lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes methylation of the sphingoid base component of glucosylceramides (GluCers) at the C9-position. Sphingolipid C9-methylation requires 4,8-desaturated ceramides as substrates (By similarity). Glucosylceramides play important roles in growth, differentiation and pathogenicity. The methyl group at the C9-position distinguishes fungal glucosylceramides from those of plants and animals and may thus play a role in host-pathogen interactions enabling the host to recognize the fungal attack and initiate specific defense responses (By similarity).
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSEEKKSVELSGDIDFIETPPAKASQFETGEDCGIEVTKAAAIPNPPLAVDGPGNESFSNYLLGGTLVGLPAFLTWFFGGGAKTFVFFFLLSVLPVLVAFWTYASTFSPRTNEKVKLPGRPVEHYITFKREEDKAKWHGKNKIPMQTFAEMYLDGLVDFNGDTLDVMEYRHDWANFSFTWDLFKFIVGTFFVDVLFHTKAQDEEQVRPNYDSGNDHYAWFLGPRMIYTSGIISDPEKEETLEEMQDNKMAIVCEKIGLKEGETMLDIGCGWGTLARFASLNYGAKVTGLTIAENQTAWGNDALRKAGIPEEQSKILCMDYRDAPRTKFDKITQLEMGEHVGIRRLTGFFRQCYDMLKDDGAMYVQLSGLRQAWQYEDFIWGLYLNKYIFRGADASTPLWYYVKCLEQAGFEVKGIDTVGVHYSGTLWRWYRNWVGNVEAIKAKYGPRWYRIWELFLAWSVIASRQGSATCYQMVVVKNLNSTHRINGVASQFGLAGALAASRAAGKSRLP
The following text describes a protein:
Function:
Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MKKINIITSSLLLLILITFSSLIKSDETTTVESERDESTKKKTESLDQIPIGLNGLNDTLYWGTYRPHTYFGMKSRSTLPINTGLIWSTPNIGMGTYNKFHYKVVQGGDNGIKSYTWTKHDGKNFGSQEIIDVQGHLNLTTSFIKNSGQKGGDWSVRISGKSNYTNKGGVPLVSLIYYIHDESLKKSSENGLNINIADNNNNNNNNNNNNNNNNNNNNNNNNNNNNNIHIKGEHPEIGKYTLHFKDIKSSNDNDDNNNNNCLEEMRKEEYNLVDSQKDLCDWRFYGSSNYDLNSNWNVFNNIFDQDFNQHNEAVFRTWHTQRFKHFIPTLPNKLKQNSNVIAVQRVLTVPFNIEISFISHEFHNEKELSEEKVEEIVKSILTGSEFDKTYSKFEKQFDDKFNKKFLGEKLKKHKPEIYKVSKESLSNLLGGFGYWYGSGITKKSLKSDKIIKSKPVALFSATPSRPAFPRGFLWDEGFQQLLASTFDVELTIESLSHWLNIMDENGWIPREQILGLEAASMVPEEFRLQLPNIANPPSIILAINKLLEISQAYKERTTTNNNNNNNVDSNNFKINMIRDLSVIIENNKEYDSIQRFLHSALPRIERFYQYYWNTQSSGLIENSFRWRGRKVNHTLASGLDDYPRALEPSTSEIHVDLNSWVAFFAKSLSTLTKYLGGSDNKNQEKSELYFKQFTLIRSNIEQMHWDEEENLFHDILIHKNGSKQFIRTYGYMNYFPMLLGVLDVDSAKLSPLLTTLKDVNGIWSRWGIRSMSLKDKNFGTHENYWKGPIWININYLFVHSMNKFYTKTPSINECYQTLRFNLINNIGNIYSETGNIYEQYDPITGLGTRNRPFNGWTALVSLISSEQY
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MESRDTSFARQEKRTTREEQNIAGSEAVKEEIRVPNDLPMESIRDFWERAVPEDLTREPRKGLQQRWESQLQEFLKALESPHAEGRSPQLLGPRPRNHARPIMTPFKGTTNSSLQLKAERVSQHMPSSSRGSLQAVAKSKAEDSKAKCLVLGQAASNLHEECRLFRRFGYQETDGPREACRHLRKLCHQWLKPESHTKEQIVELVILEQFLAVLPSEMKSWVRECSPQTCTQAVILAEDFLLRQQENQMQKDETISPFEEEEDNLMEEAALDTWKRPHFKQEDQRDIDQLADKKQYRPEKNNPGNSAEPDSRWMLSGRVEQNILPYANREEISEILYGSCLERESGKFINSQGAYEDLDESILHQAMLPSGERDNACHMCGKVFRRRSNLIAHERTHSGERWYNCSDCGKCFVSRAAFLIHQRVHTGEKPYKCSYCGKGFNTGSSLTRHKRIHTGEKPYECPACGKRFNDYSNFIVHKRIHTGEKPYECSVCGKRFSDNSNFIKHHH
The following text describes a protein:
Function:
Probable transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MGRGKIEIKRIENATNRQVTFSKRRGGLLKKANELAVLCDARVGVVIFSSTGRMFEYSSPTSSLRELIQQYQNTTNSQFEEINHDQQIFVEMTRMRNELEKLESGIRQYTGDDLSSLSLADVGDIEQQLELSASKVRARKIQLINQQADNLRRKGHILEDQNTLLCRMYNESQQHGVGGSGGGEVKMMGMSPVLSMLPPSAFPATPYYGGGGGEESSSTALQLTSPLQAAEAAAAAAGFRLQPTQPNLQDPACSSLHAGHGLHL
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.
Subcellular Localization:
Secreted.
Sequence:
MASDSRVAMMWCVLVLVLQSAGGGDMPCRREEQPEGERRAQGRLPQAQLSAGGVHCSGRGRQGPLREPGPRRGPDPHGLPRLLRPRLRRVGPPNFPSLRGFEVIDEAKSILERACPGVVSCADTLAFAARDSAYFLSRSRINYAIPSGRFDGNVSLESEALEFLPPPSFNLSQLVASFEAKKLDADDLVVLSGAHTIGVSHCSSFTDRLPPNNTSDMNPRLATLLQGQCPANPNFTDDTVVQDVVTPKLMDSQYYRNVLKKDVLFRYDAALLESRRTARKVLQNAFVRGRWERGSLRRPWSRCPGSSSRPPPMARSGECAGSSTANWVAACRLAISLKLTVDRTCTLLLPFRFLLQFSVMFCIAVVLVD
The following text describes a protein:
Function:
Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures.
Sequence:
MTTNKDVECLVEPTSNISITEENKNVTSETTTTTNNTQNKETETTDNINKEETADKENKEEQQQEENPENLIKHPLQNRWSLWYDYQSGKINPEHWVDSLKKVISFDSVEDFWCVFNNLPNVSNLKQGSSYHLFKDDIEPKWEHESNKRGGKWFVMVKDKSRCDNQWLQSVMACVGETFDSSDEICGIVYNSRKNGDKISVWTKTAQDEKATRDVGNCLKKILEIDQTIQYTPHEDFIRSSKGSKNLYEC
The following text describes a protein:
Function:
Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate in the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. In conditions where the essential linoleic and alpha linoleic fatty acids are lacking it is also involved in the synthesis of Mead acid from oleic acid; Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate to the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell projection, dendrite. Membrane; Multi-pass membrane protein. Note=In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree.
Sequence:
MKMVVIPGAFLFPSPRCLAAGASLQHPSPLGLPRVLLLPPRRFSELLLPPVGPRGFKMENFDASLSPYFRALLGPRDTRVKGWFLLDNYIPTFICTAIYLLVVWLGPKYMRTRQPFSCRGILVVYNLGLTLLSLFMFYELVTGVWENNYNFFCQGTRSAGEADMKIVEVLWWYYFSKLIEFMDTFFFILRKNNHQITVLHVYHHATMLNIWWFVMNWVPCGHSYFGATLNSFIHVLMYSYYGLSSIPSMRPYLWWKKYITQGQLLQFVLTIIQTSCGVIWPCTFPLGWLYFQIGYMISLIALFTNFYIQTYNKKSASRRKERLREHQNGSVAAVNGHTTSFSSLENNVKLRKQRKD
The following text describes a protein:
Function:
Elicits a high humoral and a low T-cell response. Could be involved in directing the host toward development of a more humoral type of immune response.
Sequence:
MNFAVLPPEVNSARIFAGAGLGPMLAAASAWDGLAEELHAAAGSFASVTTGLAGDAWHGPASLAMTRAASPYVGWLNTAAGQAAQAAGQARLAASAFEATLAATVSPAMVAANRTRLASLVAANLLGQNAPAIAAAEAEYEQIWAQDVAAMFGYHSAASAVATQLAPIQEGLQQQLQNVLAQLASGNLGSGNVGVGNIGNDNIGNANIGFGNRGDANIGIGNIGDRNLGIGNTGNWNIGIGITGNGQIGFGKPANPDVLVVGNGGPGVTALVMGGTDSLLPLPNIPLLEYAARFITPVHPGYTATFLETPSQFFPFTGLNSLTYDVSVAQGVTNLHTAIMAQLAAGNEVVVFGTSQSATIATFEMRYLQSLPAHLRPGLDELSFTLTGNPNRPDGGILTRFGFSIPQLGFTLSGATPADAYPTVDYAFQYDGVNDFPKYPLNVFATANAIAGILFLHSGLIALPPDLASGVVQPVSSPDVLTTYILLPSQDLPLLVPLRAIPLLGNPLADLIQPDLRVLVELGYDRTAHQDVPSPFGLFPDVDWAEVAADLQQGAVQGVNDALSGLGLPPPWQPALPRLF
The following text describes a protein:
Function:
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
Sequence:
MSYLVLARKWRPQTFSDLTGQEHVSRTLQNAIDSGRIAHAFLFTGARGVGKTSSARILAKALNCEQGMSPEPCNVCPACTEITAGTSVDVLEIDGASNTGVDDIRELRENVKYLPSRLRYKIFIIDEVHMLSTNAFNALLKTLEEPPPHVKFIFATTEPHKLPITILSRCQRFDFRRIPLAKVVARLRYIVDREGISISDESLAVVARKGDGSMRDSLSVLDQVLAFCGETVNDDDVVSLLGVVDRRLLLEASAAVLGRDTRSVLGVVARVDEFGYNMRQFCGELIDHFRNLTIMRAVGDAGDLLDLSEAELQSVREQASSALLEDLQRHMTILLRADGELAHSGYPRLVLEMALVRMATLAPLVPVGELLDRLGRIEERGSGVAADARASWRPSPPPEAGVAPVPRPAPSALAEQRPRPVPAGAEAKPPPSRSDSPVQEPRRTGDEWADFVAFVKGAKPRIGTSLEYGSPLHIAADRLEIGFPENSFALSSLRDGDAQASLKALAERFFSAPMTVALKVLTGEGHAPPNLLEKKRAEDEQRRTGLKRSAESHPAVSSALEVFDGTLAEVAPLGTRGKL
The following text describes a protein:
Function:
Catalyzes the reversible conversion of L-aspartate to fumarate and ammonia. In the reverse reaction, consumption of fumarate is observed in the presence of not only NH4(+), but also hydroxylamine (NH(2)OH). Is specific for L-aspartate and cannot use structural analogs of L-aspartate such as D-aspartate, DL-alpha-methylaspartate, DL-beta-methylaspartate, DL-threo-beta-hydroxy-aspartate, DL-erythro-beta-hydroxyaspartate, L-cysteate, L-alpha-aminobutyrate, L-asparagine, L-alanine or L-glutamate. Represents the central enzyme for nitrogen assimilation from L-aspartate in E.coli.
Domain:
Contains three domains, which are composed almost completely of alpha helices. The active site is located in a region that contains side chains from three different subunits. The divalent metal ion binds at the activator site and not at the enzyme active site.
Sequence:
MSNNIRIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISDIPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEVLNNGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYSSLIKLVDAINQLREGFERKAVEFQDILKMGRTQLQDAVPMTLGQEFRAFSILLKEEVKNIQRTAELLLEVNLGATAIGTGLNTPKEYSPLAVKKLAEVTGFPCVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMPAKVNPVVPEVVNQVCFKVIGNDTTVTMAAEAGQLQLNVMEPVIGQAMFESVHILTNACYNLLEKCINGITANKEVCEGYVYNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTEAELDDIFSVQNLMHPAYKAKRYTDESEQ
The following text describes a protein:
Function:
Member of the two-component regulatory system PhoR/PhoB involved in the phosphate regulon genes expression. PhoR may function as a membrane-associated protein kinase that phosphorylates PhoB in response to environmental signals.
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Sequence:
MQSVVNQDWRGALIRHLLLVLAASLVLGVVSGHYGWALALGLALYLGWTLWQLLRLHQWLRNHQPDEPPPDSYGLWGEVFDNIYHLQRRNQRARGRLQAVIDRIQESTAALRDAVIMLDSDGNLEWWNLAAENLLGLKTPQDGGQPVSNLIRHPRFKEYFDQEDYREPLEIPSPINERLRLQFHITLYGNREHLMLVRDVTRVHQLEQMRKDFVANVSHELRTPLTVIAGYLETLLDNVEDVNPRWLRALQQMQQQAGRMQNLLNDLLLLAKLEATDYPGDNKPVAVDALLASIRNDAQALSAGRNHRISLDAAPAVQLKGSEAELRSAFSNLVFNAVKYTPDEGEIRIRWWADEQGAHLSVQDTGIGVDPKHLPRLTERFYRVDSSRASNTGGTGLGLAIVKHVLIRHRARLEISSVPGKGSTFTCHFAPAQVAEAERKAPK
The following text describes a protein:
Function:
Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer (By similarity). Plays a crucial role in Notch signaling. Initial fucosylation of Notch/N by O-fut1 generates a substrate for Fringe/Fng, an acetylglucosaminyltransferase that can then extend the fucosylation on the Notch EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by Delta/Dl or Serrate/Ser. Also required for the transport of Notch/N to the early endosome.
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
MQWLKMKLRFVNLILLLISSTCAQLGGDPNGYLTYCPCMGRFGNQADHFLGSLAFAKALNRTLILPPWVEYRRGELRSRQVPFNTYFEVEPLKEYHRVITMADFMWHLADDIWPESERVSFCYKERYSLQQEKNDPDKPNCHAKDGNPFGPFWDTFHIDFVRSEFYAPLHFDVHHSNEAAKWQTKYPAESYPVLAFTGAPASFPVQLENCKLQRYLQWSQRYREASKDFIREQLPRGAFLGIHLRNGIDWVRACEHVKDSQHLFASPQCLGYKNERGALYPELCMPSKEAIIRQLKRTIKNVRQTQPDNEIKSVFVASDSNHMIGELNTALSRMGISVHKLPEDDPYLDLAILGQSNHFIGNCISSYSAFEKRERDVHGFPSYFWGFPKEKDRKHTNVHEEL
The following text describes a protein:
Function:
Catalyzes the stereospecific oxidation of D-lactate to pyruvate.
Subcellular Localization:
Mitochondrion.
Sequence:
MWKRLLSSTSSRLVTGVVTVASTSFFAYRYGQASSTGQSLLPLGSTAKLSSLKPPQYCPESEIPNIMSKIQQLGISVVNSKPEIDHHTGNDFTTHKPLPNEVPQFIIYPDSTEQVSQALKILNEYKVPVVPFSGGTSLEGHFHSTRRGVVIDTSKLNKILAINDNDLDVVVQAGVNWQDLNQVLEPYGLMFGTDCGHNGLISGMIGTNASGINASRYGAMSANVISVTAVLPDGTIIKTRNRPRKSSAGYNLTNLFVGSEGTLGIVTEAVCKVYPIPKSETVVVVQFPSILDSTNAVAQVFRSGIQPTAIELLDKDMMHCLNYSGYTTRDWLECPTIFFKIGGINETVVKENVNILQQIMQANHANAFVFAQNKQEQEELFSARKNAFYAMINYGKNEIDEDVRIWVTDIAVPLSKLSKVLNEINSLIKASPFQSIILAHAGDGNFHADIFYKHEQRAEVEQLVNKMIELGLQNEGTCTGEHGVGNAKRNFLQLELGSDTIDLMRKIKLAVDPNRILNPDKIFKIDPTDPGEY
The following text describes a protein:
Function:
Plays a major role as delta(8)-fatty-acid desaturase which introduces a double bond at the 8-position in the long-chain base (LCB) of ceramides with or without a hydroxy group at the 4-position. The enzyme produces both the 8E and 8Z isomers (in a 4:1 ratio). This structural modification contributes to the quantitative partitioning of ceramides between the two major sphingolipid classes, glucosylceramides and glycosylinositolphosphoryl ceramides. Sphingolipids are important membrane components involved in environmental stress responses, such as resistance to chilling, and act as cell signaling molecules.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The histidine box domains may contain the active site and/or be involved in metal ion binding.
Sequence:
MADQTKKRYVTSEDLKKHNKPGDLWISIQGKVYDVSDWVKSHPGGEAAILNLAGQDVTDAFIAYHPGTAWHHLEKLHNGYHVRDHHVSDVSRDYRRLAAEFSKRGLFDKKGHVTLYTLTCVGVMLAAVLYGVLACTSIWAHLISAVLLGLLWIQSAYVGHDSGHYTVTSTKPCNKLIQLLSGNCLTGISIAWWKWTHNAHHIACNSLDHDPDLQHIPIFAVSTKFFNSMTSRFYGRKLTFDPLARFLISYQHWTFYPVMCVGRINLFIQTFLLLFSKRHVPDRALNIAGILVFWTWFPLLVSFLPNWQERFIFVFVSFAVTAIQHVQFCLNHFAADVYTGPPNGNDWFEKQTAGTLDISCRSFMDWFFGGLQFQLEHHLFPRLPRCHLRTVSPVVKELCKKHNLPYRSLSWWEANVWTIRTLKNAAIQARDATNPVLKNLLWEAVNTHG
The following text describes a protein:
Function:
Required for bipolar spindle formation and proper chromosome segregation. Has an indirect role in connecting the kinetochores and the plus end of pole to chromosome microtubules by targeting alp14 to the spindle pole body. Involved in the emergence of large microtubule organizing centers (MTOC) in interphase cells. Attaches to the minus ends of microtubules and associates with the sites of microtubule attachment on the nuclear envelope. This leads to the stabilization of the microtubule bundles.
Subcellular Localization:
Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore. Note=Associated with the equatorial MTOC, spindle midzones, spindle pole body and mitotic kinetochore periphery. Spindle and kinetochore localization is alp14-dependent.
Sequence:
MSDIVSSSTDYSRRSPSSSSIGTNETDHTGFHEKRQGASSESLIPPAQRSSEESMPAPKLFPKLTSKPNPQLNLKDTLNKRVSDRLQALELNKSFDFSGTPRPMHPISHPLSQHKTPEFKHRKRNVESILTPKNPSLFSSSNAASQRGSLNTAPSNFAYSHSSSLQTSASSRPPVLSNGSFPRQTNTAPLNPPVHLKDNIRNSATPSTSQADIPTQYPINSTQKQQAKYEAEIEGYKAKLAGTYHEISVLQNTIVNVSGQLIAVNDQLQQLRSGKASTSPSTKDTNMRLVEGHNEETLALQRGKYTQEEVDKLIQERMEKVAEDLHAQYSAKHTQKINAFKANYARKYEATIQELQNQIGTAPNAPKISNSNWEEERRALKADNQTLQKQLEKAIQERQDMSDFLNNFKADMAKSDKLLMQQQSQQTGDLETLRLQLQALQEELRVEREERQQLIQMSEDLVIAMDQLNLEQKS
The following text describes a protein:
Function:
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MDKNNNNLRLILAIALSFLFIALYSYFFQKPNKTTTQTTKQETTNNHTATSPNAPNAQHFSTTQTTPQENLLSTISFEHARIEIDSLGRIKQVYLKDKKYLTPKQKGFLEHVGHLFSSKENAQPPLKELPLLAADKLKPLEVRFLDPTLNNKAFNTPYSASKTTLGPNEQLVLTQDLGTLSIIKTLTFYDDLHYDLKIAFKSPNNLIPSYVITNGYRPVADLDSYTFSGVLLENSDKKIEKIEDKDAKEIKRFSNTLFLSSVDRYFTTLLFTKDPQGFEALIDSEIGTKNPLGFISLKNEANLHGYIGPKDYRSLKAISPMLTDVIEYGLITFFAKGVFVLLDYLYQFVGNWGWAIILLTIIVRIILYPLSYKGMVSMQKLKELAPKMKELQEKYKGEPQKLQAHMMQLYKKHGANPLGGCLPLILQIPVFFAIYRVLYNAVELKSSEWILWIHDLSIMDPYFILPLLMGASMYWHQSVTPNTMTDPMQAKIFKLLPLLFTIFLITFPAGLVLYWTTNNILSVLQQLIINKVLENKKRMHAQNKKEH
The following text describes a protein:
Function:
The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase.
Sequence:
MQTVIFGRSGCPYCVRAKDLAEKLSNERDDFQYQYVDIRAEGITKEDLQQKAGKPVETVPQIFVDQQHIGGYTDFAAWVKENLDA
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.
Subcellular Localization:
Secreted.
Sequence:
MASAWYVRLCAVVIILSLDSFVSASKYDKVHHNSGTHHVPDGGLRDNYYHRSCPHVEKIIFKEISKCFKADKKIAPGILRMSFHDCFVRGCDCSLLLKGNNTERSSRSNANLHGFEALNAAKDAVEKACPGVVSCSDVLQYATRDVVILAGGFGWNVPGGRRDGTVSKVEDVNLTNLPSPRANATNLIQLFESKGMTLAQMVVLSGAHTIGKATCITFDNRLHSDIPEPYADPYSPSFKLYLKSQCPNPNMFVRVNLDSTPEKFDGRYFHDLVHHRGLLTSDQTLMSDSRTRHCVYKNRDDGVFKKNFAEAMVAMSKIGVLTGKDGEIRRRMEVVNSK
The following text describes a protein:
Function:
Required for normal meiosis.
Subcellular Localization:
Chromosome. Nucleus.
Sequence:
MVVVSKNNEQQSLILTTELLRTAIFNISYIRGLFPVRYFKDMSVPALDLKMKKLMPMDAESRRLIGWMEKGVYDALHKKHLKKLIFYICETVDGPLIEEYIFSFSYSDSDSQDVRMNINITGINTYGGTLNSTADNSTADMTLNQMSSVDEDFGQNARRSNAFVTYQRFSVYISFHIANYRLCYFFASVQRTILMKLLYYEYVPPDYQPPFFRGCSEEEEAQYVWPKIPLRMEIGNVNSQHHVLTVKVKSVLDPYDPCEDENDNMQDDERSKGPDSLHDDQPCKVFTKPSKLILTENKDADHGEVNEEKLLLITPICEILQDVKQDQVEHQLAKVKDTKGRPASIVQNPILQSHEYDIRRLKARLQRLERHISVPDSPQEGIRKWFAAVSSQLFYKVMEACTRRKPILGDAILSSTVKVQNFNAKICSKLLKKPASIYRKKHFTLNSASLRISGLAGSIFAWAVGFCLFSAQIGHVFVQPKTRSSESKPKVTMEELEEKLTPPSSEPKSAPPSSEPKSAPPSSEPLEKLAVIRRILPEIFAQRCGQRNSSFEAFAQRRTTYDYYNIRLNPREIIFRRLQEESKVALALSSANYFVLSILYRFFRQWSEVSLVRRNSRLTGNPSNEAQSSRSNRIEIPTLLDEPDREGSGGHLAAPEDPVDFLAQFDPLIDLEDAYNTQPQYTEAEVNARLLHEDHVEFDLVPVVSWNTEITAKKTLSTTESVAEVFALCGSGDRPLTCMIPGENERPWNPPRGYVCMYEAYFRQCHLWFPIPSLIISFLNRRHMAFSQLTPAAICNFVAALTFGAEEGYLVNVRCFEEMTTLKAIRSPGYWVVNNRPKHNFLPGPKVSNFKNWEEYYFYVRVDLESYERPFSGRKRMWTEFPDRYRPSPDFPVEFEGVLEAIFRARRRTWKDVTRSRVNRIMGKVRKSFISFAAGLLNMPPPPAPIEEERQPLDGEAAASNPPVSAGPSGVDQVSHEMVNPESQDRMCLEGADVVPAQEIAECDRSQSVQVVEPEVQNITDDRSVVVYAAPPAGEEVNTGLTILDQDKDETVAEPGISRRSREEKGKGGANQSKKRSASEAGLDEAAAPKTFRLSRGETLNSDQFTFKYSGEKFLVRDQEAASHLWRNLMLPGTKDFPNPDDLVLKEGYQKFARSSLETAALANDLIATYDRKLKLKLADREAFDNLKKCADQAKAIYAKDMKEMASLRDAAEIHKAEMSSLNDEVKRLNSREADLQKEFSDLQVALVAVKEHGERECNRLRNDRAAKVARTTKKAQARLDRVKAYLKEQEDLVGPKVDAENQARGAEEIVGILMQRGAKIAASELSGLKELTKRATDEVNALNVIELGDDDLNMSPDQLGFSRQISQVAPVADQHGSNVDLLAEVIRRVSVEETNQTT
The following text describes a protein:
Function:
Involved in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins, possibly by tethering VCP to the endoplasmic reticulum membrane. May play a role in reproduction.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MLYSGTWRTVGIRCPRKKAQICQQQECCIERPPLRLRGFGAALTTTPRLHRPCPPTSGADFTSRNLFPPGIKDFLLLCGRILLLLALLTLTISVTTSWLNSFKSPQVYLKEEEEKNEKRQKLVRKKQQEAQGEKASRYIENVLKPHQEMKLRKLEERFYQMTGEAWKLSSGHKLGGDEGTSQTSFETSNREAAKSQNLPKPLTEFPSPAEQPTCKEIPDLPEEPSQTAEEVVTVALRCPSGNVLRRRFLKSYSSQVLFDWMTRIGYHISLYSLSTSFPRRPLAVEGGQSLEDIGITVDTVLILEEKEQTN
The following text describes a protein:
Function:
Extracellular purine-specific hydrolase present in the apoplastic fluid involved in the degradation of extracellular nucleosides, including inosine and adenosine, and which may participate in wound and pathogen responses (e.g. Botrytis cinerea).
Subcellular Localization:
Secreted, extracellular space, apoplast. Note=Present in the apoplastic fluid.
Sequence:
MLTSPTLKSLWFLFTILGLLGQNLPCVLSSSHRILVDTDVDTDDLFAILYLLKLNKSEFDLVGITLSANAWTNAGHAVNQVYDLLHMMDRDDIPVGVGGEGGISDDGTIHSDVGGYFPIIEQGMTTTGECRYRQAIPKGLGGLLDIDSNYGFRKQFLPQGNRRYTPLQQPTAQKVIVDKISEGPTTVILLGSHTNFALFLMSNPHLKHNIQHIYIMGGGVRSQNPTGCCPANSTVAECQPRQCGNRGNLFTDYTSNPYSEFNIFADPFAAYQVFHSGVPVTLVPLDATNTIPINQKFFETFENNYQRTYEAQYVFLSLKIARDTWFDDEFYKSYFMWDSFTAGVAVSIMRNSANKNNKNGENDFAEMEYMNITVVTSNKPYGRSDGSNPFFDNRRTPKFNLALGGVHSGHVQTGLRDPTCLPKSGIGRGKCKDGYTQEISGSDSVRVLVATRAKPNINIKSKLDREFYVDFLEVLNRPEETGRFNFSSQFPYYKEELFRPDLSKTRPGKPVVFDMDMSAGDFLSLFYLLKVPVDKIDLKAIIVSPTGWANAATIDVVYDLLHMMGRDDIPVGLGDMLALNQSDPIFPPVGGCKYVKAIPRGCGGFLDSDTLYGLARDLPRSPRRYTAENSVTHGAPRDTDRPELRQPLAIEVWQNLTKSGNGVSKITVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGHINREKSDKGNIFTIPSNAYAEFNMFLDPLAAKTVLESALNITLVPLATQHKLSSFQTMLDRLYSSTKTPEARFVKRLLVRLQALHQKHRRYTHIDMFLGEVLGAVLLGGDDASLKPKMRAEHIKVIAEGDESRDGKILIDKLRGKQIKILERVDLISISESFASRLDDKKQSAVIGSFEEQKKIWSTPPS
The following text describes a protein:
Function:
Cleaves aggrecan, a cartilage proteoglycan, at the '392-Glu-|-Ala-393' site and may be involved in its turnover. Also cleaves COMP. May play an important role in the destruction of aggrecan in arthritic diseases.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Domain:
The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. The spacer domain is also required for cleavage of COMP (By similarity); The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Sequence:
MSQMGLHPRRGLTGHWLQRFQPCLPLHTVQWRRLLLLAFLLSLAWPASPLPREEEIVFPEKLNGSSILPGSGVPARLLYRLPAFGEMLLLELEQDPGVQVEGLTVQYLGQAPEMLGGAEPGTYLTGTINGDPESVASLHWDGGALLGVLQYRGAELHLQPLEGGALNSAGGPGAHILRRKSPASSQGPMCTVKAPSGSPSPISRRTKRFASLSRFVETLVVADDKMAAFHGTGLKRYLLTVMAAAAKAFKHPSIRNPVNLVVTRLVILGSGQEGPQVGPSAAQTLRSFCTWQRGLNTPNDSDPDHFDTAILFTRQDLCGVSTCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNSKPCTNLNGQGGSSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLLDKPEAPLHLPATFPGKDYDADRQCQLTFGPDSSHCPQLPPPCAALWCSGHLNGHAMCQTKHSPWADGTPCGSSQACMGGRCLHVDQLKDFNVPQAGGWGPWGPWGDCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTENCPHGSALTFREEQCAAYNHRTDLFKSFPGPMDWVPRYTGVAPRDQCKLTCQARALGYYYVLEPRVADGTPCSPDTSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSRCSKQSGSFKKFRYGYSDVVTIPAGATHILVRQQGGSGLKSIYLALKLSDGSYALNGEYTLMPSPTDVVLPGAVSLRYSGATAASETLSGHGPLAQPLTLQVLVAGNPQNARLRYSFFVPRPVPSTPRPPPQDWLQRRAEILKILRKRPWAGRK
The following text describes a protein:
Function:
Degradation of glucosinolates (glucose residue linked by a thioglucoside bound to an amino acid derivative) to glucose, sulfate and any of the products: thiocyanates, isothiocyanates, nitriles, epithionitriles or oxazolidine-2-thiones.
Subcellular Localization:
Vacuole.
Sequence:
MSTKKIVLKSSDGESFEVDEAVALESQTIAHMVEDDCVDNGIPLPNVTSKILAKVIEYCKKHVDAGKQHRDVALSTSKSMGTCVTMDDQDMKLISLCKAGKIGIAHTPAWFDQNELTDEPHKLSEEEHATPATNLIDFVLGWHLNPTTYGDYPQSMKDHVGDRLPEFTEAQKNKLKNSADFVGINYYYSLFALHGEEQDPSKPSWQSDSLIDYEPRYVDRFNAFTIKPDVAKVDVYSNGLRRLLNYIKDKYGNPEVIITGNGYGEDLGEQDRSLVLALSDHHRTYYIQKHLLSLHQAICEDKVNVTGYFLWSLMDNFEWQEGYSARFGLYYVDYKNNLTRHEKLSAQWYSSFLQDGKEFEFDQHDEYHEHDEYHEHDEL
The following text describes a protein:
Function:
Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria.
Subcellular Localization:
Secreted.
Sequence:
MNFNKIFVFMALILAISLGNTEAGWLRKLGKKIERIGQHTRDASIQVLGIAQQAANVAATARG
The following text describes a protein:
Function:
The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. Acts as a ligand for IGF1R. Binds to the alpha subunit of IGF1R, leading to the activation of the intrinsic tyrosine kinase activity which autophosphorylates tyrosine residues in the beta subunit thus initiatiating a cascade of down-stream signaling events leading to activation of the PI3K-AKT/PKB and the Ras-MAPK pathways. Binds to integrins. Its binding to integrins and subsequent ternary complex formation with integrins and IGFR1 are essential for IGF1 signaling.
Subcellular Localization:
Secreted.
Sequence:
MPTCHAKRLQIMPGFMLKVPSWRSVCVLYSLCCVLILPDNTEGARARCGRELVDDLEFVCGDRGFYIGKPGAARSGGPRSRGKGIVDQCCVRGCDLQHLELYCAKSKKVRRDVPASVLQTPEDQFWLVFQRRYQKLADLQRDEESASQRIRERTLYQQNLLNTKTSTQTSSTHLSSTTETPTFISHIR