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
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Q2QW44 | MDLSGAQGELPLPMHAAASPYLGLHHDHHHHHGGGGGGGGMNGRHMSPPTPPAAAEESKAVVVVSSSATAAARYRECLKNHAAAIGGSATDGCGEFMPGGEEGSLDALRCSACGCHRNFHRKELDAAAAPPLHHHHHQLLGVGAHPRGHGHHHHHLLVAALPPPTRMVMPLSAMHTSESDDAAARPGGGAAARKRFRTKFTAEQKARMLGFAEEVGWRLQKLEDAVVQRFCQEVGVKRRVLKVWMHNNKHTLARRHLHPSPAAAAGDDDDDGAPPPHPDPRRRELAAAAAPPPAPVTQHIKKSVDNKSLISSLAALHCIALLLFHQIDA | 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
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Q53N87 | MVSILQLQTRTEASPASSASAAATRIFAVRRQQQEQEGEEEEEEFEFQERMDLSGAQGELPIPMHASAAASPFAGMGAHGGAGGGHVVELHRHEHVGNNGQAMAMASPPPTNVAVAAEQEGSPVAGKKRGGMAVVGGGGGVAVKYRECLKNHAAAIGGNATDGCGEFMPSGEEGSLEALKCSACGCHRNFHRKEADDLDADSCAAALRAAAGRHHHLLGPALPHHHHKNGGGLLVAGGDPYGAAYAAARALPPPPPPPPHGHHHHHQIIMPLNMIHTSESDEMDVSGGGGGVGRGGGSSSSSKKRFRTKFTAEQKARMLEFAERVGWRLQKLDDAMVHHFCQEIGVKRRVLKVWMHNNKHNLAKKPLPSSPPPPPQIPPMSMPPSPPPPQIPPMSMPPSPPPMPMPMPPSPPQLKLE | 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
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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 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
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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
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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
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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
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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
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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
Sequence Mass (Da): 32842
Sequence Length: 297
Subcellular Location: Cell inner membrane
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Q9P2Y4 | MEGSRPRAPSGHLAPSPPAFDGELDLQRYSNGPAVSAGSLGMGAVSWSESRAGERRFPCPVCGKRFRFNSILALHLRAHPGAQAFQCPHCGHRAAQRALLRSHLRTHQPERPRSPAARLLLELEERALLREARLGRARSSGGMQATPATEGLARPQAPSSSAFRCPYCKGKFRTSAERERHLHILHRPWKCGLCSFGSSQEEELLHHSLTAHGAPERPLAATSAAPPPQPQPQPPPQPEPRSVPQPEPEPEPEREATPTPAPAAPEEPPAPPEFRCQVCGQSFTQSWFLKGHMRKHKASFDHACPVCGRCFKEPWFLKNHMKVHASKLGPLRAPGPASGPARAPQPPDLGLLAYEPLGPALLLAPAPTPAERREPPSLLGYLSLRAGEGRPNGEGAEPGPGRSFGGFRPLSSALPARARRHRAEEPEEEEEVVEAEEETWARGRSLGSLASLHPRPGEGPGHSASAAGAQARSTATQEENGLLVGGTRPEGGRGATGKDCPFCGKSFRSAHHLKVHLRVHTGERPYKCPHCDYAGTQSGSLKYHLQRHHREQRSGAGPGPPPEPPPPSQRGSAPQSGAKPSPQPATWVEGASSPRPPSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGGEAGPGGALHRCLFCPFATGAPELMALHLQVHHSRRARGRRPPQADASPPYARVPSGETPPSPSQEGEEGSGLSRPGEAGLGGQER | 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 SOX9 (By similarity). Plays a role in chondrocyte differentiation (By similarity).
Sequence Mass (Da): 76877
Sequence Length: 722
Domain: C2H2-type zinc-finger domains 5 and 6 are important for the interaction with SOX9.
Subcellular Location: Nucleus
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Q6IQX8 | MEGSRPRILVGHLEPSPPAFDGELDLQRYSNGPGVSGTPGPGSPGMGAVGWSETRAGERRFPCPVCGKRFRFNSILALHLRAHPGAQAFQCPHCGHRAAQRALLRSHLRTHQPERPRSPAARLLLELEERALLREARLGRARSSGGMQSSPAAEGLARPQVPSSSAFRCPFCKGKFRTSAERERHLHILHRPWKCSLCSFGSSQEEELLHHSLTAHGASERPLAATSTPEPPPPPQQEPRSALEPEPEPEPRPEPDREANPAPTPAPPEEPPAPPEFRCQVCGQSFTQSWFLKGHMRKHKASFDHACPVCGRCFKEPWFLKNHMKVHTSKLGPLRAPGPGSAPARAPQPPDLSLLAYEPLGPALLLAPAPAPAERREPPSLLGYLSVRAGEVRPNGEGADPGGGRSYGGFRPLPSALPNRARRHRTEEPEEEEEVVEAEEESWARGRSLGSLTSLHPNPGEGSGQPAPAAGTQARSTATQEENGLLVGGTRSEAGRGATGKDCPFCGKSFRSAHHLKVHLRVHTGERPYKCPHCDYAGTQSGSLKYHLQRHHREQRSSAGPGPPPEPPPPSQRGSLQPQSGAKPTQASATWVEGTASTRPPSSSTGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGGEAGAGGALHRCLFCPFATGAPELMALHLQVHHSRRARGRRQPRADTSPTYVRAPSGETPPSPPLEEEGSPGLSRSGEAGLGGQER | 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 expression, as part of a complex with SOX9 . Plays a role in chondrocyte differentiation .
Sequence Mass (Da): 77796
Sequence Length: 726
Domain: C2H2-type zinc-finger domains 5 and 6 are important for the interaction with SOX9.
Subcellular Location: Nucleus
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Q96IT1 | MPTALCPRVLAPKESEEPRKMRSPPGENPSPQGELPSPESSRRLFRRFRYQEAAGPREALQRLWDLCGGWLRPERHTKEQILELLVLEQFLAILPREIQSWVRAQEPESGEQAVAAVEALEREPGRPWQWLKHCEDPVVIDDGDSPLDQEQEQLPVEPHSDLAKNQDAQPITLAQCLGLPSRPPSQLSGDPVLQDAFLLQEENVRDTQQVTTLQLPPSRVSPFKDMILCFSEEDWSLLDPAQTGFYGEFIIGEDYGVSMPPNDLAAQPDLSQGEENEPRVPELQDLQGKEVPQVSYLDSPSLQPFQVEERRKREELQVPEFQACPQTVVPQNTYPAGGNPRSLENSLDEEVTIEIVLSSSGDEDSQHGPYCTEELGSPTEKQRSLPASHRSSTEAGGEVQTSKKSYVCPNCGKIFRWRVNFIRHLRSRREQEKPHECSVCGELFSDSEDLDGHLESHEAQKPYRCGACGKSFRLNSHLLSHRRIHLQPDRLQPVEKREQAASEDADKGPKEPLENGKAKLSFQCCECGKAFQRHDHLARHRSHFHLKDKARPFQCRYCVKSFTQNYDLLRHERLHMKRRSKQALNSY | 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
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Q9BS31 | MTKAQESLTLEDVAVDFTWEEWQFLSPAQKDLYRDVMLENYSNLVSVGYQAGKPDALTKLEQGEPLWTLEDEIHSPAHPEIEKADDHLQQPLQNQKILKRTGQRYEHGRTLKSYLGLTNQSRRYNRKEPAEFNGDGAFLHDNHEQMPTEIEFPESRKPISTKSQFLKHQQTHNIEKAHECTDCGKAFLKKSQLTEHKRIHTGKKPHVCSLCGKAFYKKYRLTEHERAHRGEKPHGCSLCGKAFYKRYRLTEHERAHKGEKPYGCSECGKAFPRKSELTEHQRIHTGIKPHQCSECGRAFSRKSLLVVHQRTHTGEKPHTCSECGKGFIQKGNLNIHQRTHTGEKPYGCIDCGKAFSQKSCLVAHQRYHTGKTPFVCPECGQPCSQKSGLIRHQKIHSGEKPYKCSDCGKAFLTKTMLIVHHRTHTGERPYGCDECEKAYFYMSCLVKHKRIHSREKRGDSVKVENPSTASHSLSPSEHVQGKSPVNMVTVAMVAGQCEFAHILHS | 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: Nucleus
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Q2HJ10 | MQTMDKQNLLESTRGARSFLGSLWKSEASRIPPVDLPAVELAVQSNHYCHAQKDSGSHPDPEKQRARRKLYVASAICLVFMIGEIIGGYLAQSLAIMTDAAHLLTDFASMLISLFALWVSSRPATKTMNFGWHRAEILGALLSVLSIWVVTGVLVYLAVQRLISGDYEIKGDTMLITSGCAVAVNLIMGLALHQSGHGHSHGNSRDDSSQQQNPSVRAAFIHVIGDLLQSVGVLVAAYIIYFKPEYKYVDPICTFLFSILVLGTTLTILRDVILVLMEGTPKGVDFTTVKNLLLSVDGVEALHSLHIWALTVAQPVLSVHIAIAQNADAQAVLKVARDRLQGKFNFHTMTIQIEKYSEDMKNCQACQGPLE | 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 concentration of milk, through the transport of zinc ions into secretory vesicles of mammary cells (Probable). By concentrating zinc ions into lysosomes participates to lysosomal-mediated cell death during early mammary gland involution (By similarity).
PTM: Phosphorylated at Ser-295. Phosphorylation at Ser-295 prevents localization to lysosomes. Dephosphorylation of Ser-295 which triggers localization to lysosomes, accumulation of zinc into lysosomes and lysosomal-mediated cell death is induced by TNF-alpha.
Location Topology: Multi-pass membrane protein
Catalytic Activity: 2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out)
Sequence Mass (Da): 40639
Sequence Length: 371
Subcellular Location: Cytoplasmic vesicle
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Q62941 | MASRSFFGALWKSEASRIPPVNLPSVELAVQSNHYCHAQKDSGSHPNSEKQRARRKLYVASAICLVFMIGEIIGGYLAQSLAIMTDAAHLLTDFASMLISLFSLWVSSRPATKTMNFGWQRAEILGALLSVLSIWVVTGVLVYLAVQRLISGDYEIKGDTMLITSGCAVAVNIIMGLALHQSGHGHSHGHSHEDSSQQQQNPSVRAAFIHVVGDLLQSVGVLVAAYIIYFKPEYKYVDPICTFLFSILVLGTTLTILRDVILVLMEGTPKGVDFTTVKNLLLSVDGVEALHSLHIWALTVAQPVLSVHIAIAQNVDAQAVLKVARDRLQGKFNFHTMTIQIESYSEDMKSCQECQGPSE | 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 concentration of milk, through the transport of zinc ions into secretory vesicles of mammary cells (By similarity). By concentrating zinc ions into lysosomes participates to lysosomal-mediated cell death during early mammary gland involution (By similarity).
PTM: Phosphorylated at Ser-283. Phosphorylation at Ser-283 prevents localization to lysosomes. Dephosphorylation of Ser-283 which triggers localization to lysosomes, accumulation of zinc into lysosomes and lysosomal-mediated cell death is induced by TNF-alpha.
Location Topology: Multi-pass membrane protein
Catalytic Activity: 2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out)
Sequence Mass (Da): 39277
Sequence Length: 359
Subcellular Location: Cytoplasmic vesicle
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Q08E25 | MEPSPTTGGSETTRLVGPRDRGGAGGGLRLKSLFTEAPEPLPEEPKPVEMSFHHCHRDPLPQPGLTPERMQAQRQLCTACAVCCVFMAGEVVGGYLAHSLAIMTDAAHLLADVGSMMGSLFSLWLSTRPATRTMTFGWHRSETLGALASVVSLWMVTGILLYLAFIRLLHSDYHIEGGAMLLTASIAVCANLLMAFVLHQAGPPHSHGSRGAEYAPLEEGSGEPLPLGNTSVRAAFVHVLGDLLQSLGVLIASILIYFKPQYKAADPISTFLFSICALGSTAPTLRDVLRVLMEGTPRSVSFEPVRDTLLSVPGVRAIHELHLWSLTFTHYVASAHLAIDSTADPEAVLAEATSRLHSRFGFSSCTLQVEQYQPEMAQCLRCQEPPQA | 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 (Da): 41820
Sequence Length: 388
Subcellular Location: Cytoplasmic vesicle
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Q99726 | MEPSPAAGGLETTRLVSPRDRGGAGGSLRLKSLFTEPSEPLPEESKPVEMPFHHCHRDPLPPPGLTPERLHARRQLYAACAVCFVFMAGEVVGGYLAHSLAIMTDAAHLLADVGSMMGSLFSLWLSTRPATRTMTFGWHRSETLGALASVVSLWMVTGILLYLAFVRLLHSDYHIEGGAMLLTASIAVCANLLMAFVLHQAGPPHSHGSRGAEYAPLEEGPEEPLPLGNTSVRAAFVHVLGDLLQSFGVLAASILIYFKPQYKAADPISTFLFSICALGSTAPTLRDVLRILMEGTPRNVGFEPVRDTLLSVPGVRATHELHLWALTLTYHVASAHLAIDSTADPEAVLAEASSRLYSRFGFSSCTLQVEQYQPEMAQCLRCQEPPQA | 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
Catalytic Activity: 2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out)
Sequence Mass (Da): 41945
Sequence Length: 388
Subcellular Location: Cytoplasmic vesicle
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P97441 | MEPSLATGGSETTRLVSARDRSSAGGGLRLKSLFTEPSEPLPEEPKLEGMAFHHCHKDPVPQSGLSPERVQARRQLYAACAVCFIFMAGEVVGGYLAHSLAIMTDAAHLLADIGSMLASLFSLWLSTRPATRTMTFGWHRSETLGALASVVSLWIVTGILLYLAFLRLLHSDYHIEAGAMLLTASIAVCANLLMAFVLHQTGAPHSHGSTGAEYAPLEEGHGYPMSLGNTSVRAAFVHVLGDLLQSFGVLAASILIYFKPQYKVADPISTFLFSICALGSTAPTLRDVLLVLMEGAPRSVEFEPVRDTLLSVPGVRATHDLHLWALTLTYHVASAHLAIDSTADPEAVLAEASSRLYSRFGFSSCTLQVEQYQPEMAQCLRCQEPSQA | 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 (Da): 41824
Sequence Length: 388
Subcellular Location: Cytoplasmic vesicle
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Q5R617 | MEPSPAAGGLETTRLVSPRDRGGAGGSLRLKSLFTEPSEPLPEESKPVEMPFHHCHRDPLPPPGLTPERLHARRQLYAACAVCFVFMAGEVVGGYLAHSLAIMTDAAHLLADVGSMMGSLFSLWLSTRPATRTMTFGWHRSETLGALASVVSLWMVTGILLYLAFVRLLHSDYHIEGGAMLLTASIAVCANLLMAFVLHQAGPPHSHGSKGAEYAPLEEGPEEPLPLGNTSVRAAFVHVLGDLLQSFGVLAASILIYFKPQYKAADPISTFLFSICALGSTAPTLRDVLRILMEGTPRNVGFEPVRDTLLSVPGVRATHELHLWALTLTYHVASAHLAIDSTADPEAVLAEASSRLYSRFGFSSCTLQVEQYQPEMAQCLRCQEPPQA | 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 (Da): 41917
Sequence Length: 388
Subcellular Location: Cytoplasmic vesicle
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O14863 | MAGSGAWKRLKSMLRKDDAPLFLNDTSAFDFSDEAGDEGLSRFNKLRVVVADDGSEAPERPVNGAHPTLQADDDSLLDQDLPLTNSQLSLKVDSCDNCSKQREILKQRKVKARLTIAAVLYLLFMIGELVGGYIANSLAIMTDALHMLTDLSAIILTLLALWLSSKSPTKRFTFGFHRLEVLSAMISVLLVYILMGFLLYEAVQRTIHMNYEINGDIMLITAAVGVAVNVIMGFLLNQSGHRHSHSHSLPSNSPTRGSGCERNHGQDSLAVRAAFVHALGDLVQSVGVLIAAYIIRFKPEYKIADPICTYVFSLLVAFTTFRIIWDTVVIILEGVPSHLNVDYIKEALMKIEDVYSVEDLNIWSLTSGKSTAIVHIQLIPGSSSKWEEVQSKANHLLLNTFGMYRCTIQLQSYRQEVDRTCANCQSSSP | 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
Catalytic Activity: 2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out)
Sequence Mass (Da): 47483
Sequence Length: 429
Subcellular Location: Endosome membrane
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O55174 | MAGPGAWKRLKSLLRKDDAPLFLNDTSAFDFLDEVSDEGLSRFNKLRVVVADDDSEAPERPVNGAHPALQADDDSLLDQELPLTNSQLSLKMDPCDNCSKRRELLKQRKVKTRLTIAAVLYLLFMIGELVGGYMANSLAIMTDALHMLTDLSAIILTLLALWLSSKSPTRRFTFGFHRLEVLSAMISVMLVYVLMGFLLYEAMQRTIHMNYEINGDVMLITAAVGVAVNVIMGFLLNQSGHHHSHAHSHSLPSNSPSMVSSGHSHGQDSLAVRAAFVHALGDLVQSVGVLIAAYIIRFKPEYKIADPICTYIFSLLVAFTTLRIIWDTVVIILEGVPSHLNVDYIKESLMKIEDVYSVEDLNIWSLTSGKATAIVHMQLIPGSSSKWEEVQSKAKHLLLNTFGMYKCTVQLQSYRQEATRTCANCQSSST | 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
Sequence Mass (Da): 47702
Sequence Length: 430
Subcellular Location: Endosome membrane
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Q8TAD4 | MEEKYGGDVLAGPGGGGGLGPVDVPSARLTKYIVLLCFTKFLKAVGLFESYDLLKAVHIVQFIFILKLGTAFFMVLFQKPFSSGKTITKHQWIKIFKHAVAGCIISLLWFFGLTLCGPLRTLLLFEHSDIVVISLLSVLFTSSGGGPAKTRGAAFFIIAVICLLLFDNDDLMAKMAEHPEGHHDSALTHMLYTAIAFLGVADHKGGVLLLVLALCCKVGFHTASRKLSVDVGGAKRLQALSHLVSVLLLCPWVIVLSVTTESKVESWFSLIMPFATVIFFVMILDFYVDSICSVKMEVSKCARYGSFPIFISALLFGNFWTHPITDQLRAMNKAAHQESTEHVLSGGVVVSAIFFILSANILSSPSKRGQKGTLIGYSPEGTPLYNFMGDAFQHSSQSIPRFIKESLKQILEESDSRQIFYFLCLNLLFTFVELFYGVLTNSLGLISDGFHMLFDCSALVMGLFAALMSRWKATRIFSYGYGRIEILSGFINGLFLIVIAFFVFMESVARLIDPPELDTHMLTPVSVGGLIVNLIGICAFSHAHSHAHGASQGSCHSSDHSHSHHMHGHSDHGHGHSHGSAGGGMNANMRGVFLHVLADTLGSIGVIVSTVLIEQFGWFIADPLCSLFIAILIFLSVVPLIKDACQVLLLRLPPEYEKELHIALEKIQKIEGLISYRDPHFWRHSASIVAGTIHIQVTSDVLEQRIVQQVTGILKDAGVNNLTIQVEKEAYFQHMSGLSTGFHDVLAMTKQMESMKYCKDGTYIM | 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 enzymes involved in phosphatidylinositol glycan anchor biosynthesis . Through the transport of zinc into secretory granules of pancreatic beta-cells, plays an important role in the storage and secretion of insulin .
PTM: Could homodimerize through the formation of dityrosine bonds upon oxidative stress.
Location Topology: Multi-pass membrane protein
Catalytic Activity: 2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out)
Sequence Mass (Da): 84047
Sequence Length: 765
Subcellular Location: Golgi apparatus
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Q8R4H9 | MEEKYGGDARPGPGGGLGPVDVPSARLTRYILLLCLTKCLKAVGLFESYDLLKAVHIVQFIFILKLGTAFFMVLFQKPFSSGKPITKHQWIKIFKHAVAGCIISLLWFFGLTLCGPLRTLLLFEHSDIVVISLLSVLFTSSGGGPAKTRGAAFFIIAVICLLLFDNDDLMAKMAEHPEGHHDSALTHMLYTAIAFLGVADHKGGVLLLVLALCCKVGFHTASRKLSIDVGGAKRLQALSQLVSVFLLCPWVIVLSVTTESKVESWFSLIMPFTTVIFFVMILDFYMDSVCSVKMDVSKCARYGSFPIFISALLFGNFWTHPITDQLRAMNRAAHQESTEHVLSGGVVVSAVFFILSANILSSPSKRGQKGTLIGYSPEGTPLYHFMGDAFQHSSQSVPRFIKDSLKQVLEESDSRQIFYFLCLNLLFTFVELFYGVLTNSLGLISDGFHMLFDCSALVMGLFAALMSRWKATRIFSYGYGRIEILSGFINGLFLIVIAFFVFMESVARLIDPPELDTNMLTPVSVGGLIVNLIGICAFSHAHSHGHGASQGNCHSDHGHSHHAHGHGHDHGHSHGFTGGGMNANMRGVFLHVLADTLGSIGVIVSTVLIEQFGWFIADPLCSLFIAVLIFLSVIPLIKDACQVLLLRLPPDHEKELHIALEKIQKIEGLISYRDPHFWRHSASIVAGTIHIQVTSEVLEQRIVQQVTGILKDAGVNNLTIQVEKEAYFQHMSGLSTGFHDVLAMTKQMESLKYCKDGTYIM | 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 enzymes involved in phosphatidylinositol glycan anchor biosynthesis. Through the transport of zinc into secretory granules of pancreatic beta-cells, plays an important role in the storage and secretion of insulin.
PTM: Could homodimerize through the formation of dityrosine bonds upon oxidative stress.
Location Topology: Multi-pass membrane protein
Catalytic Activity: 2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out)
Sequence Mass (Da): 83773
Sequence Length: 761
Subcellular Location: Golgi apparatus
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Q6GPY1 | MGTIYLFRKTQRSLLGKLTQEFRLVTADRRSWKILLFGAINVVCTGFLLTWCSSTNSMALTAYTYLTIFDLFSLITSLISYWVMMKKPSPTYSFGFERLEVLAVFASTVLAQLGALFILKESAERFLEQPEIHTGRLLVGTFVALFFNLFTMLSIRNKPFAYVSEAASTSWLQEHVADLSRSLCGVIPGLSSIFLPRMNPFVLIDIAGALALCITYMLIEINNYFAVDTASAIAIAVMTFGTMYPMSVYSGKVLLQTTPPHVIGQLDKLLREVSTLDGVLEVRNEHFWTLGFGTMAGSVHVRIRRDANEQMVLAHVTNRLSTLVSTPTVQIFKDDWARPVLASGTMPPNMLNIPEHHVIQMPSLKSTVDELNPMTSTPSKPSGPPPEFAFNTPGKNMNPVILSNNQTRPFGVGYGTTPYTTTFNQGLGVPGVGNTQGLRTGLTNVANRYGTYTPGQFTQFRQ | 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 secretory pathway and regulates the activation and folding of enzymes like alkaline phosphatases and enzymes involved in phosphatidylinositol glycan anchor biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51166
Sequence Length: 462
Subcellular Location: Golgi apparatus
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Q5ZIH3 | MGTIHLFRKSQRSLVGKLTHEFRLVAADRRSWKILLFGAINLICIGFLLMWCSSTNSIALTAYTYLTIFDLFSLITCLISYWVMVKKPSPVYSFGFERFEVLAVFASTVLAQLGALFILKESAERFLEQPEIHTGRLLVGTFVALFFNLFTMLSVRNKPFAYVSEAASTSWLQEHVADLSRSICGIIPGLSSIFLPRMNPFVLIDIAGALALCITYMLIEINNYYAVDTASAIAIALMTFGTMYPMSVYSGKVLLQTTPPHVFGQLDKLLREVSTLDGVLEVRNEHFWTLGFGTLAGSVHVRIRRDANEQMVLAHVTNRLYTLVSTLTVQIFKDDWIRPTLSSVPIANNMLNLSDHHVITMPSLKAADNLNPVTSTPAKPSSPPPEFSFNTPGKNVNPVILLNTQTRPYGLGLNHGSTPYSSVLNQGFGIPGMGATQGFRTGFTNVPSRYGTNTRGQSRP | 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 the early secretory pathway and regulates the activation and folding of enzymes like alkaline phosphatases and enzymes involved in phosphatidylinositol glycan anchor biosynthesis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50936
Sequence Length: 460
Subcellular Location: Golgi apparatus
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Q9ZSK5 | MALNDKSIPHETKVVVLLIPFPAQGHLNQFLHLSRLIVAQNIPVHYVGTVTHIRQATLRYNNPTSNIHFHAFQVPPFVSPPPNPEDDFPSHLIPSFEASAHLREPVGKLLQSLSSQAKRVVVINDSLMASVAQDAANISNVENYTFHSFSAFNTSGDFWEEMGKPPVGDFHFPEFPSLEGCIAAQFKGFRTAQYEFRKFNNGDIYNTSRVIEGPYVELLELFNGGKKVWALGPFNPLAVEKKDSIGFRHPCMEWLDKQEPSSVIYISFGTTTALRDEQIQQIATGLEQSKQKFIWVLREADKGDIFAGSEAKRYELPKGFEERVEGMGLVVRDWAPQLEILSHSSTGGFMSHCGWNSCLESITMGVPIATWPMHSDQPRNAVLVTEVLKVGLVVKDWAQRNSLVSASVVENGVRRLMETKEGDEMRQRAVRLKNAIHRSMDEGGVSHMEMGSFIAHISK | 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 (Da): 51412
Sequence Length: 459
EC: 2.4.1.203
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F2QXM5 | MKFAISTLLIILQAAAVFAAFPISDITVVSERTDASTAYLSDWFVVSFVFSTAGSDETIAGDATIEVSIPNELEFVQYPDSVDPSVSEFFTTAGVQVLSTAFDYDSHVLTFTFSDPGQVITDLEGVVFFTLKLSEQFTESASPGQHTFDFETSDQTYSPSVDLVALDRSQPIKLSNAVTGGVEWFVDIPGAFGDITNIDISTVQTPGTFDCSEVKYAVGSSLNEFGDFTPQDRTTFFSNSSSGEWIPITPASGLPVESFECGDGTISLSFAGELADDEVLRVSFLSNLADDVLEVQNVVNVDLTTADSRKRALTSFVLDEPFYRASRTDTAAFEAFAAVPADGDITSTSTAITSVTATVTHTTVTSVCYVCAETPVTVTYTAPVITNPIYYTTKVHVCNVCAETPITYTVTIPCETDEYAPAKPTGTEGEKIVTVITKEGGDKYTKTYEEVTYTKTYPKGGHEDHIVTVKTKEGGEKVTKTYEEVTYTKGPEIVTVVTKEGGEKVTTTYHDVPEVVTVITKEGGEKVTTTYPATYPATYTEGHSAGVPTSASTPPQATYTVSEAQVNLGSKSAVGLLAIVPMLFLAI | 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 phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
Location Topology: Lipid-anchor
Sequence Mass (Da): 62905
Sequence Length: 587
Subcellular Location: Cell membrane
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A7ZI10 | MSWLNSVLLALTSVQPYMVPATVIGLVSFAFLCFIFFYFFRAVKIINGLKKYTQSINGIENNEPGNQLQHLQSLFVQPELKHAWNEFEESLHSQYELEDGEEKIVRIRATAPSASFFSEQQLVDIPLNTEFFKHLPGILTGVGIIGTFYGLMIGLNHFDPSTPEQVSSSVNNLLRDVLYAFLGSAFAITFSILITWLEKFCLAKCYKYLEKFTAALDALYDSGVGEEYLASLVKSSNESATQARHLKESLVTDLRDMLLHLANSQKVENERLATTLSTTYRETGQQFAEQVSGAIENSLKSPLDKIAGAVQTASGDQSGMVQNMLQDVLTAFMAKLDTTFGQQFTNLNEMMGQTVGAIQTMQTGFGALLQDMRQVSDDSRQGSAQLIEQLLSEMKSGQQAMQAGMNDMLTSLQTSVAKIGAEGEGAGERMARQLEKMFADSEAREKAQAEHMTAFIEAIQNSVQQGQSATMEKMAASVESLGEQLGSLFGQIDKGQQQISANQQANQQSLHEQTQRVMSEVDDQIKQLVETVASQHQGTTETLRLLAEQTNRQIQDMHTGADKMRLAAERFEHAGDRVSEANHLTADVLNKAQSAGSSLSLATSELTSVVADYRNNREAVSKSIAMLELLAANTQSEQTTRTQFIADLKQHGERLQSYNREAQAFMENVSDVLGKGFEDFSEGVSRSLDKTLGKLDVEMAKASTLLAGSVEQIGESVSELDDVLSRVRA | 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 abortive infection, a minority produce viable phage progeny. These eventually accumulate to a high multiplicity of infection, leading to culture collapse by 2 hours after initial infection . ZorA and ZorB probably assemble in the cell inner membrane and exert their effect there (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80261
Sequence Length: 729
Subcellular Location: Cell inner membrane
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P0DW01 | MLAQLFEQLFQSIDSTLITNIFIWAVIFVFLSAWWCDKKNIHSKFREYAPTLMGALGILGTFIGIIIGLLNFNTESIDTSIPVLLGGLKTAFITSIVGMFFAILFNGMDAFFFANKRSALAENNPESVTPEHIYHELKEQNQTLTKLVSGINGDSEGSLIAQIKLLRTEISDSSQAQLANHTHFSNKLWEQLEQFADLMAKGATEQIIDALRQVIIDFNENLTEQFGENFKALDASVKKLVEWQGNYKTQIEQMSEQYQQSVESLVETKTAVAGIWEECKEIPLAMSELREVLQVNQHQISELSRHLETFVAIRDKATTVLPEIQNKMAEVGELLKSGAANVSASLEQTSQQILLNADSMRVALDEGTEGFRQSVTQTQQAFASMAHDVSNSSETLTSTLGETITEMKQSGEEFLKSLESHSKELHRNMEQNTTNVIDMFSKTGEKINHQLSSNADNMFDSIQTSFDKAGAGLTSQVRESIEKFALSINEQLHAFEQATEREMNREMQSLGNALLSISKGFVGNYEKLIKDYQIVMGQLQALISANKHRG | 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 eventually accumulate to a high multiplicity of infection, leading to culture collapse by 170 minutes after initial infection . ZorA and ZorB probably assemble in the cell inner membrane and exert their effect there (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61483
Sequence Length: 550
Subcellular Location: Cell inner membrane
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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 abortive infection, a minority produce viable phage progeny. These eventually accumulate to a high multiplicity of infection, leading to culture collapse by 2 hours after initial infection . ZorA and ZorB probably assemble in the cell inner membrane and exert their effect there (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 28126
Sequence Length: 246
Subcellular Location: Cell inner membrane
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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 eventually accumulate to a high multiplicity of infection, leading to culture collapse by 170 minutes after initial infection . ZorA and ZorB probably assemble in the cell inner membrane and exert their effect there (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27330
Sequence Length: 235
Subcellular Location: Cell inner membrane
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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 the mRNA is degraded. Base pairing occurs between 18 bases in the 5' UTR of zorO mRNA and the 5' end of OrzO sRNA. sRNA OrzP, which differs only in 4 of these 18 bases, does not repress ZorO toxicity . Integration of the protein into the inner membrane damages membrane integrity and affects membrane potential. It leads to increased levels of hydroxyl radicals .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3263
Sequence Length: 29
Subcellular Location: Cell inner membrane
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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-pass membrane protein
Sequence Mass (Da): 3249
Sequence Length: 29
Subcellular Location: Membrane
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O31688 | MNEQVIVQRDPHEPLKTDKREKNWAQHAELIAALVSGALILAGWLLSGYQVLSIILFLLAFVIGGFAKAKEGIEETLESKTLNVELLMIFAAIGSALIGYWAEGAILIFIFSLSGALETYTMNKSSRDLTSLMQLEPEEATLMVNGETKRVPVSDLQAGDMIVIKPGERVAADGIIESGSTSLDESALTGESMPVEKNTGDTVFTGTVNRNGSLTVRVTKANEDSLFRKIIKLVESAQNSVSPAQAFIERFENAYVKGVLIAVALLLFVPHFALGWSWSETFYRAMVFMVVASPCALVASIMPAALSLISNGARNGMLVKGSVFLEQLGSVQMIAFDKTGTVTKGQPAVETIRIAEGFSEAEVLEAVYAIETQSSHPLAQAITAYAESRGVNQSGYISIEETSGFGVMAEVSGAKWKVGKAGFIGEEMAAQFMKQTASDVIQSGHTIVFVKKDDQIAGCIALKDQIRPEAKEVMEELNRLGIKTAMLTGDHEDTAQAIAKEAGMTTVVAECLPDQKVNEIKRLKEEFGTIAMVGDGINDAPALKAADVGIAMGGGTDVALETADMVLMKNDLKKLVNMCRLSRKMNRIIKQNIVFSLAVICLLICANFLQAMELPFGVIGHEGSTILVILNGLRLLK | 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(in) + H(+)(in) + phosphate(in) + Zn(2+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68566
Sequence Length: 637
Subcellular Location: Cell membrane
EC: 7.2.2.20
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P60852 | MAGGSATTWGYPVALLLLVATLGLGRWLQPDPGLPGLRHSYDCGIKGMQLLVFPRPGQTLRFKVVDEFGNRFDVNNCSICYHWVTSRPQEPAVFSADYRGCHVLEKDGRFHLRVFMEAVLPNGRVDVAQDATLICPKPDPSRTLDSQLAPPAMFSVSTPQTLSFLPTSGHTSQGSGHAFPSPLDPGHSSVHPTPALPSPGPGPTLATLAQPHWGTLEHWDVNKRDYIGTHLSQEQCQVASGHLPCIVRRTSKEACQQAGCCYDNTREVPCYYGNTATVQCFRDGYFVLVVSQEMALTHRITLANIHLAYAPTSCSPTQHTEAFVVFYFPLTHCGTTMQVAGDQLIYENWLVSGIHIQKGPQGSITRDSTFQLHVRCVFNASDFLPIQASIFPPPSPAPMTQPGPLRLELRIAKDETFSSYYGEDDYPIVRLLREPVHVEVRLLQRTDPNLVLLLHQCWGAPSANPFQQPQWPILSDGCPFKGDSYRTQMVALDGATPFQSHYQRFTVATFALLDSGSQRALRGLVYLFCSTSACHTSGLETCSTACSTGTTRQRRSSGHRNDTARPQDIVSSPGPVGFEDSYGQEPTLGPTDSNGNSSLRPLLWAVLLLPAVALVLGFGVFVGLSQTWAQKLWESNRQ | 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 zona pellucida.
PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 70049
Sequence Length: 638
Domain: The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.
Subcellular Location: Zona pellucida
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Q62005 | MAWGCFVVLLLLAAAPLRLGQRLHLEPGFEYSYDCGVRGMQLLVFPRPNQTVQFKVLDEFGNRFEVNNCSICYHWVTSEAQEHTVFSADYKGCHVLEKDGRFHLRVFIQAVLPNGRVDIAQDVTLICPKPDHTVTPDPYLAPPTTPEPFTPHAFALHPIPDHTLAGSGHTGLTTLYPEQSFIHPTPAPPSLGPGPAGSTVPHSQWGTLEPWELTELDSVGTHLPQERCQVASGHIPCMVNGSSKETCQQAGCCYDSTKEEPCYYGNTVTLQCFKSGYFTLVMSQETALTHGVLLDNVHLAYAPNGCPPTQKTSAFVVFHVPLTLCGTAIQVVGEQLIYENQLVSDIDVQKGPQGSITRDSAFRLHVRCIFNASDFLPIQASIFSPQPPAPVTQSGPLRLELRIATDKTFSSYYQGSDYPLVRLLREPVYVEVRLLQRTDPSLVLVLHQCWATPTTSPFEQPQWPILSDGCPFKGDNYRTQVVAADREALPFWSHYQRFTITTFMLLDSSSQNALRGQVYFFCSASACHPLGSDTCSTTCDSGIARRRRSSGHHNITLRALDIVSSPGAVGFEDAAKLEPSGSSRNSSSRMLLLLLAITLALAAGIFVGLIWAWAQKLWEGIRY | 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 zona pellucida.
PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 68723
Sequence Length: 623
Domain: The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.
Subcellular Location: Zona pellucida
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Q9U3F4 | MGPPPPPPPPPLLPSGEILPSRKWKTEDAPRRNNHPAPAPPKPSRPTVDASALQHAAARLRKTGYNEPVRGDVENLSDGRLDRPHQQLPDGDRTYRANLQQLAQPKTRAEIPSPPTYSNQPRPLGDFHRDPNALSQFQQSREALLSSTSPTSNYSPINKFSSSTLTQYANKSPSPPSFGNSNSEATYVSPYSSKHSYPTNFRSYHKDDDYFNNTATTATTTTSSNSLNENNNSNKYGNKETVLQWSEPYDPSKIRRSQSPIRNAREMIHEYSTTNYVTEVQQPPPPPPDLYQRMTQARTFLQNSLAKQLRDEGLTESQKAANRNQTGALSASSSIPFDASQIVKNSYNGDEVDHLVHQMRTKLNQPADTSPSIVQYPRRQAPDSSRANYSATTSTSFSSSTTRKIMNINICVGCGKEITGDQPGCNAMNQIFHVDCFKCGQCSKTLAGASFYNIDDKPTCEGCYQNSLEKCTACNRAISDKLLRACGGVYHVNCFVCFSCKKSLDGIPFTLDKDNNVHCVPCFHDKFAPRCALCSKPIVPQDGEKESVRVVAMDKSFHVDCYKCEDCGMQLSSKLEGQGCYPIDNHLLCKTCNGNRLRVVSST | 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 .
Sequence Mass (Da): 66774
Sequence Length: 603
Domain: The LIM domains are sufficient for the role in PLM synaptogenesis.
Subcellular Location: Nucleus
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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
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Q196W5 | MSVDSFTSRLAVVMTAVVLVWWAQALPVPSPRRGESDCDAACRKFLLQYGYLDLGEENCTEVDSNRKLCSVDDELVGVPRPLARVDLAAGVSHLQTMAGLEPTGRIDASTARLFTSPRCGVPDVSKYIVAAGRRRRTRRESVIVCTTRWTTTKSNSNETLVKWWLDQSSMQWLNSTLNWVSLTNVLHHSFWKWSKESMLAFQQVSLERDAQIVVRFENGSHGDGWDFDGPGNVLAHAFQPGQSLGGDIHLDAAEPWTIYDIDGHDGNSILHVVLHEIGHALGLEHSRDPTSIMYAWYTPFKYDLGPEDVSAVAGLYGAKPASSVAAWNPKIQKFYWDRHVRNDLLPLLERDLDAEEEDSDEVR | 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-peptide release activates the enzyme.
Subcellular Location: Secreted
EC: 3.4.24.-
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Q6GZN0 | MGIKGLKPLLRSYGVHEYTVPLSQMSGKTIAVDGTFLLHKYKNCHSVPWHYLTLYTLSNLRLRNVKVLFIFDGMSPPEKSREKSNRRCRKQALMEKGTLVKAQLEVWKKDGGEQAPELAAVSERLVKTRGLDPSLTDPETVQVLTDYVDNMSRDTRVTSDDYELMRRSLDAFGFPYADAPDEAELCCVRVVQMGIADAPMTIDSDALACGALHGVDVVYTDLHGETLTAMSTSKSKEALGLNGEQFMDLCVMCGTDFNQRVHKLGPVTALKLIKAHGSIENIPSAAPSMSCLEAVRTREILSGGDMESRRKDYEAMVQKPVSAELIRSVFPPEFLDKLLHENWQLRDAMKRMAPEAFEKCKRK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Probable endonuclease.
Sequence Mass (Da): 40621
Sequence Length: 363
Subcellular Location: Host nucleus
EC: 3.1.-.-
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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. Negatively regulates the kinase activity of PDPK1.
PTM: Ser-232 is probably phosphorylated by CK1.
Sequence Mass (Da): 27764
Sequence Length: 245
Subcellular Location: Cytoplasm
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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 . Promotes cytosolic retention and inactivation of TFEB transcription factor by binding to phosphorylated TFEB . Induces ARHGEF7 activity on RAC1 as well as lamellipodia and membrane ruffle formation . In neurons, regulates spine maturation through the modulation of ARHGEF7 activity (By similarity).
PTM: The delta, brain-specific form differs from the zeta form in being phosphorylated (Probable). Phosphorylation on Ser-184 by MAPK8; promotes dissociation of BAX and translocation of BAX to mitochondria . Phosphorylation on Thr-232; inhibits binding of RAF1 . Phosphorylated on Ser-58 by PKA and protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion . Phosphorylation on Ser-58 by PKA; disrupts homodimerization and heterodimerization with YHAE and TP53 .
Sequence Mass (Da): 27745
Sequence Length: 245
Subcellular Location: Cytoplasm
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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. Promotes cytosolic retention and inactivation of TFEB transcription factor by binding to phosphorylated TFEB. Induces ARHGEF7 activity on RAC1 as well as lamellipodia and membrane ruffle formation (By similarity). In neurons, regulates spine maturation through the modulation of ARHGEF7 activity (By similarity).
PTM: The delta, brain-specific form differs from the zeta form in being phosphorylated (Probable). Phosphorylation on Ser-184 by MAPK8; promotes dissociation of BAX and translocation of BAX to mitochondria (By similarity). Phosphorylation on Thr-232; inhibits binding of RAF1 (By similarity). Phosphorylated on Ser-58 by PKA and protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion . Phosphorylation on Ser-58 by PKA; disrupts homodimerization and heterodimerization with YHAE and TP53 (By similarity).
Sequence Mass (Da): 27771
Sequence Length: 245
Subcellular Location: Cytoplasm
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Q91FG3 | MTSIINQRWPLGNLMDGFPNGEKQNKLSFGGVPEKGYFEEFNKDPKYISFSGTPEKAYFEEFNRYRNIDEDDNRDTFPLFNEISSNPESESYLQTFVDNVRINTDINFVSKTNSFSQNDLSYLNATYVDKSLSLELPIKFNWAKTTSADSPDVVAKKKLISKPDNQYLCGSCWAVSVAGVVGDVFAVAGLVNWVPNISATYALIHYPQGRCKGGDPATLLYNIANNGIPSKHCVDYSWCSQNRTCTTADSAAHFGSDLSPLIPKDRGCYFDSEHYIFKIDSNIRTIVAGSGAIDVSNVQRTIKEYIYTTGPAVGGYIIFRNFTSKVPFGPHKGNSTFNVINGGVYLEKANYAQYRGEYGEHITEGLTFSSSNTDSDNYAGGHAISIMGWGIQPRIRVGNGPNDIADVPYWYCRNSWGTKWGMNGGYFKIAMYPYNRKSQFSKIVELMTPQGQHIRLGGVLAFTVSNPPVLKKLPANKQPPNPNSLSKLLDYYKNDEDDIVTKLPNIVPPSDGKKSTTSKTNNWYIYALIIIFILIIFFVLRK | Function: Probable cysteine protease.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60620
Sequence Length: 542
Subcellular Location: Membrane
EC: 3.4.-.-
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D7UER1 | MAMETGLIFHPYMRPGRSARQTFDWGIKSAVQADSVGIDSMMISEHASQIWENIPNPELLIAAAALQTKNIKFAPMAHLLPHQHPAKLATMIGWLSQILEGRYFLGIGAGAYPQASYMHGIRNAGQSNTATGGEETKNLNDMVRESLFIMEKIWKREPFFHEGKYWDAGYPEELEGEEGDEQHKLADFSPWGGKAPEIAVTGFSYNSPSMRLAGERNFKPVSIFSGLDALKRHWEVYSEAAIEAGHTPDRSRHAVSHTVFCADTDKEAKRLVMEGPIGYCFERYLIPIWRRFGMMDGYAKDAGIDPVDADLEFLVDNVFLVGSPDTVTEKINALFEATGGWGTLQVEAHDYYDDPAPWFQSLELISKEVAPKILLPKR | 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-campholide with (S,S) configuration, that presumably undergoes spontaneous hydrolysis to form 2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetate . Is also able to convert (-)-camphor to the corresponding lactone in vitro . Shows no conversion of (+)-camphor, (+)-fenchone, (-)-fenchone, and (+)-nopinone. Acts on other bicyclic ketones but very poorly on a few 2- and 4-substituted monocyclic ketones .
Catalytic Activity: (1S,4S)-bornane-2,5-dione + FMNH2 + O2 = (1S,4S)-5-oxo-1,2-campholide + FMN + H(+) + H2O
Sequence Mass (Da): 42314
Sequence Length: 378
EC: 1.14.14.155
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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-cholan-24-oate (3-oxo-LCA), respectively. Is also able to catalyze the oxidation of cholate (CA) and chenodeoxycholate (CDCA) into 3-dehydrocholate (3-oxo-CA) and 7-alpha-hydroxy-3-oxo-5-beta-cholan-24-oate (3-oxo-CDCA), respectively. Can also catalyze the reverse reactions in vitro. Accepts both NADPH and NADH as cosubstrates. The conversion of the abundant bile acid DCA into isoDCA by the gut bacterium R.gnavus favors the growth of the keystone commensal genus Bacteroides, since isoDCA is less cytotoxic than its parent compound, DCA; iso-bile acids have thus a potential role in modulating gut community composition.
Catalytic Activity: lithocholate + NADP(+) = 3-oxo-5beta-cholan-24-oate + H(+) + NADPH
Sequence Mass (Da): 26568
Sequence Length: 250
EC: 1.1.1.-
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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-cholan-24-oate (3-oxo-LCA), respectively. Is also able to catalyze the oxidation of cholate (CA) and chenodeoxycholate (CDCA) into 3-dehydrocholate (3-oxo-CA) and 7-alpha-hydroxy-3-oxo-5-beta-cholan-24-oate (3-oxo-CDCA), respectively. Can also catalyze the reverse reactions in vitro. Prefers NADH to NADPH as cosubstrate. The conversion of the abundant bile acid DCA into isoDCA by the gut bacterium E.lenta favors the growth of the keystone commensal genus Bacteroides, since isoDCA is less cytotoxic than its parent compound, DCA; iso-bile acids have thus a potential role in modulating gut community composition.
Catalytic Activity: lithocholate + NAD(+) = 3-oxo-5beta-cholan-24-oate + H(+) + NADH
Sequence Mass (Da): 27383
Sequence Length: 259
EC: 1.1.1.-
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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: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
Subcellular Location: Cytoplasm
EC: 1.13.11.6
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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): 21245
Sequence Length: 185
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
EC: 1.13.11.6
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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: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
Subcellular Location: Cytoplasm
EC: 1.13.11.6
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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: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
Subcellular Location: Cytoplasm
EC: 1.13.11.6
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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
Subcellular Location: Secreted
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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 with 19-fold lower efficiency. Displays no proline racemase activity.
Catalytic Activity: trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline
Sequence Mass (Da): 33029
Sequence Length: 308
EC: 5.1.1.8
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A1BBM5 | MTQYIFPCIDGHTCGNPVRLVAGGAPRLEGATMLEKRAHFLREFDWIRTGLMFEPRGHDMMSGAILYPPTRGDCDVAVLYIETSGCLPMCGHGTIGTITMGIENGLIVPRTPGRLSIETPAGKVDIEYRQEGRHVEEVRLTNVPGFLYAEGLTAEVEGLGEIVVDVAYGGNFYAIVEPQKNFRDMADHTAGELIGWSLTLRAALNQKYEFTHPEHPQINGLSHIQWTGAPTVPGAHARNAVFYGDKAIDRSPCGTGTSARMAQLAARGRLGVGDEFWHESIIGSIFKGRIEAAATVAGRDAIIPSIAGWARQTGLNTIFIDAERDPFAHGFVVK | 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 alternative catabolic pathway that degrades trans-4-hydroxy-L-proline betaine (tHyp-B) to alpha-ketoglutarate; this pathway would permit the utilization of tHyp-B as a sole carbon and nitrogen source .
Catalytic Activity: trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline
Sequence Mass (Da): 36301
Sequence Length: 334
EC: 5.1.1.8
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D5SQS4 | MTYIPRQWIQVVDSHTGGEPTRLIYDGQHWPFAGSREGALTSQESPSPSVLSGLRKAIDRSSLILPKTMSERRQFLETEADWLRTASLLEPRGSDVLVGAILTPPEHASSQAGVVFCNNTGYLGMCGHGMIGVIVSLGQMGLIAPGPVTIDTPVGSIAATWSGSASVTLTNVWSYRYRHAVSLSVPGLGVVTGDIAWGGNWFFLIGEEVHQKSLDLGNLSDLLAYTSQIRSELGRQGIAGAQGAEIDHVELFASCDSSIADSQNFVLCPGGAYDRSPCGTGTSAKLACLVADGKVAEGGLWRQKSIVGSCFQAKALSIREGERGLEVLPQLTGEAYVTGVSTLQIDEADPFRWGILPPQ | 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
Sequence Mass (Da): 38173
Sequence Length: 359
EC: 5.1.1.8
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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 role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways. Cannot use L-proline, trans-3-hydroxy-L-proline (t3LHyp) and pyrrolidone-5-carboxylate (P5C) as substrate.
Catalytic Activity: trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline
Sequence Mass (Da): 33528
Sequence Length: 314
EC: 5.1.1.8
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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-proline = cis-4-hydroxy-D-proline
Sequence Mass (Da): 32363
Sequence Length: 310
EC: 5.1.1.8
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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
Sequence Mass (Da): 33285
Sequence Length: 313
EC: 5.1.1.8
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D2AV87 | MRTKRVFHAVDSHTEGMPTRVITGGVGVIPGSTMAERREHFLAEMDHVRTLLMYEPRGHSAMSGAILQPPTRPDADYGVLYIEVSGCLPMCGHGTIGVATVLVETGMVEVVEPVTTIRLDTPAGLVVAEVRVEDGAATAVTITNVPSFSAGLDRTVKVPGIGEVTYDLAYGGNFYAILPIESVGLPFDRAHKQQILDAGLAIMDAINEQDEPVHPLDAGIRGCHHVQFTAPGSDARHSRHAMAIHPGWFDRSPCGTGTSARMAQLHARGELPLDTDFVNESFIGTRFVGRLVEETEVTDLPAVVPTITGRAWVTGTAQYFLDPRDPFPEGFLL | 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
Sequence Mass (Da): 35886
Sequence Length: 333
EC: 5.1.1.8
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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 with 500-fold lower efficiency. Displays no proline racemase activity.
Catalytic Activity: trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline
Sequence Mass (Da): 32711
Sequence Length: 312
EC: 5.1.1.8
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Q8GWW6 | MHHHHHPCNRKPFTTIFSFFLLYLNLHNQQIIEARNPSQFTTNPSPDVSIPEIKRHLQQYGYLPQNKESDDVSFEQALVRYQKNLGLPITGKPDSDTLSQILLPRCGFPDDVEPKTAPFHTGKKYVYFPGRPRWTRDVPLKLTYAFSQENLTPYLAPTDIRRVFRRAFGKWASVIPVSFIETEDYVIADIKIGFFNGDHGDGEPFDGVLGVLAHTFSPENGRLHLDKAETWAVDFDEEKSSVAVDLESVAVHEIGHVLGLGHSSVKDAAMYPTLKPRSKKVNLNMDDVVGVQSLYGTNPNFTLNSLLASETSTNLADGSRIRSQGMIYSTLSTVIALCFLNW | 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(2) (QF24) and beta-casein .
Location Topology: Lipid-anchor
Sequence Mass (Da): 38506
Sequence Length: 342
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-peptide release activates the enzyme.
Subcellular Location: Cell membrane
EC: 3.4.24.-
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P28222 | MEEPGAQCAPPPPAGSETWVPQANLSSAPSQNCSAKDYIYQDSISLPWKVLLVMLLALITLATTLSNAFVIATVYRTRKLHTPANYLIASLAVTDLLVSILVMPISTMYTVTGRWTLGQVVCDFWLSSDITCCTASILHLCVIALDRYWAITDAVEYSAKRTPKRAAVMIALVWVFSISISLPPFFWRQAKAEEEVSECVVNTDHILYTVYSTVGAFYFPTLLLIALYGRIYVEARSRILKQTPNRTGKRLTRAQLITDSPGSTSSVTSINSRVPDVPSESGSPVYVNQVKVRVSDALLEKKKLMAARERKATKTLGIILGAFIVCWLPFFIISLVMPICKDACWFHLAIFDFFTWLGYLNSLINPIIYTMSNEDFKQAFHKLIRFKCTS | 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 signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries.
PTM: Phosphorylated. Desensitization of the receptor may be mediated by its phosphorylation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43568
Sequence Length: 390
Domain: Ligands are bound in a hydrophobic pocket formed by the transmembrane helices.
Subcellular Location: Cell membrane
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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 effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32669
Sequence Length: 291
Subcellular Location: Cell membrane
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P21577 | MALQQFGLIGLAVMGENLALNIERNGFSLTVYNRTAEKTEAFMADRAQGKNIVPAYSLEDFVASLERPRRILVMVKAGGPVDAVVEQLKPLLDPGDLIIDGGNSLFTDTERRVKDLEALGLGFMGMGVSGGEEGALNGPSLMPGGTQAAYEAVEPIVRSIAAQVDDGPCVTYIGPGGSGHYVKMVHNGIEYGDMQLIAEAYDLLKSVAGLNASELHDVFAAWNKTPELDSFLIEITADIFTKVDDLGTGQPLVELILDAAGQKGTGRWTVETALEIGVAIPTIIAAVNARILSSIKAERQAASEILSGPITEPFSGDRQAFIDSVRDALYCSKICSYAQGMALLAKASQVYNYGLNLGELARIWKGGCIIRAGFLNKIKQAYDADPTLANLLLAPEFRQTILDRQLAWRRVIAIAAERGIPVPAFSASLDYFDSYRRDRLPQNLTQAQRDYFGAHTYERTDRSGSFHAQWF | 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 degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3.
EC: 1.1.1.44
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P52208 | MQFNVAIMTKRTFGVIGLAVMGENLALNVESRGFPIAVFNRSPNKTEKFMAERAVGKDIKAAYTVEEFVQLLERPRKILVMVKAGGPVDAVINELKPLLEEGDMIIDGGNSLYEDTERRTKDLEATGLGFVGMGVSGGEEGALLGPSLMPGGTPAAYKELEPILTKIAAQVEDPDNPACVTFIGPGGAGHYVKMVHNGIEYGDMQLIAEAYDILKNGLGLSNEQLHEVFGQWNQTDELNSFLIEISTDIFAKKDPETGGHLIDYILDAAGQKGTGRWTVMSGLELGVPIPTIYAAVNARVMSSLKEERVAASGQLSGPSKTFSGDVEAWIPKVRDALYCSKMCSYAQGMALIAKASQEFGYDVNLPEIARIWKGGCIIRAGFLDKIKKAFKDNPQLPNLLLAPEFKQSILDRQGPWREVLMLANEMGIAVPAFSSSLDYFDSYRRAVLPQNLTQAQRDYFGAHTYERTDKPRGEFFHTEWLD | 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 degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3.
EC: 1.1.1.44
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O83351 | MGADIGFIGLAVMGENLVLNIERNGFSVAVFNRTTTVVDRFLAGRAHGKRITGAHSIAELVSLLARPRKIMLMVKAGSAVDAVIDQILPLLEKGDLVIDGGNSHYQDTIRRMHALEAAGIHFIGTGVSGGEEGALRGPSLMPGGSAQAWPLVSPIFCAIAAKADDGTPCCDWVGSDGAGHYVKMIHNGIEYGDMQIIAEGYWFMKHALGMSYEHMHHTFTRWNTGRLHSYLIEITAAILAHQDTDGTPLLEKILDAAGQKGTGRWTCVAALEEGSPLTLITESVMARSLSAQKQARCKAHRVFGSPVKVSKAETLSAQQREELVSALEDALYCAKIVSYAQGFELLSHTAKRRGWTLDFSRIASLWRGGCIIRSGFLSKISAAFAQQHDLENLVLAPFFAEELKRACPGWRTIVAESVRQALPVPALSAALAWFDGFTGAALPANLLQAQRDYFGAHTYERTDAPRGEFFHTNWTGTGGDTIAGTYSI | 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 degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3.
EC: 1.1.1.44
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P31072 | MSMDVGVVGLGVMGANLALNIAEKGFKVAVFNRTYSKSEEFMKANASAPFAGNLKAFETMEAFAASLKKPRKALILVQAGAATDSTTEQLKKVFEKGDILVDTGNAHFKDQGRRAQQLEAAGLRFLGMGISGGEEGARKGPAFFPGGTLSVWEEIRPIVEAAAAKADDGRPCVTMNGSGGAGSCVKMYHNSGEYAILQIWGEVFDILRAMGLNNDEVAAVLEDWKSKNFLKSYMLDISIAAARAKDKDGSYLTEHVMDRIGSKGTGLWSAQEALEIGVPAPSLNMAVVSRQFTMYKTERQANASNAPGITQSPGYTLKNKSPSGPEIKQLYDSVCIAIISCYAQMFQCLREMDKVHNFGLNLPATIATFRAGCILQGYLLKPMTEAFEKNPNISNLMCAFQTEIRAGLQNYRDMVALITSKLEVSIPVLSASLNYVTAMFTPTLKYGQLVSLQRDVFGRHGYERVDKDGRESFQWPELQ | 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 degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3.
EC: 1.1.1.44
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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 6-phosphate (oxidative stage): step 2/3.
Subcellular Location: Cytoplasm
EC: 3.1.1.31
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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 (oxidative stage): step 2/3.
EC: 3.1.1.31
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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 6-phosphate (oxidative stage): step 2/3.
Subcellular Location: Cytoplasm
EC: 3.1.1.31
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A0A517FNC4 | MDSRVLGALAALLAAAAAWVMRAAAEWLWWRPRRLERSLRSQGVDGNLYRFLNGDLKETVRLTKEARAQPISPPSHRFLHRINPLLLRAISHHGKFALTWIGPTPRVSIMDPELVREVLSNKFGHFAKPKAAPIVKLLATGLANYEGEKWVRHRRIINPAFHLEKLKRMLPAFFSCCSELIGRWESLVGCDESREVDVWPELQNLTGDVISRTAFGSSYAEGRRIFQLQSEQAELLIQAVQTVYIPGYRFLPTPKNIRRTKIDKEVRALLRSIIEKRENAMKMGDVHDDLLGLLMEYNLKESEHFNSKNIGMTTEDVIEECKLFYFAGQETTSVLLTWTMILLGMHPSWQDRAREEVSQVFGKNKPDFDGLSRLKTVTMILYEVLRLYPPIIFLTRRTYKPMMLGGITFPPEVQLALPIIFIHHDPEFWGEDAEEFNPDRFADGVSKASKNQMAFFPFGWGPRICIGQGFAMLEAKMGLSMILQRFSFELSPNYSHAPHTKITLQPQHGAQMVLHRL | 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, may catalyze the 27-monohydroxylation of furostanol-type steroid to an intermediate product that undergoes a stereospecific formation of the terminal heterocycle to yield diosgenin .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59250
Sequence Length: 517
Pathway: Steroid metabolism; cholesterol metabolism.
Subcellular Location: Membrane
EC: 1.14.14.-
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K7NBW3 | MEKGDTHILVFPFPSQGHINPLLQLSKRLIAKGIKVSLVTTLHVSNHLQLQGAYSNSVKIEVISDGSEDRLETDTMRQTLDRFRQKMTKNLEDFLQKAMVSSNPPKFILYDSTMPWVLEVAKEFGLDRAPFYTQSCALNSINYHVLHGQLKLPPETPTISLPSMPLLRPSDLPAYDFDPASTDTIIDLLTSQYSNIQDANLLFCNTFDKLEGEIIQWMETLGRPVKTVGPTVPSAYLDKRVENDKHYGLSLFKPNEDVCLKWLDSKPSGSVLYVSYGSLVEMGEEQLKELALGIKETGKFFLWVVRDTEAEKLPPNFVESVAEKGLVVSWCSQLEVLAHPSVGCFFTHCGWNSTLEALCLGVPVVAFPQWADQVTNAKFLEDVWKVGKRVKRNEQRLASKEEVRSCIWEVMEGERASEFKSNSMEWKKWAKEAVDEGGSSDKNIEEFVAMLKQT | 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 Length: 454
EC: 2.4.1.350
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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. Also required for cleavage of PCSK2 but does not appear to be involved in its folding. Plays a role in regulating pituitary hormone secretion. The C-terminal peptide inhibits PCSK2 in vitro.
PTM: Proteolytically cleaved in the Golgi by a furin-like convertase to generate bioactive peptides.
Sequence Mass (Da): 23866
Sequence Length: 212
Subcellular Location: Secreted
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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. Also required for cleavage of PCSK2 but does not appear to be involved in its folding. Plays a role in regulating pituitary hormone secretion. The C-terminal peptide inhibits PCSK2 in vitro.
PTM: Proteolytically cleaved in the Golgi by a furin-like convertase to generate bioactive peptides.
Sequence Mass (Da): 23659
Sequence Length: 211
Subcellular Location: Secreted
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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 required for cleavage of pcsk2 but does not appear to be involved in its folding.
PTM: Proteolytically cleaved in the Golgi by a furin-like convertase to generate bioactive peptides.
Sequence Mass (Da): 23021
Sequence Length: 208
Subcellular Location: Secreted
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U5NH37 | MGSQETNLPPHVLIFPLPIQGHVNSMLRLAELLCLAELDITFIVSEFSHSRLIKHTNVASRFARYPGFQFQPISDGLPDDHPRAGERVMDILPSTKNVTGPLFKQMMVENKCFSSATRRPITCIIADGVLSFAGDFAQEKGIPLIYFRTVSACSFWACFCMPELIESGDIPIKGNGMDLIVKSVPGMETFLRRRDLPGFCRVNDINEPKLQILKTETRQTTRAQAAILNTFEDLEGPILSQIRKHMPRLFTIGPSHSHLTSRLETKNIKTLISSGSFWEEDRSCVDWLDAQPPRSVLYVSFGSITVVTRDQLLEFWYGLVNSGQRFLWVMRPDSIMGKDGQSQIPADLEEGTKARGYMVGWAPQEEVLNHPAIGGFLTHSGWNSTLESIVAGVPMICWPYFADQMINSRFVSEIWKIGLDMKDTCDRETIVKMVRELMEIRKDEFLQRADHMAKLAKEAVSEGGSSYSNLDGLVDYIKSLII | 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, iridodial, iridotrial, 8-OH-geraniol, jasmonic acid, gibberellic acid, indole acetic acid, salicylic acid, abscisic acid, zeatin and luteolin .
Catalytic Activity: 7-deoxyloganetate + UDP-alpha-D-glucose = 7-deoxyloganate + H(+) + UDP
Sequence Mass (Da): 54271
Sequence Length: 482
Pathway: Alkaloid biosynthesis.
Subcellular Location: Nucleus
EC: 2.4.1.323
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Q06BR2 | MGPSVRPGFLVVVIGLQFVAASMEVNSRKFEPMVAFICNKPAMHRVPSGWVPDDDPAKSCVKQPEEILEYCKKLYPDHDITNVLQASYKVTIPNWCGFNVTHCHKHGNHTVRPFRCLVGPFQSEALLVPEHCIFDHYHDPRVCNEFDQCNETAMSKCSARGMTTQSFAMLWPCQEPGHFSGVEFVCCPKVSLIPESTEAPKSSPPTPAKTENGLDDYTAYLKGDSKYMSKYANEHERFKAAEKVMQQFQRERDTKMMKDWKAARDSVREKKKTDPKKAMELNKELTERYQKIYHAYEQESIAEKKQLVNTHQQHIQSWLNNRKQVLMEKLQDALLAKPPKKSKIEKAATAYIKVEEKDKMHTYNHFQHLRDTDPEDAANIQDRVLEHLNLIDDRIRRVLDWLKRDPEIEKQVRPNIDKFMAKYKDINANSMKLLLRQEPTPKEAPVETQKAEDYSEEDEAAVTGTANKVKPTEARPEQQEDIKTPGFDSETFEDERPAIAEQTIHDLPNHRKKGYIAHVQQQPMIADEVSLDNLYANSHANSVLGIAIGGVVVFIIIVVAVVMLKRRTQRQRVTHGFVEVDPAASPEERHVANMQMSGYENPTYKYFEMQNQ | 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
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P14599 | MCAALRRNLLLRSLWVVLAIGTAQVQAASPRWEPQIAVLCEAGQIYQPQYLSEEGRWVTDLSKKTTGPTCLRDKMDLLDYCKKAYPNRDITNIVESSHYQKIGGWCRQGALNAAKCKGSHRWIKPFRCLGPFQSDALLVPEGCLFDHIHNASRCWPFVRWNQTGAAACQERGMQMRSFAMLLPCGISVFSGVEFVCCPKHFKTDEIHVKKTDLPVMPAAQINSANDELVMNDEDDSNDSNYSKDANEDDLDDEDDLMGDDEEDDMVADEAATAGGSPNTGSSGDSNSGSLDDINAEYDSGEEGDNYEEDGAGSESEAEVEASWDQSGGAKVVSLKSDSSSPSSAPVAPAPEKAPVKSESVTSTPQLSASAAAFVAANSGNSGTGAGAPPSTAQPTSDPYFTHFDPHYEHQSYKVSQKRLEESHREKVTRVMKDWSDLEEKYQDMRLADPKAAQSFKQRMTARFQTSVQALEEEGNAEKHQLAAMHQQRVLAHINQRKREAMTCYTQALTEQPPNAHHVEKCLQKLLRALHKDRAHALAHYRHLLNSGGPGGLEAAASERPRTLERLIDIDRAVNQSMTMLKRYPELSAKIAQLMNDYILALRSKDDIPGSSLGMSEEAEAGILDKYRVEIERKVAEKERLRLAEKQRKEQRAAEREKLREEKLRLEAKKVDDMLKSQVAEQQSQPTQSSTQSQAQQQQQEKSLPGKELGPDAALVTAANPNLETTKSEKDLSDTEYGEATVSSTKVQTVLPTVDDDAVQRAVEDVAAAVAHQEAEPQVQHFMTHDLGHRESSFSLRREFAQHAHAAKEGRNVYFTLSFAGIALMAAVFVGVAVAKWRTSRSPHAQGFIEVDQNVTTHHPIVREEKIVPNMQINGYENPTYKYFEVKE | 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 similarity). The clathrin-binding site is essential for its association with X11-alpha, -beta, and -gamma. The sequence specific recognition extends to peptide residues that are C-terminal to the NPXY motif. This interaction appears to be independent of phosphorylation (By similarity).
Subcellular Location: Membrane
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P05067 | MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN | 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 protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons . Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.
PTM: Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). PSEN1 cleavage is more efficient with C83 than with C99 as substrate (in vitro) . Amyloid-beta protein 40 and Amyloid-beta protein 42 are cleaved by ACE . Many other minor amyloid-beta peptides, amyloid-beta 1-X peptides, are found in cerebral spinal fluid (CSF) including the amyloid-beta X-15 peptides, produced from the cleavage by alpha-secretase and all terminating at Gln-686.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 86943
Sequence Length: 770
Domain: The transmembrane helix undergoes a conformation change and unravels partially when bound to PSEN1, facilitating cleavage by PSEN1.
Subcellular Location: Cell membrane
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O93279 | MGETTAFVLLLVATLTRSSEIPADDTVGLLTEPQVAMFCGKLNMHINVQNGKWESDPSGTKSCLNTKEGILQYCQEVYPELQITNVVEANQPVSIQNWCKKGRKQCRSHTHIVVPYRCLVGEFVSDALLVPDKCKFLHQERMNQCESHLHWHTVAKESCGDRSMNLHDYGMLLPCGIDRFRGVKFVCCPAETEQETDSSEVEGEESDVWWGGADPEYSENSPPTPSRATYVAGDAFERDENGDGDEDEEDDEDVDPTDEQESDERTANVAMTTTTTTTTESVEEVVRAVCWAQAESGPCRAMLERWYFNPKKRRCVPFLFGGCGGNRNNFESEEYCLAVCSSSLPTVAPSPPDAVDQYFEAPGDDNEHADFRKAKESLEAKHRERMSQVMREWEEAERQAKNLPRADKKAVIQHFQEKVEALEQEAAGERQQLVETHMARVEALLNSRRRLTLENYLGALQANPPRARQVLSLLKKYVRAEQKDRQHTLKHYEHVRTVDPKKAAQIRPQVLTHLRVIDERMNQSLALLYKVPSVASEIQNQIYPAAGSDCKDPVEHCVCPQVDGLVSYGNDALMPDQAYSSAPMDMGVDGLGSIDQSFNQANTENHVEPVDARPIPDRGLPTRPVSSLKLEEMPEVRTETDKRQSAGYEVYHQKLVFFADDVGSNKGAIIGLMVGGVVIATVIVITLVMLRKKQYTSIHHGVIEVDAAVTPEERHLARMQQNGYENPTYKFFEQMQN | 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
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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
Sequence Mass (Da): 21655
Sequence Length: 195
Subcellular Location: Cytoplasm
EC: 4.1.1.19
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Q9Z6M8 | MTSRTKSSKNLGTIALAGMVVSSIIGGGIFSLPQNMAATAGAGAVILSWILTGFGMFFIANTFRILSTIRPDLKEGIYMYSREGFGPYIGFTIGWGYWLCQIFGNVGYAVITMDALNYFFPPYFQGGNTLPAILGGSILIWVFNFIVLKGIRQASIINVIGTIFKIIPLIIFIILTAFFFKLAVFKTDFWGHAVTKAQPSLGSVSSQLKGTMLVTLWAFIGIEGAVVMSGRAKNPLSVGQATVLGFLGCLTIYILFSLLPFGSLFQHQLANIPNPSTAGVLDILVGKWGEVLMNVGLIIAVLSSWLSWTIIVAEIPFSAAKNGTFPEIFTIENKEKSPSVSLYITSSVMQLAMLLVYFSSNAWNTMLSITGVMVLPAYLASAAFLFKLSKSKTYPKKGSIKAPLAMITGILGVVYSLWLIYAGGLKYLFMALVLLALGIPFYIDAGKKKKNAKTFFAKKEIVGMTFIGLLALTAIFLFSTGRIKI | 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
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P55096 | MAAFSKYLTARNTSLAGAAFLLLCLLHKRRRALGLHGKKSGKPPLQNNEKEGKKERAVVDKVFLSRLSQILKIMVPRTFCKETGYLLLIAVMLVSRTYCDVWMIQNGTLIESGIIGRSSKDFKRYLFNFIAAMPLISLVNNFLKYGLNELKLCFRVRLTRYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQGPASMMAYLLVSGLFLTRLRRPIGKMTIMEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTIHSVFRKLVEHLHNFIFFRFSMGFIDSIIAKYVATVVGYLVVSRPFLDLAHPRHLHSTHSELLEDYYQSGRMLLRMSQALGRIVLAGREMTRLAGFTARITELMQVLKDLNHGRYERTMVSQQEKGIEGAQASPLVPGAGEIINTDNIIKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGKEDQKKRGISDQVLKEYLDNVQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEDYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGNYEFKKITEDTVEFGS | 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 acyl-CoA thioesterase and ATPase activities (By similarity). Probably hydrolyzes fatty acyl-CoAs into free fatty acids prior to their ATP-dependent transport into peroxisomes (By similarity). Thus, play a role in regulation of LCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation .
PTM: Ubiquitinated by PEX2 during pexophagy in response to starvation, leading to its degradation.
Location Topology: Multi-pass membrane protein
Catalytic Activity: a very long-chain fatty acyl-CoA + H2O = a very long-chain fatty acid + CoA + H(+)
Sequence Mass (Da): 75475
Sequence Length: 659
Subcellular Location: Peroxisome membrane
EC: 3.1.2.-
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O14678 | MAVAGPAPGAGARPRLDLQFLQRFLQILKVLFPSWSSQNALMFLTLLCLTLLEQFVIYQVGLIPSQYYGVLGNKDLEGFKTLTFLAVMLIVLNSTLKSFDQFTCNLLYVSWRKDLTEHLHRLYFRGRAYYTLNVLRDDIDNPDQRISQDVERFCRQLSSMASKLIISPFTLVYYTYQCFQSTGWLGPVSIFGYFILGTVVNKTLMGPIVMKLVHQEKLEGDFRFKHMQIRVNAEPAAFYRAGHVEHMRTDRRLQRLLQTQRELMSKELWLYIGINTFDYLGSILSYVVIAIPIFSGVYGDLSPAELSTLVSKNAFVCIYLISCFTQLIDLSTTLSDVAGYTHRIGQLRETLLDMSLKSQDCEILGESEWGLDTPPGWPAAEPADTAFLLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDFGPHGVLFLPQKPFFTDGTLREQVIYPLKEVYPDSGSADDERILRFLELAGLSNLVARTEGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQLGMTFISVGHRQSLEKFHSLVLKLCGGGRWELMRIKVE | 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 transport cobalamin across the lysosomal membrane .
Catalytic Activity: an R-cob(III)alamin(out) + ATP + H2O = ADP + an R-cob(III)alamin(in) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68597
Sequence Length: 606
Subcellular Location: Endoplasmic reticulum membrane
EC: 7.6.2.8
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O89016 | MAVPGPTARAGARPRLDLQLVQRFVRIQKVFFPSWSSQNVLMFMTLLCVTLLEQLVIYQVGLIPSQYYGVLGNKDLDGFKALTLLAVTLIVLNSTLKSFDQFTCNLLYVSWRKDLTEHLHHLYFRARVYYTLNVLRDDIDNPDQRISQDVERFCRQLSSVTSKLIISPFTLTYYTYQCFQSTGWLGPVSIFGYFIVGTMVNKTLMGPIVTKLVQQEKLEGDFRFKHMQIRVNAEPAAFYRAGLVEHMRTDRRLQRLLQTQRELMSRELWLYIGINTFDYLGSILSYVVIAIPIFSGVYGDLSPTELSTLVSKNAFVCIYLISCFTQLIDLSTTLSDVAGYTHRIGELQEALLDMSRKSQDCEALGESEWDLDKTPGCPTTEPSDTAFLLDRVSILAPSSDKPLIKDLSLKICEGQSLLITGNTGTGKTSLLRVLGGLWEGMKGSVQMLADFGPHGVLFLPQKPFFTDGTLREQVIYPLKEIYPDSGSADDERIVRFLELAGLSSLVARTGGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEAESELYRIGQQLGMTFISVGHRPSLEKFHSWVLRLHGGGSWELTRIKLE | 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 transport cobalamin across the lysosomal membrane.
Catalytic Activity: an R-cob(III)alamin(out) + ATP + H2O = ADP + an R-cob(III)alamin(in) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68583
Sequence Length: 606
Subcellular Location: Endoplasmic reticulum membrane
EC: 7.6.2.8
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P61221 | MADKLTRIAIVNHDKCKPKKCRQECKKSCPVVRMGKLCIEVTPQSKIAWISETLCIGCGICIKKCPFGALSIVNLPSNLEKETTHRYCANAFKLHRLPIPRPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDDPPDWQEILTYFRGSELQNYFTKILEDDLKAIIKPQYVDQIPKAAKGTVGSILDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCLYGVPSAYGVVTMPFSVREGINIFLDGYVPTENLRFRDASLVFKVAETANEEEVKKMCMYKYPGMKKKMGEFELAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGGEVPVLNVSYKPQKISPKSTGSVRQLLHEKIRDAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFDGVPSKNTVANSPQTLLAGMNKFLSQLEITFRRDPNNYRPRINKLNSIKDVEQKKSGNYFFLDD | 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 after recognition of stalled and vacant ribosomes by mRNA surveillance factors (PELO/Pelota) . Involved in the No-Go Decay (NGD) pathway: recruited to stalled ribosomes by the Pelota-HBS1L complex, and drives the disassembly of stalled ribosomes, followed by degradation of damaged mRNAs as part of the NGD pathway . Also plays a role in quality control of translation of mitochondrial outer membrane-localized mRNA . As part of the PINK1-regulated signaling, ubiquitinated by CNOT4 upon mitochondria damage; this modification generates polyubiquitin signals that recruit autophagy receptors to the mitochondrial outer membrane and initiate mitophagy . RNASEL-specific protein inhibitor which antagonizes the binding of 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) to RNASEL . Negative regulator of the anti-viral effect of the interferon-regulated 2-5A/RNASEL pathway .
PTM: Ubiquitinated by CNOT4 . Ubiquitination mediates the recruitment of autophagy receptors to the mitochondrial outer membrane and initiates mitophagy .
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 67314
Sequence Length: 599
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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Q8NE71 | MPKAPKQQPPEPEWIGDGESTSPSDKVVKKGKKDKKIKKTFFEELAVEDKQAGEEEKVLKEKEQQQQQQQQQQKKKRDTRKGRRKKDVDDDGEEKELMERLKKLSVPTSDEEDEVPAPKPRGGKKTKGGNVFAALIQDQSEEEEEEEKHPPKPAKPEKNRINKAVSEEQQPALKGKKGKEEKSKGKAKPQNKFAALDNEEEDKEEEIIKEKEPPKQGKEKAKKAEQGSEEEGEGEEEEEEGGESKADDPYAHLSKKEKKKLKKQMEYERQVASLKAANAAENDFSVSQAEMSSRQAMLENASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLKLLEEERRLQGQLEQGDDTAAERLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDAQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKELKAGGKSTKQAEKQTKEALTRKQQKCRRKNQDEESQEAPELLKRPKEYTVRFTFPDPPPLSPPVLGLHGVTFGYQGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTHGEMRKNHRLKIGFFNQQYAEQLRMEETPTEYLQRGFNLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINEYKGAVIVVSHDARLITETNCQLWVVEEQSVSQIDGDFEDYKREVLEALGEVMVSRPRE | 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 ribosomes.
Sequence Mass (Da): 95926
Sequence Length: 845
Subcellular Location: Cytoplasm
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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 UAA codon for stop in the apolipoprotein B mRNA . Also involved in CGA (Arg) to UGA (Stop) editing in the NF1 mRNA . May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation (By similarity).
Catalytic Activity: a cytidine in mRNA + H(+) + H2O = a uridine in mRNA + NH4(+)
Sequence Mass (Da): 28192
Sequence Length: 236
Subcellular Location: Cytoplasm
EC: 3.5.4.-
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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 UAA codon for stop in the apolipoprotein B mRNA . Also involved in CGA (Arg) to UGA (Stop) editing in the NF1 mRNA (By similarity). May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation (By similarity).
Catalytic Activity: a cytidine in mRNA + H(+) + H2O = a uridine in mRNA + NH4(+)
Sequence Mass (Da): 27274
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 3.5.4.-
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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 DNA demethylation.
Catalytic Activity: cytidine(6666) in apoB mRNA + H(+) + H2O = NH4(+) + uridine(6666) in apoB mRNA
Sequence Mass (Da): 25962
Sequence Length: 224
EC: 3.5.4.36
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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 DNA demethylation.
Catalytic Activity: cytidine(6666) in apoB mRNA + H(+) + H2O = NH4(+) + uridine(6666) in apoB mRNA
Sequence Mass (Da): 25703
Sequence Length: 224
EC: 3.5.4.36
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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 DNA demethylation.
Catalytic Activity: cytidine(6666) in apoB mRNA + H(+) + H2O = NH4(+) + uridine(6666) in apoB mRNA
Sequence Mass (Da): 25660
Sequence Length: 224
EC: 3.5.4.36
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Q99J72 | MQPQRLGPRAGMGPFCLGCSHRKCYSPIRNLISQETFKFHFKNLGYAKGRKDTFLCYEVTRKDCDSPVSLHHGVFKNKDNIHAEICFLYWFHDKVLKVLSPREEFKITWYMSWSPCFECAEQIVRFLATHHNLSLDIFSSRLYNVQDPETQQNLCRLVQEGAQVAAMDLYEFKKCWKKFVDNGGRRFRPWKRLLTNFRYQDSKLQEILRPCYISVPSSSSSTLSNICLTKGLPETRFWVEGRRMDPLSEEEFYSQFYNQRVKHLCYYHRMKPYLCYQLEQFNGQAPLKGCLLSEKGKQHAEILFLDKIRSMELSQVTITCYLTWSPCPNCAWQLAAFKRDRPDLILHIYTSRLYFHWKRPFQKGLCSLWQSGILVDVMDLPQFTDCWTNFVNPKRPFWPWKGLEIISRRTQRRLRRIKESWGLQDLVNDFGNLQLGPPMS | 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 activity against HIV-1, simian immunodeficiency viruses (SIVs), mouse mammary tumor virus (MMTV) and friend murine leukemia virus (FrMLV) and may inhibit the mobility of LTR retrotransposons.
Catalytic Activity: a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'-deoxyuridine in single-stranded DNA + NH4(+)
Sequence Mass (Da): 52213
Sequence Length: 440
Domain: The CMP/dCMP deaminase domain 1 confers deoxycytidine deaminase activity, whereas the CMP/dCMP deaminase domain 2 mediates RNA-dependent oligomerization and virion incorporation.
Subcellular Location: Cytoplasm
EC: 3.5.4.38
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P15891 | MALEPIDYTTHSREIDAEYLKIVRGSDPDTTWLIISPNAKKEYEPESTGSSFHDFLQLFDETKVQYGLARVSPPGSDVEKIIIIGWCPDSAPLKTRASFAANFAAVANNLFKGYHVQVTARDEDDLDENELLMKISNAAGARYSIQTSSKQQGKASTPPVKKSFTPSKSPAPVSKKEPVKTPSPAPAAKISSRVNDNNDDDDWNEPELKERDFDQAPLKPNQSSYKPIGKIDLQKVIAEEKAKEDPRLVQKPTAAGSKIDPSSDIANLKNESKLKRDSEFNSFLGTTKPPSMTESSLKNDDDKVIKGFRNEKSPAQLWAERKAKQNSGNAETKAEAPKPEVPEDEPEGEPDVKDLKSKFEGLAASEKEEEEMENKFAPPPKKSEPTIISPKPFSKPQEPVKAEEAEQPKTDYKKIGNPLPGMHIEADNEEEPEENDDDWDDDEDEAAQPPLPSRNVASGAPVQKEEPEQEEIAPSLPSRNSIPAPKQEEAPEQAPEEEIEEEAEEAAPQLPSRSSAAPPPPPRRATPEKKPKENPWATAEYDYDAAEDNELTFVENDKIINIEFVDDDWWLGELEKDGSKGLFPSNYVSLGN | 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 in linking the actin cytoskeleton to endocytosis. recruits components of the endocytotic machinery to cortical actin patches, known sites of endocytosis.
PTM: The actin depolymerizing factor homology (ADF) domain mediates actin filament binding.
Sequence Mass (Da): 65576
Sequence Length: 592
Subcellular Location: Cytoplasm
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Q0CX54 | MTKSIIASEPPSAESSGRLPWKILGQTTGFPNQDQELWWLNTAPLLNEFLAECQYDVHLQYQYLTFFRHHVIPVLGPFFAPGTTPNFASRLSKHGHPLDFSVNFQESGATVRMSLGAIGSFAGLQQDPLNQFRAREVLDKLAILYPTVDLQLFKHFESEFGINHADALKVAAKLPKLDRATKMIAIDMLKNGSMTFKVYYMVRSKAAATGLPVHTVLFNAVQRLGSAFEPGLSLLKQFLSPLCDAGETDLGLLSFDCVPTESSRIKLYAIKQVGSLDAIRNLWTLGGTMDDPTTMKGLAVLEHVCELLQFGWSGDSRVQPILFNYEIKKGSTPKPQIYIPLADRYDEFDAAKLKAVFQDLDWKRVPFYQDTGKDLASVL | 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): 42297
Sequence Length: 379
Pathway: Secondary metabolite biosynthesis.
EC: 2.5.1.-
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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
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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
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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
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P11310 | MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYKN | 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 consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA . Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) . Among the different mitochondrial acyl-CoA dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 6 to 12 carbons long primary chains .
PTM: Acetylated. Could occur at proximity of the cofactor-binding sites and reduce the catalytic activity. Could be deacetylated by SIRT3.
Catalytic Activity: a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 46588
Sequence Length: 421
Pathway: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subcellular Location: Mitochondrion matrix
EC: 1.3.8.7
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P08503 | MAAALRRGYKVLRSVSHFECRAQHTKPSLKQEPGLGFSFELTEQQKEFQTIARKFAREEIIPVAPDYDKSGEYPFPLIKRAWELGLINTHIPESCGGLGLGTFDACLITEELAYGCTGVQTAIEANSLGQMPVIIAGNDQQKKKYLGRMTEQPMMCAYCVTEPSAGSDVAGIKTKAEKKGDEYVINGQKMWITNGGKANWYFVLTRSNPDPKVPASKAFTGFIVEADTPGIHIGKKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDRTRPTVAAGAVGLAQRALDEATKYALDRKTFGKLLVEHQGVSFLLAEMAMKVELARLSYQRAAWEVDSGRRNTYFASIAKAFAGDIANQLATDAVQIFGGYGFNTEYPVEKLMRDAKIYQIYEGTAQIQRLIIAREHIEKYKN | 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 consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA . Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity). Among the different mitochondrial acyl-CoA dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 6 to 12 carbons long primary chains .
PTM: Acetylated. Could occur at proximity of the cofactor-binding sites and reduce the catalytic activity. Could be deacetylated by SIRT3.
Catalytic Activity: a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 46555
Sequence Length: 421
Pathway: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subcellular Location: Mitochondrion matrix
EC: 1.3.8.7
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