wanglab/gogpt-training-data huggingface dataset:
Protein: 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain) (BCKDE1A) (BCKDH E1-alpha) (P12694)
Organism: Homo sapiens (Human)
Function: E1 subunit of the branched-chain alpha-keto dehydrogenase complex that catalyzes both the decarboxylation of the alpha-ketoacid and the subsequent reductive acylation of the lipoyl moiety (another catalytic cofactor) that is covalently bound to E2. The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:10745006}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Branched-chain-amino-acid aminotransferase, mitochondrial
- Branched-chain-amino-acid aminotransferase, cytosolic
- Protein phosphatase Mn
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase protein X component, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
Sequence:
MAVAIAAARVWRLNRGLSQAALLLLRQPGARGLARSHPPRQQQQFSSLDDKPQFPGASAEFIDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPNPNLLFSDVYQEMPAQLRKQQESLARHLQTYGEHYPLDHFDK
Protein: Energy-coupling factor transporter ATP-binding protein EcfA1 (ECF transporter A component EcfA) (EC 7.-.-.-) (A2RI01)
Organism: Lactococcus lactis subsp. cremoris (strain MG1363)
Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. In this organism these probably include biotin, thiamine precursor, niacin, pantothenic acid, queuosine precursor, riboflavin and thiamine. Uptake of niacin or riboflavin into proteosomes containing EcfA1A2T and Niax or RibU has been demonstrated. Uptake requires hydrolyzable Mg-ATP and is substrate-specific; NiaX-containing proteosomes did not transport riboflavin.
Subcellular location: Cell membrane {ECO:0000305|PubMed:21135102}; Peripheral membrane protein {ECO:0000305|PubMed:21135102}.
Interaction partners:
- Energy-coupling factor transporter transmembrane protein EcfT
- Energy-coupling factor transporter ATP-binding protein EcfA2
- Biotin transporter BioY
- Pantothenic acid transporter PanT
- Putative cobalt ABC transporter permease protein
- Thiamine precursor transporter HmpT
- Thiamine transporter ThiT
- Riboflavin transporter RibU
- Biotin transporter BioY2
- Putative hemin import ATP-binding protein HrtA
Sequence:
MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGIVKIDGERLTAENVWNLRRKIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRSEIMRVIHEIKDKYHLTVLSITHDLDEAASSDRILVMRAGEIIKEAAPSELFATSEDMVEIGLDVPFSSNLMKDLRTNGFDLPEKYLSEDELVELLADKLG
Protein: Exportin-T (Exportin(tRNA)) (Karyopherin-beta) (tRNA exportin) (O94258)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: tRNA nucleus export receptor which facilitates tRNA translocation across the nuclear pore complex. Involved in pre-tRNA splicing, probably by affecting the interaction of pre-tRNA with splicing endonuclease (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}.
Interaction partners:
- GTP-binding nuclear protein spi1
- Uncharacterized protein C328.01c
- Uncharacterized protein C11G11.07
- Exportin-1
- La protein homolog
- Importin subunit beta-2
- mRNA export factor mex67
- Ran GTPase-activating protein 1
- Repressor of RNA polymerase III transcription maf1
- Probable methionine--tRNA ligase, cytoplasmic
Sequence:
MSAQDVENAVEAALDPSVGPIIKQQATDFIGSLRSSSTGWKICHEIFSEKTKYKPSTRLICLQTLSEKVREWNNESNLLELQMIRDSVWSYIKELSFLDEPAYISNAVQHLLTLLFLQLYPSNWNDFFASLQGVIAASSQSEFSNFYLKVLLSIGDEIADSLVLKTDVQIQKDNLVKDAIRANDMSDIVSFVYEMMLAYSNAKNYGTVGLCLQVYAQWVSWININLIVNEPCMNLLYSFLQIEELRCAACETMTEIVNKKMKPLEKLNLLNILNLNLFFSKSQEQSTDPNFDEHVAKLINAQGVELVAIKSDPSELSPELKENCSFQLYNLFPYLIRYLSDDYDETSTAVFPFLSDLLVSLRKESSSKELSASLKEFLKSLLEAIIKKMKYDESQEWDDDPDSEEEAEFQEMRKKLKIFQDTINSIDSSLFSSYMYSAITSSLSTAATLSPENSWQLIEFALYETYIFGEGLRGPDAFFNEVDKSPTVLSQILALVTTSQVCRHPHPLVQLLYMEILVRYASFFDYESAAIPALIEYFVGPRGIHNTNERVRPRAWYLFYRFVKSIKKQVVNYTESSLAMLGDLLNISVSPVTDMDAPVPTLNSSIRNSDFNSQLYLFETVGVLISSGNLTPEEQALYCDSLINALIGKANAALSSDLSALENIISVYCSLMAIGNFAKGFPARGSEEVAWLASFNKASDEIFLILDRMGFNEDIRGAVRFTSGRIINVVGPDMLPKVPQLISILLNSIDMNELVDVLSFISQLIHIYKDNMMEITNRMLPTLLMRIFSSLSAAPQGTDDAVKQNDLRKSYISFILQLLNKGFGSILFTEENQVYFDPLINSILHFANLVGEPATQKSSIALVSKMVSLWGGKDGIAGFENFTLSLTPLCFEMPVNPNFNTRDGQSLVVLGELAGLQKIILEKLGDIYKSYLVTVYFPTVNFPDVMASEYLQALSNLDSRSFKQFFQKFIQALKSGNV
Protein: Na(+)/dicarboxylate cotransporter 3 (NaDC-3) (mNaDC3) (Na(+)-coupled carboxylate transporter 3) (NaC3) (Sodium-dependent high-affinity dicarboxylate transporter 2) (Solute carrier family 13 member 3) (Q91Y63)
Organism: Mus musculus (Mouse)
Function: High-affinity sodium-dicarboxylate cotransporter that accepts a range of substrates with 4-6 carbon atoms, such as the citric acid cycle intermediates succinate and alpha-ketoglutarate (2-oxoglutarate), as well as other compounds including N-acetyl-L-aspartate. Transports the dicarboxylate into the cell with a probable stoichiometry of 3 Na(+) for 1 divalent dicarboxylate, rendering the process electrogenic. Can transport citrate in a Na(+)-dependent manner, recognizing the divalent form of citrate rather than the trivalent form which is normally found in blood (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MAALAALAKKVWSARRLLVLLLVPLALLPILFALPPKEGRCLYVILLMAVYWCTEALPLSVTALLPIILFPFMGILPSSKVCPQYFLDTNFLFLSGLIMASAIEEWNLHRRIALKVLMLVGVQPARLILGMMVTTSFLSMWLSNTASTAMMLPIASAILKSLFGQREARKDLPREGDESTAAVQGNGLRTVPTEMQFLASSEGGHTEDAEAPMELPDDSKEEEHRRNIWKGFLISIPYSASIGGTATLTGTAPNLILLGQLKSFFPQCDVVNFGSWFIFAFPLMLLFLLVGWLWISFLYGGMSWRSWRKKKSKIRADAEDQAKAVIQEEFQNLGPIKFAEQAVFILFCTFAILLFSRDPKFIPGWASLFAPGFVSDAVTGVAIVTILFFFPSQKPSLKWWFDFKAPNSETEPLLSWKKAQETVPWNIILLLGGGFAMAKGCEESGLSAWIGGQLHPLEHVPPLLAVLLITVVIAFFTEFASNTATIIIFLPVLAELAIRLHVHPLYLMIPGTVGCSYAFMLPVSTPPNSIAFSTGHLLVKDMVRTGLLMNLMGVLLLSLAMNTWAQTIFQLGTFPDWANTHAANATALPPALTNNTVQTF
Protein: Neurogenic protein big brain (P23645)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential for proper differentiation of ectoderm. Acts synergistically with neurogenic locus proteins Notch and Delta during the separation of neural and epidermal cell lineages in response to the lateral inhibition signal. Voltage-insensitive monovalent cation channel. Ion transport is blocked by the presence of divalent cations.
Subcellular location: Membrane {ECO:0000269|PubMed:9367444}; Multi-pass membrane protein {ECO:0000269|PubMed:9367444}.
Interaction partners:
- Aquaporin
- Entomoglyceroporin 1
Sequence:
MADESLHTVPLEHNIDYHIVTLFERLEAMRKDSHGGGHGVNNRLSSTLQAPKRSMQAEIRTLEFWRSIISECLASFMYVFIVCGAAAGVGVGASVSSVLLATALASGLAMATLTQCFLHISGAHINPAVTLALCVVRSISPIRAAMYITAQCGGGIAGAALLYGVTVPGYQGNLQAAISHSAALAAWERFGVEFILTFLVVLCYFVSTDPMKKFMGNSAASIGCAYSACCFVSMPYLNPARSLGPSFVLNKWDSHWVYWFGPLVGGMASGLVYEYIFNSRNRNLRHNKGSIDNDSSSIHSEDELNYDMDMEKPNKYQQSQGTYPRGQSNGNGGGQAAGNGQHQAANMGQMPGVVANAGQGNYCQNLYTAPPLSSKYDQQQEPLYGGTRSLYCRSPTLTRSNLNRSQSVYAKSNTAINRDIVPRPGPLVPAQSLYPMRTQQQQQQQQQQQQQVAPAPQSSHLQNQNVQNQMQQRSESIYGMRGSMRGQQQPIQQQQQQQQQQQLQQQQPNMGVQQQQMQPPPQMMSDPQQQPQGFQPVYGTRTNPTPMDGNHKYDRRDPQQMYGVTGPRNRGQSAQSDDSSYGSYHGSAVTPPARHPSVEPSPPPPPMLMYAPPPQPNAAHPQPIRTQSERKVSAPVVVSQPAACAVTYTTSQGSAVTAQQQQQQQQQQQQQQQQQQQQMMMQQQQQHYGMLPLRPN
Protein: Malic enzyme (Q9U1J1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSKPDSKLDKYAQRDRLGLWGTGDNEVVGSLSGFTRLLDKRYSKGLAFTHEERQQLGIHGMLPYVVREPSEQVEHCRALLARLDQDLDKYMYLISLSERNERLFYNVLSSDIAYMMPLVYTPTVGLACQRYSLIHQNAKGMFISIKDKGHIYDVLKNWPETDVRAIVVTDGERILGLGDLGANGMGIPVGKLSLYTALAGIKPSQCLPITLDVGTNTESILEDPLYIGLRERRATGDLYDEFIDEFMHACVRRFGQNCLIQFEDFANANAFRLLSKYRDSFCTFNDDIQGTASVAVAGLLASLKIKKTQLKDNTLLFLGAGEAALGIANLCLMAMKVEGLTEEEAKARIWMVDRCRYIIKIHPDTYRCFLCSRGVITRDRPKGGLTEHKLHFAQLHEPIDTLAEAVRKVRPNVLIGAAAQGGAFNQEILELMADINETPIIFALSNPTSKAECTAEEAYTYTKGRCIFASGSPFAPVTYNNKKFYPGQGNNSYIFPGVALGVLCAGMLNIPEQVFLVAAERLAELVSKDDLAKGSLYPPLSSIVSCSMAIAERIVEYAYKNGLATVRPEPVNKLAFIKAQMYDLDYPRSVPATYKM
Protein: Sperm-specific dynein intermediate chain 1, isoform C (M9NE47)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MGLVLIKFLRSTYSTLSGGKKQPLNLSVYNVQATNIPPKETLVYTKQTQTTSTGGGNGDGYMEDWWRPRKDDEESSLQNLGNGFTSKLPPGYLTHGLPTVKDVAPAITPLEIKKETEVKKEVNELSEEQKQMIILSENFQRFVVRAGRVIERALSENVDIYTDYIGGGDSEEANDERSHARLSLNRVFYDERWSKNRCITSMDWSTHFPELVVGSYHNNEESPNEPDGVVMVWNTKFKKSTPEDVFHCQSAVMSTCFAKFNPNLILGGTYSGQIVLWDNRVQKRTPIQRTPLSAAAHTHPVYCLQMVGTQNAHNVISISSDGKLCSWSLDMLSQPQDTLELQQRQSKAIAITSMAFPANEINSLVMGSEDGYVYSASRHGLRSGVNEVYERHLGPITGISTHYNQLSPDFGHLFLTSSIDWTIKLWSLKHQPFAATPGLHPACASATRPASCTCTTWPRTWRSHRATNGRGSTPILARSR
Protein: Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase (Golgi-resident PAP phosphatase) (gPAPP) (EC 3.1.3.7) (3'(2'), 5'-bisphosphate nucleotidase 2) (Inositol monophosphatase domain-containing protein 1) (Myo-inositol monophosphatase A3) (Phosphoadenosine phosphate 3'-nucleotidase) (Q9NX62)
Organism: Homo sapiens (Human)
Function: Exhibits 3'-nucleotidase activity toward adenosine 3',5'-bisphosphate (PAP), namely hydrolyzes adenosine 3',5'-bisphosphate into adenosine 5'-monophosphate (AMP) and a phosphate. May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',5'-bisphosphate produced by Golgi sulfotransferases during glycosaminoglycan sulfation. Has no activity toward 3'-phosphoadenosine 5'-phosphosulfate (PAPS) or inositol phosphate (IP) substrates including I(1)P, I(1,4)P2, I(1,3,4)P3, I(1,4,5)P3 and I(1,3,4,5)P4.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:18695242}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:18695242}; Single-pass type II membrane protein {ECO:0000255, ECO:0000269|PubMed:18695242}. Note=The catalytic core is predicted to reside within the Golgi lumen. {ECO:0000269|PubMed:18695242}.
Interaction partners:
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
- Inositol monophosphatase 1
- Inositol monophosphatase 2
- 3'
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Inositol polyphosphate 1-phosphatase
- Myotubularin
- Inositol polyphosphate 4-phosphatase type II
- Inositol polyphosphate-4-phosphatase type I A
Sequence:
MAPMGIRLSPLGVAVFCLLGLGVLYHLYSGFLAGRFSLFGLGGEPGGGAAGPAAAADGGTVDLREMLAVSVLAAVRGGDEVRRVRESNVLHEKSKGKTREGAEDKMTSGDVLSNRKMFYLLKTAFPSVQINTEEHVDAADQEVILWDHKIPEDILKEVTTPKEVPAESVTVWIDPLDATQEYTEDLRKYVTTMVCVAVNGKPMLGVIHKPFSEYTAWAMVDGGSNVKARSSYNEKTPRIVVSRSHSGMVKQVALQTFGNQTTIIPAGGAGYKVLALLDVPDKSQEKADLYIHVTYIKKWDICAGNAILKALGGHMTTLSGEEISYTGSDGIEGGLLASIRMNHQALVRKLPDLEKTGHK
Protein: Small ribosomal subunit protein mL103 (rPPR7) (Pentatricopeptide repeat-containing protein At4g36680, mitochondrial) (Q9M065)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022}.
Interaction partners:
- ARM repeat superfamily protein
- Fanconi anemia group I-like protein
- Fanconi anemia group E protein FANCE protein
- Fanconi anemia group F protein
- At5g01015
- RING-type E3 ubiquitin transferase
- ATP-dependent protease La
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Phosphorylase superfamily protein
- At4g24340
Sequence:
MASSRISLRLVRRFASAAADGTTTAPSSGKISVSKAKSTLRKEHDPDKALKIYANVSDHSASPVSSRYAQELTVRRLAKCRRFSDIETLIESHKNDPKIKEEPFYSTLIRSYGQASMFNHAMRTFEQMDQYGTPRSAVSFNALLNACLHSKNFDKVPQLFDEIPQRYNKIIPDKISYGILIKSYCDSGTPEKAIEIMRQMQGKGMEVTTIAFTTILSSLYKKGELEVADNLWNEMVKKGCELDNAAYNVRIMSAQKESPERVKELIEEMSSMGLKPDTISYNYLMTAYCERGMLDEAKKVYEGLEGNNCAPNAATFRTLIFHLCYSRLYEQGYAIFKKSVYMHKIPDFNTLKHLVVGLVENKKRDDAKGLIRTVKKKFPPSFLNAWKKLEEELGLYSKTDAFPSSAKEAAAA
Protein: Metabotropic glutamate receptor 1 (mGluR1) (P23385)
Organism: Rattus norvegicus (Rat)
Function: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system. May participate in the central action of glutamate in the CNS, such as long-term potentiation in the hippocampus and long-term depression in the cerebellum. May function in the light response in the retina (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q13255}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13255}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P97772}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000250|UniProtKB:P97772}. Note=Located in dendrioles, small dendrites that makes up a brush structure found as the terminal specialization of a dendrite of a unipolar brush cell. {ECO:0000250|UniProtKB:P97772}.
Interaction partners:
- Homer protein homolog 3
- Homer protein homolog 1
- Metabotropic glutamate receptor 5
- Guanine nucleotide-binding protein G
- Spectrin beta chain, non-erythrocytic 2
- Homer protein homolog 2
- Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein G
Sequence:
MVRLLLIFFPMIFLEMSILPRMPDRKVLLAGASSQRSVARMDGDVIIGALFSVHHQPPAEKVPERKCGEIREQYGIQRVEAMFHTLDKINADPVLLPNITLGSEIRDSCWHSSVALEQSIEFIRDSLISIRDEKDGLNRCLPDGQTLPPGRTKKPIAGVIGPGSSSVAIQVQNLLQLFDIPQIAYSATSIDLSDKTLYKYFLRVVPSDTLQARAMLDIVKRYNWTYVSAVHTEGNYGESGMDAFKELAAQEGLCIAHSDKIYSNAGEKSFDRLLRKLRERLPKARVVVCFCEGMTVRGLLSAMRRLGVVGEFSLIGSDGWADRDEVIEGYEVEANGGITIKLQSPEVRSFDDYFLKLRLDTNTRNPWFPEFWQHRFQCRLPGHLLENPNFKKVCTGNESLEENYVQDSKMGFVINAIYAMAHGLQNMHHALCPGHVGLCDAMKPIDGRKLLDFLIKSSFVGVSGEEVWFDEKGDAPGRYDIMNLQYTEANRYDYVHVGTWHEGVLNIDDYKIQMNKSGMVRSVCSEPCLKGQIKVIRKGEVSCCWICTACKENEFVQDEFTCRACDLGWWPNAELTGCEPIPVRYLEWSDIESIIAIAFSCLGILVTLFVTLIFVLYRDTPVVKSSSRELCYIILAGIFLGYVCPFTLIAKPTTTSCYLQRLLVGLSSAMCYSALVTKTNRIARILAGSKKKICTRKPRFMSAWAQVIIASILISVQLTLVVTLIIMEPPMPILSYPSIKEVYLICNTSNLGVVAPVGYNGLLIMSCTYYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITTCFAVSLSVTVALGCMFTPKMYIIIAKPERNVRSAFTTSDVVRMHVGDGKLPCRSNTFLNIFRRKKPGAGNANSNGKSVSWSEPGGRQAPKGQHVWQRLSVHVKTNETACNQTAVIKPLTKSYQGSGKSLTFSDASTKTLYNVEEEDNTPSAHFSPPSSPSMVVHRRGPPVATTPPLPPHLTAEETPLFLADSVIPKGLPPPLPQQQPQQPPPQQPPQQPKSLMDQLQGVVTNFGSGIPDFHAVLAGPGTPGNSLRSLYPPPPPPQHLQMLPLHLSTFQEESISPPGEDIDDDSERFKLLQEFVYEREGNTEEDELEEEEDLPTASKLTPEDSPALTPPSPFRDSVASGSSVPSSPVSESVLCTPPNVTYASVILRDYKQSSSTL
Protein: Acetaldehyde dehydrogenase (acetylating) EutE (EC 1.2.1.10) (Ethanolamine utilization protein EutE) (P41793)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Acts as the second step in ethanolamine degradation by converting acetaldehyde into acetyl-CoA (Probable). Has a very strong preference for NAD(+) over NADP(+) in both catalytic directions. May play a role in bacterial microcompartment (BMC) assembly or maintenance (Probable). Directly targeted to the BMC.
Subcellular location: Bacterial microcompartment {ECO:0000269|PubMed:27450681, ECO:0000305|PubMed:23585538}. Note=Probably located inside the BMC. {ECO:0000305|PubMed:27450681}.
Interaction partners:
- Probable alcohol dehydrogenase EutG
- Phosphate acetyltransferase EutD
- Ethanolamine utilization protein EutJ
- Bacterial microcompartment shell vertex protein EutN
- 1-propanol dehydrogenase PduQ
- Ethanolamine ammonia-lyase small subunit
- Bacterial microcompartment shell protein EutM
- Ethanolamine ammonia-lyase large subunit
- Bacterial microcompartment shell protein EutK
- Phosphate acetyltransferase
Sequence:
MNQQDIEQVVKAVLLKMKDSSQPASTVHEMGVFASLDDAVAAAKRAQQGLKSVAMRQLAIHAIREAGEKHARELAELAVSETGMGRVDDKFAKNVAQARGTPGVECLSPQVLTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGGPENLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAVVDAARKHTNKRLIAAGAGNPPVVVDETADLPRAAQSIVKGASFDNNIICADEKVLIVVDSVADELMRLMEGQHAVKLTAAQAEQLQPVLLKNIDERGKGTVSRDWVGRDAGKIAAAIGLNVPDQTRLLFVETPANHPFAVTEMMMPVLPVVRVANVEEAIALAVQLEGGCHHTAAMHSRNIDNMNQMANAIDTSIFVKNGPCIAGLGLGGEGWTTMTITTPTGEGVTSARTFVRLRRCVLVDAFRIV
Protein: Acetyl-coenzyme A thioesterase (EC 3.1.2.1) (Acyl-CoA thioester hydrolase 12) (Acyl-coenzyme A thioesterase 12) (Acyl-CoA thioesterase 12) (Cytoplasmic acetyl-CoA hydrolase 1) (CACH-1) (mCACH-1) (Q9DBK0)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Preferentially hydrolyzes acetyl-CoA.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8WYK0}.
Interaction partners:
- Acetyl-coenzyme A synthetase, cytoplasmic
- Acetyl-coenzyme A synthetase 2-like, mitochondrial
- Acetyl-Coenzyme A acetyltransferase 3
- Acetyl-CoA acetyltransferase, cytosolic
- Acylphosphatase-1
- Acetyl-CoA acetyltransferase, mitochondrial
- Acetyl-CoA carboxylase 1
- Acetyl-CoA carboxylase 2
- Aldehyde dehydrogenase X, mitochondrial
- Aldehyde dehydrogenase family 3 member A2
Sequence:
MESMVAPGEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFSTSMEISIKVIVQDKFTGIQKLLCVAFSTFVAKPVGKEKVHLKPVLLQTEQEQVEHNLASERRKVRLQHENTFNNIMKESSRFSDSICNEEEGTATTMGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVEVGVRVEAFDCQEWAEGQGRHINSAFLIYNAVDDQEKLITFPRIQPISKDDFRRYQGAIARRRIRLGRKYVISHKKEVPLSAQWDISKKGSLSNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDAISVKVEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSRRKPLKDNNTYTVALRSVVLPSVPSSPQYIRSEVICAGFLIQAVDSNSCTVTYLNQMSDSILPYFAGNIGGWSKSIEEAAASCIKFIENATPDGLKSVL
Protein: Succinate-semialdehyde dehydrogenase (EC 1.2.1.24) (X5D299)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|RuleBase:RU365091}.
Interaction partners:
Sequence:
MATCIWLRSCGARRLGSTFPGCRLRPRAGGLVPASGPAPGPAQLRCYAGRLAGLSAALLRTDSFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAEVNQGFLLDLDPLLLASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL
Protein: Lysozyme g (EC 3.2.1.17) (C1BHT6)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MGVGVGVGIGGLITFLTLASCFGDITKVDTSGASEITARQDKLTVQGVDASHKLAEHDLVRMNKYKKLITRVGQKHGLDPAIIAGIISRESRAGAVLDHGWGDHGNGFGLMQVDKRYHKIVGTWDSEEHISQGSEILKEFIRRIQAKFPAWPKEHQLKGGISAYNAGDKNVRTYERMDVGTTGGDYSNDVVARSQWFKRQGY
Protein: HIT-type domain-containing protein (Q23644)
Organism: Caenorhabditis elegans
Interaction partners:
- Glutaminyl-peptide cyclotransferase
- Nop domain-containing protein
- HIT-type domain-containing protein
- Protein BCCIP homolog
- General transcription factor 3C polypeptide 5
- Paired amphipathic helix protein sin-3
- Vacuolar protein sorting-associated protein 72 homolog
Sequence:
MTTSHTPEPKEVEDYQEDGEILDDDDDVPTEIPNITSEFLVNYPSSEDEKSPEDVIKAYKRKIENQKNVENEESVIPAIDPKLCKVCLKNEHKYKCPRCEMRTCSLDCSKKHKADNNCDGVRQAFTKVDKLSQYDPQKSIDDQKFMHLMKEKVGLGAEPVGGVGNDVNSSDGEEKPVDPNALRYTTNSPTERYLLNAARFRHIWLGFVGEQENESRHEQHSDTIFWTLKLSFKKQTADGGIEVFEKIVNNIPETIRVATVLKQFFKPRQYGCIVSESDLDVEKLKPFIDRGIDDVNVYMEVHANPERYYGIITDSTILEMTRTRVVADFPKLVITMKDEFIESMQLLSMEELAEIQTKYGGVGNQRFGGGGRGRGGRGFHRGGANRGGGGSNHNIFRKRPGQDGGQDGGFKRGRGGNFHGGSRRGGYQNRTHQNIDTFDPFEPFSGPNRLPMEYN
Protein: Fasciclin-like arabinogalactan protein 6 (A9XTL1)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MRKLLAFAFLFFFFWDKTLAQIAPAPPLKVDNITSILEKGGQFTTFIKLLKATQVADQLNNQLSTPDPNDGITVFAPSDNAFSGLKPGTLNSLSDQEKLQLVQFHILPTLMSTSQFQTASNPLRTQAGDVKGGKFPLNVTAEGNQVNVTTGVVNATVENSVFSDRRIAVYQVDKVLLPLEIFGTAPEPAPAPVVPENGGLVSSPKTAVKGADAAGAVSLKFHALAMGFSSFAVFWAIFGGF
Protein: Long-chain-fatty-acid--CoA ligase 4 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 4) (LACS 4) (O60488)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially activates arachidonate and eicosapentaenoate as substrates. Preferentially activates 8,9-EET > 14,15-EET > 5,6-EET > 11,12-EET. Modulates glucose-stimulated insulin secretion by regulating the levels of unesterified EETs (By similarity). Modulates prostaglandin E2 secretion.
Subcellular location: Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24269233}; Single-pass type III membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:24269233}.
Interaction partners:
- Fatty acid synthase
- Carnitine O-palmitoyltransferase 1, liver isoform
- Nuclear protein AMMECR1
- Lipoprotein lipase
- Monoglyceride lipase
- Lysosomal thioesterase PPT2
- Palmitoyl-protein thioesterase 1
- Long-chain fatty acid transport protein 2
- Phospholipid hydroperoxide glutathione peroxidase GPX4
- Lysophospholipid acyltransferase 5
Sequence:
MKLKLNVLTIILLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYRSVTHFDSLAVIDIPGADTLDKLFDHAVSKFGKKDSLGTREILSEENEMQPNGKVFKKLILGNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEYPEGFEIHSMQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLCNLLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMYGGK
Protein: Fanconi anemia, complementation group F (cDNA FLJ10854 fis, clone NT2RP4001507, highly similar to Fanconi anemia group F protein) (A3KME0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MESLLQHLDRFSELLAVSSTTYVSTWDPATVRRALQWARYLRHIHRRFGRHGPIRTALERRLHNQWRQEGGFGRGPVPGLANFQALGHCDVLLSLRLLENRALGDAARYHLVQQLFPGPGVRDADEETLQESLARLARRRSAVHMLRFNGYRENPNLQEDSLMKTQAELLLERLQEVGKAEAERPARFLSSLWERLPQNNFLKVIAVALLQPPLSRRPQEELEPGIHKSPGEGSQVLVHWLLGNSEVFAAFCRALPAGLLTLVTSRHPALSPVYLGLLTDWGQRLHYDLQKGIWVGTESQDVPWEELHNRFQSLCQAPPPLKDKVLTALETCKAQDGDFEVPGLSIWTDLLLALRSGAFRKRQVLGLSAGLSSV