wanglab/gogpt-training-data huggingface dataset:
Protein: FAD-dependent monooxygenase fmqB (EC 1.-.-.-) (Fumiquinazoline biosynthesis cluster protein B) (Q4WLW7)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the antitumor fumiquinazolines that confer a dual-usage capability to defend against phagocytes in the environment and animal hosts. The simplest member is fumiquinazoline F (FQF) with a 6-6-6 tricyclic core derived from anthranilic acid (Ant), tryptophan (Trp), and alanine (Ala). The trimodular NRPS fmqA is responsible for FQF formation. Modules 1, 2 and 3 of fmqA are predicted to activate and load Ant, Trp and Ala, respectively, providing for the assembly of an Ant-Trp-Ala-S-enzyme intermediate that would undergo double cyclization for chain release and generation of the tricyclic 6-6-6 product fumiquinazoline F. The presence of an E domain predicted for module 2 of fmqA is consistent with epimerization of L-Trp to D-Trp during assembly to generate the R-stereocenter at C14 of FQF. The FAD-dependent monooxygenase fmqB and the monomodular NRPS fmqC then maturate FQF to FQA. FmqB oxidizes the 2',3'-double bond of the indole side chain of FQF, and fmqC activates L-Ala as the adenylate, installs it as the pantetheinyl thioester on its carrier protein domain, and acylates the oxidized indole for subsequent intramolecular cyclization to create the 6-5-5-imidazolindolone of FQA. The FAD-linked oxidoreductase fmqD introduces a third layer of scaffold complexity by converting FQA to the spirohemiaminal FQC, presumably by catalyzing the formation of a transient imine within the pyrazinone ring. FQC subsequently converts nonenzymatically to the known cyclic aminal FQD.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24612080}.
Interaction partners:
- Nonribosomal peptide synthetase fmqA
- Nonribosomal peptide synthetase fmqC
- FAD-linked oxidoreductase fmqD
- MFS transporter fmqE
Sequence:
MKLPAAAGDAIVIGPNAVRLIKSWGEQLCEEIEPHLSNATHAEMLDHHDRFIVRHELAGRGKGWFTNRGRLISILYEHARKLGIDIRLGSRVTKYWEEDGRAGVIVNDRERLAADCVICADGVHSAARAWLTGQVDTQQHSGWANFRAHMTTEQLAKDPEASWVLQGTREKDRVYVWFGDGINLAIMTMKRGQELAWALMHTDKFNAHESWAGGRASIDDALATLSPWPGRLRPSSVIRHTLPEKLVDHALIYRPPLDTWVSAGGRVMLIGDAAHPYFPVVGQGGSQAIEDGVVVATALELAGKENVPLALRIRATLTEENNVLMEAGNSRYPRATVIQLGSSTLQEHLFWPDWEAVAKDPSVFAFPNPEWILGHDCREYTHQVFDTVVRAVRGEGEYIPRNIPADGAYRVEDTYSPE
Protein: Probable beta-glucosidase D (EC 3.2.1.21) (Beta-D-glucoside glucohydrolase D) (Cellobiase D) (Gentiobiase D) (Q5AUW5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Probable glucan endo-1,3-beta-glucosidase eglC
- Glycosyl hydrolases family 32 superfamily
- Probable beta-glucosidase K
- beta-glucosidase
- Probable beta-glucosidase H
- Probable beta-glucosidase J
- Beta-glucosidase B
- Probable beta-glucosidase I
- Endo-beta-1,4-glucanase A
Sequence:
MRVPSLSVLSFLLGTALAAASNFEAGLLSSGKVSLGDWKSAHEKASQFVAKLNTTEKIKLITGSSVTTTNGETFTALDILDGDMGAQAYYYVSAFSLSSALAMTWDKEAMYEQGRAIAAEFYGKGIQMVAGPTSQPLGRTPWGGRLVESFGPDPYLNGIATGLETRAYADVGVIAGAKHFILNEQETNRTGGMGGGGGAPGGGGMGRGAEFSSSVPGGMSPTSSAGAIPSSTSTPGGSGMGGGMAGSSAFSSSSSSGAPYSSNADDKTLHETYLWSFYDAVHSGLGGVMCAMTKVNGTLSCQSSSLLLDILKTELGFPGMVWPDTNGQQDALASAANGLDYGSSSLWSESTIEGYLESNNITEARLNDMAIRNLMGYYYVNLDNGTQPSTAAQDDYVDVRANHAKLIRSHGSKSMVLLKNKNNTLPLYKPHKMAIFGSHARAAVAGPNMQFSVEGSGPTYDGHIATDSGSGQASLPYLITPENALNIKASQDGTMLRWIANDTYSSSTGSALVMQGSSSTSVTPSVSAYSENMDVCLVFINALAGEGADRTELRNTDQDNLINEVADNCDNTVVVINTVGARILDSWIEHENVTAVLYGSLLGQESGNSIVDVLYGDVNPSGRLTYTIAKTESDYNVDICYTAQCNFTEGNYIDYRYFDAYNVTPRYEFGYGLSYTDFAYSNLHIQGPSALSTYPTGQLAVGGYEDLWDTVAKVTVTIRNAGSLDGAEVPQLYISYPDVAKQPVRQLRGFHNVYIKKGQSTKVTFELRRRDISYWDVQHQKWAVAPGTYEAWVGASSRDLRTHGSFVVKTKA
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1 (EC 3.1.4.11) (Phosphoinositide phospholipase C-zeta-1) (Phospholipase C-zeta-1) (PLC-zeta-1) (Q8K4D7)
Organism: Mus musculus (Mouse)
Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function.
Subcellular location: Nucleus {ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}. Note=Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronuclei at interphase following meiosis and mitosis. {ECO:0000269|PubMed:14701816, ECO:0000269|PubMed:15159452, ECO:0000269|PubMed:15385165, ECO:0000269|PubMed:15809052, ECO:0000269|PubMed:18322275}.
Interaction partners:
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
- Inositol polyphosphate multikinase
- Protein kinase C alpha type
- Inositol polyphosphate-5-phosphatase A.
- Protein kinase C gamma type
- Protein kinase C beta type
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- 1-phosphatidylinositol 3-phosphate 5-kinase
Sequence:
MESQLHELAEARWFLSKVQDDFRGGKINVEITHKLLEKLDFPCHFAHVKHIFKENDRQNQGRITIEEFRAIYRCIVHREEITEIFNTYTENRKILSENSLIEFLTQEQYEMEIDHSDSVEIINKYEPIEEVKGERQMSIEGFARYMFSSECLLFKENCKTVYQDMNHPLSDYFISSSHNTYLISDQILGPSDIWGYVSALVKGCRCLEIDCWDGSQNEPIVYHGYTFTSKLLFKTVVQAINKYAFVTSDYPVVLSLENHCSPGQQEVMASILQSTFGDFLLSDMLEEFPDTLPSPEALKFKILVKNRKVGTLSETHERIGTDKSGQVLEWKEVIYEDGDEDSGMDPETWDVFLSRIKEEREADPSTLSGIAGVKKRKRKMKIAMALSDLVIYTKAEKFRNFQYSRVYQQFNETNSIGESRARKLSKLRVHEFIFHTAAFITRVYPKMMRADSSNFNPQEFWNVGCQMVALNFQTPGLPMDLQNGKFLDNGGSGYILKPDILRDTTLGFNPNEPEYDDHPVTLTIRIISGIQLPVSSSSNTPDIVVIIEVYGVPNDHVKQQTRVVKNNAFSPKWNETFTFLIQVPELALIRFVVETQQGLLSGNELLGQYTLPVLCMNKGYRRVPLFSKSGANLEPSSLFIYVWYFRE
Protein: E3 ubiquitin-protein ligase RNF182 (EC 2.3.2.27) (RING finger protein 182) (RING-type E3 ubiquitin transferase RNF182) (Q8N6D2)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that mediates the ubiquitination of ATP6V0C and targets it to degradation via the ubiquitin-proteasome pathway. Also plays a role in the inhibition of TLR-triggered innate immune response by mediating 'Lys'-48-linked ubiquitination and subsequent degradation of NF-kappa-B component RELA.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:18298843, ECO:0000269|PubMed:31432514}.
Interaction partners:
Sequence:
MASQPPEDTAESQASDELECKICYNRYNLKQRKPKVLECCHRVCAKCLYKIIDFGDSPQGVIVCPFCRFETCLPDDEVSSLPDDNNILVNLTCGGKGKKCLPENPTELLLTPKRLASLVSPSHTSSNCLVITIMEVQRESSPSLSSTPVVEFYRPASFDSVTTVSHNWTVWNCTSLLFQTSIRVLVWLLGLLYFSSLPLGIYLLVSKKVTLGVVFVSLVPSSLVILMVYGFCQCVCHEFLDCMAPPS
Protein: EG:BACR25B3.2 protein (Q9NEF8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MANSKVVAHDESLQGINDSEWQLMGDDIDDGLLDDVDETLKPMETKSEEEDLPTGNWFSQSVHRVRRSINRLFGSDDNQERGRRQQRERSQRNRDAINRQKELRRRQKEDHNRWKQMRMERQLEKQRLVKRTNHVVFNRATDPRKRASDLYDENEASGYHEEDTTLYRTYFVVNEPYDNEYRDRESVQFQNLQKLLDDDLRNFFHSNYEGNDDEEQEIRSTLERVEPTNDNFKIRVQLRIELPTSVNDFGSKLQQQLNVYNRIENLSAATDGVFSFTESSDIEEEAIDVTLPQEEVEGSGSDDSSCRGDATFTCPRSGKTICDEMRCDREIQCPDGEDEEYCNYPNVCTEDQFKCDDKCLELKKRCDGSIDCLDQTDEAGCINAPEPEPEPEPEPEPEPESEPEAEPEPEPEPEPESEPEQEPEPQVPEANGKFY
Protein: E3 ubiquitin-protein ligase RNF25 (EC 2.3.2.27) (RING finger protein 25) (RING finger protein AO7) (Q96BH1)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NKD2 (By similarity). Stimulates transcription mediated by NF-kappa-B.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q7SXJ6}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 D2
- Ubiquitin-conjugating enzyme E2 D1
- E2 ubiquitin-conjugating enzyme
- Zinc finger protein 408
- Ubiquitin-conjugating enzyme E2 E3
Sequence:
MAASASAAAGEEDWVLPSEVEVLESIYLDELQVIKGNGRTSPWEIYITLHPATAEDQDSQYVCFTLVLQVPAEYPHEVPQISIRNPRGLSDEQIHTILQVLGHVAKAGLGTAMLYELIEKGKEILTDNNIPHGQCVICLYGFQEKEAFTKTPCYHYFHCHCLARYIQHMEQELKAQGQEQEQERQHATTKQKAVGVQCPVCREPLVYDLASLKAAPEPQQPMELYQPSAESLRQQEERKRLYQRQQERGGIIDLEAERNRYFISLQQPPAPAEPESAVDVSKGSQPPSTLAAELSTSPAVQSTLPPPLPVATQHICEKIPGTRSNQQRLGETQKAMLDPPKPSRGPWRQPERRHPKGGECHAPKGTRDTQELPPPEGPLKEPMDLKPEPHSQGVEGPPQEKGPGSWQGPPPRRTRDCVRWERSKGRTPGSSYPRLPRGQGAYRPGTRRESLGLESKDGS
Protein: Carbonic anhydrase (EC 4.2.1.1) (Carbonate dehydratase) (Q8SXB6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNLLYQLRDPDFASKLNRRLSPLRSWLCTHANTSLERFQEWRDAGMKDPLIFSSETPLRRFVAYIDEEQKFALEDKLSQINTLQQMSNIASYGFLKARLESHDLHIHALWFDIYTGDIYYFSRGAKRFLPVDEDTVDRLSEEVRRFYS
Protein: Integrin alpha V (Integrin alpha-V precursor) (Q3LTM3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
MGKHFVRCWLWALVALFTTKRAPAFNLDISKPTVFSGPPGSYFGFSVAFFNPDNSQFNILVGAPRANTSDQTPSAVTERGAVFSCPWQKSGTCTQIQFDSTDDRKHSNGQQMEFKSNQWFGATVRSSGDQILACAPLYQWSTYGFSEREPVGTCYLKKGNNIVEYSPCRSKSNSPEGQGFCQAGFSADFVKKNRVVIGGPGSFYWQGQLISDDVTEVINRYNKDFLTPYSNQLSTKPAGAQYDDSYLGYSVAVGDFNEDGEDDYVTGVPRGEKALGYVNIFNGRNMESMYNFTGTQMAAYFGHSVAAVDVNNDGKMDLFVGAPLFMDRGSDGKLREVGQVYVYLGKGGFTFNSVIKLTGSEIYARYGSSVCSVGDLNMDGYNDVAIAAPYGGPFHRGLVYIHNGRSTGPNPVASQVLEGTWASVSMPSSFGYSMNGGTDVDQNGYPDLIVGAFGADKAILYRARPVISVNTTLDISPQILNPEDKSCTLPGTATKVSCFTVKYCLKASGKGAPSSLLFQVDLTLDRLKHKGAIKRVLFLYNKMSHYSKNMTVNNNQGLACEELQAYLIDDSEFRDKITPISVFMEYSLDYKSAADKTGLLPILDQSAPTNVTKQAHILLDCGEDNICKPDLKLSVVSDQNEIYIGDDNPLTLEVTAENGGEGAYEADLIVTLPSQADFTAVVRNSETLSRLSCAFKKDNQTRVVVCDLGNPMKGGTKIVAGLRFSVHQLSEQDTEVKFGLQIQSTNQFNNTSNLVSVVTKLAVLAKVELRGVSAPEQVFLPIANWQPKENPVLEDDIGPLVQHIYELRNKGPSTFSKAILDVQWPYRFNNGSLLYITKFSVDGNMNCSSNRELNPLNVTSPRFLDQNDTSASGAEGRNRHNVHRRDLEEKHGEENLEILDCGNAECQEIKCFVGRLEKGQSAILFIYSRLAVNTFLKAESQNKSYIVRSSASFSVIEMPYKNLNPELPTSTQSASLKVIWNSENPQPVPGWVVALAVLAGLLLLALLIFVMYKLGFFNRVRPPQEDRTEKEQLQPQENGDRNTEA
Protein: Fibulin-1 (FIBL-1) (O42182)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Incorporated into fibronectin-containing matrix fibers. May play a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Could be important for certain developmental processes and contribute to the supramolecular organization of ECM architecture, in particular to those of basement membranes.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Heparan sulfate proteoglycan 2.
Sequence:
MDLYMIVLLSLCGLLRAQETTDTISLDNCCEDGKKRGLESQDCSSLPLISESTTCRVVQEQCCSAVLEDSICTSGINMAKDQSSCDALLSGSSTCETKTTKMCCECCLLGSSRCRIRVSPVSSVCRWSISRGPGVRSCCVDKQPAHGVQPSKGDAQNTEDQCRAAGCAQRCLNGTCSCLDGFKLKTDGKHCEDINECLLGPHHCVTGERCINTLGSYRCQREISCGTGYELTDNNKCKDIDECDLGTHNCAAEMECQNTAGSFRCRPRMQCAAGFIQDALGSCIDINECVSVTALSRGQMCFNTVGSFICQRHSVTCGRGYHLNAEGTRCVDIDECAGPDNSCDGHGCINLVGSYRCECRTGFIFNSISRSCEDIDECRNYPGRLCAHKCENILGSYKCSCTAGFKLADDGRNCDDVNECESSPCSQGCANVYGSYQSYCRRGYQLSDADGITCEDIDECALPTGGHICSYRCHNTPGSFHCTCPASGYTLAANGRSCQDIDECLTGTHSCSESESCFNIQGGFRCLSFDCPANYRRSGDTRPRVDRADIIRCVKSCQHNDISCVLNPILSHSHTAISLPTFREFNKPEEIVFLRSPTPTHLPHMDSPEIVYDILEGNIQNSFDIIKRLDHGMIVGVVKQVRPLVGPVRTVLKLAMNYVTNGVVSHRNIINVRIYVSEFWF
Protein: Uncharacterized protein (Q382A5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTGFDTVWIPFAVVYLLYQIPPTMMEVYSYYSRGGLVSIEDIKFDDTFTCHHQWLKDKDVYFKRFCDRPTSEAGKAFFSWLDWSAEAYDRSIYVLRRNHARRDGEVSFLKRYIYGPFVFNWSKKQWLRGDDSCGMRMPAWGVGGEERARAEFAAAKEKGFDKNWHYQIMRKIRREQALRTAKEVQAQ
Protein: Receptor-like kinase TMK2 (EC 2.7.11.1) (BARK1-like kinase 3) (Leucine-rich repeat receptor-like kinases TMK2) (Transmembrane kinase 2) (Q9FYK0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in auxin signal transduction and cell expansion and proliferation regulation.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Putative nucleolar protein 5-3
- Probable methyltransferase PMT2
- SAUR-like auxin-responsive protein family
Sequence:
MIAKNFLLLLCFIALVNVESSPDEAVMIALRDSLKLSGNPNWSGSDPCKWSMFIKCDASNRVTAIQIGDRGISGKLPPDLGKLTSLTKFEVMRNRLTGPIPSLAGLKSLVTVYANDNDFTSVPEDFFSGLSSLQHVSLDNNPFDSWVIPPSLENATSLVDFSAVNCNLSGKIPDYLFEGKDFSSLTTLKLSYNSLVCEFPMNFSDSRVQVLMLNGQKGREKLHGSISFLQKMTSLTNVTLQGNSFSGPLPDFSGLVSLKSFNVRENQLSGLVPSSLFELQSLSDVALGNNLLQGPTPNFTAPDIKPDLNGLNSFCLDTPGTSCDPRVNTLLSIVEAFGYPVNFAEKWKGNDPCSGWVGITCTGTDITVINFKNLGLNGTISPRFADFASLRVINLSQNNLNGTIPQELAKLSNLKTLDVSKNRLCGEVPRFNTTIVNTTGNFEDCPNGNAGKKASSNAGKIVGSVIGILLALLLIGVAIFFLVKKKMQYHKMHPQQQSSDQDAFKITIENLCTGVSESGFSGNDAHLGEAGNIVISIQVLRDATYNFDEKNILGRGGFGIVYKGELHDGTKIAVKRMESSIISGKGLDEFKSEIAVLTRVRHRNLVVLHGYCLEGNERLLVYQYMPQGTLSRHIFYWKEEGLRPLEWTRRLIIALDVARGVEYLHTLAHQSFIHRDLKPSNILLGDDMHAKVADFGLVRLAPEGTQSIETKIAGTFGYLAPEYAVTGRVTTKVDVYSFGVILMELLTGRKALDVARSEEEVHLATWFRRMFINKGSFPKAIDEAMEVNEETLRSINIVAELANQCSSREPRDRPDMNHVVNVLVSLVVQWKPTERSSDSEDIYGIDYDTPLPQLILDSCFFGDNTLTSIPSRPSELESTFKSGQGR
Protein: ATP-dependent RNA helicase DHX30 (EC 3.6.4.13) (DEAH box protein 30) (Q7L2E3)
Organism: Homo sapiens (Human)
Function: RNA-dependent helicase. Plays an important role in the assembly of the mitochondrial large ribosomal subunit. Required for optimal function of the zinc-finger antiviral protein ZC3HAV1 (By similarity). Associates with mitochondrial DNA. Involved in nervous system development and differentiation through its involvement in the up-regulation of a number of genes which are required for neurogenesis, including GSC, NCAM1, neurogenin, and NEUROD (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29100085}. Mitochondrion {ECO:0000269|PubMed:16825194, ECO:0000269|PubMed:29100085}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:16825194, ECO:0000269|PubMed:18063578, ECO:0000269|PubMed:25683715}. Note=Localizes to mitochondrial RNA granules found in close proximity to the mitochondrial nucleoids (PubMed:16825194, PubMed:25683715). Relocalizes to stress granules upon heat stress (PubMed:29100085). {ECO:0000269|PubMed:16825194, ECO:0000269|PubMed:25683715, ECO:0000269|PubMed:29100085}.
Interaction partners:
- DNA-directed RNA polymerase, mitochondrial
- G-rich sequence factor 1
- Probable ATP-dependent RNA helicase DDX28
- FAST kinase domain-containing protein 3
- Small ribosomal subunit protein mS39
- Single-stranded DNA-binding protein, mitochondrial
- FAST kinase domain-containing protein 2
Sequence:
MFSLDSFRKDRAQHRQRQCKLPPPRLPPMCVNPTPGGTISRASRDLLKEFPQPKNLLNSVIGRALGISHAKDKLVYVHTNGPKKKKVTLHIKWPKSVEVEGYGSKKIDAERQAAAAACQLFKGWGLLGPRNELFDAAKYRVLADRFGSPADSWWRPEPTMPPTSWRQLNPESIRPGGPGGLSRSLGREEEEDEEEELEEGTIDVTDFLSMTQQDSHAPLRDSRGSSFEMTDDDSAIRALTQFPLPKNLLAKVIQIATSSSTAKNLMQFHTVGTKTKLSTLTLLWPCPMTFVAKGRRKAEAENKAAALACKKLKSLGLVDRNNEPLTHAMYNLASLRELGETQRRPCTIQVPEPILRKIETFLNHYPVESSWIAPELRLQSDDILPLGKDSGPLSDPITGKPYVPLLEAEEVRLSQSLLELWRRRGPVWQEAPQLPVDPHRDTILNAIEQHPVVVISGDTGCGKTTRIPQLLLERYVTEGRGARCNVIITQPRRISAVSVAQRVSHELGPSLRRNVGFQVRLESKPPSRGGALLFCTVGILLRKLQSNPSLEGVSHVIVDEVHERDVNTDFLLILLKGLQRLNPALRLVLMSATGDNERFSRYFGGCPVIKVPGFMYPVKEHYLEDILAKLGKHQYLHRHRHHESEDECALDLDLVTDLVLHIDARGEPGGILCFLPGWQEIKGVQQRLQEALGMHESKYLILPVHSNIPMMDQKAIFQQPPVGVRKIVLATNIAETSITINDIVHVVDSGLHKEERYDLKTKVSCLETVWVSRANVIQRRGRAGRCQSGFAYHLFPRSRLEKMVPFQVPEILRTPLENLVLQAKIHMPEKTAVEFLSKAVDSPNIKAVDEAVILLQEIGVLDQREYLTTLGQRLAHISTDPRLAKAIVLAAIFRCLHPLLVVVSCLTRDPFSSSLQNRAEVDKVKALLSHDSGSDHLAFVRAVAGWEEVLRWQDRSSRENYLEENLLYAPSLRFIHGLIKQFSENIYEAFLVGKPSDCTLASAQCNEYSEEEELVKGVLMAGLYPNLIQVRQGKVTRQGKFKPNSVTYRTKSGNILLHKSTINREATRLRSRWLTYFMAVKSNGSVFVRDSSQVHPLAVLLLTDGDVHIRDDGRRATISLSDSDLLRLEGDSRTVRLLKELRRALGRMVERSLRSELAALPPSVQEEHGQLLALLAELLRGPCGSFDVRKTADD
Protein: Endoplasmic reticulum aminopeptidase 1 (EC 3.4.11.-) (ARTS-1) (Adipocyte-derived leucine aminopeptidase) (A-LAP) (Aminopeptidase PILS) (Puromycin-insensitive leucyl-specific aminopeptidase) (PILS-AP) (Q9JJ22)
Organism: Rattus norvegicus (Rat)
Function: Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- TAP binding protein
- Interleukin-23 receptor
Sequence:
MPSLLSLVLTFLAVSSPSCCQNSDTASPKASNGASFPWNNMRLPEYITPIHYDLMIHANLSTLTFWGKTEVEITVSQPTSTIIMHSHQLQISKATLRRGAEEMLPEEPLKLMEYSAHEQVALLTAQPLLAGSVYTVIITYAANLSENFHGFYKSTYRTQEGERRILAATQFEPTAARMAFPCFDEPALKASFSIKIKRDPRHLAISNMPLVKSVTVAEGLIEDHFDITVKMSTYLVAFIISDFKSVSKMTKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLYDKEKSSASSKLGITMTVSHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVTVTHPELKVEEYFFGKCFNAMEVDALNSSHPVSTPVENPAQIREMFDEVSYEKGACILNMLRDYLSADTFKRGIVQYLQKYSYKNTKNEDLWNSMMHICPTDGTQTMDGFCSRNQHSSSTSHWRQEVIDIKSMMNTWTLQKGFPLITITVRGRNVHLKQEHYMKGSECFPETGSLWHVPLTFITSKSDSVQRFLLKTKTDVIILPEAVEWIKFNVGMNGYYIVHYGDDGWASLNGLLKEAHTTISSNDRASLINNAFQLVSIGKLSIEKALDLILYLKNETEIMPIFQGLNELIPMYKLMEKRDMVEVETQFKDFLLRLLKDLINKQTWTDEGSVSERMLRSQLLLLACVHRYQLCVQRAERYFREWKASNGNMSLPIDVTLAVFAVGAQNTEGWDFLYSKYQSSLSSTEKSQIEFSLCISQDPEKLQWLLDQSFKGEIIKTQEFPHILTLIGRNPVGYPLAWKFLKENWNKIVQKFELGSSSIAHMVMGTTNQFSTRARLEEVKGFFSSLKKNGSQLRCVQQTIETIEENIRWMDKNFDKIRLWLQKERQELL
Protein: Zcf30p (Q5A3L9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MPPKEDKKEKRTKPCCNCKRSKVKCVYTSSLPCERCVKTGQAATCQFVPKLPSFKLPSIDSNNHATRLPSTTPVLNAPSTFTPSLNNSGPLPSHLINSNLHNPIPALIPTHSSMNTQVYNNSASPPTLQNASDTAWKSQIEHRLSGFDSKIDNLVEMLKVNQQFVMNNQMQFLQQQQQQQQQQQQQYSISERQENYPSGYLTNGNSSQHVDTHRTELNSKLIGDSNESQKRKPEISETRHESPKKRKFQTEFSHDFRDGFLTKKDAHELFHFFDANISQQLFGFEISKFDVDEIWDSCPILVCAISTIASIHHPKLSTKSKQLQVYLHNLCGSIILNKPRNEQDGFNTIVALILCSFWLSDSQMFTGLALQLAKEYGLNQPNQKNKDKLKLWYLLYVLDGQQSLTFNRQPLLNSQEYSLKHSKELLLGEKGNKLSDSKSKALIKNKNKSNSKPLTDEEISKLMAKQRLTDMRLVSQVEYNQAINEAFKGTAWDLLAPASFGIPSKSNLELDRWMVSWTVLLSPESFGAIWSTKSTLIYYNFAKMHINSSAVRKITLDPNNGQFPKLDTSLSHNSTSNCSNNTLAVKKQQPNYDSEDSSDDEFDEDEFISNKELVSPDEAVINANIALNAAQTVLNLVINDKDILDNLKYVPVHIHIMLYYASLLLINPPKRSNNQTVQMNDIDYYDNLLNNLKVVRILQRKIYMNLPIDSSFGNRLIKNLQDVLGEKLHEIQIFVDELPDDHVEKHQLRTKVNALFESSENKFEEITEYEVSSSGASSKSTTPLPEKISAWPGSNHGHP
Protein: Lung seven transmembrane receptor family protein (Q9C9E6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLLHLLLLLCLSSSLKVQASVHEYRSERFVSKGNAFVFHGGSEGIYSSSPSDNFTSDSDSVSFIRFEKIKFQRPEEVSNRSSLSIHAVVFEVEDRENIGGSAYGGQRAVCCTSDLAKLGVCSHGDVIYRPSAKDSGWPQVFGVSLAENEFSVILPTRSIQVTRTGMYNLYFIHCDSDLKDLVVEGKTIWKNPTGYLPGRMAPLMYFYGFMSLAFVLLGIFWFSQCARFWREVLPLQNCLTLVITLGMCEMALWYFDYAEFNETGIRPTVITIWAVTFGSIKRTSARIIILMVSMGYGVVRPTLGGFTSKVIMLGVTFFIASEILELMENVGAVSDLSGKARLFFVLPVAILDAFFIIWIFKSLSATFKKLQTRRLLVKLDIYRKFTNALAVDILVSLGWICYELYFKSKDVYNEHWQNAWIIPAFWQLLSFSLLIVICSLWAPSQNSTRYAFSGSSGDTSAEFEKDDYTLTLIKPSPIPSHEVKNLSETRLLPADEGEPEKDLEEDKRE
Protein: Olfactomedin 1a (A2AWU2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSVPLLKIGVVLSTMAMITNWMSQTLPSLVGLNSTKLSVAPPGVPDRSTGVLPANPEESWQVYSSAQDSEGRCVCTVVAPQQTMCSRDARTKQLRQLLEKVQNMTQSIQNLDQRTQKDLQYVQRMEVQLRGLETKFKQVEESHKQNIAKQYKG
Protein: Myomegalin (Phosphodiesterase 4D-interacting protein) (Q80YT7)
Organism: Mus musculus (Mouse)
Function: Functions as an anchor sequestering components of the cAMP-dependent pathway to Golgi and/or centrosomes (By similarity).
Subcellular location: [Isoform 2]: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q5VU43}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5VU43}. Golgi apparatus {ECO:0000250|UniProtKB:Q5VU43}. Note=Associated with the microtubule network at the growing distal tip of microtubules. Targeting to the Golgi apparatus requires AKAP9. {ECO:0000250|UniProtKB:Q5VU43}.
Interaction partners:
- A-kinase anchor protein 9
- 3',5'-cyclic-AMP phosphodiesterase 4D
Sequence:
MSNGYRTLSQHLNDLKKENFSLKLRIYFLEERMQQKYEVSREDVYKRNIELKVEVESLKRELQDRKQHLDKTWADAEDLNSQNEAELRRQVEERQQETEHVYELLGNKIQLLQEEPRLAKNEATEMETLVEAEKRCNLELSERWTNAAKNREDAAGDQEKPDQYSEALAQRDRRIEELRQSLAAQEGLVEQLSQEKRQLLHLLEEPASMEVQPVPKGLPTQQKPDLHETPTTQPPVSESHLAELQDKIQQTEATNKILQEKLNDLSCELKSAQESSQKQDTTIQSLKEMLKSRESETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEGIAPAQQQVALLDLQSALFCSQLEIQRLQRLVRQKERQLADGKRCVQLVEAAAQEREHQKEAAWKHNQELRKALQHLQGELHSKSQQLHVLEAEKYNEIRTQGQNIQHLSHSLSHKEQLIQELQELLQYRDNADKTLDTNEVFLEKLRQRIQDRAVALERVIDEKFSALEEKDKELRQLRLAVRDRDHDLERLRCVLSANEATMQSMESLLRARGLEVEQLTATCQNLQWLKEELETKFGHWQKEQESIIQQLQTSLHDRNKEVEDLSATLLCKLGPGQSEVAEELCQRLQRKERMLQDLLSDRNKQAVEHEMEIQGLLQSMGTREQERQAAAEKMVQAFMERNSELQALRQYLGGKELMTSSQTFISNQPAGVTSIGPHHGEQTDQGSMQMPSRDDSTSLTAREEASIPRSTLGDSDTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAMQEEELQVQAADLESLTRNVQIKEDLIKDLQMQLVDPEDIPAMERLTQEVLLLREKVASVEPQGQEVSGNKRQQLLLMLEGLVDERSRLNEALQAERQLYSSLVKFHAQPENSERDGTLQVELEGAQVLRTRLEEVLGRSLERLSRLESLAAIGGGELESVQAQEMLHLRAEIHQHLEEKRKAEVELKELKAQIEEAGFSSVSHISRNTMLSLCLENAELKEQMGEAMSDGWEVEEDKEKGEVMLETVVAKGCLNENSLQAEFRKVQGKLKSAYNIINLLKEQLLLRSSEGNSKEMPELLVRLAREVDRMNTGLPSLGKHQHQEQENTTTARPGSRPQSLPLGAALSVDGYQLENKSQAQDSGHQPEFSLPGSTKHLRSQLAQCRQRYQDLQEKLLISEATVFAQANQLEKYRAVFSESLVKQDSKQIQVDLQDLGYETCGRSENEAEREETTSPECEEHNNLRPVVLMEGLCSEQGYLDPVLVSPPAKKPLENKPGKQEEFRAHGTPDDSSLLRKDIRDLKAQLQNANKVIQNLRSRVRSLSATSDYSSSLERPRKLRAVATLEGASPHSVTDEDEGWLSDGTGAFYPPGLQAKKDLESLIQRVSQLEAQLPKTGLEGKLAEELRCASWPGKYDSLIQDQARELSYLRQKIREGRGICYLLTQHAKDTVKSFEDLLRSNDIDYYLGQSFREQLAQGGQLTERLTSKLSTKDHKSEKEEAGLEPLALRLSRELQEKEKVIEVLQAKLDTRSLSPPSSHAVSDSHRSASTTSFLSDDIEACSDMDVASEYTHYDEKKPSPSHSAASASQGLKGESSSSPISLPTPQNPPKEASQAHPGFHFHSIPKPASLSQTPMHSALPSFVPFSPSGPPLLGCCETPMVSLAEAQQELQMLQKQLGESVSIAPPASTSTLLSNQTEASSPHYINPAQPHTPTRSTIELGRILEPGYLGSSGQWDMMRPQKGSVSGELSSGSSMYQLNSKPTGADLLEEHLGEIRNLRQRLEESICVNDRLREQLQHRLSSTARENGSTSHFYSQGLESMPQLYNENRALREENQSLQTRLSHASRGHSQEVDHLREALLSSRSQLQELEKELEQQKAERQQLSLQSELQIYESLCENPKKALKAFSLDSCHQVPGELSCLVAEIRALRGQLEQSIEVNNRLRLQLEQQMDRGAGKASLGPIAVGQSFPDKAEPANLHQGSAASPPVRDVGLNSPAMVLPNSSCSAPGSDHAIVTRTNNELSSDDSAAMKNPPKLEVDATDGPFANKHGRHVIGHVDDYDALQQQIGEGKLLIQKILSLMRSARSIPGQEAQDTEAPGNISAHELRSSAKALNHALEESTSLLNMFWRAALPNTHGPVLVGKEGQLMEKELLDLRAQVSQQEQILQNTAARLKRANQRKKSMEQFIVSHLTRTHDVLKKARTNLEMKSFRALTCTPAL