ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
O64722 | MEIASQEDPIPINTSYGNSGGGHGNMNHHHHANSAPSSLNITTSNPLLVSSNSNGLGKNHDHSHHHHVGYNIMVTNIKKEKPVVIKYKECLKNHAATMGGNAIDGCGEFMPSGEEGSIEALTCSVCNCHRNFHRRETEGEEKTFFSPYLNHHQPPPQQRKLMFHHKMIKSPLPQQMIMPIGVTTAGSNSESEDLMEEEGGGSLTFRQPPPPPSPYSYGHNQKKRFRTKFTQEQKEKMISFAERVGWKIQRQEESVVQQLCQEIGIRRRVLKVWMHNNKQNLSKKSNNVSNNVDLSAGNNDITENLASTNP | Function: Putative transcription factor.
Sequence Mass (Da): 34716
Sequence Length: 310
Domain: The homeodomain differs form the typical one by having namely 4 instead of 3 extra amino acids inserted in the loop between helix 1 and helix 2.
Subcellular Location: Nucleus
|
Q2QW44 | MDLSGAQGELPLPMHAAASPYLGLHHDHHHHHGGGGGGGGMNGRHMSPPTPPAAAEESKAVVVVSSSATAAARYRECLKNHAAAIGGSATDGCGEFMPGGEEGSLDALRCSACGCHRNFHRKELDAAAAPPLHHHHHQLLGVGAHPRGHGHHHHHLLVAALPPPTRMVMPLSAMHTSESDDAAARPGGGAAARKRFRTKFTAEQKARMLGFAEEVGWRLQKLEDAVVQRFCQEVGVKRRVLKVWMHNNKHTLARRHLHPSPAAAAGDDDDDGAPPPHPDPRRRELAAAAAPPPAPVTQHIKKSVDNKSLISSLAALHCIA... | Function: Putative transcription factor.
Sequence Mass (Da): 34952
Sequence Length: 329
Domain: The homeodomain differs form the typical one by having namely 4 instead of 3 extra amino acids inserted in the loop between helix 1 and helix 2.
Subcellular Location: Nucleus
|
Q53N87 | MVSILQLQTRTEASPASSASAAATRIFAVRRQQQEQEGEEEEEEFEFQERMDLSGAQGELPIPMHASAAASPFAGMGAHGGAGGGHVVELHRHEHVGNNGQAMAMASPPPTNVAVAAEQEGSPVAGKKRGGMAVVGGGGGVAVKYRECLKNHAAAIGGNATDGCGEFMPSGEEGSLEALKCSACGCHRNFHRKEADDLDADSCAAALRAAAGRHHHLLGPALPHHHHKNGGGLLVAGGDPYGAAYAAARALPPPPPPPPHGHHHHHQIIMPLNMIHTSESDEMDVSGGGGGVGRGGGSSSSSKKRFRTKFTAEQKARMLE... | Function: Putative transcription factor.
Sequence Mass (Da): 43962
Sequence Length: 417
Domain: The homeodomain differs form the typical one by having namely 4 instead of 3 extra amino acids inserted in the loop between helix 1 and helix 2.
Subcellular Location: Nucleus
|
Q9FRL5 | MDMRSHEMIERRREDNGNNNGGVVISNIISTNIDDNCNGNNNNTRVSCNSQTLDHHQSKSPSSFSISAAAKPTVRYRECLKNHAASVGGSVHDGCGEFMPSGEEGTIEALRCAACDCHRNFHRKEMDGVGSSDLISHHRHHHYHHNQYGGGGGRRPPPPNMMLNPLMLPPPPNYQPIHHHKYGMSPPGGGGMVTPMSVAYGGGGGGAESSSEDLNLYGQSSGEGAGAAAGQMAFSMSSSKKRFRTKFTTDQKERMMDFAEKLGWRMNKQDEEELKRFCGEIGVKRQVFKVWMHNNKNNAKKPPTPTTTL | Function: Putative transcription factor. Binds DNA at 5'-ATTA-3' consensus promoter regions. Regulates floral architecture and leaf development. Regulators in the abscisic acid (ABA) signal pathway that confers sensitivity to ABA in an ARF2-dependent manner.
Sequence Mass (Da): 33893
Sequence Length: 309
Domain: The ho... |
Q5VM82 | MELSEHEEDAGDVGGGCSSPPTPPHRVLTSAAPETIRCRYHECLRNHAAASGGHVVDGCGEFMPASTEEPLACAACGCHRSFHRRDPSPGRAGAARLPQLHLPASINSRAPPALLLPPAAAASKQGLPFPGYGTPSGGTGTTTASSSDERLRPSPVQPRRRSRTTFTREQKEQMLAFAERVGWRIQRQEEATVEHFCAQVGVRRQALKVWMHNNKHSFKQKQQQENRQEQQQ | Function: Putative transcription factor.
Sequence Mass (Da): 25383
Sequence Length: 232
Domain: The homeodomain differs form the typical one by having namely 4 instead of 3 extra amino acids inserted in the loop between helix 1 and helix 2.
Subcellular Location: Nucleus
|
Q9ZPW7 | MEVREKKDEKMEMTRRKSSALDHHRLPPYTYSQTANKEKPTTKRNGSDPDPDPDLDTNPISISHAPRSYARPQTTSPGKARYRECQKNHAASSGGHVVDGCGEFMSSGEEGTVESLLCAACDCHRSFHRKEIDGLFVVNFNSFGHSQRPLGSRHVSPIMMSFGGGGGCAAESSTEDLNKFHQSFSGYGVDQFHHYQPKKRFRTKFNEEQKEKMMEFAEKIGWRMTKLEDDEVNRFCREIKVKRQVFKVWMHNNKQAAKKKDL | Function: Putative transcription factor.
Sequence Mass (Da): 29951
Sequence Length: 262
Domain: The homeodomain differs form the typical one by having namely 4 instead of 3 extra amino acids inserted in the loop between helix 1 and helix 2.
Subcellular Location: Nucleus
|
Q688U3 | MEFRGHDEPVDEMGVAYGRTPPSSSSSPAASASAGNGAGAAEVRYHECLRNHAAAMGGHVVDGCREFMPMPGDAADALKCAACGCHRSFHRKDDGQQQQQLRLLIPSPPTPRVPLLMPPPQPQPHPHPQHPYLHPPFPYHHTPSGSGGTTTESSSEERGPPSSSAAAAQGRRKRFRTKFTPEQKEQMLAFAERVGWRMQKQDEALVEQFCAQVGVRRQVFKVWMHNNKSSIGSSSGGGSRRQPQEQQSQQQQQQQ | Function: Putative transcription factor.
Sequence Mass (Da): 27959
Sequence Length: 255
Domain: The homeodomain differs form the typical one by having namely 4 instead of 3 extra amino acids inserted in the loop between helix 1 and helix 2.
Subcellular Location: Nucleus
|
Q9SVL0 | MELGGKCNAITTTTMISTEVKPHTDPEPEAKPESDPSMALFPIKKENQKPKTRVDQGAKYRECQKNHAASTGGHVVDGCCEFMAGGEEGTLGALKCAACNCHRSFHRKEVYGHRNSKQDHQLMITPAFYSSNSSYKPRVMHPTGEIGRRTSSSSEDMKKILSHRNQNVDGKSLMMMMMRKKKRVRTKINEEQKEKMKEFAERLGWRMQKKDEEEIDKFCRMVNLRRQVFKVWMHNNKQAMKRNNSNISE | Function: Putative transcription factor.
Sequence Mass (Da): 28658
Sequence Length: 249
Domain: The homeodomain differs form the typical one by having namely 4 instead of 3 extra amino acids inserted in the loop between helix 1 and helix 2.
Subcellular Location: Nucleus
|
Q88F24 | MEIGLREWLILIGIIVIAGILFDGWRRMRGGKGKLKFRLDRSYSNLPDEEGGSAEVLGPSRVLDTHKEPELDESDLPSLSASARDREREPKPVKASKRGKRASAAADVHQGDLNLSAEPREPDLFSDSDDDFAADNNRSSGAAPASNSVKELPPAEEVLVISVISRDEGGFKGPALLQNILESGLRFGEMDIFHRHESMAGHGEVLFSMANAVKPGVFDLDDIDHFSTRAVSFFLGLPGPRHPKQAFDVMVAAARKLAHELNGELKDDQRSVLTAQTIEHYRQRIVEFERRALTQKR | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Location Topology: Single-pass type I membrane protein
Seque... |
Q9P2Y4 | MEGSRPRAPSGHLAPSPPAFDGELDLQRYSNGPAVSAGSLGMGAVSWSESRAGERRFPCPVCGKRFRFNSILALHLRAHPGAQAFQCPHCGHRAAQRALLRSHLRTHQPERPRSPAARLLLELEERALLREARLGRARSSGGMQATPATEGLARPQAPSSSAFRCPYCKGKFRTSAERERHLHILHRPWKCGLCSFGSSQEEELLHHSLTAHGAPERPLAATSAAPPPQPQPQPPPQPEPRSVPQPEPEPEPEREATPTPAPAAPEEPPAPPEFRCQVCGQSFTQSWFLKGHMRKHKASFDHACPVCGRCFKEPWFLKNH... | Function: Transcriptional regulator . Recognizes and binds 2 copies of the core DNA sequence motif 5'-GGGGG-3' . Binds to the HMGN1 promoter and may repress HMGN1 expression . Regulates SNCA expression in primary cortical neurons . Binds to the COL2A1 promoter and activates COL2A1 expression, as part of a complex with ... |
Q6IQX8 | MEGSRPRILVGHLEPSPPAFDGELDLQRYSNGPGVSGTPGPGSPGMGAVGWSETRAGERRFPCPVCGKRFRFNSILALHLRAHPGAQAFQCPHCGHRAAQRALLRSHLRTHQPERPRSPAARLLLELEERALLREARLGRARSSGGMQSSPAAEGLARPQVPSSSAFRCPFCKGKFRTSAERERHLHILHRPWKCSLCSFGSSQEEELLHHSLTAHGASERPLAATSTPEPPPPPQQEPRSALEPEPEPEPRPEPDREANPAPTPAPPEEPPAPPEFRCQVCGQSFTQSWFLKGHMRKHKASFDHACPVCGRCFKEPWFL... | Function: Transcriptional regulator . Recognizes and binds 2 copies of the core DNA sequence motif 5'-GGGGG-3' . Binds to the HMGN1 promoter and may repress HMGN1 expression (By similarity). Regulates SNCA expression in primary cortical neurons (By similarity). Binds to the COL2A1 promoter and activates COL2A1 expressi... |
Q96IT1 | MPTALCPRVLAPKESEEPRKMRSPPGENPSPQGELPSPESSRRLFRRFRYQEAAGPREALQRLWDLCGGWLRPERHTKEQILELLVLEQFLAILPREIQSWVRAQEPESGEQAVAAVEALEREPGRPWQWLKHCEDPVVIDDGDSPLDQEQEQLPVEPHSDLAKNQDAQPITLAQCLGLPSRPPSQLSGDPVLQDAFLLQEENVRDTQQVTTLQLPPSRVSPFKDMILCFSEEDWSLLDPAQTGFYGEFIIGEDYGVSMPPNDLAAQPDLSQGEENEPRVPELQDLQGKEVPQVSYLDSPSLQPFQVEERRKREELQVPE... | Function: DNA-binding transcription factor that can both act as an activator and a repressor.
Sequence Mass (Da): 66908
Sequence Length: 587
Domain: The C2H2-type zinc finger 1, also named C2HR, mediates the interaction with NSD1.
Subcellular Location: Nucleus
|
Q9BS31 | MTKAQESLTLEDVAVDFTWEEWQFLSPAQKDLYRDVMLENYSNLVSVGYQAGKPDALTKLEQGEPLWTLEDEIHSPAHPEIEKADDHLQQPLQNQKILKRTGQRYEHGRTLKSYLGLTNQSRRYNRKEPAEFNGDGAFLHDNHEQMPTEIEFPESRKPISTKSQFLKHQQTHNIEKAHECTDCGKAFLKKSQLTEHKRIHTGKKPHVCSLCGKAFYKKYRLTEHERAHRGEKPHGCSLCGKAFYKRYRLTEHERAHKGEKPYGCSECGKAFPRKSELTEHQRIHTGIKPHQCSECGRAFSRKSLLVVHQRTHTGEKPHTC... | Function: Transcriptional repressor. Regulator of transcriptional factor complexes and may suppress SRE and AP-1 transcription activities mediated by growth factor signaling pathways.
Sequence Mass (Da): 57683
Sequence Length: 505
Domain: The KRAB domain is required for transcriptional repression.
Subcellular Location:... |
Q2HJ10 | MQTMDKQNLLESTRGARSFLGSLWKSEASRIPPVDLPAVELAVQSNHYCHAQKDSGSHPDPEKQRARRKLYVASAICLVFMIGEIIGGYLAQSLAIMTDAAHLLTDFASMLISLFALWVSSRPATKTMNFGWHRAEILGALLSVLSIWVVTGVLVYLAVQRLISGDYEIKGDTMLITSGCAVAVNLIMGLALHQSGHGHSHGNSRDDSSQQQNPSVRAAFIHVIGDLLQSVGVLVAAYIIYFKPEYKYVDPICTFLFSILVLGTTLTILRDVILVLMEGTPKGVDFTTVKNLLLSVDGVEALHSLHIWALTVAQPVLSVH... | Function: Electroneutral proton-coupled antiporter concentrating zinc ions into a variety of intracellular organelles including endosomes, zymogen granules and mitochondria. Thereby, plays a crucial role in cellular zinc homeostasis to confer upon cells protection against its potential cytotoxicity . Regulates the zinc... |
Q62941 | MASRSFFGALWKSEASRIPPVNLPSVELAVQSNHYCHAQKDSGSHPNSEKQRARRKLYVASAICLVFMIGEIIGGYLAQSLAIMTDAAHLLTDFASMLISLFSLWVSSRPATKTMNFGWQRAEILGALLSVLSIWVVTGVLVYLAVQRLISGDYEIKGDTMLITSGCAVAVNIIMGLALHQSGHGHSHGHSHEDSSQQQQNPSVRAAFIHVVGDLLQSVGVLVAAYIIYFKPEYKYVDPICTFLFSILVLGTTLTILRDVILVLMEGTPKGVDFTTVKNLLLSVDGVEALHSLHIWALTVAQPVLSVHIAIAQNVDAQAV... | Function: Electroneutral proton-coupled antiporter concentrating zinc ions into a variety of intracellular organelles including endosomes, zymogen granules and mitochondria. Thereby, plays a crucial role in cellular zinc homeostasis to confer upon cells protection against its potential cytotoxicity . Regulates the zinc... |
Q08E25 | MEPSPTTGGSETTRLVGPRDRGGAGGGLRLKSLFTEAPEPLPEEPKPVEMSFHHCHRDPLPQPGLTPERMQAQRQLCTACAVCCVFMAGEVVGGYLAHSLAIMTDAAHLLADVGSMMGSLFSLWLSTRPATRTMTFGWHRSETLGALASVVSLWMVTGILLYLAFIRLLHSDYHIEGGAMLLTASIAVCANLLMAFVLHQAGPPHSHGSRGAEYAPLEEGSGEPLPLGNTSVRAAFVHVLGDLLQSLGVLIASILIYFKPQYKAADPISTFLFSICALGSTAPTLRDVLRVLMEGTPRSVSFEPVRDTLLSVPGVRAIHE... | Function: Probable proton-coupled zinc ion antiporter mediating the import of zinc from cytoplasm into synaptic vesicles and participating to cellular zinc ion homeostasis in the brain.
Catalytic Activity: 2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (... |
Q99726 | MEPSPAAGGLETTRLVSPRDRGGAGGSLRLKSLFTEPSEPLPEESKPVEMPFHHCHRDPLPPPGLTPERLHARRQLYAACAVCFVFMAGEVVGGYLAHSLAIMTDAAHLLADVGSMMGSLFSLWLSTRPATRTMTFGWHRSETLGALASVVSLWMVTGILLYLAFVRLLHSDYHIEGGAMLLTASIAVCANLLMAFVLHQAGPPHSHGSRGAEYAPLEEGPEEPLPLGNTSVRAAFVHVLGDLLQSFGVLAASILIYFKPQYKAADPISTFLFSICALGSTAPTLRDVLRILMEGTPRNVGFEPVRDTLLSVPGVRATHE... | Function: Probable proton-coupled zinc ion antiporter mediating the import of zinc from cytoplasm into synaptic vesicles and participating to cellular zinc ion homeostasis in the brain.
PTM: Homodimerization through dityrosine bonds is stimulated by oxidative stress.
Location Topology: Multi-pass membrane protein
Catal... |
P97441 | MEPSLATGGSETTRLVSARDRSSAGGGLRLKSLFTEPSEPLPEEPKLEGMAFHHCHKDPVPQSGLSPERVQARRQLYAACAVCFIFMAGEVVGGYLAHSLAIMTDAAHLLADIGSMLASLFSLWLSTRPATRTMTFGWHRSETLGALASVVSLWIVTGILLYLAFLRLLHSDYHIEAGAMLLTASIAVCANLLMAFVLHQTGAPHSHGSTGAEYAPLEEGHGYPMSLGNTSVRAAFVHVLGDLLQSFGVLAASILIYFKPQYKVADPISTFLFSICALGSTAPTLRDVLLVLMEGAPRSVEFEPVRDTLLSVPGVRATHD... | Function: Probable proton-coupled zinc ion antiporter mediating the import of zinc from cytoplasm into synaptic vesicles and participating to cellular zinc ion homeostasis in the brain.
Catalytic Activity: 2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (... |
Q5R617 | MEPSPAAGGLETTRLVSPRDRGGAGGSLRLKSLFTEPSEPLPEESKPVEMPFHHCHRDPLPPPGLTPERLHARRQLYAACAVCFVFMAGEVVGGYLAHSLAIMTDAAHLLADVGSMMGSLFSLWLSTRPATRTMTFGWHRSETLGALASVVSLWMVTGILLYLAFVRLLHSDYHIEGGAMLLTASIAVCANLLMAFVLHQAGPPHSHGSKGAEYAPLEEGPEEPLPLGNTSVRAAFVHVLGDLLQSFGVLAASILIYFKPQYKAADPISTFLFSICALGSTAPTLRDVLRILMEGTPRNVGFEPVRDTLLSVPGVRATHE... | Function: Probable proton-coupled zinc ion antiporter mediating the import of zinc from cytoplasm into synaptic vesicles and participating to cellular zinc ion homeostasis in the brain.
Catalytic Activity: 2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (... |
O14863 | MAGSGAWKRLKSMLRKDDAPLFLNDTSAFDFSDEAGDEGLSRFNKLRVVVADDGSEAPERPVNGAHPTLQADDDSLLDQDLPLTNSQLSLKVDSCDNCSKQREILKQRKVKARLTIAAVLYLLFMIGELVGGYIANSLAIMTDALHMLTDLSAIILTLLALWLSSKSPTKRFTFGFHRLEVLSAMISVLLVYILMGFLLYEAVQRTIHMNYEINGDIMLITAAVGVAVNVIMGFLLNQSGHRHSHSHSLPSNSPTRGSGCERNHGQDSLAVRAAFVHALGDLVQSVGVLIAAYIIRFKPEYKIADPICTYVFSLLVAFTT... | Function: Probable proton-coupled zinc ion antiporter mediating zinc import from cytoplasm potentially into the endocytic compartment . Controls zinc deposition in milk (By similarity).
PTM: Homodimerization through dityrosine bonds is stimulated by oxidative stress.
Location Topology: Multi-pass membrane protein
Catal... |
O55174 | MAGPGAWKRLKSLLRKDDAPLFLNDTSAFDFLDEVSDEGLSRFNKLRVVVADDDSEAPERPVNGAHPALQADDDSLLDQELPLTNSQLSLKMDPCDNCSKRRELLKQRKVKTRLTIAAVLYLLFMIGELVGGYMANSLAIMTDALHMLTDLSAIILTLLALWLSSKSPTRRFTFGFHRLEVLSAMISVMLVYVLMGFLLYEAMQRTIHMNYEINGDVMLITAAVGVAVNVIMGFLLNQSGHHHSHAHSHSLPSNSPSMVSSGHSHGQDSLAVRAAFVHALGDLVQSVGVLIAAYIIRFKPEYKIADPICTYIFSLLVAFT... | Function: Probable proton-coupled zinc ion antiporter mediating zinc import from cytoplasm potentially into the endocytic compartment (By similarity). Controls zinc deposition in milk (By similarity).
Catalytic Activity: 2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out)
Location Topology: Multi-pass membrane protein
... |
Q8TAD4 | MEEKYGGDVLAGPGGGGGLGPVDVPSARLTKYIVLLCFTKFLKAVGLFESYDLLKAVHIVQFIFILKLGTAFFMVLFQKPFSSGKTITKHQWIKIFKHAVAGCIISLLWFFGLTLCGPLRTLLLFEHSDIVVISLLSVLFTSSGGGPAKTRGAAFFIIAVICLLLFDNDDLMAKMAEHPEGHHDSALTHMLYTAIAFLGVADHKGGVLLLVLALCCKVGFHTASRKLSVDVGGAKRLQALSHLVSVLLLCPWVIVLSVTTESKVESWFSLIMPFATVIFFVMILDFYVDSICSVKMEVSKCARYGSFPIFISALLFGNFW... | Function: Together with SLC30A6 forms a functional proton-coupled zinc ion antiporter mediating zinc entry into the lumen of organelles along the secretory pathway . By contributing to zinc ion homeostasis within the early secretory pathway, regulates the activation and folding of enzymes like alkaline phosphatases and... |
Q8R4H9 | MEEKYGGDARPGPGGGLGPVDVPSARLTRYILLLCLTKCLKAVGLFESYDLLKAVHIVQFIFILKLGTAFFMVLFQKPFSSGKPITKHQWIKIFKHAVAGCIISLLWFFGLTLCGPLRTLLLFEHSDIVVISLLSVLFTSSGGGPAKTRGAAFFIIAVICLLLFDNDDLMAKMAEHPEGHHDSALTHMLYTAIAFLGVADHKGGVLLLVLALCCKVGFHTASRKLSIDVGGAKRLQALSQLVSVFLLCPWVIVLSVTTESKVESWFSLIMPFTTVIFFVMILDFYMDSVCSVKMDVSKCARYGSFPIFISALLFGNFWTH... | Function: Together with SLC30A6 forms a functional proton-coupled zinc ion antiporter mediating zinc entry into the lumen of organelles along the secretory pathway. By contributing to zinc ion homeostasis within the early secretory pathway, regulates the activation and folding of enzymes like alkaline phosphatases and ... |
Q6GPY1 | MGTIYLFRKTQRSLLGKLTQEFRLVTADRRSWKILLFGAINVVCTGFLLTWCSSTNSMALTAYTYLTIFDLFSLITSLISYWVMMKKPSPTYSFGFERLEVLAVFASTVLAQLGALFILKESAERFLEQPEIHTGRLLVGTFVALFFNLFTMLSIRNKPFAYVSEAASTSWLQEHVADLSRSLCGVIPGLSSIFLPRMNPFVLIDIAGALALCITYMLIEINNYFAVDTASAIAIAVMTFGTMYPMSVYSGKVLLQTTPPHVIGQLDKLLREVSTLDGVLEVRNEHFWTLGFGTMAGSVHVRIRRDANEQMVLAHVTNRL... | Function: Has probably no intrinsic transporter activity but together with SLC30A5 forms a functional zinc ion:proton antiporter heterodimer, mediating zinc entry into the lumen of organelles along the secretory pathway. As part of that zinc ion:proton antiporter, contributes to zinc ion homeostasis within the early se... |
Q5ZIH3 | MGTIHLFRKSQRSLVGKLTHEFRLVAADRRSWKILLFGAINLICIGFLLMWCSSTNSIALTAYTYLTIFDLFSLITCLISYWVMVKKPSPVYSFGFERFEVLAVFASTVLAQLGALFILKESAERFLEQPEIHTGRLLVGTFVALFFNLFTMLSVRNKPFAYVSEAASTSWLQEHVADLSRSICGIIPGLSSIFLPRMNPFVLIDIAGALALCITYMLIEINNYYAVDTASAIAIALMTFGTMYPMSVYSGKVLLQTTPPHVFGQLDKLLREVSTLDGVLEVRNEHFWTLGFGTLAGSVHVRIRRDANEQMVLAHVTNRL... | Function: Has probably no intrinsic transporter activity but together with SLC30A5 forms a functional zinc ion:proton antiporter heterodimer, mediating zinc entry into the lumen of organelles along the secretory pathway (Probable). As part of that zinc ion:proton antiporter, contributes to zinc ion homeostasis within t... |
Q9ZSK5 | MALNDKSIPHETKVVVLLIPFPAQGHLNQFLHLSRLIVAQNIPVHYVGTVTHIRQATLRYNNPTSNIHFHAFQVPPFVSPPPNPEDDFPSHLIPSFEASAHLREPVGKLLQSLSSQAKRVVVINDSLMASVAQDAANISNVENYTFHSFSAFNTSGDFWEEMGKPPVGDFHFPEFPSLEGCIAAQFKGFRTAQYEFRKFNNGDIYNTSRVIEGPYVELLELFNGGKKVWALGPFNPLAVEKKDSIGFRHPCMEWLDKQEPSSVIYISFGTTTALRDEQIQQIATGLEQSKQKFIWVLREADKGDIFAGSEAKRYELPKGF... | Function: May regulate active versus storage forms of cytokinins, and could have an impact on seed growth. Can also use UDP-xylose to catalyze the formation of O-xylosylzeatin but at much lower affinity.
Catalytic Activity: trans-zeatin + UDP-alpha-D-glucose = H(+) + O-beta-D-glucosyl-trans-zeatin + UDP
Sequence Mass (... |
F2QXM5 | MKFAISTLLIILQAAAVFAAFPISDITVVSERTDASTAYLSDWFVVSFVFSTAGSDETIAGDATIEVSIPNELEFVQYPDSVDPSVSEFFTTAGVQVLSTAFDYDSHVLTFTFSDPGQVITDLEGVVFFTLKLSEQFTESASPGQHTFDFETSDQTYSPSVDLVALDRSQPIKLSNAVTGGVEWFVDIPGAFGDITNIDISTVQTPGTFDCSEVKYAVGSSLNEFGDFTPQDRTTFFSNSSSGEWIPITPASGLPVESFECGDGTISLSFAGELADDEVLRVSFLSNLADDVLEVQNVVNVDLTTADSRKRALTSFVLDE... | Function: Putative adhesion protein. May be involved in cell-cell interaction, interacting with other proteins by salt bridges and hydrogen bonds.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipi... |
A7ZI10 | MSWLNSVLLALTSVQPYMVPATVIGLVSFAFLCFIFFYFFRAVKIINGLKKYTQSINGIENNEPGNQLQHLQSLFVQPELKHAWNEFEESLHSQYELEDGEEKIVRIRATAPSASFFSEQQLVDIPLNTEFFKHLPGILTGVGIIGTFYGLMIGLNHFDPSTPEQVSSSVNNLLRDVLYAFLGSAFAITFSILITWLEKFCLAKCYKYLEKFTAALDALYDSGVGEEYLASLVKSSNESATQARHLKESLVTDLRDMLLHLANSQKVENERLATTLSTTYRETGQQFAEQVSGAIENSLKSPLDKIAGAVQTASGDQSGM... | Function: Component of antiviral defense system Zorya type I, composed of ZorA, ZorB, ZorC and ZorD. Expression of Zorya type I in E.coli (strain MG1655) confers 10,000-fold resistance to phage SECphi27, 100-fold resistance to lambda, and 10-fold resistance to T7. While most T7 infected Zorya-containing cells undergo a... |
P0DW01 | MLAQLFEQLFQSIDSTLITNIFIWAVIFVFLSAWWCDKKNIHSKFREYAPTLMGALGILGTFIGIIIGLLNFNTESIDTSIPVLLGGLKTAFITSIVGMFFAILFNGMDAFFFANKRSALAENNPESVTPEHIYHELKEQNQTLTKLVSGINGDSEGSLIAQIKLLRTEISDSSQAQLANHTHFSNKLWEQLEQFADLMAKGATEQIIDALRQVIIDFNENLTEQFGENFKALDASVKKLVEWQGNYKTQIEQMSEQYQQSVESLVETKTAVAGIWEECKEIPLAMSELREVLQVNQHQISELSRHLETFVAIRDKATTV... | Function: Component of antiviral defense system Zorya type II, composed of ZorA, ZorB and ZorE. Expression of Zorya type II in E.coli (strain MG1655) confers resistance to phages SECphi7 and T7. While most T7 infected Zorya-containing cells undergo abortive infection, a minority produce viable phage progeny. These even... |
A7ZI09 | MFGNAFGVKKRRSDEAEKPFWISYADLMTAMMVLFLVVMVASLSSVTQRIQRAEQGEKTRGQDISRLCERLELHARNVNKTIVVDCHDNRISFGEAGRFDHNQFFLNAEGQKALQDVVPLVLEASNSEEGKKWFKQIVIEGFTDTDGSYLYNLHLSLQRSEWVMCSLLDSRSPLQKNISAEQQLQIRKLFLAGGVSFNNAKESKEASRRVELRMQFFGLKDKRDKADEVDFPPVVNKEVCQLVMPL | Function: Component of antiviral defense system Zorya type I, composed of ZorA, ZorB, ZorC and ZorD. Expression of Zorya type I in E.coli (strain MG1655) confers 10,000-fold resistance to phage SECphi27, 100-fold resistance to lambda, and 10-fold resistance to T7. While most T7 infected Zorya-containing cells undergo a... |
P0DW02 | MDKIIGKQLPKKDQDNEHWVSMSDLMAGLMMVFMFISIAYMHYVRIEKEKIKEVAVAYENAQLQIYNALDIEFAKDLQDWDAEIDKQTLEVRFKSPDVLFGLGSTELKPKFKLILDDFFPRYLKVLDNYQEHITEVRIEGHTSTDWTGTTNPDIAYFNNMALSQGRTRAVLQYVYDIKNIATHQQWVKSKFAAVGYSSAHPILDKTGKEDPNRSRRVTFKVVTNAELQIRKIIQE | Function: Component of antiviral defense system Zorya type II, composed of ZorA, ZorB and ZorE. Expression of Zorya type II in E.coli (strain MG1655) confers resistance to phages SECphi7 and T7. While most T7 infected Zorya-containing cells undergo abortive infection, a minority produce viable phage progeny. These even... |
Q8X3T7 | MDTLTQKLTVLIAVLELLVALLRLIDLLK | Function: Toxic component of a type I toxin-antitoxin (TA) system . Expression in the absence of its cognate antitoxin (small sRNA orzO) leads to cell stasis and a decrease in colony-forming units . Repression of ZorO toxicity requires base pairing between zorO mRNA and sRNA OrzO, as well as RNase III (rnc), suggesting... |
Q8X3T6 | MDSLTQKLTVLIAVLELLVALLRLIDLLK | Function: Toxic component of a type I toxin-antitoxin (TA) system. Overexpression leads to cell stasis and a decrease in colony-forming units . Probably repressed by cognate small RNA orzP. Base pairing occurs between 18 bases in the 5' UTR of zorP mRNA and the 5' end of OrzP sRNA (Probable).
Location Topology: Single-... |
O31688 | MNEQVIVQRDPHEPLKTDKREKNWAQHAELIAALVSGALILAGWLLSGYQVLSIILFLLAFVIGGFAKAKEGIEETLESKTLNVELLMIFAAIGSALIGYWAEGAILIFIFSLSGALETYTMNKSSRDLTSLMQLEPEEATLMVNGETKRVPVSDLQAGDMIVIKPGERVAADGIIESGSTSLDESALTGESMPVEKNTGDTVFTGTVNRNGSLTVRVTKANEDSLFRKIIKLVESAQNSVSPAQAFIERFENAYVKGVLIAVALLLFVPHFALGWSWSETFYRAMVFMVVASPCALVASIMPAALSLISNGARNGMLVK... | Function: Couples the hydrolysis of ATP with the transport of zinc into the cell. Plays an important role in protecting cells against oxidative stress. ZosA-mediated zinc transport is required for post-transcriptional control of comK and competence development.
Catalytic Activity: ATP(in) + H2O(in) + Zn(2+)(out) = ADP(... |
P60852 | MAGGSATTWGYPVALLLLVATLGLGRWLQPDPGLPGLRHSYDCGIKGMQLLVFPRPGQTLRFKVVDEFGNRFDVNNCSICYHWVTSRPQEPAVFSADYRGCHVLEKDGRFHLRVFMEAVLPNGRVDVAQDATLICPKPDPSRTLDSQLAPPAMFSVSTPQTLSFLPTSGHTSQGSGHAFPSPLDPGHSSVHPTPALPSPGPGPTLATLAQPHWGTLEHWDVNKRDYIGTHLSQEQCQVASGHLPCIVRRTSKEACQQAGCCYDNTREVPCYYGNTATVQCFRDGYFVLVVSQEMALTHRITLANIHLAYAPTSCSPTQHT... | Function: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP1 ensures the structural integrity of the ... |
Q62005 | MAWGCFVVLLLLAAAPLRLGQRLHLEPGFEYSYDCGVRGMQLLVFPRPNQTVQFKVLDEFGNRFEVNNCSICYHWVTSEAQEHTVFSADYKGCHVLEKDGRFHLRVFIQAVLPNGRVDIAQDVTLICPKPDHTVTPDPYLAPPTTPEPFTPHAFALHPIPDHTLAGSGHTGLTTLYPEQSFIHPTPAPPSLGPGPAGSTVPHSQWGTLEPWELTELDSVGTHLPQERCQVASGHIPCMVNGSSKETCQQAGCCYDSTKEEPCYYGNTVTLQCFKSGYFTLVMSQETALTHGVLLDNVHLAYAPNGCPPTQKTSAFVVFHV... | Function: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP1 ensures the structural integrity of the ... |
Q9U3F4 | MGPPPPPPPPPLLPSGEILPSRKWKTEDAPRRNNHPAPAPPKPSRPTVDASALQHAAARLRKTGYNEPVRGDVENLSDGRLDRPHQQLPDGDRTYRANLQQLAQPKTRAEIPSPPTYSNQPRPLGDFHRDPNALSQFQQSREALLSSTSPTSNYSPINKFSSSTLTQYANKSPSPPSFGNSNSEATYVSPYSSKHSYPTNFRSYHKDDDYFNNTATTATTTTSSNSLNENNNSNKYGNKETVLQWSEPYDPSKIRRSQSPIRNAREMIHEYSTTNYVTEVQQPPPPPPDLYQRMTQARTFLQNSLAKQLRDEGLTESQKA... | Function: Functions as both a mechanical stabilizer (via LIM domains) of focal adhesions and as a sensor component for muscle cell damage (via N-terminus) . Regulates, stabilizes and maintains posterior lateral mechanosensory (PLM) synaptic branch extension and new synapse formation and growth during larval development... |
Q6GZN7 | MHGCNCNRVSGHLSAVRSSGLENGPFGPSGFGPSMWFTMHSGAAERAIRGGYLTENEKAAWESWLRNLWVCIPCESCRRHYMGIVNAVDFGSVNTGDKVFRLTVDIHNMVNARLNKPHVTLQKAICIYGLDTKLGPASTITFRANTSTFN | Function: FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation.
Catalytic Activity: O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'
Sequence Mass (Da): 16507
Sequence Length: 150
EC: 1.8.3.2
|
Q196W5 | MSVDSFTSRLAVVMTAVVLVWWAQALPVPSPRRGESDCDAACRKFLLQYGYLDLGEENCTEVDSNRKLCSVDDELVGVPRPLARVDLAAGVSHLQTMAGLEPTGRIDASTARLFTSPRCGVPDVSKYIVAAGRRRRTRRESVIVCTTRWTTTKSNSNETLVKWWLDQSSMQWLNSTLNWVSLTNVLHHSFWKWSKESMLAFQQVSLERDAQIVVRFENGSHGDGWDFDGPGNVLAHAFQPGQSLGGDIHLDAAEPWTIYDIDGHDGNSILHVVLHEIGHALGLEHSRDPTSIMYAWYTPFKYDLGPEDVSAVAGLYGAKP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable endopeptidase.
Sequence Mass (Da): 40667
Sequence Length: 363
Domain: 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-pe... |
Q6GZN0 | MGIKGLKPLLRSYGVHEYTVPLSQMSGKTIAVDGTFLLHKYKNCHSVPWHYLTLYTLSNLRLRNVKVLFIFDGMSPPEKSREKSNRRCRKQALMEKGTLVKAQLEVWKKDGGEQAPELAAVSERLVKTRGLDPSLTDPETVQVLTDYVDNMSRDTRVTSDDYELMRRSLDAFGFPYADAPDEAELCCVRVVQMGIADAPMTIDSDALACGALHGVDVVYTDLHGETLTAMSTSKSKEALGLNGEQFMDLCVMCGTDFNQRVHKLGPVTALKLIKAHGSIENIPSAAPSMSCLEAVRTREILSGGDMESRRKDYEAMVQKP... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Probable endonuclease.
Sequence Mass (Da): 40621
Sequence Length: 363
Subcellular Location: Host nucleus
EC: 3.1.-.-
|
P27348 | MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIDNSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAAEGAEN | Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Neg... |
P63104 | MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN | Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways . Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif . Binding generally results in the modulation of the activity of the binding partner . ... |
P63101 | MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQPESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN | Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Pro... |
Q91FG3 | MTSIINQRWPLGNLMDGFPNGEKQNKLSFGGVPEKGYFEEFNKDPKYISFSGTPEKAYFEEFNRYRNIDEDDNRDTFPLFNEISSNPESESYLQTFVDNVRINTDINFVSKTNSFSQNDLSYLNATYVDKSLSLELPIKFNWAKTTSADSPDVVAKKKLISKPDNQYLCGSCWAVSVAGVVGDVFAVAGLVNWVPNISATYALIHYPQGRCKGGDPATLLYNIANNGIPSKHCVDYSWCSQNRTCTTADSAAHFGSDLSPLIPKDRGCYFDSEHYIFKIDSNIRTIVAGSGAIDVSNVQRTIKEYIYTTGPAVGGYIIFR... | Function: Probable cysteine protease.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60620
Sequence Length: 542
Subcellular Location: Membrane
EC: 3.4.-.-
|
D7UER1 | MAMETGLIFHPYMRPGRSARQTFDWGIKSAVQADSVGIDSMMISEHASQIWENIPNPELLIAAAALQTKNIKFAPMAHLLPHQHPAKLATMIGWLSQILEGRYFLGIGAGAYPQASYMHGIRNAGQSNTATGGEETKNLNDMVRESLFIMEKIWKREPFFHEGKYWDAGYPEELEGEEGDEQHKLADFSPWGGKAPEIAVTGFSYNSPSMRLAGERNFKPVSIFSGLDALKRHWEVYSEAAIEAGHTPDRSRHAVSHTVFCADTDKEAKRLVMEGPIGYCFERYLIPIWRRFGMMDGYAKDAGIDPVDADLEFLVDNVFL... | Function: Involved in the degradation and assimilation of (-)-camphor, which allows P.putida strain NCIMB 10007 to grow on this enantiomer of camphor as the sole carbon source . Catalyzes the FMNH(2)-dependent lactonization of 3,6-diketocamphane via a Baeyer-Villiger oxidation to produce the unstable lactone 5-oxo-1,2-... |
A7B3K3 | MFMMLKNKVAIVTGGTRGIGFAVVKKFIENGAAVSLWGSRQETVDQALEQLKELYPDAKISGKYPSLKDTAQVTAMINQVKEEFGAVDILVNNAGISQSTSFYNYQPEEFQKIVDLNVTAVFNCSQAAAKIMKEQGGGVILNTSSMVSIYGQPSGCGYPASKFAVNGLTKSLARELGCDNIRVNAVAPGITRTDMVAALPEAVIKPLIATIPLGRVGEPEDIANAFLFLASDMASYVTGEILSVDGAARS | Function: Involved in the modification of secondary bile acids into iso-bile acids (3beta-bile acids) via epimerization of the 3-OH group through a 3-oxo-intermediate. Catalyzes the oxidation of deoxycholate (DCA) and lithocholate (LCA) to yield 12-alpha-hydroxy-3-oxo-5-beta-cholan-24-oate (3-oxo-DCA) and 3-oxo-5-beta-... |
C8WMP0 | MGIYVITGATSGIGAKTAEILRERGHEVVNIDLNGGDINANLATKEGRAGAIAELHERFPEGIDAMICNAGVSGGKVPISLIISLNYFGATEMARGVFDLLEKKGGSCVVTSSNSIAQGAARMDVAGMLNNHADEDRILELVKDVDPAIGHVYYASTKYALARWVRRMSPDWGSRGVRLNAIAPGNVRTAMTANMLPEQRAAMEAIPVPTHFGEEPLMDPVEIANAMAFIASPEASGINGVVLFVDGGTDALLNSEKVY | Function: Involved in the modification of secondary bile acids into iso-bile acids (3beta-bile acids) via epimerization of the 3-OH group through a 3-oxo-intermediate. Catalyzes the oxidation of deoxycholate (DCA) and lithocholate (LCA) to yield 12-alpha-hydroxy-3-oxo-5-beta-cholan-24-oate (3-oxo-DCA) and 3-oxo-5-beta-... |
A7RIT9 | MMEWIDENSSLFVPPVCNKLMYGEGQLKIMFVGGPNTRKDYHLEEGEELFFQVKGDMCLKVLEKGKPKDIIIKEGEMFLLPSRFNHSPQRFENTVGLVIERERLPEEIDGLRYFCEDGVTVLWEKFFHCTDLTQIAPVIKEFFESEEHKTGKPSKESSCSINVDTETELMEPFPLKQWLKDNKDSYRSGSMAIFEKGEFKVHAHGSGEQEGHSQGEMWFWQLEGKATVNVDEITRELNKNDVLMITAGSDFRVKREEGSVGLSITVDSLANK | Function: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Catalytic Activity: 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde
Sequence Mass (Da): 31200
Sequence Length: 272
Pathway: Cofact... |
Q83V26 | MMFTFGKPLNFQRWLDDHSDLLRPPVGNQQVWQDSDFIVTVVGGPNFRTDFHDDPMEEFFYQFKGNAYLNIMDRGQMDRVELKEGDIFLLPPHLRHSPQRPEAGSRCLVIERQRPKGMLDGFEWYCLSCNGLVYRVDVQLNSIVTDLPPLFDIFYGNVGLRKCPQCGQVHPGKAAIEAVARGDQP | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Catalytic Activity: 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde
Sequence Mass (Da):... |
P46953 | MERCVRVKSWVEENRASFQPPVCNKLMHREQLKIMFVGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGEHRDVVIRQGEIFLLPARVPHSPQRFANTMGLVIERRRMETELDGLRYYVGDTEDVLFEKWFHCKDLGTQLAPIIQEFFHSEQYRTGKPNPDQLLKEPPFPLSTRSVMEPMSLKAWLESHSRELQAGTSLSLFGDSYETQVIAHGQGSSKGPRQDVDVWLWQLEGSSKVTMGGQCVALAPDDSLLVPAGFSYMWERAQGSVALSVTQDPACKKPLG | Function: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Catalytic Activity: 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde
Sequence Mass (Da): 32582
Sequence Length: 286
Pathway: Cofact... |
Q4P2Q7 | MPFPLPLNFPKWLSENEHLLQPPVGNFCLFRTRDYTVMAVGGPNARSDYHYQPTEEFFYQYKGDMLLKVIDEDGKFQDIPIKQGEMFMLPAHTPHSPVRFANTVGIVVERTRPDGSPDAMRWYCPNKEAHGETPTLVKEVHFQCTDLGTQLKPIIDAWVNDEAGRQCSHCGYTQGARELPA | Function: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Catalytic Activity: 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde
Sequence Mass (Da): 20640
Sequence Length: 181
Pathway: Cofact... |
P0C547 | DCCHNTQLPFIYKTCPEGCNL | Function: Has hemolytic activity under low-lecithin conditions . Has low cytotoxic activity (By similarity). Inhibits the expression of VEGF and bFGF in human non-small-cell lung cancer cell line NCI-H1299 in a dose-dependent manner .
PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 2400
Sequence Length: 21
Subcell... |
Q7NU77 | MKQVEIIDSHTGGEPTRLVLSGFPALAGATMADKRDALRERHDQWRRACLLEPRGSDVLVGALYCEPVSPDAACGVIFFNNTGYIGMCGHGTIGLIASLHCLGRIAPGAHKIDTPVGPVDAVLHEDGSVTLRNVPAYRYRRQAAVEVPGHGTVIGDIAWGGNWFFLVAEHGLSVRLDNVAALSAFSCATMQALEEQGITGADGARIDHVELFADDEQADSRNFVMCPGKAYDRSPCGTGTSAKLACLAADGKLAEGEQWVQAGITGSRFVGHYQREGDFIRPYITGRAHITARAMLLIDEQDPFAWGI | Function: Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Can also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp), albeit ... |
A1BBM5 | MTQYIFPCIDGHTCGNPVRLVAGGAPRLEGATMLEKRAHFLREFDWIRTGLMFEPRGHDMMSGAILYPPTRGDCDVAVLYIETSGCLPMCGHGTIGTITMGIENGLIVPRTPGRLSIETPAGKVDIEYRQEGRHVEEVRLTNVPGFLYAEGLTAEVEGLGEIVVDVAYGGNFYAIVEPQKNFRDMADHTAGELIGWSLTLRAALNQKYEFTHPEHPQINGLSHIQWTGAPTVPGAHARNAVFYGDKAIDRSPCGTGTSARMAQLAARGRLGVGDEFWHESIIGSIFKGRIEAAATVAGRDAIIPSIAGWARQTGLNTIFI... | Function: Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate, which would allow P.denitrificans to grow on t4LHyp as a sole carbon source . Also seems to be involved in an alternat... |
D5SQS4 | MTYIPRQWIQVVDSHTGGEPTRLIYDGQHWPFAGSREGALTSQESPSPSVLSGLRKAIDRSSLILPKTMSERRQFLETEADWLRTASLLEPRGSDVLVGAILTPPEHASSQAGVVFCNNTGYLGMCGHGMIGVIVSLGQMGLIAPGPVTIDTPVGSIAATWSGSASVTLTNVWSYRYRHAVSLSVPGLGVVTGDIAWGGNWFFLIGEEVHQKSLDLGNLSDLLAYTSQIRSELGRQGIAGAQGAEIDHVELFASCDSSIADSQNFVLCPGGAYDRSPCGTGTSAKLACLVADGKVAEGGLWRQKSIVGSCFQAKALSIRE... | Function: Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Displays no proline racemase activity.
Catalytic Activity: trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline
Sequenc... |
Q9I476 | MQRIRIIDSHTGGEPTRLVIGGFPDLGQGDMAERRRLLGERHDAWRAACILEPRGSDVLVGALLCAPVDPEACAGVIFFNNSGYLGMCGHGTIGLVASLAHLGRIGPGVHRIETPVGEVEATLHEDGSVSVRNVPAYRYRRQVSVEVPGIGRVSGDIAWGGNWFFLVAGHGQRLAGDNLDALTAYTVAVQQALDDQDIRGEDGGAIDHIELFADDPHADSRNFVLCPGKAYDRSPCGTGTSAKLACLAADGKLLPGQPWRQASVIGSQFEGRYEWLDGQPGGPIVPTIRGRAHVSAEATLLLADDDPFAWGIRR | Function: Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important ... |
A0NXQ7 | MRVIDSHTAGEPTRVVLDGGPDLGSGTLAERAARLEAEHLDFCASVVLEPRGHDAIIGALLVPPSDPACAAGVIYFNNLQNLGMCGHATIGLGVTLAHLGRIRPGRHRFETPVGVVEIDLIDANTVSVVNIESYRLAKDVTVEVEGVGPVTGDVAWGGNWFFLVKNSPIALTGANIRPLTDLTLKIRTALEKAGVTGKDGAWIDHIELFGPAEDPAAQSRNFVLCPGGAYDRSPCGTGCSAKLACLAADGALAPGQDYLQESVIGSTYKISYQPGPGGGVIPTITGQAFVTSDATLIFNPADPYRSGIRL | Function: Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). May be involved in a degradation pathway of t4LHyp, which would allow L.aggregata to grow on t4LHyp as a sole carbon source. Displays no proline racemase activity.
Catalytic Activity: trans-4-hydroxy-L-proli... |
Q5LKW3 | MHVIDSHTGGEPTRVILSGGPHLGSGPLSERAARLARESRAFYRSVMLEPRGQPAMVGALLVEPVDPDCITGVIFFDAEAVLGMCGHGTIGLTVTLAHMGRIRAGTHKIETPVGIVEVCLSDANTVTITNIESRRVHRARQVDVDGFGPVTGDVAYGGNWFFIVDPSPIPIERTNIRALSDAALAIRTAVIANGIGGEEGQPIDHVIFYEMSPRSAVHSRSFVFCPDGTYDRSPCGTGSSARLACLAAEGLLNAGEEIIQESVIGSTYRLSYQPGPNGGVIPKITGQAHVMAESTLHFHTDDPYRNGICHAPQ | Function: Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Displays no proline racemase activity.
Catalytic Activity: trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline
Sequenc... |
D2AV87 | MRTKRVFHAVDSHTEGMPTRVITGGVGVIPGSTMAERREHFLAEMDHVRTLLMYEPRGHSAMSGAILQPPTRPDADYGVLYIEVSGCLPMCGHGTIGVATVLVETGMVEVVEPVTTIRLDTPAGLVVAEVRVEDGAATAVTITNVPSFSAGLDRTVKVPGIGEVTYDLAYGGNFYAILPIESVGLPFDRAHKQQILDAGLAIMDAINEQDEPVHPLDAGIRGCHHVQFTAPGSDARHSRHAMAIHPGWFDRSPCGTGTSARMAQLHARGELPLDTDFVNESFIGTRFVGRLVEETEVTDLPAVVPTITGRAWVTGTAQYF... | Function: Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Displays no proline racemase activity.
Catalytic Activity: trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline
Sequenc... |
Q8P833 | MHTIDVIDSHTAGEPTRVVLAGFPDLGDGDLAQCRERFRSDFDHWRSAIACEPRGSDTMVGALLLPPRDPSACTGVIFFNNVGYLGMCGHGTIGVVRTLAELGRIAPGQHRIETPVGTVGVALADDGTVSIDNVESYRHAAGVEVDVPGHGRVRGDVAWGGNWFFITEQAPCALGLAQQRELTAYTEAIRLALEAAGITGEAGGEIDHIEISGVAPDGSGAARNFVLCPGLAYDRSPCGTGTSAKLACLAADGKLAEGERWLQQGILGSAFEGSYRHSGRGIAPRISGHAFITARSQLLIDPADPFAWGIVA | Function: Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Can also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp), albeit ... |
Q8GWW6 | MHHHHHPCNRKPFTTIFSFFLLYLNLHNQQIIEARNPSQFTTNPSPDVSIPEIKRHLQQYGYLPQNKESDDVSFEQALVRYQKNLGLPITGKPDSDTLSQILLPRCGFPDDVEPKTAPFHTGKKYVYFPGRPRWTRDVPLKLTYAFSQENLTPYLAPTDIRRVFRRAFGKWASVIPVSFIETEDYVIADIKIGFFNGDHGDGEPFDGVLGVLAHTFSPENGRLHLDKAETWAVDFDEEKSSVAVDLESVAVHEIGHVLGLGHSSVKDAAMYPTLKPRSKKVNLNMDDVVGVQSLYGTNPNFTLNSLLASETSTNLADGSR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Matrix metalloproteinases (MMPs) or matrixins may play a role in the degradation and remodeling of the extracellular matrix (ECM) during development or in response to stresses (By similarity). Active on myelin basic protein (MBP) and, to some extent, on McaPLGLDpaAR-NH(... |
P28222 | MEEPGAQCAPPPPAGSETWVPQANLSSAPSQNCSAKDYIYQDSISLPWKVLLVMLLALITLATTLSNAFVIATVYRTRKLHTPANYLIASLAVTDLLVSILVMPISTMYTVTGRWTLGQVVCDFWLSSDITCCTASILHLCVIALDRYWAITDAVEYSAKRTPKRAAVMIALVWVFSISISLPPFFWRQAKAEEEVSECVVNTDHILYTVYSTVGAFYFPTLLLIALYGRIYVEARSRILKQTPNRTGKRLTRAQLITDSPGSTSSVTSINSRVPDVPSESGSPVYVNQVKVRVSDALLEKKKLMAARERKATKTLGIIL... | Function: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for ergot alkaloid derivatives, various anxiolytic and antidepressant drugs and other psychoactive substances, such as lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signal... |
P79400 | AMTDLLVSILVMPISIPYTITQTWSFGQLLCDIWLSSDITCCTASILHLCVIALDRYWAITDALEYSKRRTAGHAAAMIAIVWAISICISIPPLFWRQARAHEEISDCLVNTSQISYTIYSTCGAFYIPSLLLIILYGRIYRAARNRILNPPSLYGKRFTTAHLITGSAGSSLCSLNPSLHEGHSHSAGSPLFFNHVKIKLADSVLERKRISAARERKATKTLGIILGAFIICWLPFFVASLVLPICRDSCWIHPALFDFFTWLGYLNSLINPIIYTVFNEEFRQAFQKVV | Function: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream eff... |
P21577 | MALQQFGLIGLAVMGENLALNIERNGFSLTVYNRTAEKTEAFMADRAQGKNIVPAYSLEDFVASLERPRRILVMVKAGGPVDAVVEQLKPLLDPGDLIIDGGNSLFTDTERRVKDLEALGLGFMGMGVSGGEEGALNGPSLMPGGTQAAYEAVEPIVRSIAAQVDDGPCVTYIGPGGSGHYVKMVHNGIEYGDMQLIAEAYDLLKSVAGLNASELHDVFAAWNKTPELDSFLIEITADIFTKVDDLGTGQPLVELILDAAGQKGTGRWTVETALEIGVAIPTIIAAVNARILSSIKAERQAASEILSGPITEPFSGDRQA... | Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Catalytic Activity: 6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate + NADPH
Sequence Mass (Da): 51073
Sequence Length: 471
Pathway: Carbohydrate degradat... |
P52208 | MQFNVAIMTKRTFGVIGLAVMGENLALNVESRGFPIAVFNRSPNKTEKFMAERAVGKDIKAAYTVEEFVQLLERPRKILVMVKAGGPVDAVINELKPLLEEGDMIIDGGNSLYEDTERRTKDLEATGLGFVGMGVSGGEEGALLGPSLMPGGTPAAYKELEPILTKIAAQVEDPDNPACVTFIGPGGAGHYVKMVHNGIEYGDMQLIAEAYDILKNGLGLSNEQLHEVFGQWNQTDELNSFLIEISTDIFAKKDPETGGHLIDYILDAAGQKGTGRWTVMSGLELGVPIPTIYAAVNARVMSSLKEERVAASGQLSGPSK... | Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Catalytic Activity: 6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate + NADPH
Sequence Mass (Da): 52874
Sequence Length: 482
Pathway: Carbohydrate degradat... |
O83351 | MGADIGFIGLAVMGENLVLNIERNGFSVAVFNRTTTVVDRFLAGRAHGKRITGAHSIAELVSLLARPRKIMLMVKAGSAVDAVIDQILPLLEKGDLVIDGGNSHYQDTIRRMHALEAAGIHFIGTGVSGGEEGALRGPSLMPGGSAQAWPLVSPIFCAIAAKADDGTPCCDWVGSDGAGHYVKMIHNGIEYGDMQIIAEGYWFMKHALGMSYEHMHHTFTRWNTGRLHSYLIEITAAILAHQDTDGTPLLEKILDAAGQKGTGRWTCVAALEEGSPLTLITESVMARSLSAQKQARCKAHRVFGSPVKVSKAETLSAQQR... | Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Catalytic Activity: 6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate + NADPH
Sequence Mass (Da): 52767
Sequence Length: 488
Pathway: Carbohydrate degradat... |
P31072 | MSMDVGVVGLGVMGANLALNIAEKGFKVAVFNRTYSKSEEFMKANASAPFAGNLKAFETMEAFAASLKKPRKALILVQAGAATDSTTEQLKKVFEKGDILVDTGNAHFKDQGRRAQQLEAAGLRFLGMGISGGEEGARKGPAFFPGGTLSVWEEIRPIVEAAAAKADDGRPCVTMNGSGGAGSCVKMYHNSGEYAILQIWGEVFDILRAMGLNNDEVAAVLEDWKSKNFLKSYMLDISIAAARAKDKDGSYLTEHVMDRIGSKGTGLWSAQEALEIGVPAPSLNMAVVSRQFTMYKTERQANASNAPGITQSPGYTLKNK... | Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Catalytic Activity: 6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate + NADPH
Sequence Mass (Da): 52154
Sequence Length: 479
Pathway: Carbohydrate degradat... |
Q9LMX8 | MALTWTHKDRGEIRVHENLEELSIDLVDYIAEISEASIKEHGAFCIVLSGGSLISFMGKLIEPPYDKIVDWAKWYVFWADERVVAKNHDDSNYKLAKDNLLSKVNVFPRHICSINDTVSAEEAATEYEFAIRQMVRSRTVAASDNSDSPRFDLILLGMGSDGHVASLFPNHPALEVKDDWVTFLTDSHKPPPERITFTLPVINSAANVVVVATGESKANAIHLAIDDLPLPDSSLSLPARLVHPSNGNLIWFMDKQAGSKLDRFKFSE | Function: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequence Mass (Da): 29887
Sequence Length: 268
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose... |
Q75IV7 | MLSWNNSWHSSSTENRTMEREIVASYEPKKNNEIRMFESSDEMATDLAEYISQVSEISIKERGYFAIALSGGPLISFMRKLCEAPYNKTLDWSKWYIFWADERAVAKNHVDSYYKSTKEDFLSKVPILNGHVYSINDNVTVEDAATDYEFVIRQLVKIRTVGVSESNDCPKFDLILLSIGSDGHVASLFPNHPALELKDDWVTYITDSPVPPPERITFTLPVINSASNIAVVATGEDKAKAVYFAISDGTEGPDAPSIPARMVQPTDGKLVWFLDKASASFLEAKTKNDGYEHPKY | Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequence Mass (Da): 33270
Sequence Length: 296
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (... |
Q8LG70 | MAPVKRRVFKTNNEMAVELAKYTADLSSKFCKERGVFTVVLSGGDLIAWLWKLLEAPYIDSIEWSKWHIFWVDERVCAWDHADSNYKLAYDGFLSKVPVPAENIYAIDNGLGAEGNAELAAERYEECLKQKVNQNIIRTYKSSGFPQFDLQLLGMGPDGHMASLFPGHAQINEKVKWVTSITDSPKPPSKRITLTLPVINCASYNVMAVCDKEQADSVAAALNHTKDLPAGRLTADVEVVWFLDQAAASKLPHGWCSIL | Function: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequence Mass (Da): 28863
Sequence Length: 259
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose... |
A0A517FNC4 | MDSRVLGALAALLAAAAAWVMRAAAEWLWWRPRRLERSLRSQGVDGNLYRFLNGDLKETVRLTKEARAQPISPPSHRFLHRINPLLLRAISHHGKFALTWIGPTPRVSIMDPELVREVLSNKFGHFAKPKAAPIVKLLATGLANYEGEKWVRHRRIINPAFHLEKLKRMLPAFFSCCSELIGRWESLVGCDESREVDVWPELQNLTGDVISRTAFGSSYAEGRRIFQLQSEQAELLIQAVQTVYIPGYRFLPTPKNIRRTKIDKEVRALLRSIIEKRENAMKMGDVHDDLLGLLMEYNLKESEHFNSKNIGMTTEDVIEE... | Function: Involved in the biosynthesis of spiroketal steroid and saponin natural products from cholesterol such as diosgenin and analogs (e.g. furostanol and spirostanol), plant defense compounds used as main precursors for the industrial production of steroid hormones . During the 5,6-spiroketalization of cholesterol,... |
K7NBW3 | MEKGDTHILVFPFPSQGHINPLLQLSKRLIAKGIKVSLVTTLHVSNHLQLQGAYSNSVKIEVISDGSEDRLETDTMRQTLDRFRQKMTKNLEDFLQKAMVSSNPPKFILYDSTMPWVLEVAKEFGLDRAPFYTQSCALNSINYHVLHGQLKLPPETPTISLPSMPLLRPSDLPAYDFDPASTDTIIDLLTSQYSNIQDANLLFCNTFDKLEGEIIQWMETLGRPVKTVGPTVPSAYLDKRVENDKHYGLSLFKPNEDVCLKWLDSKPSGSVLYVSYGSLVEMGEEQLKELALGIKETGKFFLWVVRDTEAEKLPPNFVES... | Function: Catalyzes the transfer of a glucose moiety to the C-3 hydroxyl of mogrol to form mogroside IE . Besides mogrol, UGT74AC1 also shows activity in vitro with quercetin and naringenin as substrate .
Catalytic Activity: mogrol + UDP-alpha-D-glucose = H(+) + mogroside IE + UDP
Sequence Mass (Da): 51275
Sequence Len... |
P12961 | MASRLVSAMLSGLLFWLMFEWNPAFAYSPRTPDRVSETDIQRLLHGVMEQLGIARPRVEYPAHQAMNLVGPQSIEGGAHEGLQHLGPFGNIPNIVAELTGDNIPKDFSEDQGYPDPPNPCPLGKTADDGCLENAPDTAEFSREFQLDQHLFDPEHDYPGLGKWNKKLLYEKMKGGQRRKRRSVNPYLQGKRLDNVVAKKSVPHFSEEEKEAE | Function: Acts as a molecular chaperone for PCSK2/PC2, preventing its premature activation in the regulated secretory pathway. Binds to inactive PCSK2 in the endoplasmic reticulum and facilitates its transport from there to later compartments of the secretory pathway where it is proteolytically matured and activated. A... |
A5A6J6 | MVSRMVSTMLSGLLFWLASGWTPAFAYSPRTPDRVSEADIQRLLHGVMEQLGIARPRVEYPAHQAMNLVGPQSIEGGAHEGLQHLGPFGNIPNIVAELTGDNIPKDFSEDQGYPDPPNPCPVGKTDDGCLENTPDTAEFSREFQLHQHLFDPEHDYPGLGKWNKKLLYEKMKGGERRKRRSVNPYLQGQRLDNVVAKKSVPHFSDEDKDPE | Function: Acts as a molecular chaperone for PCSK2/PC2, preventing its premature activation in the regulated secretory pathway. Binds to inactive PCSK2 in the endoplasmic reticulum and facilitates its transport from there to later compartments of the secretory pathway where it is proteolytically matured and activated. A... |
P18844 | MGMYSAIPLALPMVLLMVYGLTPSLGHSPRTPDRVSEADIQRLLHGVMEELGIARPRVEYPAHQAMNLVGPQSIEGGAHEGLQHLGPYGNIPNIVAELTGDNIPKDFREDQGYPNPPNPCPVGKTGDGCLEDTPDTAQFSREYQLHQNLYDPEHNYPGASTWNKKLLYEKIKGASQRQKRTVNPYLQGQKLDKVVAKKSVPHFSGEEE | Function: Acts as a molecular chaperone for pcsk2, preventing its premature activation in the regulated secretory pathway. Binds to inactive pcsk2 in the endoplasmic reticulum and facilitates its transport from there to later compartments of the secretory pathway where it is proteolytically matured and activated. Also ... |
U5NH37 | MGSQETNLPPHVLIFPLPIQGHVNSMLRLAELLCLAELDITFIVSEFSHSRLIKHTNVASRFARYPGFQFQPISDGLPDDHPRAGERVMDILPSTKNVTGPLFKQMMVENKCFSSATRRPITCIIADGVLSFAGDFAQEKGIPLIYFRTVSACSFWACFCMPELIESGDIPIKGNGMDLIVKSVPGMETFLRRRDLPGFCRVNDINEPKLQILKTETRQTTRAQAAILNTFEDLEGPILSQIRKHMPRLFTIGPSHSHLTSRLETKNIKTLISSGSFWEEDRSCVDWLDAQPPRSVLYVSFGSITVVTRDQLLEFWYGLV... | Function: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vincristine, quinine, and strychnine) biosynthesis pathway . Catalyzes the glucosylation of 7-deoxyloganetic acid to form 7-deoxyloganic acid using UDP-glucose as the sugar donor . Inactive with loganetic acid, loganetin,... |
Q06BR2 | MGPSVRPGFLVVVIGLQFVAASMEVNSRKFEPMVAFICNKPAMHRVPSGWVPDDDPAKSCVKQPEEILEYCKKLYPDHDITNVLQASYKVTIPNWCGFNVTHCHKHGNHTVRPFRCLVGPFQSEALLVPEHCIFDHYHDPRVCNEFDQCNETAMSKCSARGMTTQSFAMLWPCQEPGHFSGVEFVCCPKVSLIPESTEAPKSSPPTPAKTENGLDDYTAYLKGDSKYMSKYANEHERFKAAEKVMQQFQRERDTKMMKDWKAARDSVREKKKTDPKKAMELNKELTERYQKIYHAYEQESIAEKKQLVNTHQQHIQSWLN... | Function: Acts as a kinesin I membrane receptor, thereby playing a role in axonal anterograde transport of cargo towards synapes in axons.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 70322
Sequence Length: 612
Subcellular Location: Cell membrane
|
P14599 | MCAALRRNLLLRSLWVVLAIGTAQVQAASPRWEPQIAVLCEAGQIYQPQYLSEEGRWVTDLSKKTTGPTCLRDKMDLLDYCKKAYPNRDITNIVESSHYQKIGGWCRQGALNAAKCKGSHRWIKPFRCLGPFQSDALLVPEGCLFDHIHNASRCWPFVRWNQTGAAACQERGMQMRSFAMLLPCGISVFSGVEFVCCPKHFKTDEIHVKKTDLPVMPAAQINSANDELVMNDEDDSNDSNYSKDANEDDLDDEDDLMGDDEEDDMVADEAATAGGSPNTGSSGDSNSGSLDDINAEYDSGEEGDNYEEDGAGSESEAEVE... | Function: During development, plays a role in the regulation of the neddylation pathway. Appl and APP-BP1 interact antagonistically during development.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 98333
Sequence Length: 887
Domain: The NPTY motif mediates the interaction with clathrin (By ... |
P05067 | MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFF... | Function: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis . Involved in cell mobility and transcription regulation through pr... |
O93279 | MGETTAFVLLLVATLTRSSEIPADDTVGLLTEPQVAMFCGKLNMHINVQNGKWESDPSGTKSCLNTKEGILQYCQEVYPELQITNVVEANQPVSIQNWCKKGRKQCRSHTHIVVPYRCLVGEFVSDALLVPDKCKFLHQERMNQCESHLHWHTVAKESCGDRSMNLHDYGMLLPCGIDRFRGVKFVCCPAETEQETDSSEVEGEESDVWWGGADPEYSENSPPTPSRATYVAGDAFERDENGDGDEDEEDDEDVDPTDEQESDERTANVAMTTTTTTTTESVEEVVRAVCWAQAESGPCRAMLERWYFNPKKRRCVPFLF... | Function: Functional neuronal receptor which couples to intracellular signaling pathway through the GTP-binding protein G(O).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 82857
Sequence Length: 737
Subcellular Location: Membrane
|
Q9Z6M7 | MAYGTRYPTLAFHTGGIGESDDGMPPQPFETFCYDSALLQAKIENFNIVPYTSVLPKELFGNIVPVDTCVKSFKHGAVLEVIMAGRGAALSDGTHAIATGIGICWGKDKNGELIGGWAAEYVEFFPTWINDEIAETHAKMWLKKSLQHELDLRSIAKHSEFQFFHNYINIKQKFGFCLTALGFLNFENAEPAKVN | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Part of the AaxABC system, catalyzes the decarboxylation of L-arginine. The arginine uptake by the bacterium in the macrophage may be a virulence factor against the host innate immune response.
Catalytic Activity: H(+) + L-arginine = agmatine + CO2
Sequ... |
Q9Z6M8 | MTSRTKSSKNLGTIALAGMVVSSIIGGGIFSLPQNMAATAGAGAVILSWILTGFGMFFIANTFRILSTIRPDLKEGIYMYSREGFGPYIGFTIGWGYWLCQIFGNVGYAVITMDALNYFFPPYFQGGNTLPAILGGSILIWVFNFIVLKGIRQASIINVIGTIFKIIPLIIFIILTAFFFKLAVFKTDFWGHAVTKAQPSLGSVSSQLKGTMLVTLWAFIGIEGAVVMSGRAKNPLSVGQATVLGFLGCLTIYILFSLLPFGSLFQHQLANIPNPSTAGVLDILVGKWGEVLMNVGLIIAVLSSWLSWTIIVAEIPFSAA... | Function: Catalyzes the exchange of L-arginine for agmatine. The arginine uptake by the bacterium in the macrophage may be a virulence factor against the host innate immune response.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52548
Sequence Length: 485
Subcellular Location: Cell inner membrane
|
P55096 | MAAFSKYLTARNTSLAGAAFLLLCLLHKRRRALGLHGKKSGKPPLQNNEKEGKKERAVVDKVFLSRLSQILKIMVPRTFCKETGYLLLIAVMLVSRTYCDVWMIQNGTLIESGIIGRSSKDFKRYLFNFIAAMPLISLVNNFLKYGLNELKLCFRVRLTRYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQGPASMMAYLLVSGLFLTRLRRPIGKMTIMEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTIHSVFRKLVEHLHNFIFFRFSMGFIDSII... | Function: Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that catalyzes the transport of long-chain fatty acids (LCFA)-CoA, dicarboxylic acids-CoA, long-branched-chain fatty acids-CoA and bile acids from the cytosol to the peroxisome lumen for beta-oxydation. Has fatty ac... |
O14678 | MAVAGPAPGAGARPRLDLQFLQRFLQILKVLFPSWSSQNALMFLTLLCLTLLEQFVIYQVGLIPSQYYGVLGNKDLEGFKTLTFLAVMLIVLNSTLKSFDQFTCNLLYVSWRKDLTEHLHRLYFRGRAYYTLNVLRDDIDNPDQRISQDVERFCRQLSSMASKLIISPFTLVYYTYQCFQSTGWLGPVSIFGYFILGTVVNKTLMGPIVMKLVHQEKLEGDFRFKHMQIRVNAEPAAFYRAGHVEHMRTDRRLQRLLQTQRELMSKELWLYIGINTFDYLGSILSYVVIAIPIFSGVYGDLSPAELSTLVSKNAFVCIYL... | Function: Lysosomal membrane protein that transports cobalamin (Vitamin B12) from the lysosomal lumen to the cytosol in an ATP-dependent manner . Targeted by LMBRD1 lysosomal chaperone from the endoplasmic reticulum to the lysosomal membrane . Then forms a complex with lysosomal chaperone LMBRD1 and cytosolic MMACHC to... |
O89016 | MAVPGPTARAGARPRLDLQLVQRFVRIQKVFFPSWSSQNVLMFMTLLCVTLLEQLVIYQVGLIPSQYYGVLGNKDLDGFKALTLLAVTLIVLNSTLKSFDQFTCNLLYVSWRKDLTEHLHHLYFRARVYYTLNVLRDDIDNPDQRISQDVERFCRQLSSVTSKLIISPFTLTYYTYQCFQSTGWLGPVSIFGYFIVGTMVNKTLMGPIVTKLVQQEKLEGDFRFKHMQIRVNAEPAAFYRAGLVEHMRTDRRLQRLLQTQRELMSRELWLYIGINTFDYLGSILSYVVIAIPIFSGVYGDLSPTELSTLVSKNAFVCIYL... | Function: Lysosomal membrane protein that transports cobalamin (Vitamin B12) from the lysosomal lumen to the cytosol in an ATP-dependent manner. Targeted by LMBRD1 lysosomal chaperone from the endoplasmic reticulum to the lysosomal membrane. Then forms a complex with lysosomal chaperone LMBRD1 and cytosolic MMACHC to t... |
P61221 | MADKLTRIAIVNHDKCKPKKCRQECKKSCPVVRMGKLCIEVTPQSKIAWISETLCIGCGICIKKCPFGALSIVNLPSNLEKETTHRYCANAFKLHRLPIPRPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDDPPDWQEILTYFRGSELQNYFTKILEDDLKAIIKPQYVDQIPKAAKGTVGSILDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCLYGVPSAYGVVTMPFSVREGINIFLDGYVPTE... | Function: Nucleoside-triphosphatase (NTPase) involved in ribosome recycling by mediating ribosome disassembly . Able to hydrolyze ATP, GTP, UTP and CTP . Splits ribosomes into free 60S subunits and tRNA- and mRNA-bound 40S subunits . Acts either after canonical termination facilitated by release factors (ETF1/eRF1) or ... |
Q8NE71 | MPKAPKQQPPEPEWIGDGESTSPSDKVVKKGKKDKKIKKTFFEELAVEDKQAGEEEKVLKEKEQQQQQQQQQQKKKRDTRKGRRKKDVDDDGEEKELMERLKKLSVPTSDEEDEVPAPKPRGGKKTKGGNVFAALIQDQSEEEEEEEKHPPKPAKPEKNRINKAVSEEQQPALKGKKGKEEKSKGKAKPQNKFAALDNEEEDKEEEIIKEKEPPKQGKEKAKKAEQGSEEEGEGEEEEEEGGESKADDPYAHLSKKEKKKLKKQMEYERQVASLKAANAAENDFSVSQAEMSSRQAMLENASDIKLEKFSISAHGKELFV... | Function: Isoform 2 is required for efficient Cap- and IRES-mediated mRNA translation initiation. Isoform 2 is not involved in the ribosome biogenesis.
PTM: Isoform 2 is phosphorylated at phosphoserine and phosphothreonine. Isoform 2 phosphorylation on Ser-109 and Ser-140 by CK2 inhibits association of EIF2 with riboso... |
P41238 | MTSEKGPSTGDPTLRRRIEPWEFDVFYDPRELRKEACLLYEIKWGMSRKIWRSSGKNTTNHVEVNFIKKFTSERDFHPSMSCSITWFLSWSPCWECSQAIREFLSRHPGVTLVIYVARLFWHMDQQNRQGLRDLVNSGVTIQIMRASEYYHCWRNFVNYPPGDEAHWPQYPPLWMMLYALELHCIILSLPPCLKISRRWQNHLTFFRLHLQNCHYQTIPPHILLATGLIHPSVAWR | Cofactor: Binds 1 Zn(2+) ion per subunit.
Function: Cytidine deaminase catalyzing the cytidine to uridine postranscriptional editing of a variety of mRNAs . Form complexes with cofactors that confer differential editing activity and selectivity. Responsible for the postranscriptional editing of a CAA codon for Gln to a... |
P38483 | MSSETGPVAVDPTLRRRIEPHEFEVFFDPRELRKETCLLYEINWGGRHSIWRHTSQNTNKHVEVNFIEKFTTERYFCPNTRCSITWFLSWSPCGECSRAITEFLSRYPHVTLFIYIARLYHHADPRNRQGLRDLISSGVTIQIMTEQESGYCWRNFVNYSPSNEAHWPRYPHLWVRLYVLELYCIILGLPPCLNILRRKQPQLTFFTIALQSCHYQRLPPHILWATGLK | Cofactor: Binds 1 Zn(2+) ion per subunit.
Function: Cytidine deaminase catalyzing the cytidine to uridine postranscriptional editing of a variety of mRNAs. Form complexes with cofactors that confer differential editing activity and selectivity. Responsible for the postranscriptional editing of a CAA codon for Gln to a ... |
Q3SYR3 | MAQKEEAAAAAEPASQNGEEVENLEDPEKLKELIELPPFEIVTGERLPAHYFKFQFRNVEYSSGRNKTFLCYVVEAQSKGGQVQASRGYLEDEHATNHAEEAFFNSIMPTFDPALRYMVTWYVSSSPCAACADRIVKTLNKTKNLRLLILVGRLFMWEEPEIQAALRKLKEAGCRLRIMKPQDFEYIWQNFVEQEEGESKAFEPWEDIQENFLYYEEKLADILK | Cofactor: Binds 1 Zn(2+) ion per subunit.
Function: Probable C to U editing enzyme whose physiological substrate is not yet known. Does not display detectable apoB mRNA editing. Has a low intrinsic cytidine deaminase activity. May play a role in the epigenetic regulation of gene expression through the process of active... |
Q9Y235 | MAQKEEAAVATEAASQNGEDLENLDDPEKLKELIELPPFEIVTGERLPANFFKFQFRNVEYSSGRNKTFLCYVVEAQGKGGQVQASRGYLEDEHAAAHAEEAFFNTILPAFDPALRYNVTWYVSSSPCAACADRIIKTLSKTKNLRLLILVGRLFMWEEPEIQAALKKLKEAGCKLRIMKPQDFEYVWQNFVEQEEGESKAFQPWEDIQENFLYYEEKLADILK | Cofactor: Binds 1 Zn(2+) ion per subunit.
Function: Probable C to U editing enzyme whose physiological substrate is not yet known. Does not display detectable apoB mRNA editing. Has a low intrinsic cytidine deaminase activity. May play a role in the epigenetic regulation of gene expression through the process of active... |
Q9WV35 | MAQKEEAAEAAAPASQNGDDLENLEDPEKLKELIDLPPFEIVTGVRLPVNFFKFQFRNVEYSSGRNKTFLCYVVEVQSKGGQAQATQGYLEDEHAGAHAEEAFFNTILPAFDPALKYNVTWYVSSSPCAACADRILKTLSKTKNLRLLILVSRLFMWEEPEVQAALKKLKEAGCKLRIMKPQDFEYIWQNFVEQEEGESKAFEPWEDIQENFLYYEEKLADILK | Cofactor: Binds 1 Zn(2+) ion per subunit.
Function: Probable C to U editing enzyme whose physiological substrate is not yet known. Does not display detectable apoB mRNA editing. Has a low intrinsic cytidine deaminase activity. May play a role in the epigenetic regulation of gene expression through the process of active... |
Q99J72 | MQPQRLGPRAGMGPFCLGCSHRKCYSPIRNLISQETFKFHFKNLGYAKGRKDTFLCYEVTRKDCDSPVSLHHGVFKNKDNIHAEICFLYWFHDKVLKVLSPREEFKITWYMSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRPWKRLLTNFRYQDSKLQEILRPCYISVPSSSSSTLSNICLTKGLPETRFWVEGRRMDPLSEEEFYSQFYNQRVKHLCYYHRMKPYLCYQLEQFNGQAPLKGCLLSEKGKQHAEILFLDKIRSMELSQVTITC... | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. Exhibits antiviral act... |
P15891 | MALEPIDYTTHSREIDAEYLKIVRGSDPDTTWLIISPNAKKEYEPESTGSSFHDFLQLFDETKVQYGLARVSPPGSDVEKIIIIGWCPDSAPLKTRASFAANFAAVANNLFKGYHVQVTARDEDDLDENELLMKISNAAGARYSIQTSSKQQGKASTPPVKKSFTPSKSPAPVSKKEPVKTPSPAPAAKISSRVNDNNDDDDWNEPELKERDFDQAPLKPNQSSYKPIGKIDLQKVIAEEKAKEDPRLVQKPTAAGSKIDPSSDIANLKNESKLKRDSEFNSFLGTTKPPSMTESSLKNDDDKVIKGFRNEKSPAQLWAE... | Function: Regulates ARP2/3 complex-mediated actin assembly. Recruits ARP2/3 complex to sides of preexisting actin filaments, which may promote nucleation or stabilization of filament branches. Binds to actin filaments, but not actin monomers. Actin binding is required for ARP2/3 complex activation. May also have a role... |
Q0CX54 | MTKSIIASEPPSAESSGRLPWKILGQTTGFPNQDQELWWLNTAPLLNEFLAECQYDVHLQYQYLTFFRHHVIPVLGPFFAPGTTPNFASRLSKHGHPLDFSVNFQESGATVRMSLGAIGSFAGLQQDPLNQFRAREVLDKLAILYPTVDLQLFKHFESEFGINHADALKVAAKLPKLDRATKMIAIDMLKNGSMTFKVYYMVRSKAAATGLPVHTVLFNAVQRLGSAFEPGLSLLKQFLSPLCDAGETDLGLLSFDCVPTESSRIKLYAIKQVGSLDAIRNLWTLGGTMDDPTTMKGLAVLEHVCELLQFGWSGDSRVQP... | Function: Trans-prenyltransferase that acts in both the aspulvinones and butyrolactones pathways . Prenylates aspulvinone E and butyrolactone II to yield repectively aspulvinone H and butyrolactone I .
Catalytic Activity: aspulvinone E + 2 dimethylallyl diphosphate = aspulvinone H + 2 diphosphate
Sequence Mass (Da): 42... |
Q8Z3X3 | MQPNDITFFQRFQNDILAGRKTITIRDASESHFKAGDALRVGRFEDDGYFCTIEVTGTSTVTLDTLNEKHAQQENMSLDELKRVIAEIYPNQTQFYVIDFKCL | Function: Catalyzes the hydrolysis of N(4)-acetylcytidine (ac4C).
Catalytic Activity: H2O + N(4)-acetylcytidine = acetate + cytidine + H(+)
Sequence Mass (Da): 11871
Sequence Length: 103
EC: 3.5.1.135
|
A8GFL3 | MSREITFFSRFEQDILAGRKTITIRDASESHFQPGEVLRVSRNEDNVFFCQIEVLSVTPVRLDGLTEQHARQENMSLGELKQVIKEIYPGLDELFVITFAKR | Function: Catalyzes the hydrolysis of N(4)-acetylcytidine (ac4C).
Catalytic Activity: H2O + N(4)-acetylcytidine = acetate + cytidine + H(+)
Sequence Mass (Da): 11817
Sequence Length: 102
EC: 3.5.1.135
|
Q8EFP8 | MLTEITFFERFEHDILMGKKTITLRNEAESHVIPGQILPVSTFETHRWFCDIQVLEVTPITLSGLTTLHAQQENMTLAELRLVIAEIYPDLEQLYMIRFKVLTK | Function: Catalyzes the hydrolysis of N(4)-acetylcytidine (ac4C).
Catalytic Activity: H2O + N(4)-acetylcytidine = acetate + cytidine + H(+)
Sequence Mass (Da): 12147
Sequence Length: 104
EC: 3.5.1.135
|
P11310 | MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAIS... | Function: Medium-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats . The first step of fatty acid beta-oxidation... |
P08503 | MAAALRRGYKVLRSVSHFECRAQHTKPSLKQEPGLGFSFELTEQQKEFQTIARKFAREEIIPVAPDYDKSGEYPFPLIKRAWELGLINTHIPESCGGLGLGTFDACLITEELAYGCTGVQTAIEANSLGQMPVIIAGNDQQKKKYLGRMTEQPMMCAYCVTEPSAGSDVAGIKTKAEKKGDEYVINGQKMWITNGGKANWYFVLTRSNPDPKVPASKAFTGFIVEADTPGIHIGKKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDRTRPTVAAGAVGLAQRALDEATKYALDRKTFGKLLVEHQGVS... | Function: Medium-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats . The first step of fatty acid beta-oxidation... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.