wanglab/gogpt-training-data huggingface dataset:
Protein: Seed linoleate 9S-lipoxygenase (EC 1.13.11.58) (Lipoxygenase) (P24095)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MFGIFDKGQKIKGTVVLMPKNVLDFNAITSIGKGGVIDTATGILGQGVSLVGGVIDTATSFLGRNISMQLISATQTDGSGNGKVGKEVYLEKHLPTLPTLGARQDAFSIFFEWDASFGIPGAFYIKNFMTDEFFLVSVKLEDIPNHGTIEFVCNSWVYNFRSYKKNRIFFVNDTYLPSATPAPLLKYRKEELEVLRGDGTGKRKDFDRIYDYDVYNDLGNPDGGDPRPILGGSSIYPYPRRVRTGRERTRTDPNSEKPGEVYVPRDENFGHLKSSDFLTYGIKSLSHDVIPLFKSAIFQLRVTSSEFESFEDVRSLYEGGIKLPTDILSQISPLPALKEIFRTDGENVLQFPPPHVAKVSKSGWMTDEEFAREVIAGVNPNVIRRLQEFPPKSTLDPTLYGDQTSTITKEQLEINMGGVTVEEALSTQRLFILDYQDAFIPYLTRINSLPTAKAYATRTILFLKDDGTLKPLAIELSKPHPDGDNLGPESIVVLPATEGVDSTIWLLAKAHVIVNDSGYHQLVSHWLNTHAVMEPFAIATNRHLSVLHPIYKLLYPHYRDTININGLARQSLINADGIIEKSFLPGKYSIEMSSSVYKNWVFTDQALPADLVKRGLAIEDPSAPHGLRLVIEDYPYAVDGLEIWDAIKTWVHEYVSLYYPTDAAVQQDTELQAWWKEAVEKGHGDLKEKPWWPKMQTTEDLIQSCSIIVWTASALHAAVNFGQYPYGGLILNRPTLARRFIPAEGTPEYDEMVKNPQKAYLRTITPKFETLIDLSVIEILSRHASDEIYLGERETPNWTTDKKALEAFKRFGSKLTGIEGKINARNSDPSLRNRTGPVQLPYTLLHRSSEEGLTFKGIPNSISI
Protein: Parathyroid hormone (Q6WQ24)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Tuberoinfundibular peptide of 39 residues
- Parathyroid hormone 1 receptor b
- Parathyroid hormone 2 receptor
- Parathyroid hormone/parathyroid hormone-related peptide receptor
- Parathyroid hormone 1a.
- Parathyroid hormone 2 receptor
- Parathyroid hormone-like hormone
- Sodium calcium exchanger 1n
- Parathyroid hormone 4
Sequence:
MLLIRCLEKAMLIIVLWSLCSFLFLEGLPISKRSISEVQLMHNVREHKEMLDRQDWLQLKLNNIIIPSVNDSQKERKGKTNGPSVKRLRKGEGATWSFY
Protein: tRNA uridine(34) acetyltransferase (EC 2.3.1.311) (Elongator complex protein 3 homolog) (DmcElp3) (A0A1C7D1B7)
Organism: Dehalococcoides mccartyi (strain CBDB1)
Function: tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L-methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'-dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not show protein lysine acetyltransferase activity (By similarity).
Interaction partners:
Sequence:
MKKLSRTISGVTPVAVMTKPLPCPGKCIYCPTFAATPQSYTPESPAVLRAKSCEYQAYKQVALRLRIIQDMGHPTDKVELIIMGGTFLSADITYQYGFIKDCYDALNGVVAGSLEEAKTINETAQHRCVGLCIETRPDICGKAEIQRMIDFGTTRVELGVQMLDDDIYKLVERGHRVSDVAEATCLLREYGLKVHYHWMPGLPGSSPEKDLALSRMVFEDPRFCPDGLKLYPTMVVEGTILEQWWKEGRYTPYPNGTMTGLIADIKALVPPYVRISRVLRDIPAVFISAGLKDSLRDGVRQILESRHQKCRCIRCREYGHRQRKGQTSGEPTLRRLDYPASGGKEIFLSFEDASDTLYGLLRLRIPCASLPVLGQKYGAKTGLVRELHVYGTELSLGEQGDQSAQHRGLGRKLLAEAECLARDEFGLDSLAILSGVGAREYYRSLGYELVAGYMCKHLD
Protein: Uncharacterized protein (Q388Q8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVLCVDVYIFIFCMCDACVLFLSQVGWGRGLCTVMTFISFHSLAEALRSAFPCLPRLMLRWGYIVLRKRRDFLKRTGETRCPTVAPNSLLPLSATPCYYCPEGVQETLLNYINDGNFRYPTISANPVPSMRDWCVGSSSAQSLLLSTTKVSVEPSEVPGASPTPIIIQLFRCEQRLNIADCMRTRLLQKELRRTEGGLQFLHQLSKGSNLMDQNMVAALESKPSLAAESVSTVSAVETPYSGHIVWEKDGWFFDDIFSSSEIELPASSSDSTGYWRAWIVPFRGPFSKYFLPRMQDIHQFHVEEDITLMNVDFSDRANQRRYSANYSSFHAGRVLNYWAATGEPVQLENRMDNEDMEENDDAQIHLASTPCCWFTMTEISERKLCLRHGGTVRNLPFHFDCCGFFLHLCPPWFVLSETEVLQRYPISNESLVGACFIPEYGNTENVVSASRQEGPLCGGVIFVLQELGEWCVFPHQHVTVNFGRVSLPSTDSLHRDKKPLLFVEINAAVEMMYSWSSEHCKQTSVECDFLKQVIDIFLSISSKCSAASFINSFIGCCGHPLPYCEELSPLADAKDSPATLCILGTEDQHMPHVVETNRTPYSLNSGEMVTGPSHLQRGVYEGLIEVGRSRSKRTSQIPNQKCELPFIHENNLGPCGDAWDIGIVLLSFEYCIPAVKAMDTELVA
Protein: Protocadherin related 15 (A0A8I6GEC2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MSPQFALWKCMPHGILLASLLIVSWGQYDDDCKLARGGPPATIVAIDEESRNGTILVDNMLIKGTAGGPDPTIELSLKDNVDYWVLLDPVKQMLFLNSTGRVLDRDPPMNIHSIVVQVQCVNKKVGTVIYHEVRIVVRDRNDNSPTFKHESYYATVNELTPVGTTIFTGFAGDNGATDIDDGPNGQIEYVIQYNPEDPTSNDTFEIPLMLTGNVVLRKRLNYEDKTRYYVIIQANDRAQNLNERRTTTTTLTVDVLDGDDLGPMFLPCVLVPNTRDCRPLTYQAAIPELRTPEELNPILVTPPIQAIDQDRNIQPPSDRPGILYSILVGTPEDYPRFLHMHPRTAELTLLEPVNRDFHQKFDLVIKAEQDNGHPLPAFASLHIEILDENNQSPYFTMPSYQGYILESAPVGATISESLNLTTPLRIVALDKDIEDTKDPELHLFLNDYTSVFTVTPTGITRYLTLLQPVDREEQQTYTFLITAFDGVQESEPVVVNIRVMDANDNTPTFPEISYNVYVYTDMSPGDSVIQLTAVDADEGSNGEISYEILVGSKGDFVINRTTGLVSIAPGVELVVGQTYALTVQASDNAPPAERRHSICTVYIEVLPPNNQSPPRFPQLMYSLEVSEAMRIGAVLLNLQATDREGDPITYAIENGDPQRVFNLSETTGILSLGKALDRESTDRYILIVTASDGRPDGTSTATVNIVVTDVNDNAPVFDPYLPRNLSVVEEEANAFVGQVRATDPDAGINGQVHYSLGNFNNLFRITSNGSIYTAVKLNREARDHYELVVVATDGAVHPRHSTLTLYIKVLDIDDNSPVFTNSTYTVVVEENLPAGTAFLQIEAKDVDLGANVSYRIRSPEVKHLFALHPFTGELSLLRSLDYEAFPDQEASITFLVEAFDIYGTMPPGIATVTVIVKDMNDYPPVFSKRIYKGMVAPDAVKGTPITTVYAEDADPPGLPASRVRYRVDDVQFPYPASIFDVEEDSGRVITRVNLNEEPTTIFKLVVVAFDDGEPVMSSSATVRILVLHPGEIPRFTQEEYRPPPVSELAARGTVVGVISAAAINQSIVYSIVAGNEDDKFGINNVTGVIYVNSPLDYETRTSYVLRVQADSLEVVLANLRVPSKSNTAKVYIEIQDENDHPPVFQKKFYIGGVSEDARMFTSVLRVKATDRDTGNYSAMAYRLIIPPIKEGKEGFVVETYTGLIKTAMLFHNMRRSYFKFQVIATDDYGKGLSGKADVLVSVVNQLDMQVIVSNVPPTLVEKKIEDLTEILDRYVQEQIPGAKVVVESIGARRHGDAFSLEDYSKCDLTVYAIDPQTNRAIDRNELFKFLDGKLLDINKDFQPYYGEGGRILEIRTPEAVTSIKKRGESLGYTEGALLALAFIIILCCIPAILVVLVSYRQRQAECTKTARIQSAMPAAKPAAPVPAAPPPPPPPPPPGAHLYEELGESAILFLLYHFEQSRGNNPVPEDRSSHRDGMAFSSSTTESHEPAHVEGPLDNQANPARTFSFLPDEDDLSTHNPLYMESIGQRSTNSDLQPGTEFGELFVPRTQVKSQSLRGPREKIQRVWNQSVRFPRRLMWKTPNRPETIDLVEWQITRQRAECEKTRCHPSQQGSSNLMVTTEDARGSEKEGGHRDTLIVQQTEQLKSLSSGSSFSSSWSHFSFSTLPTISRAVELGSEPDVVTSPADCTLELSPPRRPRVLNSLGSKRETPTCASDTETKRNSFEMVPHPPSISAPLPQLPLPQPPIAFTTFPLPLSSPNPPRPQLLTFSLPISTTPASSLPPPPPPSLPPPPRPPAPRLFPLPPSTSVPSTDSISTPAAKCTASVTHARETMSTTQPPASNPPCGAEPHRHPKGILRHVKNLAELEKSVSNMYSHIEKNCPPTELSKLHPFCPAEKTNMKITCDQSQETLVRVVEGIDVQTHSQSTSL
Protein: GDNF family receptor alpha-1 (GDNF receptor alpha-1) (GDNFR-alpha-1) (GFR-alpha-1) (RET ligand 1) (TGF-beta-related neurotrophic factor receptor 1) (Q62997)
Organism: Rattus norvegicus (Rat)
Function: Receptor for GDNF. Mediates the GDNF-induced autophosphorylation and activation of the RET receptor.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23333276}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:8674117}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:23333276}. Endosome {ECO:0000269|PubMed:23333276}. Endosome, multivesicular body {ECO:0000269|PubMed:23333276}. Note=Localizes mainly to the plasma membrane. In the presence of SORL1, shifts to vesicular structures, including trans-Golgi network, endosomes and multivesicular bodies. {ECO:0000269|PubMed:23333276}.
Interaction partners:
- Glial cell line-derived neurotrophic factor
- Neurturin
- Proto-oncogene tyrosine-protein kinase receptor Ret
- Artemin
- Persephin
- Neural cell adhesion molecule 1
- Beta-nerve growth factor
- Neurotrophic factor BDNF precursor form
- High affinity nerve growth factor receptor
- Neurotrophin-3
Sequence:
MFLATLYFALPLLDLLMSAEVSGGDRLDCVKASDQCLKEQSCSTKYRTLRQCVAGKETNFSLTSGLEAKDECRSAMEALKQKSLYNCRCKRGMKKEKNCLRIYWSMYQSLQGNDLLEDSPYEPVNSRLSDIFRAVPFISDVFQQVEHISKGNNCLDAAKACNLDDTCKKYRSAYITPCTTSMSNEVCNRRKCHKALRQFFDKVPAKHSYGMLFCSCRDIACTERRRQTIVPVCSYEERERPNCLSLQDSCKTNYICRSRLADFFTNCQPESRSVSNCLKENYADCLLAYSGLIGTVMTPNYVDSSSLSVAPWCDCSNSGNDLEDCLKFLNFFKDNTCLKNAIQAFGNGSDVTMWQPAPPVQTTTATTTTAFRVKNKPLGPAGSENEIPTHVLPPCANLQAQKLKSNVSGSTHLCLSDSDFGKDGLAGASSHITTKSMAAPPSCSLSSLPVLMLTALAALLSVSLAETS
Protein: Regulatory protein ADR1 (P07248)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for transcriptional activation of glucose-repressible alcohol dehydrogenase (ADH2).
Subcellular location: Nucleus.
Interaction partners:
- Regulatory protein CAT8
- Carbon catabolite-derepressing protein kinase
- Alcohol dehydrogenase 2
- Protein SIP4
- Acetyl-coenzyme A synthetase 1
- Protein BMH1
- Serine/threonine-protein kinase RIM15
- Glucose transport transcription regulator RGT1
- SNF1 protein kinase subunit beta-2
- 5'-AMP-activated protein kinase subunit gamma
Sequence:
MANVEKPNDCSGFPVVDLNSCFSNGFNNEKQEIEMETDDSPILLMSSSASRENSNTFSVIQRTPDGKIITTNNNMNSKINKQLDKLPENLRLNGRTPSGKLRSFVCEVCTRAFARQEHLKRHYRSHTNEKPYPCGLCNRCFTRRDLLIRHAQKIHSGNLGETISHTKKVSRTITKARKNSASSVKFQTPTYGTPDNGNFLNRTTANTRRKASPEANVKRKYLKKLTRRASFSAQSASSYALPDQSSLEQHPKDRVKFSTPELVPLDLKNPELDSSFDLNMNLDLNLNLDSNFNIALNRSDSSGSTMNLDYKLPESANNYTYSSGSPTRAYVGANTNSKNASFNDADLLSSSYWIKAYNDHLFSVSESDETSPMNSELNDTKLIVPDFKSTIHHLKDSRSSSWTVAIDNNSNNNKVSDNQPDFVDFQELLDNDTLGNDLLETTAVLKEFELLHDDSVSATATSNEIDLSHLNLSNSPISPHKLIYKNKEGTNDDMLISFGLDHPSNREDDLDKLCNMTRDVQAIFSQYLKGEESKRSLEDFLSTSNRKEKPDSGNYTFYGLDCLTLSKISRALPASTVNNNQPSHSIESKLFNEPMRNMCIKVLRYYEKFSHDSSESVMDSNPNLLSKELLMPAVSELNEYLDLFKNNFLPHFPIIHPSLLDLDLDSLQRYTNEDGYDDAENAQLFDRLSQGTDKEYDYEHYQILSISKIVCLPLFMATFGSLHKFGYKSQTIELYEMSRRILHSFLETKRRCRSTTVNDSYQNIWLMQSLILSFMFALVADYLEKIDSSLMKRQLSALCSTIRSNCLPTISANSEKSINNNNEPLTFGSPLQYIIFESKIRCTLMAYDFCQFLKCFFHIKFDLSIKEKDVETIYIPDNESKWASESIICNGHVVQKQNFYDFRNFYYSFTYGHLHSIPEFLGSSMIYYEYDLRKGTKSHVFLDRIDTKRLERSLDTSSYGNDNMAATNKNIAILIDDTIILKNNLMSMRFIKQIDRSFTEKVRKGQIAKIYDSFLNSVRLNFLKNYSVEVLCEFLVALNFSIRNISSLYVEEESDCSQRMNSPELPRIHLNNQALSVFNLQGYYYCFILIIKFLLDFEATPNFKLLRIFIELRSLANSILLPTLSRLYPQEFSGFPDVVFTQQFINKDNGMLVPGLSANEHHNGASAAVKTKLAKKINVEGLAMFINEILVNSFNDTSFLNMEDPIRNEFSFDNGDRAVTDLPRSAHFLSDTGLEGINFSGLNDSHQTVSTLNLLRYGENHSSKHKNGGKGQGFAEKYQLSLKYVTIAKLFFTNVKENYIHCHMLDKMASDFHTLENHLKGNS
Protein: Mineralization regulator ANKH (ATP carrier protein ANKH) (Progressive ankylosis protein homolog) (ANK) (Q9HCJ1)
Organism: Homo sapiens (Human)
Function: Regulates intra- and extracellular levels of inorganic pyrophosphate (PPi), probably functioning as PPi transporter.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20943778}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Alkaline phosphatase, tissue-nonspecific isozyme
Sequence:
MVKFPALTHYWPLIRFLVPLGITNIAIDFGEQALNRGIAAVKEDAVEMLASYGLAYSLMKFFTGPMSDFKNVGLVFVNSKRDRTKAVLCMVVAGAIAAVFHTLIAYSDLGYYIINKLHHVDESVGSKTRRAFLYLAAFPFMDAMAWTHAGILLKHKYSFLVGCASISDVIAQVVFVAILLHSHLECREPLLIPILSLYMGALVRCTTLCLGYYKNIHDIIPDRSGPELGGDATIRKMLSFWWPLALILATQRISRPIVNLFVSRDLGGSSAATEAVAILTATYPVGHMPYGWLTEIRAVYPAFDKNNPSNKLVSTSNTVTAAHIKKFTFVCMALSLTLCFVMFWTPNVSEKILIDIIGVDFAFAELCVVPLRIFSFFPVPVTVRAHLTGWLMTLKKTFVLAPSSVLRIIVLIASLVVLPYLGVHGATLGVGSLLAGFVGESTMVAIAACYVYRKQKKKMENESATEGEDSAMTDMPPTEEVTDIVEMREENE
Protein: ATP synthase peripheral stalk subunit F6 (C1BG59)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MAASLLRIGRLGSLKCVQAESSLRRAPAAVALCTNAGGPKKPKKSSSETQLDPIQKLFLHSIREYSSKSAASGGLVDAGPAYEKNLAEELTKLQRLYGGGDLTAFPEFKSPEPKLEEVAPK
Protein: Basal cell adhesion molecule (Auberger B antigen) (B-CAM cell surface glycoprotein) (F8/G253 antigen) (Lutheran antigen) (Lutheran blood group glycoprotein) (CD antigen CD239) (P50895)
Organism: Homo sapiens (Human)
Function: Laminin alpha-5 receptor. May mediate intracellular signaling.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15238148, ECO:0000269|PubMed:31413112}; Single-pass type I membrane protein.
Interaction partners:
- Laminin subunit alpha-5
- Contactin-6
- PDZ domain-containing protein 4
Sequence:
MEPPDAPAQARGAPRLLLLAVLLAAHPDAQAEVRLSVPPLVEVMRGKSVILDCTPTGTHDHYMLEWFLTDRSGARPRLASAEMQGSELQVTMHDTRGRSPPYQLDSQGRLVLAEAQVGDERDYVCVVRAGAAGTAEATARLNVFAKPEATEVSPNKGTLSVMEDSAQEIATCNSRNGNPAPKITWYRNGQRLEVPVEMNPEGYMTSRTVREASGLLSLTSTLYLRLRKDDRDASFHCAAHYSLPEGRHGRLDSPTFHLTLHYPTEHVQFWVGSPSTPAGWVREGDTVQLLCRGDGSPSPEYTLFRLQDEQEEVLNVNLEGNLTLEGVTRGQSGTYGCRVEDYDAADDVQLSKTLELRVAYLDPLELSEGKVLSLPLNSSAVVNCSVHGLPTPALRWTKDSTPLGDGPMLSLSSITFDSNGTYVCEASLPTVPVLSRTQNFTLLVQGSPELKTAEIEPKADGSWREGDEVTLICSARGHPDPKLSWSQLGGSPAEPIPGRQGWVSSSLTLKVTSALSRDGISCEASNPHGNKRHVFHFGTVSPQTSQAGVAVMAVAVSVGLLLLVVAVFYCVRRKGGPCCRQRREKGAPPPGEPGLSHSGSEQPEQTGLLMGGASGGARGGSGGFGDEC
Protein: 2-dehydropantoate 2-reductase (EC 1.1.1.169) (Ketopantoate reductase) (KPA reductase) (KPR) (P38787)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Interaction partners:
- Pantoate--beta-alanine ligase
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- Pantothenate kinase CAB1
Sequence:
MTAPHRSTIHILGLGAMGTVLAVDLLRFTNALVVPLFRSQERLAQFQKTNGNNISIRKLYLEGSPIFSYPVEKCECPETFSKKPIDNLVVTTKTYQTKEALAPYLPYINKNTNLILIQNGLGVLELLREEIFTDSKNRPHLFQGVISHGVYQDKAGVFNHAGWAGMKIAKLPWTEEEMIQKKSVVEDDAANNSLVKLLTEPKFAKEFGIEHSTYQEMLFGQLFKFLVNACMNPVTAILDCVNGEMKASCGPVFTSIIDECLQILRVAYRPLFQYHEKYSGNEEYPEMDVNAVLTTDNMVSEVTRIGCDINSRNSSSMRQDTLFLRDIEIEYINGYVVKLADNLNLDPNCCKVNKTIGELATMRLALNRSRSINGDWRKD
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q4JI29)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Interaction partners:
Sequence:
MSKPKVFFDITIDGKSAGRIVIELRADVVPKTAENFRALCTGEKGFGYKGSGFHRVIPGFMCQGGDFTNHNGTGGKSIYGNKFADENFTLKHTGPGIMSMANAGPNTNGSPFFICTEKTSWLDGKHVVFGSVVDGMDVVRVVEGRGSSSGKCSAKIVIADCGQL
Protein: Cadherin-17 (BILL-cadherin) (Liver-intestine cadherin) (LI-cadherin) (P130) (Q9R100)
Organism: Mus musculus (Mouse)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. LI-cadherin may have a role in the morphological organization of liver and intestine.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Catenin beta-1
- Catenin delta-1
Sequence:
MVSAQLHFLCLLTLYLTCGYGEEGKFSGPLKPMTFSIFEGQEPSQVIFQFKTNPPAVTFELTGETDGIFKIEKDGLLYHTRALDRETRAVHHLQLAALDSHGAIVDGPVPITIEVKDINDNRPTFLQSKYEGSVRQNSRPGKPFMYVNATDLDDPATPNGQLFYQIVIQLPQINDVMYFQIDSKTGAISLTPEGSQELDPVKNPSYNLVVSVKDMGGQSENSFSDTTYVDISIRENIWKAPEPVEIRENSTDPHPIKITQVQWNDPGAQYSLVNKEKLSPFPFSIDQEGNIYVTQALDREEKNSHVFFATAKDENGKPLAYPLEIYVKVIDINDNPPTCLSPVTVFEVQENEPLGNSIGIFEAHDMDEANNINSILKYKLVDQTPKVPSDGLFLIGEYEGKVQLSKQSLKKQDSPQYNLSIEVSDVDFKTLCYIQVNVIDINDQIPIFETSNYGSKTLSEDTAIGSTILIIQATDADEPFTGSSKILYKIVQGDTEGRLEVVTDPTTNAGYVKIKKPLDFETQPVSSIVFQAENPEPLVKGIEYNASSFASFELIVTDVNEVPVFPQRIFQANVSEDAAVGSRVGNVTARDPEGLTVSYSLKGNMRGWLKIDSVTGEIFSAAPLDRETESVYRVQVVATEVGGSSLSSTADFHLVLTDVNDNPPRLAKDYTGLFFCHPLSAPGSLIFEVTDDDQQSLRRPKFTFALGREGLQSDWEVSKINGTHARLSTRHTRFEEQVYNIPIRINDGGQPPMEGTVFLPVTFCQCVEGSCFRPAGRQDGIPTVGMAVGILLTTFLVIGIILAVVFIRMRKDKVENPQSPENKPLRS
Protein: Low density lipoprotein receptor-related protein 3 (E9Q1T6)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane, coated pit {ECO:0000256|ARBA:ARBA00037878}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MEKRAAAGPEGAPGARAPLAVVCLVNLFLTGRLSSAVPALGKAGATWGFGFQAATEPTGTQAACSGKLEQHTERRGVIYSPAWPLNYPPGTNCSWYIQGDRGDMITISFRNFDVEESHQCSLDWLLLGPAAPPRQEAFRLCGSAIPPAFISARDHVWIFFHSDASSSGQAQGFRLSYIRGKLGQTSCQTDEFRCDNGKCLPGPWQCNMVDECGDGSDEGNCSAPASEPPGSLCPGGTFPCSGARSTRCLPVERRCDGTQDCGDGSDEAGCPDLACGRRLGSFYGSFASPDLFGAARGPSDLHCTWLVDTQDPRRVLLQLELRLGYDDYVQVYEGLGERGDRLLQTLSYRSNHRPVSLEAAQGRLTVAYHARARSAGHGFNATYQVKGYCLPWEQPCGSSEGDDDSTGEQGCFSEPQRCDGWWHCASGRDEQGCPACPPDQYPCEGGSGLCYAPADRCNNQKSCPDGADEKNCFSCQPGTFHCGTNLCIFETWRCDGQEDCQDGSDEHGCLAAVPRKVITAALIGSLVCGLLLVIALGCAFKLYSLRTQEYRAFETQMTRLEAEFVRREAPPSYGQLIAQGLIPPVEDFPVYSASQASVLQNLRTAMRRQMRRHASRRGPSRRRLGRLWNRLFHRPRAPRGQIPLLTAARTSQTVLGDGLLQAAPGPVPEPPAPNTDTGSPREAGDGPPSGSGHAPEVGPSVPPPPLNLRDPEYRPEDKERKACVEPLEDSPAPVDTPPEPCLAQDPHPQTPTASGTQDPHSAEPLGVCRSPPPPCSPILEASDDEALLVC
Protein: Dehydrogenase/reductase SDR family member 4 (EC 1.1.1.184) (EC 1.1.1.300) (NADPH-dependent carbonyl reductase) (CR) (NADPH-dependent retinol dehydrogenase/reductase) (NDRD) (mouNRDR) (Peroxisomal short-chain alcohol dehydrogenase) (PSCD) (Short chain dehydrogenase/reductase family 25C member 2) (Protein SDR25C2) (Q99LB2)
Organism: Mus musculus (Mouse)
Function: NADPH-dependent oxidoreductase which catalyzes the reduction of a variety of compounds bearing carbonyl groups including ketosteroids, alpha-dicarbonyl compounds, aldehydes, aromatic ketones and quinones. Reduces all-trans-retinal and 9-cis retinal. Reduces 3-ketosteroids and benzil into 3alpha-hydroxysteroids and S-benzoin, respectively, in contrast to the stereoselectivity of primates DHRS4s which produce 3beta-hydroxysteroids and R-benzoin. In the reverse reaction, catalyzes the NADP-dependent oxidation of 3alpha-hydroxysteroids and alcohol, but with much lower efficiency. Involved in the metabolism of 3alpha-hydroxysteroids, retinoid, isatin and xenobiotic carbonyl compounds.
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:Q8WNV7}.
Interaction partners:
- Aldehyde dehydrogenase 1A1
- Dehydrogenase/reductase SDR family member 9
- Aldehyde oxidase 1
- Beta,beta-carotene 15,15'-dioxygenase
- Lecithin retinol acyltransferase
- Cytochrome P450 26A1
- Retinaldehyde dehydrogenase 3
- Retinal dehydrogenase 2
- All-trans-retinol 13,14-reductase
- Short-chain dehydrogenase/reductase 3
Sequence:
MQKAGRLLGGWTQAWMSVRMASSGLTRRNPLSNKVALVTASTDGIGFAIARRLAEDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGIVCHVGKAEDREKLITTALKRHQGIDILVSNAAVNPFFGNLMDVTEEVWDKVLSINVTATAMMIKAVVPEMEKRGGGSVVIVGSVAGFTRFPSLGPYNVSKTALLGLTKNFAAELAPKNIRVNCLAPGLIKTRFSSVLWEEKAREDFIKEAMQIRRLGKPEDCAGIVSFLCSEDASYINGETVVVGGGTPSRL
Protein: Aspartyl aminopeptidase 1 (EC 3.4.11.21) (O36014)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Aspartyl aminopeptidase that is able to remove aspartyl residue at N-terminus of angiotensin I. Acts also as a chaperone and efficiently suppressed the thermal aggregation of citrate synthase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Vacuole lumen {ECO:0000269|PubMed:34169534}. Note=Transported from the cytosol into the vacuole during selective autophagy. This functions through Nbr1-mediated vacuolar targeting (NVT), in which the autophagy receptor Nbr1 cooperates with the endosomal sorting complexes required for transport (ESCRTs) to transport cytoplasmic materials into the vacuole. {ECO:0000269|PubMed:34169534}.
Interaction partners:
- Autophagy receptor Nbr1
- Alpha-mannosidase
- Aminopeptidase 1
- Autophagy-related protein 9
Sequence:
MQLHGKMTATAKSCALDFLDFVNASPTPYHAVQNLAEHYMSHGFQYLSEKSDWQSKIEPGNSYFVTRNKSSIIAFSIGKKWKPGNGFSIIATHTDSPTLRLKPKSQKSAYGYLQVGVEKYGGGIWHTWFDRDLSLAGRVMVEEEDGRVIQYNVHIDRPLLRIPTLAIHLDPSANSSFSFNMETEFVPLIGLENELAKEETSDNGDKYHHPVLLSLLANEISKSLETTIDPSKIVDFELILGDAEKARLGGIHEEFVFSPRLDNLGMTFCASQALTKSLENNSLDNESCVRVVPSFDHEEIGSVSAQGAESTFLPAVLQRICELGKESSLFSISMVKSFLVSADMAHAMHPNYSSRYENSNTPFLNKGTVIKVNANQRYTTNSAGIVLLKKVAQLADVPIQSFVVRNDSPCGSTIGPKLAAMTGMRTLDLGNPMLSMHSCREMCGSKDFEYAVVLFSSFFQNFANLEEKIIIDE
Protein: Beta-2 adrenergic receptor (Beta-2 adrenoreceptor) (A0A060XC03)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Early endosome {ECO:0000256|ARBA:ARBA00004412}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
- GNAS complex locus
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Endothelin-3
- Neuropeptide Y
- GNAS complex locus
- GNAS complex locus
- Guanine nucleotide-binding protein G
- GNAS complex locus
- Guanine nucleotide-binding protein G
Sequence:
MESVSTPAVFNLSDLSVEMNSSSRQWSYSEYSEAVAVLLGILMALLVMCIVFGNVLVITAIVRFQRLQTVTNMFITSLACADLVMGLLVVPFGACYILLNTWHFGSFLCEFWTAADVLCVTASIETLCVIALDRYLAITSPLRYPSLLTKRKACVVVVTVWGVAALISFLPIHMKWWVSDEPEALSCLEDAHCCDFNTNAAYAVASSVVSFYIPLAVMAFVYGRVFQEARKQLEKIRGSEGRFHAQMIDNNQGQDGGNGKRPKFCLKEHKALKTLGIIMGTFTLCWLPFFVLNVVVTIWKVDNIKMPFRILNWIGYANSAFNPLIYCRSPEFRYAFQEILCLRGAAFPTNGYIYRGHSLRLSPKDKPGSLSNNVGTVELGSLSSVTNINGYCNNPPLASIV
Protein: 1,8-cineole synthase (CnsA) (bCinS) (EC 4.2.3.108) (Monoterpene synthase) (B5GMG2)
Organism: Streptomyces clavuligerus
Function: In vitro, catalyzes the formation of 1,8-cineole from geranyl diphosphate (GPP). Can also accept neryl diphosphate (NPP) as substrate to produce 1,8-cineole.
Interaction partners:
Sequence:
MPAGHEEFDIPFPSRVNPFHARAEDRHVAWMRAMGLITGDAAEATYRRWSPAKVGARWFYLAQGEDLDLGCDIFGWFFAYDDHFDGPTGTDPRQTAAFVNRTVAMLDPRADPTGEHPLNIAFHDLWQRESAPMSPLWQRRAVDHWTQYLTAHITEATNRTRHTSPTIADYLELRHRTGFMPPLLDLIERVWRAEIPAPVYTTPEVQTLLHTTNQNINIVNDVLSLEKEEAHGDPHNLVLVIQHERQSTRQQALATARRMIDEWTDTFIRTEPRLPALCGRLGIPLADRTSLYTAVEGMRAAIRGNYDWCAETNRYAVHRPTGTGRATTPW
Protein: Deoxyhypusine synthase (DHS) (EC 2.5.1.46) (Q9XXJ0)
Organism: Caenorhabditis elegans
Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a critical lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. This is the first step of the post-translational modification of that lysine into an unusual amino acid residue named hypusine. Hypusination is unique to mature eIF-5A factor and is essential for its function.
Interaction partners:
- Deoxyhypusine hydroxylase
- Eukaryotic translation initiation factor 5A-2
- Eukaryotic translation initiation factor 5A-1
- (3R)-3-hydroxyacyl-CoA dehydrogenase (17-beta-hydroxysteroid dehydrogenase 8) (Estradiol 17-beta-dehydrogenase 8) (Testosterone 17-beta-dehydrogenase 8)
- PABS domain-containing protein
- DeHydrogenases, Short chain
- Protein dhs-3
- Meiotic recombination protein spo-11
- Arginase
- Probable delta-1-pyrroline-5-carboxylate synthase
Sequence:
MSTNEAAASQEDIALAQGAVLVKSCQVPDGSIPIRGFDFSTASGPDFSLSAILSSYMSTGFQATHLAQAIQQVNQMLSLRDTPLTCDDDEKLFPYPEGRQKRSCTIFLGYTSNLVTSGLREVLRYCVQRNLVDCIVTSAGGIEEDLIKCLKPSYLGTFTMDGAKLRSNGMNRAGNVLIPNDNYCAFEDWLMPILDECLVEQEEKHLNWTPSKLIQRLGERIGDESSILYWAAKHRIPVFCPALTDGSLGDMLYFHSVKSSPGLRVDIVEDVRHINTIAVKSFKTGSIILGGGVVKHHINNANLMRNGADHTVYINTGQEFDGSDSGAQPDEAVSWGKVKPSAGAVKVHAEATLVFPLLVAETFAKHEGHKD
Protein: Dolichyl-phosphooligosaccharide-protein glycotransferase (EC 2.4.99.21) (Oligosaccharyl transferase) (OST) (OTase) (Q2EMT4)
Organism: Methanococcus voltae
Function: Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcGlc-2,3-diNAcAGlcNAc in M.voltae) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (Probable). Involved in the assembly of an N-linked disaccharide that decorates the S-layer glycoprotein and flagellins.
Subcellular location: Cell membrane {ECO:0000305|PubMed:23624439}; Multi-pass membrane protein {ECO:0000305|PubMed:23624439}.
Interaction partners:
Sequence:
MTENNEKVKNSDSANNQSSKNSKFNFNFEDKKVKCAKTILIIIFLAFLSFQMRAQTADMGFTTNEQYLDVFSDDNGRMYLTALDPYYYLRMSENYLENGHTGDTLKNIDGQQVPWDSYKYGPTGARATFNLLSVVTVWVYQVWHAMDSTVTLMNAAFWVPAILSMFLITPIFFTVRRITSSDIGGAVAAILASLSPSIFVKTVAGFSDTPILEILPLLFIVWFIIEAIHYSKEKNYKSLIYGLLATLMLALYPFMWSAWWYGYYIVIAFLVIYAIYKGISYNSIAKYTKSKNNNHKDKIESEKLEMLNILKISGLFIIGGAVLITALYGVSTTMNALQAPLNYLGLDEVSSQTGWPNVLTTVSELDTASLDEIISSSLGSIHLFAIGLIGIFLSLFRKVLTPVKQISNGLAEKLDIKYALLLIIWFAVTFLAASKGVRFVALMVPPLSIGVGIFVGFIEQFIKNNLDKKYEYVAYPTIAIIVLYALFTIYRADSADLVRMLLPSNYVPIAEGIMLASLAVLIIYKVAELIAESNKKLVMNKIFMILLAIGLITPTIATIVPFYSVPTYNDGWGESLEWINTQTPNNSVVTCWWDNGHIYTWKTDRMVTFDGSSQNTPRAYWVGRAFSTSNESLANGIFRMLASSGDKAYTTDSVLIKKTGSIKNTVDVLNEILPLTKSDAQKALKNSSYKFTDTEVSEILDATHPKVTNPDYLITYNRMTSIASVWSYFGNWDFNLPAGTSRSEREAGSFQGLQTYATNINDTLIVRSLIQQTAEYNIYTLIEVRNETLTGAMMAVTNDGQMQTQQLNMHKVKLMVNENGKSKMYNSLADPDGQLSLLIKVDKNSIIGTDGSNNPVYSSSSWMATANLEDSVYSKLHFFDGEGLDTIKLEKESLDPTANGVQPGFKVFSVDYGNYSK