wanglab/gogpt-training-data huggingface dataset:
Protein: Acetylornithine aminotransferase, mitochondrial (ACOAT) (EC 2.6.1.11) (P18544)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: catalyzes the conversion of N-acetylglutamate-gamma-semialdehyde (NAGSA) to N-acetylornithine in arginine biosynthesis.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:205532}.
Interaction partners:
- Protein ARG5,6
- Arginine biosynthesis bifunctional protein ArgJ, mitochondrial
- Ornithine carbamoyltransferase
- Argininosuccinate synthase
- Argininosuccinate lyase
- Arginase
- Amino-acid acetyltransferase, mitochondrial
- Carbamoyl phosphate synthase arginine-specific small chain
- Carbamoyl phosphate synthase arginine-specific large chain
- Inositol polyphosphate multikinase
Sequence:
MFKRYLSSTSSRRFTSILEEKAFQVTTYSRPEDLCITRGKNAKLYDDVNGKEYIDFTAGIAVTALGHANPKVAEILHHQANKLVHSSNLYFTKECLDLSEKIVEKTKQFGGQHDASRVFLCNSGTEANEAALKFAKKHGIMKNPSKQGIVAFENSFHGRTMGALSVTWNSKYRTPFGDLVPHVSFLNLNDEMTKLQSYIETKKDEIAGLIVEPIQGEGGVFPVEVEKLTGLKKICQDNDVIVIHDEIQCGLGRSGKLWAHAYLPSEAHPDIFTSAKALGNGFPIAATIVNEKVNNALRVGDHGTTYGGNPLACSVSNYVLDTIADEAFLKQVSKKSDILQKRLREIQAKYPNQIKTIRGKGLMLGAEFVEPPTEVIKKARELGLLIITAGKSTVRFVPALTIEDELIEEGMDAFEKAIEAVYA
Protein: Mannosylglycerate hydrolase MGH1 (EC 3.2.1.170) (D8QTR2)
Organism: Selaginella moellendorffii (Spikemoss)
Function: Catalyzes the hydrolysis of alpha-D-mannosyl-glycerate (MG) to D-glycerate and D-mannose. Can also hydrolyze alpha-D-glucopyranosyl-glycerate (GG)with lower efficiency.
Interaction partners:
Sequence:
MAGPVRCLPPVVEATSIPHAPPVISKEVSEIVNNMLSVAIPAAAAASAQDQRFASQFRCGPEFTTMKAQALEACRKILAENDQGGYTIPAKGLYPYQWNWDSALVSLGLAEMEEERAWEELDRLMSAQWEDGMVPHIVFHKPSSTYFPGPEIWGSPDKPRNTTGITQPPVAAISVRRLLEEAKDKALALAMARKLFPKLLAWHRWFYRARDPEGTGLVATIHPWETGMDNSPAWDEALARVPIDDIPPYVRRDLGHVDAKMRPQKAEYDRYLTLLYRFRALDYDEAKLYYETPFRVTDLCTNCILHKANEDLLWLAGATGACTDESEIRGWTARANVAFDTLFDVEAGLYRCKDQLTGQFLPAATSAGFLPLFAGVASGEKASAVARTLGRWLDDVAYGIPSCDPRDPQFEALRYWRGPVWLIVNWMVSEGLKRYGYGELAQRVERDSYELVKNGGIFEYYCPLTGMGAGGGCFSWTAAMCLAWLFKT
Protein: Transcription factor GAMYB (OsGAMyb) (Q0JIC2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcriptional activator of gibberellin-dependent alpha-amylase expression in aleurone cells. Involved in pollen and floral organs development. May bind to the 5'-TAACAAA-3' box of alpha-amylase promoter. Required for anther development. Functions in parallel with UDT1 to regulate early anther development. Functions upstream of the transcription factor TDR and may positively regulate its transcription. Required for pollen development. Probably required for controlling tapetal cell size and promoting tapetal programmed cell death (PCD) during anther development. Required for exine and Ubisch body formation in anthers. Interacts with the DNA specific motifs of giberrellin-up-regulated genes of anthers and regulates their expression. Positively regulates the expression of the laurate hydroxylase CYP703A3, known to be essential for the development of pollen exine and anther epicuticular layer. Functions with MYBS1 to integrate diverse nutrient starvation and gibberellin (GA) signaling pathways during germination of grains. Sugar, nitrogen and phosphate starvation signals converge and interconnect with GA to promote the co-nuclear import of GAMYB and MYBS1, resulting in the expression of a large set of GA-inducible hydrolases, transporters and regulators that are essential for mobilization of nutrient reserves in the endosperm to support seedling growth.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MYRVKSESDCDMIHQEQMDSPVADDGSSGGSPHRGGGPPLKKGPWTSAEDAILVDYVKKHGEGNWNAVQKNTGLFRCGKSCRLRWANHLRPNLKKGAFTAEEERLIIQLHSKMGNKWARMAAHLPGRTDNEIKNYWNTRIKRCQRAGLPIYPTSVCNQSSNEDQQCSSDFDCGENLSNDLLNANGLYLPDFTCDNFIANSEALPYAPHLSAVSISNLLGQSFASKSCSFMDQVNQTGMLKQSDGVLPGLSDTINGVISSVDQFSNDSEKLKQAVGFDYLHEANSTSKIIAPFGGALNGSHAFLNGNFSASRPTSGPLKMELPSLQDTESDPNSWLKYTVAPALQPTELVDPYLQSPAATPSVKSECASPRNSGLLEELIHEAQTLRSGKNQQTSVISSSSSVGTPCNTTVLSPEFDMCQEYWEEQHPGPFLNDCAPFSGNSFTESTPPVSAASPDIFQLSKVSPAQSTSMGSGEQVMGPKYEPGDTSPHPENFRPDALFSGNTADPSVFNNAIAMLLGNDLSIDCRPVLGDGIMFNSSSWSNMPHACEMSEFK
Protein: RING-H2 finger protein ATL2 (EC 2.3.2.27) (Protein ARABIDOPSIS TOXICOS EN LEVADURA 2) (Protein ATL2) (RING-type E3 ubiquitin transferase ATL2) (Q8L9T5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the early steps of the plant defense signaling pathway.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- At2g15580
- At1g23710
- At1g32920/F9L11_25
- Zinc finger CCCH domain-containing protein 29
- Probable WRKY transcription factor 40
Sequence:
MNSNDQDPIPFRPEDNNFSGSKTYAMSGKIMLSAIVILFFVVILMVFLHLYARWYLLRARRRHLRRRSRNRRATMVFFTADPSTAATSVVASRGLDPNVIKSLPVFTFSDETHKDPIECAVCLSEFEESETGRVLPNCQHTFHVDCIDMWFHSHSTCPLCRSLVESLAGIESTAAAREREVVIAVDSDPVLVIEPSSSSGLTDEPHGSGSSQMLREDSGRKPAAIEVPRRTFSEFEDELTRRDSPASQSFRSPMSRMLSFTRMLSRDRRSASSPIAGAPPLSPTLSCRIQMTESDIERGGEESR
Protein: CSN8/PSMD8/EIF3K domain-containing protein (Q381P3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNA-binding protein, putative
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit 7-like protein
- Eukaryotic translation initiation factor 3 subunit 8, putative
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit A
- Translation initiation factor, putative
- Eukaryotic translation initiation factor 3 subunit E
- 40S ribosomal protein S15, putative
- 40S ribosomal protein S8
Sequence:
MNQDLDKELREALQQDKYDLQLFLRFLKSYVVSGSQPEKQLLLGILLQALPRFHTSDFSACISLISSHVQDASYIEKDIILIYDLENYLSSGNFPQFWQVWRESEGTLPARPSFEPNMRAAILTVIGCTLGHIQTKDLSVYLGLKSGEKLEEVLREAARIAGDAVQLVGADEQAVVFQKSVFNAPESDSNQELKRFSDTVTIVSL
Protein: Archaemetzincin (EC 3.4.-.-) (O29917)
Organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
Function: Probable zinc metalloprotease whose natural substrate is unknown.
Interaction partners:
- Zinc metalloprotease
- Pheromone shutdown protein
Sequence:
MKIYIQPLSVNSHTVEVLANSLPKIFNAEVFVLPASDVSLKCYNASRRQYNSTCILRMLPPIKVTLGVTGKDIYAKGMNFVFGEAELGGARAVLSVFRLTTADSELYRERVVKEAVHEIGHVLGLKHCSNNCVMRFSNSVQDVDRKPVSFCRECASKIRY
Protein: Cell wall protein 1 (Surface antigen protein 1) (Wall protein 1) (G1UB63)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Heme-binding protein involved in heme-iron utilization. The ability to acquire iron from host tissues is a major virulence factor of pathogenic microorganisms. Required for biofilm formation.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:10652105, ECO:0000269|PubMed:19555771, ECO:0000269|PubMed:23243062, ECO:0000269|PubMed:23728625}. Membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Cell wall protein IFF4
Sequence:
MLPSIVISIVLASFVSAESSITEAPTTTAEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSICSVAGVWDPYWMVPANVQSSLSAAATAVASSSEQPVETSSEPAGSSQSVESSQPAETSSSEPAETSSSEPAETSSETSSEQPASSEPAETSSEESSTITSAPSTPEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSICSVAGVWDPYWMVPANVQSSLSAAATAVPSSSEQSVETSSESAESSQSVESSQPAETSSEQPSETSSETSSQQLSSITSAPDSSATSSSSTTSTFIRTASINGFADKLYDQLPECAKPCMFQNTGITPCPYWDAGCLCVMPQFAGAIGSCVADSCKGQDIVSVTSLGTSVCSVAGVNAPYWMLPASVKSSLSVAATAVPTSDSASETASQEPSETSSEQPSETASQQPAETSSEESSTITSAPSTPEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGSSICSVAGVWDPYWMLPANVQSSLNAAATAVATSDSASEVASASESASQVPQETSAASSQSANNSVASAAPSNSSVSAAPSSNSSGVPAAPSNNSSGASVVPSQSANNSSASAAPSNNSSSAISESVAPSSYGNSTIAQPSTSTKSDAASITGPITTDKVITNESGIVFTSTVIITHVSEYCDQTSAAAVQSSACEEQSSAKSEQASASSEQVKVITSVVWCESSIQSIESVKTSAEAAHKTEVIASCASELSSLSSAKSEAMKTVSSLVEVQKSAVAKQTSLAAVQSSAASVQLSAAHAQKSSEAVEVAQTAVAEASKAGDEISTEIVNITKTVSSGKETGVSQATVAANTHSVAIANMANTKFASTMSLLVASFVFVGLFI
Protein: Putative purine nucleoside phosphorylase (PNP) (EC 2.4.2.1) (Inosine phosphorylase) (Inosine-guanosine phosphorylase) (Q9UTG1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine and inosine (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Adenine phosphoribosyltransferase
- Adenine deaminase
- Adenosine kinase
- Uncharacterized protein C24B11.05
- Uncharacterized deaminase C1683.02
- Probable guanine deaminase
- IMP-specific 5'-nucleotidase 1
- Probable nicotinate phosphoribosyltransferase
- Uracil phosphoribosyltransferase 2
- Putative uracil phosphoribosyltransferase urg2
Sequence:
MTATSFLHQAKQQPHHTEPYIKALEAREYIIEQVPEELSKPKVAIICGSGLGTLASGLSAPVYEVPYEDIPHFHVSHVPGHASKLYFAFLGEKRVPTMILAGRYHSYEGYPIEATTFPVRLMKVMGVEVMVVTNAAGGLNQGFKVGDLMILKDHINFPGLAGMNPLRGPNAHEFGVRFPPLSDAYDLELRKLVYDAAKAHKVSRTIHEGCYAFVSGPCFETRAESRMLALMGADCVGMSTVPEVVVARHCGIRVLAISLVTNNVVVEESPSAKDLVEVDSNVMSKGAANHLEVLEVGIAAAADVRTMVETIVNFI
Protein: Protein lifeguard 2 (Fas apoptotic inhibitory molecule 2) (Neural membrane protein 35) (Q8K097)
Organism: Mus musculus (Mouse)
Function: Antiapoptotic protein which protects cells uniquely from Fas-induced apoptosis. Regulates Fas-mediated apoptosis in neurons by interfering with caspase-8 activation. Plays a role in cerebellar development by affecting cerebellar size, internal granular layer (IGL) thickness, and Purkinje cell (PC) development.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Membrane raft {ECO:0000269|PubMed:17635665}. Postsynaptic cell membrane {ECO:0000250}.
Interaction partners:
- Bcl-2-like protein 1
- Protein transport protein Sec16B
Sequence:
MTQGKLSVANKAPGTEGQQHQANGEKKDAPAVPSAPPSYEEATSGEGLKAGTFPQGPTAVPLHPSWAYVDPSGSSGYEGGFPAGHHEHFTTFSWDDQKVRRLFIRKVYTILLVQLLVTLAVVALFTFCDVVKDYVQANPGWYWASYAVFFATYLTLACCSGPRRHFPWNLILLTIFTLSMAYLTGMLSSYYNTTSVLLCLVITALVCLSVTIFSFQTKFDFTSCQGVLFVLLMTLFFSGLLLAVLLPFQYVPWLHAVYAVLGAGVFTLFLAFDTQLLMGNRRHSLSPEEYIFGALNIYLDIIYIFTFFLQLFGTNRE
Protein: Regulator of free ubiquitin chains 1 (Q08003)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Inhibitor of the DOA4 deubiquitinase involved in the regulation of protein degradation by the proteasome and maintenance of a normal level of free ubiquitin.
Subcellular location: Endosome {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Vacuolar-sorting protein BRO1
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin
- NEDD8-like protein RUB1
- Ubiquitin carboxyl-terminal hydrolase 4
- Vacuolar protein-sorting-associated protein 24
- 26S proteasome regulatory subunit RPN10
- 26S proteasome regulatory subunit RPN2
- 26S proteasome regulatory subunit RPN9
- 26S proteasome regulatory subunit RPN7
Sequence:
MKSSKQLVQDAKDYRFNPAIPLRIYLKTCIGILEKAQCAFQANDLSLSFIYYFRYVDLLTNKLSRHPELLRMDASSSSSSSYIHKREYLQLIKLEVPAVCKIIESLRTQIDSQYSKLQTSLANNIAKPNINANTTPVQVEQQPLPKKSFDEYSFNQSISFFQKISNAQLNTGASSQSQATARDEAYRLNYPELPRLTFST
Protein: F-box protein At1g10780 (Q9SAC4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDSLPDAILQYILSYLTSARDVAACNCVSKRWKESTDSVKSVVFHRNSFESIMETDDSDSIVRKMISSSRRLEELVVYSPFTSSGLASWMMHVSSSLRLLELRMDNLASEEVVVEGPLKLDCIGVAKNLEILKLWGVLMMSPPKWDMFPNLRSLEIVGAKMDDSSLSHALRACPNLSNLLLLACEGVKSISIDLPYLEHCKLDFYGQGNTLLVLTSQRLVSLDVQGCSWIRVPETKFLKNLSISSVTGRVYMVDFNNLSSLEALSIRGVQWCWDAICMILQQARDVKHLFMKVEFTGNEALQPFPEIDFVEFFNNHPKLQTFDIHGAMFAALCQKNSLKKLETGFTIPCLEEVVITVRSPLNAEQKMNTLESLVKYARGLKRMVIRILRMKSNHSSADDFCDDICKFRHMNEHLVHIE
Protein: Acyl-acyl carrier protein thioesterase ATL1, chloroplastic (EC 3.1.2.-) (Acyl-ACP thioesterase ATL1) (Acyl-lipid thioesterase 1) (Q9C7I5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acyl-ACP thioesterase involved in the production of fatty acids and beta-keto fatty acids. Can produce fatty acids of medium to long chain (12:0, 14:1, 14:0, 16:1 and 16:0) when expressed in a heterologous organism (E.coli). Possesses thioesterase activity toward lauroyl-ACP (12:0-ACP) in vitro. May play a role in cuticular wax synthesis.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:24214063}.
Interaction partners:
- RING-H2 finger protein ATL3
- At5g23680
- Omega-amidase, chloroplastic
- Protein ALUMINUM SENSITIVE 3
- Probable sodium/metabolite cotransporter BASS1, chloroplastic
- ABC transporter-like protein
Sequence:
MLKATGTVAPAMHVVFPCFSSRPLILPLRSTKTFKPLSCFKQQGGKGMNGVHEIELKVRDYELDQFGVVNNAVYANYCQHGQHEFMETIGINCDEVSRSGEALAVSELTIKFLAPLRSGCKFVVKTRISGTSMTRIYFEQFIFKLPNQEPILEAKGMAVWLDKRYRPVCIPSYIRSNFGHFQRQHVVEY
Protein: Glutathione S transferase T2 (EC 1.11.1.9, EC 2.5.1.18) (A1Z7X7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Glutathione S transferase O1
- Bifunctional glutamate/proline--tRNA ligase
- Glutathione S transferase O2, isoform A
- Glutathione S transferase O3
- Glutathione S transferase E11, isoform A
- Glutathione S transferase E2
- Glutathione S transferase E6
- Glutathione S transferase E13, isoform A
- FI01423p
- Inactive glutathione S-transferase D3
Sequence:
MSKPIRFYYDLLSPIARGLWIGLKFSNSPVEYCPIALRKFEQLTDEYKKINRFQKVPAIVGGDFHLSETIAIIRYLADKGQFDEKLYPKTLENRARVDEFLEWQHLNIRLACSMYFRDAWLFPMNGIAPKPKPEQIQALIEGVENNLGLLERLWLENDFLVGKNLTMADILGSSEINQLRLCQYRVDEKKFPKVVKWLERVRVSANPYHDEGLTFIDRKSKQSTAAKL
Protein: Putative uncharacterized protein DDB_G0284097 (Q54Q48)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MNNRGGFSHPPGKFHMRGSKTYTPRNGGQGQGQPQQAAPAFDQQQQQQQQQQQQQQQQQQNFDQQQQQPQQPQQQQGGNNYYFQSKFGNKSHRGGYHGNGNGNNNGNNNNNNTSPNLNSTSHNNNNNNNNNNNNNNNNNNNTHFTNSRGGHRGGSSRGGSSRGGNSGSSRGGSRGGYRGQSSFYNSSYQKSGPRLLTSIVSLPPFSGGAIIGVKGSLWGLLNKATTARLKVFKNTAIIKCADAQQLDRAKEIVLKLKNTSPKYLSLIDYKGEQKIKFVHQPSFSEVILESGAIDPLATDGVQLMQDLINSHESQYVARLNETFSTLYSEKGSSTPFIDIEAGKIWYLHSSNIPSTPMTADKYELYTESLASVFQPSNVINEQFITSSQYKLFKQKKQFTFISVLDTESLDLLCIKCSEEKITPTTTTTTNTQQSPNSDSSEYKFTDPFIYKLNHINSSKVLFPQIKSGSDLRVTIDTHSKSKLVSGTGQHQYDNLIKFIDSIKIHKNSSGNNTYQIPDSNLFMTESIITRKVLMYRSDDNSLQFHVNEDIATRYTTSTPEVNRESTTVFCTSPALYDLFKSKNWTVDQASDELKKLSKNLRLLVSKHLDSTKFQPPSADHTTQFEQDDEEEEN
Protein: UPF0450 protein C17orf58 (Q2M2W7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTARAFWLLCLIVGSSPEAPVAERKTSPPHSRKPDSRGCPSAEETPGPRAQPLLEAPQRPRAAEVAPAARAWPDPRRRKPPPPADNQASFREAARAPAGPPGPRLAQAENRASPRREPASEDAPRRARSRALRFPAARPPALATEGSAGHAHPNRPRAAALAPGPAPAPPPRFSLSFGLSPPQRDAEPGAEPCARACRSDLDEREAFCESEFAVNGIVHDVDVLGAGIRLVTLLVDRDGLYKMNRLYLTPDGFFFRVHMLALDSSSCNKPCPEFKPGSRYIVMGHIYHKRRQLPTALLQVLRGRLRPGDGLLRSSSSYVKRFNRKREGQIQGAIHTQCI
Protein: Fructose-bisphosphate aldolase C (EC 4.1.2.13) (Brain-type aldolase) (P09117)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- ATP-dependent 6-phosphofructokinase, muscle type
- ATP-dependent 6-phosphofructokinase, platelet type
- Triosephosphate isomerase
- Triosephosphate isomerase.
- ATP-dependent 6-phosphofructokinase, liver type
- Glyceraldehyde-3-phosphate dehydrogenase
- Triosephosphate isomerase
- Fructose-1,6-bisphosphatase 1
- Transaldolase
- Fructose-1,6-bisphosphatase isozyme 2
Sequence:
MPHSYPALSAEQKKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQEKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQFVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCSLPRPWALTFSYGRALQASALSAWRGQRDNAGAATEEFIKRAEMNGLAAQGKYEGSGDGGAAAQSLYVANHAY
Protein: Transporter (Q8IMC1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MYTNSASDGDGGGDVCKHESIEMSKELGHTTSLQSSSPTTTDTSNKQQLVKIEQLPDRGSWSSKMDFILSVVGLAIGLGNVWRFPYLCYKNGGGAFILPYIITLFLAGIPMFFMELALGQMLTIGGLGVFKIAPIFKGIGYAAAVMSCWMNVYYIVILAWAVFYFFMSMRADVPWRTCNNWWNTVNCVSQYERKNLHCWDKIINGTTQKVCSVSALNITSLELTDPVKEFWERRALQISHGIEEIGNIRWELAGTLLLVWILCYFCIWKGVKWTGKVVYFTALFPYVLLTILLVRGITLPGALEGIKFYIIPNFSKLTNSEVWIDAVTQIFFSYGLGLGTLVALGSYNKFTNNVYKDALIVCTVNSSTSMFAGFVIFSVIGFMAHEQQRPVADVAASGPGLAFLVYPSAVLQLPGSPMWSCLFFFMLLLIGLDSQFCTMEGFITAIIDEWPQLLRKRKEIFIAIVCALSYLVGLTCITQLAAFAYCGSYSLNVFQYLGAMEWIDFMTE
Protein: V-type proton ATPase subunit G 3 (V-ATPase subunit G 3) (V-ATPase 13 kDa subunit 3) (Vacuolar proton pump subunit G 3) (Q96LB4)
Organism: Homo sapiens (Human)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.
Interaction partners:
- V-type proton ATPase subunit F
- V-type proton ATPase subunit D
- V-type proton ATPase subunit E 2
- V-type proton ATPase subunit E 1
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit H
- V-type proton ATPase subunit d 2
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase 116 kDa subunit a 4
- V-type proton ATPase subunit B, kidney isoform
Sequence:
MTSQSQGIHQLLQAEKRAKDKLEEAKKRKGKRLKQAKEEAMVEIDQYRMQRDKEFRLKQSKIMGSQNNLSDEIEEQTLGKIQELNGHYNKYMESVMNQLLSMVCDMKPEIHVNYRATN
Protein: Lactose permease (Lactose-proton symport) (P02920)
Organism: Escherichia coli (strain K12)
Function: Responsible for transport of beta-galactosides into the cell, with the concomitant import of a proton (symport system). Can transport lactose, melibiose, the synthetic disaccharide lactulose or the analog methyl-1-thio-beta,D-galactopyranoside (TMG), but not sucrose or fructose. The substrate specificity is directed toward the galactopyranosyl moiety of the substrate.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:2164211, ECO:0000269|PubMed:7000781, ECO:0000269|PubMed:7028742}; Multi-pass membrane protein {ECO:0000269|PubMed:2164211}.
Interaction partners:
- Galactoside O-acetyltransferase
- Beta-galactosidase
- Lactose operon repressor
- Glycerol-3-phosphate transporter
- L-fucose-proton symporter
- Melibiose permease
- D-xylose-proton symporter
- Phenylalanine-specific permease
- Multidrug resistance protein D
- Rhomboid protease GlpG
Sequence:
MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTGIIFAAISLFSLLFQPLFGLLSDKLGLRKYLLWIITGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNAGAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALCASIVGIMFTINNQFVFWLGSGCALILAVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFDQQFANFFTSFFATGEQGTRVFGYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMSVRIIGSSFATSALEVVILKTLHMFEVPFLLVGCFKYITSQFEVRFSATIYLVCFCFFKQLAMIFMSVLAGNMYESIGFQGAYLVLGLVALGFTLISVFTLSGPGPLSLLRRQVNEVA
Protein: Sfi1 spindle body domain-containing protein (Q583W7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTESDMYRGSCSVLLQAVLTQACRIILALCATAKGKGTVSERITATVAAYISTVEASSVVEGASKYAMLTAVHMIHCEHHPYRACQHQHGELGAAVGVVLKEAGLRLHILTALTQLIMKRCGSSEGSVGVLLSRAASLESVRHEAASTMPNAEENVSTELLLQVFPELGVAPSKAESGAVVIIHAVHCGCPHQWFSLMLPTFLLAATMEEHVRVWRRTTLLLKAFRRLQQRRGMRLLRAIVEEVNAPSSVAPPMERLQALPDTITCGAGQEGYIETSIVGVSTVMLEDEEVGKKDESRDGIHTGENRSDPPESAVTNSSIVGTCIIRGDSDKPTVSGGVPDPVRHLSSSTREPDSVSSAGHIRDKLVNDFVKKRNTLAAEHLKRFCLSHWRYARMHERCAIKQQLRKLAERTTQECWTHWKSRWQCHREMRRKQDMEKQCDSFVTEKLLKLQKHVFSFWRALFLLRQFQICRLGRRCFVRWRCAYTFIIHSRGDKLPLMLRQDMGSRCFLQWRDAYRQRVADRMCARRYFSLMRERLERWSIWREQEQVAVMRERTAVQRRCLSNWYRAWRVQSLCTRFISSACKRLKCRVMTVWRVRWLRREDTAERLRTLYAWWNRRIAAHSFHWWCKRVRLQRSGRRLSDVRERRFYRFAWARWSSRVLSHQRLTQKHELNASRRRQWGLLRATWCTWHRRYAKRVQQRHARNQEETLKYAAAMREQSLVASAYFTWKRKAHMIRRRLPGKPPAAVGAGGGTSIPLGLNRSFTNRDVSLLTNDESCDGEKTGEDCSYANIHRVPTYKTSHTGVFNVSKRCLDHREPPEALRAERLLIRSLDSPRWQAIAHSRLFNIGGNITRSNTKVDKSTVCTQADYRQFQHQKRYYEQARWNRNDELLDVTPTMPSDIENDACPSVEDSQLPD
Protein: Slc17a3 protein (Solute carrier family 17 member 3) (Q6AZ69)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MATVVELSPTSEQCEFVLGLPVNKKTPPRKAQNSIISITMVAMVNNTDQPSHLNSSTEWFPDGLNGDQHEASKHLSIKAPVYNWSPQTQGIIFSSVQYGMMLMQGPGGYLAGKLGTKKVVGIALLGSSLLTLCIPLAANLGLAFLLATRAVQGLTQGAGYGGQFALWQKWAPPNERSRLCSIAMSGMILGIFAVLLVGGIISEALGWPFVFYIFGSIGVVCCLLWLILVYDDPVSHPWISSPEKEYILSSLDQQFNSEEQPLPIKAMLKSLPLWSMCLCSMTHQWLVNTLIIYTPTYISSVFKVNIRDNGLLSSLPFFVAWVIGILGGLLADFLLSKNFRLITVRKIITILGNTPPAALVVALPYVQSSYIATTTFLTLSCGLSPLCQSGVYINALDIAPRYASLLMGTSRGLAHSSAVMVPIVAGFFLNQDSEFGWRNFFFVLFAINLFGLIIYLVFAKADIQEWARERKLTRL
Protein: Peroxisomal bifunctional enzyme (PBE) (PBFE) (L-bifunctional protein) (LBP) (Multifunctional enzyme 1) (MFE1) [Includes: Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase (EC 4.2.1.17) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)] (Q08426)
Organism: Homo sapiens (Human)
Function: Peroxisomal trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities. Catalyzes two of the four reactions of the long chain fatty acids peroxisomal beta-oxidation pathway (By similarity). Can also use branched-chain fatty acids such as 2-methyl-2E-butenoyl-CoA as a substrate, which is hydrated into (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA (By similarity). Optimal isomerase for 2,5 double bonds into 3,5 form isomerization in a range of enoyl-CoA species (Probable). Also able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species (By similarity). With HSD17B4, catalyzes the hydration of trans-2-enoyl-CoA and the dehydrogenation of 3-hydroxyacyl-CoA, but with opposite chiral specificity. Regulates the amount of medium-chain dicarboxylic fatty acids which are essential regulators of all fatty acid oxidation pathways (By similarity). Also involved in the degradation of long-chain dicarboxylic acids through peroxisomal beta-oxidation.
Subcellular location: Peroxisome {ECO:0000305}.
Interaction partners:
- Trifunctional enzyme subunit beta, mitochondrial
- 3-ketoacyl-CoA thiolase, peroxisomal
- Peroxisomal acyl-coenzyme A oxidase 1
- 3-ketoacyl-CoA thiolase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 3
- Peroxisomal multifunctional enzyme type 2
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Acetyl-CoA acetyltransferase, cytosolic
- Enoyl-CoA hydratase, mitochondrial
Sequence:
MAEYTRLHNALALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAPRTFGLTLGHVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDPVEEAIRFAQRVSDQPLESRRLCNKPIQSLPNMDSIFSEALLKMRRQHPGCLAQEACVRAVQAAVQYPYEVGIKKEEELFLYLLQSGQARALQYAFFAERKANKWSTPSGASWKTASARPVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSGPKPRLTSSVKELGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEGSKPEEVDQVLEEFGFKMGPFRVSDLAGLDVGWKSRKGQGLTGPTLLPGTPARKRGNRRYCPIPDVLCELGRFGQKTGKGWYQYDKPLGRIHKPDPWLSKFLSRYRKTHHIEPRTISQDEILERCLYSLINEAFRILGEGIAASPEHIDVVYLHGYGWPRHKGGPMFYASTVGLPTVLEKLQKYYRQNPDIPQLEPSDYLKKLASQGNPPLKEWQSLAGSPSSKL