVDESGDESDIEALISIDFITEDDKDFMSPSSTKAFERMPARLERRDRFSFSFYTEQYSKRQDVEKVQGISKEKVGLRTAQQDDDDLQFDRVKLVGSNRKLSVLQLGIKQHNNKVQQKLYGVTHFSRIQIPVSSDPLTGLYMTASGFDSEILSLQRKFGQWREDDSSEEHRDLQFYEYVEAVKLTGDNLVPAGQVVFRAKVGKHYQLPHKGIIPRELGVVARYKGERRIADPGFQNPRWVDGELLILDGKFIRDGPVIAFFYWTSNFHLFEFFRRLKLPD
The following text describes a protein:
Function:
Flavonoid 3-O-glycosyltransferase involved in the biosynthesis of anthocyanins conferring flower red/pink colors, mainly anthocyanidin 3-O-glycosides. Catalyzes the addition of UDP-sugar to the 3-OH of anthocyanidin, with a preference for UDP-galactose (UDP-Gal) as sugar donor and cyanidin as substrate; able to use delphinidin, pelargonidin, peonidin and petunidin as substrates in the presence of UDP-Gal, but barely active on malvidin. Can also use UDP-glucose (UDP-Glu) as sugar donor with cyanidin, delphinidin, pelargonidin, peonidin and petunidin as substrates, but not active on malvidin.
Sequence:
MTNSSKGRHVAVLPFPFSTHAAPILSIIRRLASAAPDVTFSFFSTPQSIQTLFPSENPENNIRPHAISDGVPEGFVFSGKHHEDINLFLAAGKESFEAGMKAAEAETGRRIDCVVSDAFMWFSCELAEEMGVPWVTLWVSGACSLAAHCYTDLIRETVGMHDTAGREDEIVKFVPGFSEVRLGDLPSGVVYGNLESPFSMMLYKMGQVLHKAAAVAINSFDELEPEPVKVLASKLKLLTCGPFNPISPPPSSNLDEYGCIPWLDRRKAASVAYIGFGTVATPPPVELAALAEALEASSTPFLWSLRDNPKQHLPEGFLKRTSELQKIVPWAPQAQVLAHRSVGVFINHCGWNSVVESVEAGVPIIGRPFFGDHQVDAWMVENVWKIGVRVEGAVFTKGITMSALELVLSHDQKQKELREQVGKYKEFALKAFGPKQRSTCNLSTLLEIVAGYNL
The following text describes a protein:
Function:
May be involved in telomere capping.
Sequence:
MRELQGDDSSRKSPPSDSVVKNSSPIDYEHSLKSLQDERTLNYPNKQFNSENPSSYYNMDDSGELCNFELEKDSLESMIHESSTALSAQSNTAQDGDQLASSSTISKDHSETLDNKLNDSKILIKKASNSFANFSESVRSSTIVAYSQTPTQRLQGLTSISSSSFDDGSYGSRRISFNSQGVSGRLRRNMDSTVIIPSEDEDLQLPSNSNSNVEYGPFDSTTFDRQLSIEVNQPVGAMSLSPCGRDIALASRYGLLVLDLDNPYNPPRMLRHSTPWEVADTQWNVHAARDQWVVSTSSQKTIVWNLALPNDRAIEFMLHGHTRAVTDMNWHRQNPDVLATCSIDSSVHCWDLRSPRFPVNSFYDWHNGATQVKWNYKNPHILASSHGRLVRIWDDRYGSAPLHTIKTSENITKINGLEFNRACETRLLTCAMDRTVKFWNYEKSTEEPEHLITTDSPVWKARFTPFGDGVILMPQRGDNSVHMYDCRNLDKEGPRAVHRFAGHTDQVKEFLWRCRGEDVFDRDLRDFQLITWSKDHHVRLWPIGNDILNSMGHDRTKPVPFKLTRLGAKYRTYSREPLKQSLINTECDSSDAMNSFDSNFGAERANTSDLSRGFVAFANRKKSKYNLPGSSGFMTRSTKSTNPMTPLNWLRGISMGRLGNADWEVPQNLGEELSWIGQKYSNVSFEKIDVAERTCTISLNAPILPDDGYAYIRLHVYFPNNYPISATPVFQLERSSAFNDEQFNYVFNTLTSISDQCISSHKYCMDACLSYLSGNLSVDEIWKLGFQKDNSDSSSESSADIFQDVFPSMPDFRGGDRGLSHKHQNIPLPKTCAAIFCGNDELVCFFTIKADESAAQATANRETHGRQKLFESFGVLDSSNSVADSDSTNYDDENSLNRGGTSESDSEFIWDVDESNSGSIVFPKSKTSINLNNINSASASIMGSRFGAADIFMSKRPSTKGSNRPSILLSKPSHDFHVVRIISMSKYLPVKRALAAEYVVDTGDKVTVCNKNAEVSAKHNYYRLAKVWLMLGRLLGHLSRTENKDHINDEEAFPWLKSPLAKWVVNSLLDYYASQCNTQMLAMLACVLDIPNPKKQSGNTSADQVLFNQPKQVTEKLGVQLNLPKTKILEKVSSHSLAQITALREKEPKDADSTYSKEKIFSATSTVHLQLMDYDKQNNDFVDAQEIAYTKLLQQKFIQWRATYAEQLDLWGFFIPKLEMLKFNAHEFSSPSEKTLVNHCNSCNSTTSNTRICEKCYSLVPRMSCTFCCLSIHGLCIVCGLCLHVMHEDCYKEWFSNGDSISQSCSSGCGCKCQFQHMSLEKV
The following text describes a protein:
Function:
Probable transcriptional regulator. May mediate E2- or E3-dependent ubiquitination. Required to gate light sensitivity during the night. Regulates the speed of the clock by acting in the feedback loop between CCA1, LHY and APRR1/TOC1. Promotes the expression of CCA1 at night but not by days. This activational effect is enhanced by interaction with ADO1/ZTL. Association with ADO1/ZTL is not leading to the degradation of NFXL2. Confers sensitivity to osmotic stress such as high salinity. Prevents H(2)O(2) production and abscisic acid accumulation. Part of a regulatory network that integrates the biosynthesis and action of abscisic acid, reactive oxygen species and cuticle components.
Subcellular Localization:
Nucleus. Membrane; Single-pass membrane protein.
Domain:
The RING-type zinc finger domain interacts with an ubiquitin-conjugating enzyme (E2) and facilitates ubiquitination.
Sequence:
MTNMAGTATTEFRWKSPPQPPSQEQPISDSDSDSGSDSENHQHRHNDLSNSIFEAYLDCHSSSSPSSIDLAKIQSFLASSSSGAVSCLICLERIKRTDPTWSCTSSCFAVFHLFCIQSWARQCLDLQAARAVTRPSSNPTEPEAVWNCPKCRSSYQKSKIPRRYLCYCGKEEDPPADNPWILPHSCGEVCERPLSNNCGHCCLLLCHPGPCASCPKLVKAKCFCGGVEDVRRCGHKQFSCGDVCERVLDCNIHNCREICHDGECPPCRERAVYKCSCGKVKEEKDCCERVFRCEASCENMLNCGKHVCERGCHAGECGLCPYQGKRSCPCGKRFYQGLSCDVVAPLCGGTCDKVLGCGYHRCPERCHRGPCLETCRIVVTKSCRCGVTKKQVPCHQELACERKCQRVRDCARHACRRRCCDGECPPCSEICGKKLRCRNHKCQSPCHQGPCAPCPIMVTISCACGETHFEVPCGTETNQKPPRCRKLCHITPLCRHGQNQKPHKCHYGACPPCRLLCDEEYPCGHKCKLRCHGPRPPPNREFILKPTKKMLHIQAESTPGSPCPRCPEPVWRPCVGHHLAAEKRMICSDRTQFACDNLCGNPLPCGNHYCSYFCHALDIRSSSLDKRSESCEKCDLRCQKERTPRCQHPCPRRCHPEDCPPCKTLVKRSCHCGAMVHAFECIYYNTMSEKDQMKARSCRGPCHRKLPNCTHLCPEICHPGQCPLPEKCGKKVVVRCKCLTLKKEWVCQDVQAAHRATGSDPKEVPKNQFGVGLLPCDSNCKSKLQVAESVLTQRNVKEIEEKEEPSGKNASKRRKRRGRGQDIQETTRLQKLAVTTKRILMVVMLVAMLAAVSYYGYKGLLWLSDWMNEVEEQRQKSRRYPRI
The following text describes a protein:
Function:
Cell surface proteoglycan.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MSYFVFVCISLSHCCFSFALIADMFRSLLSFSQGHLSSLLEDTYSSLFHHAQPHVHQLFSSLSQYLSGANISVETTVHNFFNSIFPLVYEKLINPDMEGSLMEGSVISDCLRTTRKEVNPFGYHPALMAQELAGALGAGRQLSLALKEGLKAINATEDAGLTKDCEKNLVKMMYCSHCRGLTLFKPCMGYCLNVMRGCLASLSELDQPWRRYISLLEQLTLAVAGHHSLELALLGVRGHINEALLYARLHSPIITTMPVEFFLFLLQDKYGSFFNTLLLFRSVSKGSRTGYYWESLGHELSRHNKEKIGKSPIKVASLIGPWCKRLFQCLGWFSSSEYRLVGFILNRFPPELHVLRRPW
The following text describes a protein:
Function:
Reversible hydration of carbon dioxide.
Sequence:
MGFSLYLLTLHLLLSQCKAQWCYQRQYCDDTCKDPSSWETEFPRCGGLHQSPINIVTRKVHVTNNLPPLIFIGYTDIINITVENKGHSAHFALPPSVRLTGGALPGYYRAAQFHFHWGGKGRPGSEHTIDGERFPMELHIVHIKEPYSSLAEAQHDMAGIALLAFLFEETTDNHPHLDTVIAALGLVQNNGSTTVIPNFRLSDIIPPASDLHHYYRYVGSMTTPGCEHAVAWTVFHRTLSISSRQLDAIIKQCRFWTGLPMTDIYRPTQPLDGRIVYSTNSGTAPKSVIHLWNSFFLAVLLTSALTQ
The following text describes a protein:
Function:
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Tyr residues of target mitochondrial proteins (AMPylation). Involved in redox homeostasis by regulating the cellular response to oxidative stress. Regulates protein S-glutathionylation levels possibly by AMPylation of deglutathionylation enzymes such as glutaredoxins.
Subcellular Localization:
Mitochondrion.
Sequence:
MSKKLKDLPVSSTFTSNLPPDPLVPTVQAMKKADDRILHVPRFVEGGGLFTYLTPSLKANSQLLAYSPSSVKSLGLEESETQTEAFQQLVVGSNVDVNKCCPWAQCYGGYQFGDWAGQLGDGRVVSLCELTNPETGKRFEIQVKGAGRTPYSRFADGKAVLRSSIREYLCCEALYALGIPTTQALAISNLEGVVAQRETVEPCAVVCRMAPSWIRIGTFDLQGINNQIESLRKLADYCLNFVLKDGFHGGDTGNRYEKLLRDVAYRNAKTVAKWQAYGFMNGVLNTDNTSILGLSIDYGPFGFLDVYNPSFTPNHDDVFLRYSYRNQPDIIIWNLSKLASALVELIGACDKVDDLQYMEQLHNSTDLLKKAFAYTSEVFEKIVEEYKNIVQNDFYDLMFKRVGLPSDSSNKILITDLLQILEDYELDMPNCFSFLSRNSPSSMENEEYAAKLMQACICLNPNNERVRNESVKAFTNWVGRYSEATKTQEDSSRLASMKKVNPHFTLRNWVLEEVIKEAYIGKFELFKKVCKMAACPFEDTWGFSKEEEDYLCYNTTPSKSQIQCSCSS
The following text describes a protein:
Function:
Member of a two-component regulatory system.
Subcellular Localization:
Cell inner membrane.
Sequence:
MIMIKRSISGRLALMFALASILIVSALGIVLRSSLHNSLQKQMHNELQFTESLMAPWILSRTTLDGWQTLATKFTDLAAAEGGRVQYWVLSDDPQLQVGGPAPRGVTWASLSKGFSKVPGATDESCSLFLLMSEIPAQGERPALRYVVAIDSTPYMGTLNEFTRTLIVITAIGVLFVALLGFVIARIGMRPVNKLSEQAQHLAPGNHGQRLDTLTLPDELQKLAVAFNGVLERQEIAWRQLESFNADVAHELRTPLTNLMGQTQLGLSRKRETHELEDLLESNLEELERMTSIVNDMLFLSHAQAGEHATQLTDVSLREETYKTTEYVEPSFAEKNLSIHVEGDITARIDRRLFHRSLANLLENSARHAVTGTTVKVTISRENNLASIAVANIGAPIAAEHLNRLFERFYRVDSSRARSDTHHGLGLSIVRAVAIMHRGDVFASSQNGINTFGLTLAITDPYI
The following text describes a protein:
Function:
May be involved in endothelial cell morphology changes during cell spreading. Required for eye pigmentation. In the retinal pigment epithelium, regulates the biogenesis of melanosomes and promotes their association with the apical cell surface by inducing gamma-tubulin redistribution.
Subcellular Localization:
Apical cell membrane. Cell junction, tight junction. Cytoplasm, cytoskeleton. Note=Associates with cortical F-actin.
Domain:
The ASD1 domain mediates F-actin binding.
Sequence:
MLVLGCLQCFTSAWGFASRRICHSSSATPGQHSVGLGHGYQHGAQSWAERFLLRYKGLLWFVGSRAHSGGEETNGKLQAGGCYSYWRGSLGIYFERGKEHGEPLIITKVEDGNKAADILMAGDEIVNINDQQLLGYRQEAICLVKGSHKILKMIVKRRNDISYRPHSWHSNKLIESAMDTVTPQMSNASPFWNARYRSSSSSHDLSNPWDQTSLQRNSGHFSSMGSMDSIDQTYQFGRLSSAKSNNSIDYVGSQNKRDSAYGSFSASFSTPDHTLSKTASASTENILYKNNEWDNTKLGYGKTSPSMNEVRRSADRQVLQSTSINETSKIQRTEDNTEPRYSGRSNFGPVWNIPDKKKTASPPPPPPPQRSDSYAVTKIHEKPTNLMHLDASSTQHFNVANRSQAKPDWSLEISEQQRPIRAHDRTVADTRRTSNSSYHAGLNADQGLSPYKDKYPSNLPNVSRIQASLSTNDVRFAQPAYNYHHQRQYSDESTLFQSTRTSAQHKSQQQPMKYESSVNQVPSDLTYVYHPHQFRAPATSAGFSSGKQNVENNGQNHFHVVSIKHPQGNTTHHQFKEEENYAPEVNSGRKSVQPENTVISIEIPAYSLPQESFEPSQINCEKNYLKISEKKDNYLGNNEQIINKTTGYSEEKCNDRFSQLDHSEKGSYRSSQDYSWRKEENKITPLVTPMLHSLAQEGRNRSESFPDTGNEKLSFPDAGKQSRRSDRFATTLRNEIQQRRARLQKSKSTAALTESNETETSDNWKQDSLESMSPTSEGSFSSTYRSHLQEAQARVLRATSFKRRDLDTGISDHLSLFQDRNMQISSFSGLSLDPVQPKKNTAVNSSQNVSRIGARKRFTTQQKLMSYSEPEKINEVGVEDQYNFRTENSTKRTVGSFADRWKFFEETSKCAQPKVPPKVVSSSQSEETSEIAINRDYAKSSEGQESKRALAVSGQNPADENGFPDKVTTERRQRLGTFAEYEASWKEQKTQLERKNSGRCHSADNILDADLEQNPKAQYIHERSKSSPTTDFYAQAAAVESKQQSESVRRDTENSNSTHCRSSTGDSPTRTVEAGDQCGATNEQEVLTCNTKWKPHDKSFPIPETSNESQQSRARSGTLPNDYRFAHENVNQGNRDISFSAVPISEACPDFSNADSDQLQDHPSVFKKRSAAPQRPPPPKLENKYWRQNGSSSSLATSSESLLTAQARRAQSYSPSSQDTFPPQSLQKQSPSTYPDKNPSIHIYDYQLSVPPENDRYHLEKKYFESELSSKSHLQIPGMEPSRSPSPQFAPQKLTDKPPLLVPEENLSRIERVIDNTTVKMVPIKIVHSETHAEKESRHNLLSAIEPTALPTGLAKDQLKTLSTSEQSYSRFCAYTRQESREEEESRVTDLYSCQRNAEDDNENDVSSLAPSNAKSKDAIYADLKSEELVREIVDKDKSLADILDPNAKMRTTMDLMEGIFPKDEHLLEEAQQRRKHLPKIPSPRSTDDKKDEQNVPSAVSLTTSSTYYSTSAAKAELLIKMKDMQEQQHIAENSEDELGQNLSEKKQELIDSISKKLQVLRDAKETLLEDVQCNNALGEEVEIIVKEVCKPNEFDKFRMFIGDLEKIVNLLLSLSGRLARVENALNNLDETVSPEERKTLLEKRKLLTRQHEDAKELKENLDRRERTVYEILANYLNEENLADYEHFVKMKSALILEQRELEDKIKLRESQLKCLTDSLPLDRIK
The following text describes a protein:
Function:
Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Subcellular Localization:
Nucleus.
Sequence:
MAGMDPGGGGGTASHYLELLRAQQLQHQQPSAPLSPSSHVKMERSAPSPENVDPGGDQPALEGSGGSGGPMRKPRGRPPGSKNKPKPPIIITRDSPNALHSHVLEVAAGADIVECVSEYARRRCRGVCVLSGGGAVSNLALRQPGAEPPGSLVATLRGQFEILSLTGTVLPPPAPPGASSLSVYVAGGQGQVMGGSVVGQLIAAGPVVLMAASFANAVYERLPLEAEEEEAATAAAAAAAATETQGAAEPAEGQPQQQEASQSSGVTGGDGGGGGIGHGMSLYDLGGNAAGYQLPGENFGTWSGEKLLNPAFRLKATL
The following text describes a protein:
Function:
Catalyzes the reversible ATP-dependent phosphorylation of mevalonate 5-phosphate to produce mevalonate diphosphate and ADP, a key step in the mevalonic acid mediated biosynthesis of isopentenyl diphosphate and other polyisoprenoid metabolites.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MAPRGGAPCLVLLVSGKRKSGKDFVAEALRSRLGADVCAVLRLSGPLKEQYAKEHDLDFQRLLDASAYKEAFRRDMIRWGEEKRQADPGFFCRKVVEGVFQPVWLVSDTRRVSDIQWFREAYGALTQTVRVVASEQSRQQRGWVFTTGVDDAESECGLDNFGAFDWVIENHGDEQRLEEQLEKLVVFVRSRL
The following text describes a protein:
Function:
Methylates MRF1 on 'Gln-270' using S-adenosyl L-methionine as methyl donor.
Subcellular Localization:
Mitochondrion.
Sequence:
MRLPRITKFALYRENPCLLPLYHATRDPSLAKREWTWICKELKLLYPEISKHGLRKKIVNACQLRARNYPLQYILKSQPFGNIKIDCQQGVLIPRWETEEWVERVVDKLNRLERLKPLKILDLCTGSGCISSFVLANLRVPHTIEAVDVSKKALKLAVKNCDRAIAHGTVGKINFHQIDVLNEHERVESLLQTSHVLLCNPPYISDDDFAAQTDISVRKYEPKLALLAKNGGNEFYYKFSQYIKRMLQRNAKDFVPLSLIVFEIGSTHQAKIVKSLFDDTNWQANIEQDGAHQDRVVIITRKDRRLIDI
The following text describes a protein:
Function:
Responsible for addition of the terminal mannose residues to the outer chain of core N-linked polysaccharides and to O-linked mannotriose. Implicated in late Golgi modifications (By similarity). Involved in virulence.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MGLLSIPYQSKSKLWIAIFLVVWSLISMHFIWQSQANSGLILKNELSSTSSIPHEFEMLIDTNYPKFKPTSGHSGSQTYSNLFKNQDRNAAIFTILKNFDLEQRCQLYFKNVKNDKLIVDPDHDFKFDRFDYLNWDEYRDESIKRLKGDNDEFVATSSDLDTIKKNFDKAKSRIASDLQLLHDYFSHIKIYNQCYIDRNTSFIKKQHELIDGLNWKTSFKRSSFLSGKQIVTEQQMYPWLSQKSPEYNCLATGQTTKFAANKNSFLNTLKNNLNGKGIVMTIADAHIDYCIRLIHLLRYLKNTLPIQIIYTSNDLSAESKSQLHQASVSDFDGLPQQNITLVNVTPAIKPQYLHKFNEFGNKILAILFNTFEEMIFIDADAILIENPEKFFQLTKYKNSGALFFRDRNTSEYRPDHDIEMFLKLMNSQYDEIIFGLLQITEKTMSIPLFDRKISHVMESGLVLLNRKVHFSQPLIMANMNFFEPIRERVYGDKEMFWLSLSIIGDENYQFNSHPAAAIGQLTTYQERVKTFENPPSSFKSQEICANHPAHISDEDNHTLLWFNSGFQFCNQLEKVNYEDEFSHKERYSQFDTIDKFKTFWQSSLVIESAIIPPENTNSNGGDGYEPSVSWKHMEPYCAGYTWCAYSSIGNGDQANDRGLVINYSPEEIEHFKKLGEIWMRGYNYL
The following text describes a protein:
Function:
Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular Localization:
Secreted.
Sequence:
MAIIRENCVRDRGLILALVVMNLCLASVHVIGQTDIPTTTDPLLSFGFYATSCPRAERIVRDAMHEYYLNDPRHAPAILRLFFHDCFVQGCDASVLLDTADPKEPAEKEAAPNLHSLRGFELIDDIKSRIEAICPRVVSCADIIALAARESVLLTRGPRFAMLTGRRDARTSSAARAQRDIPLPDADYDTITKSFRSRGLNEVDVAALLGAHTIGRSQCKFVRNRNVESTTCSNHGNHTTDLDIGSGGIFDNHFFVNLRRGRGILTVDDALMSRLNSYLRVTAFAYDNELFFDQFVSSLLKMSSIGVLTGVDGEIRQNCSVVNGPGPLNPFNDEVVTPRHHPPRHPKKPVVISGRATGSQS
The following text describes a protein:
Function:
Somatostatin inhibits the release of somatotropin.
Subcellular Localization:
Secreted.
Sequence:
MASSQLHLTATLLCLAMMAGIICGRSHMLLNSALQASRGTSADEEIPERYSLSELEWLLSNSDPAVFQPDSSSLGSLHSGLELMRRDTKEERKTGCKNYFWKSRTAC
The following text describes a protein:
Function:
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Does not accept 4'-phosphopantothenoylcysteine as a substrate.
Subcellular Localization:
Cytoplasm.
Sequence:
MAAPEDSKMSPANSFGAVVLGGTFDRLHDGHRMFLKAAAELARDRIVVGVCDGPMLTKKQFSDMIQPIEERMRNVETYVKSIKPELVVQAEPITDPYGPSIVDENLEAIVVSKETLPGGLSVNRKRAERGLSQLKIEVVEIVSDGSSGNKISSSTLRKMEAEKASKQKQPAEEKAS
The following text describes a protein:
Function:
Golgi membrane protein involved in vesicular trafficking.
Miscellaneous:
MISCELLANEOUS: Present with 4540 molecules/cell in log phase SD medium.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MSVIPPKFFKIANISIGCIDIIAALSQLTYIFTNLNVFLLAVYGLALSVPIVYLEFKVPSNLYRYASFYFSFLGRGLSYILLSLIISFGGIYNILAGMFTFILGVAFIVFHFSQFVEEPANFRAPGSSLSIGDDDIDDDDDMI
The following text describes a protein:
Function:
Constitutive trypsin that is expressed 2 days after emergence, coinciding with host seeking behavior of the female.
Subcellular Localization:
Secreted.
Sequence:
MSNKITILLAVLLAVVACAQAHASHQRRVPYPLPRFLPRPHHTVSNHRIVGGFEIDVAETPYQVSLQRSKRHICGGSVLSGKWILTAAHCTDGSQPASLTVRLGSSRHASGGSVIHVARIVQHPDYDQETIDYDYSLLELESVLTFSNKVQPIALPEQDEAVEDGIMTIVSGWGSTKSAIESNAILRAANVPTVNQDECNQAYHKSEGITERMLCAGYQQGGKDACQGDSGGPLVAEDKLIGVVSWGAGCAQPGYPGVYARVAVVRDWIRETCGV
The following text describes a protein:
Function:
Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Plays a role in both the assembly of the exocyst and the polarization of this complex to specific sites of the plasma membrane for exocytosis. Also involved in assembly of the spliceosome (By similarity).
Subcellular Localization:
Cytoplasmic vesicle, secretory vesicle. Note=Cell periphery. The polarization of EXO84 requires actin cables (By similarity).
Sequence:
MSLEPPNQSLRSHRQTANPHVMAAAVQKQKPYIQDSTHLQLPNVGDKDRERVGNMVKRRFSARIPGQGVPYDAAAAPSLPVGAGSMIDDAVAAGGVPVTKSKTMTSPAKAAPVASGASGMLLKEDLDAHTFVTQQLATSNAEEVDRFVSKLKSLKSRLVDEQREAMYTNYNSFLTVNKEILALNSEVKSLGQAVSNFNVAVSAMVEDALESTSSKSQESSQSSLALPDSSARNRNSMVMLENMWANELASLFKHVEGAVKYLPAIPGRHVVAESGAWYQLNAATWKPLRPVHMFLLNDHLLIAAKNRKKDNMQMQQTQTLVADQCWPLSDIEFLDLSVSRRGTHPVVPNAVSVVCGGVTCVYQTEKPAQHAKVVSAFKKVAGEGRKNDTNKTQQQIRLRESMTYYAARNPSLRGHKELLQGLSNSKGHSRSSSVDITGRTKNLREIDDLVNDLDVKIAHRRFAEATDIILENIKDDKESTDITQQVLDIKLHQRQDELVAHLIDDVATDTSNTAVTHALGLLVRLGHGDQARGVYLETRRNLIHKRTRQVELLGDIPGYIAQVAVTYFRLIRSTAEVFRKCYTDNHLASSIAEWAKSMVEEFVLLFARQLYGVKPDTQTYQQCVSITRQQAAQLSEVGLNLDYLLDYVLSPARASKA
The following text describes a protein:
Function:
Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, may regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, and exocytosis. Phosphorylates inositol hexakisphosphate (InsP6).
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MTQSNSIQDFPPSATQDNCSSDIGCATGSDERNALIATPLPNMVPDQTGDKSSFTLLYDPVSPSSRASPSNGQFHQNKPQTSDVMTDHAGGARVALSARSSSRTPRRLSGSTATSSVSEAETGPSSIGRIGVCALDVKARSKPSQNILTRLQAKGGFEVIVFGDKVILDEAVENWPVCDFLIAFFSDGFPLEKAIAYARLRKPFCVNDLPMQKVLWDRRLCLRILDHMNVPTPKRLEVNRDGGPRLESPELAQHVYRLTGVKLEGPEDGTGGGSQKTQVVTMSEDGEALIVDGKSIRKPFVEKPVNGENHNIHIYFPNDHQYGGGGRRLFRKVGNKSSEYDPHLVVPRSVTEKDTSYIYEQFLRVDNSEDVKAYTVGPDFCHAETRKSPVVDGVVRRNTHGKELRYITKLSQDEAAIASKISNGFGQRICGFDMLRVGDKSYVIDVNGWSFVKDNNDYYDKCASILSDMFLNEKRKREGLQRSLEMVSPDTSHHVRHSVSHRHTLKTLLKSPSTSKLYGGHKSLDNSFQDLAALPPASCGAESMDYKRSRTSPDARQIDSDIGDLDQKNRELTGHPDETIPPPPPPASKHSWKLKGMVAVIRHADRTPKQKFKFTFHSQPFIDLLKGHQEEVVIKGQAALASVSEAVRLAMDQKLEDMEKLKLLRTSLEKKGGWPGTKVQIKPMFRKRTQEELSMHSSENSNSDGAQINWTQVADDASGDKENFPRTSTRSDSISGTTFSRFSAAENDLILDKLQLVIKWGGEPTHAARYQSQDLGLNMRDDLKLMNKEALNNVRIFTSSERRVSTSAQIWACSFLDQKELPDDFIQVRKDLLDDSNAAKDVMDKVKKKLKLLLREGSAPSQFTWPKDNIPEPSVVLATVVELMKFHRNVMRHNFEKLNNSPHCASSISPLSDNPTSQDVIQGTVSPTLTSIQGRWCTGEDPMLFKERWEKLFAEFCDTEKVDPSKLSELYDSMKFDALHNRHFLEWVFMPPDEGTNEHERHSSNSNNTNRHDLAEDRLPGHDSITSEGIEENVENPTLSHLLRFKKRAHAFDSIPHLRALDDSYDHYFKLYPGSSPTKTKMDGRLSKLRELYKLAKVLFDYVTPQEYGITDSEKLEIGLLTSLPLLQEIVRDLEEVQASPDAKSFFYFTKESHIYTLLNCIIEGGIQTKIARSAIPELDYLSQICFELYEAKDCESSTSSYSIRISISPGCHAFDPLDVQLDSRHAIGCAPRRSLTAHQDWKEVIETLKAKFDTVKLPKTFIAVNLSDKHVSSYISLPSCM
The following text describes a protein:
Function:
Its primary physiological function is unclear. Has cytoprotective activity against internal or environmental stresses. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor. Golgi apparatus. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis.
Domain:
The normal, monomeric form has a mainly alpha-helical structure. The disease-associated, protease-resistant form forms amyloid fibrils containing a cross-beta spine, formed by a steric zipper of superposed beta-strands. Disease mutations may favor intermolecular contacts via short beta strands, and may thereby trigger oligomerization; Contains an N-terminal region composed of octamer repeats. At low copper concentrations, the sidechains of His residues from three or four repeats contribute to the binding of a single copper ion. Alternatively, a copper ion can be bound by interaction with the sidechain and backbone amide nitrogen of a single His residue. The observed copper binding stoichiometry suggests that two repeat regions cooperate to stabilize the binding of a single copper ion. At higher copper concentrations, each octamer can bind one copper ion by interactions with the His sidechain and Gly backbone atoms. A mixture of binding types may occur, especially in the case of octamer repeat expansion. Copper binding may stabilize the conformation of this region and may promote oligomerization.
Sequence:
MGKIQLGYWILVLFIVTWSDLGLCKKPKPRPGGGWNSGGSNRYPGQPGSPGGNRYPGWGHPQGGGTNWGQPHPGGSNWGQPHPGGSSWGQPHGGSNWGQGGYNKWKPDKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPVIHFGNEYEDRYYRENQYRYPNQVMYRPIDQYSSQNNFVHDCVNITVKQHTTTTTTKGENFTETDIKIMERVVEQMCITQYQAEYEAAAQRAYNMAFFSAPPVTLLFLSFLIFLIVS
The following text describes a protein:
Function:
Multifunctional RNA binding protein that plays a role in RNA metabolism and DNA maintenance. Participates in the resolution of DNA stress and the maintenance of genome integrity by localizing to sites of DNA insults. Also plays a role in proper nucleolar organization by limiting nucleolar size and regulating nucleolar number. Mechanistically, regulates the nucleolar levels of fibrillarin and nucleolin, two key players in pre-rRNA processing and ribosome assembly.
Subcellular Localization:
Nucleus, nucleolus. Nucleus. Cytoplasm.
Sequence:
MGRNKKKKRDGDDRRPRLVLSFDEEKRREYLTGFHKRKVERKKAAIEEIKQRLKEEQRKLREERHQEYLKMLAEREEALEEADELDRLVTAKTESVQYDHPNHTVTVTTISDLDLSGARLLGLTPPEGGAGDRSEEEASSTEKPTKALPRKSRDPLLSQRISSLTASLHAHSRKKVKRKHPRRAQDSKKPPRAPRTSKAQRRRLTGKARHSGE
The following text describes a protein:
Function:
DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair and base excision repair. Resolves abortive DNA ligation intermediates formed either at base excision sites, or when DNA ligases attempt to repair non-ligatable breaks induced by reactive oxygen species. Catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined (By similarity).
Subcellular Localization:
Nucleus.
Domain:
The HIT domain is required for enzymatic activity; The C2H2-type zinc finger mediates DNA-binding.
Sequence:
MSWSSALIKDISKPENLIISSEIAVVIADKFPKAQHHYLVLPLADIPSIFHLNRSHLSLLEELHLLARNVVEVKGVRWQDFNVGFHAEPSMQRLHLHVISKDFVSTSLKTKKHWNSFNTELFVPYTKLYAQLEKENSISRLPKSLKDELLAKPLICNQCEFVARNLPSLKGHLVGHLQDPKSVCQRVRLGNQFFPTAGYRTSELAYCFDFVDFYEYKKQMEVDKLAYIRDELQRKLNDKRNFLIESDRAVVMKADYPKSQYHFRVVAKEEFRDITQLTEAQLPLLDHMMDLANQIIEKQKHLESRNFLIGFKVNTFWNRLNLHVISNDFYSMAMKRISHWNSFNTELFMPFQIAYMMLSVQGSIESISEETYNNLQEKTPLRCNQCEFVTNMLLDLKAHLYQHWQRKEDERDQKKKVDKIIQMISETKLDEAEAKPKLLNEEEPIQAQPVAAIAQYPNEHLGKPLTPQQQPGKQQAQNVYDKNINGPSVNMMNQNNPNNPFRNTPHLNRQSQKPPHPRSGPRGPMAPWTGPRFPCHQQQNRFRPPGFNACRQPYPPYHSGHQQFPNASSVGGGQTGLPGQGQGPRPKWNSNKIFNQQNRQNTVQAQPQAQNQQTNQQQIQNSNKNQTPKKKPWKNRLQPVGKVQNQGGANRDPAPPSNSKPS