wanglab/gogpt-training-data huggingface dataset:
Protein: S-adenosyl-L-methionine-dependent Diels-Alderase iliD (EC 2.1.-.-) (C-methyltransferase iliD) (Ilicicolin H biosynthesis cluster protein D) (Pericyclase iliD) (P0DO33)
Organism: Neonectria sp. (strain DH2)
Function: S-adenosyl-l-methionine-dependent Diels-Alderase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain. IliD catalyzes the Diels-Alder reaction that converts the acyclic 2-pyridone intermediate to 8-epi-ilicicolin H. The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (Probable).
Interaction partners:
Sequence:
MTSTEAAGTGKAPAIRANPALQTYYESQESYLVYEVVLRGSHHFGFYEKDTYWPFPVGRSLERMEAKLLSALALPSGSQILDAGCGFGPVAISMAKKGMRVTAIDIIDHHVTKARRNVEKAGLPKGQVTVEKMDYQHLESIASESHDDAKAAATGFFRILKPGGRIAFFEAQRSRTSGDYDEGDELAGHLKLVNEYTAMPTNELSREDYFKDLLEDAGFVDVEFTLPPGTREPREHWSYSALKA
Protein: Ras-related protein RABG3d (AtRABG3d) (Ras-related protein Rab72) (AtRab72) (Q9C820)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Intracellular vesicle trafficking and protein transport.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Protein VACUOLELESS1
- Geranylgeranyl transferase type-2 subunit beta 1
- Vacuolar protein-sorting-associated protein 33 homolog
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar sorting protein 18
- Vacuolar protein-sorting-associated protein 11 homolog
- Vacuolar fusion protein MON1 homolog
- Guanosine nucleotide diphosphate dissociation inhibitor 2
- Proline-rich spliceosome-associated
- ADP-ribosylation factor
Sequence:
MSSRRRVLLKVIILGDSGVGKTSLMNQFVNRKFSNQYKATIGADFLTKEVQIDDRIFTLQIWDTAGQERFQSLGVAFYRGADCCVLVYDVNVMKSFDNLNNWREEFLIQASPSDPENFPFVVLGNKTDVDGGKSRVVSEKKAKAWCASKGNIPYFETSAKEGFNVDAAFECITKNAFKNEPEEEPYLPDTIDVAGGQQQRSTGCEC
Protein: AcrIIA6 (A0A2U7VJX7)
Organism: Streptococcus phage D1024
Interaction partners:
Sequence:
MKINDDIKELILEYMSRYFKFENDFYKLPGIKFTDANWQKFKNGGTDIEKMGAARVNAMLSCLFEDFELAMIGKAQTNYYIDNSLKLNMPFYAYYDMFKKQLLINWLKNNRDDVICGTGRMYTASGNYIANAYLEVALESSRLGGGEYMLQMRFKNYSRSQEPIPSGRQNRLEWIENNLENIR
Protein: Importin subunit alpha (A0A8I5Y0C8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MRRRRIEVNVELRKAKKDDQMLKRRNVSSFPDDATSPLQENRNNQVNTGTVNWSVEDIVKGINSNNLESQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGKTDCSPIQFESAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNIAGDGSVFRDLVIKHGAIDPLLALLAVPDLSSLACGYLRNLTWTLSNLCRNKNPAPPLDAVEQILPTLVRLLHHNDPEVLADSCWAISYLTDGPNERIEMVVKKGVVPQLVKLLGATELPIVTPALRAIGNIVTGTDEQTQKVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQIQQVVNHGLVPFLVGVLSKADFKTQKEAAWAITNYTSGGTVEQIVYLVHCGIIEPLMNLLSAKDTKIIQVILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQSHENESVYKASLNLIEKYFSVEEEEDQNVVPETTSEGFAFQVQDGAPGTFNF
Protein: Fatty acid elongase 2 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELO2) (Elongation of fatty acids protein 2) (Fenpropimorph resistance protein 1) (Glucan synthesis protein 1) (Very-long-chain 3-oxoacyl-CoA synthase 2) (v-SNARE bypass mutant gene 2 protein) (P25358)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of a microsomal membrane-bound long-chain fatty acid elongation system, which produces the 20-26-carbon very long-chain fatty acids (VLCFA) from long-chain fatty acid precursors and is involved ceramide and inositol sphingolipid biosynthesis. Component of elongase II, which elongates 16-18 carbon fatty acyl-CoAs such as palmitoyl-CoA and stearoyl-CoA to 20-22-carbon fatty acids by incorporation of malonyl-CoA. Involved in the synthesis of 1,3-beta-glucan. The enzymes active site faces the cytosol, whereas VLCFA length is determined by a lysine near the luminal end of transmembrane helix 6. Plays an important role in lipotoxic cell death induced by oleic acid through maintaining a balanced fatty acid composition in thr plasma membrane.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12087109, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9832547}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Fatty acid elongase 1
- Fatty acid elongase 3
- Acyl-CoA desaturase 1
- Very-long-chain 3-oxoacyl-CoA reductase
- Very-long-chain enoyl-CoA reductase
- Very-long-chain
- 3-oxoacyl-[acyl-carrier-protein] synthase homolog
- Fatty acid synthase subunit alpha reductase
- Mannosyl phosphorylinositol ceramide synthase SUR1
Sequence:
MNSLVTQYAAPLFERYPQLHDYLPTLERPFFNISLWEHFDDVVTRVTNGRFVPSEFQFIAGELPLSTLPPVLYAITAYYVIIFGGRFLLSKSKPFKLNGLFQLHNLVLTSLSLTLLLLMVEQLVPIIVQHGLYFAICNIGAWTQPLVTLYYMNYIVKFIEFIDTFFLVLKHKKLTFLHTYHHGATALLCYTQLMGTTSISWVPISLNLGVHVVMYWYYFLAARGIRVWWKEWVTRFQIIQFVLDIGFIYFAVYQKAVHLYFPILPHCGDCVGSTTATFAGCAIISSYLVLFISFYINVYKRKGTKTSRVVKRAHGGVAAKVNEYVNVDLKNVPTPSPSPKPQHRRKR
Protein: Guanylate kinase (EC 2.7.4.8) (GMP kinase) (Q9P6I5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential for recycling GMP and indirectly, cGMP.
Interaction partners:
- Inosine triphosphate pyrophosphatase
- GMP synthase
- Adenine phosphoribosyltransferase
- Nucleoside diphosphate kinase
- Ribonucleoside-diphosphate reductase large chain
- Adenylate kinase
- Ribonucleoside-diphosphate reductase small chain
- Pyruvate kinase
- Golgi apyrase
- 3',5'-cyclic-nucleotide phosphodiesterase
Sequence:
MTPQLSSSVASKLVTLKLKPVVVFGPSGVGKSTLLKRLLKDHGDKLGFSVSHTTRTPRAGEKDGIDYHFVTKEEFQKLVAEEKFVEWAVFSGNMYGTSIMAIQELEAVNKKAILDIDLQGVLQVKASPIDAQYVFLAPPSIEQLEVRLRGRGTENESAILQRLERARAEIEYSEKPGNFDALIVNDDVEKAYKQLEAICLSD
Protein: Sodium channel regulatory subunit beta-1 (Q00954)
Organism: Rattus norvegicus (Rat)
Function: Regulatory subunit of multiple voltage-gated sodium channel complexes that play important roles in excitable membranes in brain, heart and skeletal muscle. Enhances the presence of the pore-forming alpha subunit at the cell surface and modulates channel gating characteristics and the rate of channel inactivation. Modulates the activity of a variety of pore-forming alpha subunits, such as SCN1A, SCN2A, SCN3A, SCN4A, SCN5A and SCN10A.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11470829}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q07699}. Perikaryon {ECO:0000250|UniProtKB:P97952}. Cell projection {ECO:0000250|UniProtKB:P97952}. Cell projection, axon {ECO:0000269|PubMed:11470829}. Note=Detected at nodes of Ranvier on the sciatic nerve. {ECO:0000269|PubMed:11470829}.
Interaction partners:
- Sodium channel regulatory subunit beta-2
- Sodium channel protein type 1 subunit alpha
- Sodium channel regulatory subunit beta-4
- Sodium channel protein type 3 subunit alpha
- Sodium channel protein type 5 subunit alpha
- Sodium channel protein type 9 subunit alpha
- Sodium channel protein type 2 subunit alpha
- Sodium channel protein type 8 subunit alpha
- Sodium channel protein type 4 subunit alpha
- Sodium channel protein type 7 subunit alpha
Sequence:
MGTLLALVVGAVLVSSAWGGCVEVDSETEAVYGMTFKILCISCKRRSETTAETFTEWTFRQKGTEEFVKILRYENEVLQLEEDERFEGRVVWNGSRGTKDLQDLSIFITNVTYNHSGDYECHVYRLLFFDNYEHNTSVVKKIHLEVVDKANRDMASIVSEIMMYVLIVVLTIWLVAEMVYCYKKIAAATEAAAQENASEYLAITSESKENCTGVQVAE
Protein: Ras-related protein Rac1 (P40792)
Organism: Drosophila melanogaster (Fruit fly)
Function: During various developmental processes, regulates changes in cell morphology in response to extracellular signals. During oogenesis, mediates signaling from the tyrosine kinase (RTK) chemoattractant receptors (Egfr and Pvr) to the guidance pathway that control the directional persistent collective migration of the border cell (BC) cluster through the nurse cells to the oocyte. Once activating by Pvr and Egfr, promotes the formation of forward-directed actin protrusions which stabilize the DE-cadherin (shg)-mediated adhesions. In turn, DE-mediated adhesion between the leader border cells and nurse cells further promotes Rac1 signaling creating a positive feedback loop that amplifies the output of RTK activity and leads to higher Rac activity at the front, thus promoting polarization of the border cell cluster and directionally persistent migration. Involved in axon outgrowth and myoblast fusion. Plays a role in regulating dorsal closure during embryogenesis. Involved in integrin alpha-PS3/beta-nu-mediated phagocytosis of Gram-positive S.aureus by hemocytes.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- non-specific serine/threonine protein kinase
- Mitogen-activated protein kinase kinase kinase
- Stress-activated protein kinase JNK
- Myoblast city, isoform B
- LD29223p
- Rho GDP-dissociation inhibitor 3
- Ras-like GTP-binding protein Rho1
- Protein vav
- Trio, isoform A
- non-specific serine/threonine protein kinase
Sequence:
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDAKPINLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVNPASFENVRAKWYPEVRHHCPSTPIILVGTKLDLRDDKNTIEKLRDKKLAPITYPQGLAMAKEIGAVKYLECSALTQKGLKTVFDEAIRSVLCPVLQPKSKRKCALL
Protein: Dihydrolipoyl dehydrogenase, apicoplast (EC 1.8.1.4) (Q8IAZ6)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- 2-oxoglutarate dehydrogenase E1 component
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Pyruvate dehydrogenase E1 component subunit alpha
- dihydrolipoyllysine-residue succinyltransferase
- 3-methyl-2-oxobutanoate dehydrogenase
- 2-oxoisovalerate dehydrogenase subunit alpha
- Aminomethyltransferase, mitochondrial, putative
- Glycine cleavage system H protein
Sequence:
MVIRQNIKHIVKLNVVTLIWLSYLFLLKPHGTLKNMMVCNAVLLPFNEKNKGINNFVYINPKNIILNKIKKDVIKLEKDNIILCQHNRKRDNYIKQQKRKEKNANNFTFMLKGSTQNIMNINEKEYDLAIIGCGVGGHAAAINAMERNLKVIIFAGDENCIGGTCVNVGCIPSKALLYATNKYRELKNLDKLYYYGIHSNIFQNNKNTEIENNQLVSNSFQINITKLKEYTQSVIDKLRNGISHGFKTLKFNKNSEHVQVIYEHGQLLDKNTIKSKKSGNTYKVKNIIIATGSVPNIPNNVEIDDKSVFTSDMAVKLVGLKNYMSIIGMGIIGLEFADIYTALGSEITFLEYSSELLPIIDNDVAKYFERVFLKNKPVNYHLNTEVKYIKASKNNNPVIIGYSHRTGNDDNEKKNMTDVKELYVDSCLVATGRNPNTQNLGLEKLKIQMNRGYVSVNDNLQVKMENNEIYDNIFCIGDANGKQMLAHTASYQALKVIDFIEKKEKKNVNINVENNLSKPILYKNIPSVCYTNPELAFIGLTEKEAKVLYPDNVGVEISYYKSNSKILCENNISLNNNKKNNSYNKGQYNINDNTNGMVKIIYKEDTKEILGMFIVGNYASVLIHEAVLAINLKLSAFDLAYMVHSHPTVSEVLDTAFKSISKIRTH
Protein: Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial (Protein N27C7-4) (Q8WYQ3)
Organism: Homo sapiens (Human)
Function: May be involved in the maintenance of mitochondrial organization and mitochondrial cristae structure.
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:24934289}. Note=Enriched at the cristae junctions. {ECO:0000269|PubMed:24934289}.
Interaction partners:
- MICOS complex subunit MIC25
- MICOS complex subunit MIC19
- MICOS complex subunit MIC60
- MICOS complex subunit MIC13
- MICOS complex subunit MIC26
- MICOS complex subunit MIC27
- Coiled-coil-helix-coiled-coil-helix domain-containing protein 2
- MICOS complex subunit MIC10
- Mitochondrial intermembrane space import and assembly protein 40
- Matrin-3
Sequence:
MPRGSRSAASRPASRPAAPSAHPPAHPPPSAAAPAPAPSGQPGLMAQMATTAAGVAVGSAVGHVMGSALTGAFSGGSSEPSQPAVQQAPTPAAPQPLQMGPCAYEIRQFLDCSTTQSDLSLCEGFSEALKQCKYYHGLSSLP
Protein: Protein LURE 1.3 (AtLURE1.3) (Cysteine-Rich Peptide 810_1.3) (CRP810_1.3) (Defensin-like protein 214) (Q4VP10)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pollen tube attractants guiding pollen tubes to the ovular micropyle. Attracts pollen tubes from both A.thaliana and A.lyrata.
Subcellular location: Secreted {ECO:0000269|PubMed:23271953}. Note=found at the micropylar end of the female gametophyte, possibly at the filiform apparatus of the synergid cell. Difuses to the surface of the funiculus of the ovule through the micropyle. {ECO:0000269|PubMed:23271953}.
Interaction partners:
- Pollen receptor-like kinase 5
- Pollen receptor-like kinase 3
- Pollen receptor-like kinase 4
- Pollen receptor-like kinase 6
- MDIS1-interacting receptor like kinase 1
Sequence:
MKLPFIFLITLLIFVSSCTSILINESSDEERTYSFSPTTSPFDPRSLNQELKIGRIGYCFDCARACMRRGKYIRTCSFERKLCRCSISGIK
Protein: 3'\5'-cyclic-nucleotide phosphodiesterase PDE1 (Q5AGE4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Phosphodiesterase
- Adenylate cyclase
- Guanylate kinase
- GMP synthase
- Adenosine kinase
- AMP deaminase
- Adenine phosphoribosyltransferase
- Inosine triphosphate pyrophosphatase
- Apyrase
- Adenylosuccinate lyase
Sequence:
MSFEITILGSSGGPLEGSTCSILLKPANISYHDIINDNLPDQVLCIDAGSGMGKLAEIIHQETTTKTSYCNFLQYYPDCETVSYYYHPNVTITTPFSNFQPGRPILHTQNIFNNLQNYLISHSHLDHVCSVVINSAGFNKNMSNKILYGSHYTINAMQQHLFNGKVWPNMPSFKIVNLNYLESNRSERIGIYTVKMFDLSHGEFNKLTEDKEDAQHHSNSNSNSNNIWGKRYDRRRSSITTIPQNTSGLIIKNSEALNHHYLSSAFLITLEVPCTIKEPPSSILVFGDFESDLTSKLSRNLFIWKSIAPLILRNQLKAIVLECSNCKEIAANELYGHLTPKLLIYELKQLAHECKQLDTATTSTEQPLLGLNVIVNHVKEPIADPNQESQLHDPRKRILAELNKLNEIEKLGCNISIALSGTSIIV
Protein: Myosin-9 (Myosin XI C) (AtXIC) (F4HXP9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Involved in trafficking of Golgi stacks and mitochondria.
Interaction partners:
- Myosin-binding protein 7
- Myosin-binding protein 1
- Nuclear transport factor 2
Sequence:
MVRECFTFLNIFVLHSIGSHVWFEDPEVAWIDGEVEKINGQEVVIQATTGKKVTAKLSKIYPKDVEAPAGGVDDMTKLSYLHEPGVLQNLKIRYELNEIYTYTGNILIAINPFQRLPHIYDAHMMQQYKGAPLGELSPHVFAVADVAYRAMINEGKSNSILVSGESGAGKTETTKMLMRYLAYLGGRAVTEGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKQGRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPQEEIEKYKLGHPKTFHYLNQSKCFELVGISDAHDYLATRRAMDIVGISEKEQEAIFRVVAAILHIGNIDFTKGKEVDSSVPKDEKSKFHLKTAAELLMCDLKALEDALCKRVMITPEEVIKRSLDPQSAVTSRDGLAKTVYSRLFDWLVDKINKSIGQDANSRSLIGVLDIYGFESFKTNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEAIDWSYIEFVDNQDVLDLIEKKPGGIVALLDEACMFPKSTHETFANKLYQTFKTHKRFIKPKLSRTDFAVAHYAGEVLYQSELFLDKNKDYVIPEHQDLLGASKCPFVVGLFPPLPEETSKSSKFSSIGSRFKLQLQQLMETLNCTEPHYIRCVKPNNLLKPAIFENVNIMQQLRCGGVLEAIRISCAGYPTRKPFFEFINRFGLLSPAALEGNFDEKVACQKILDNMGLKGYQIGKTKVFLRAGQMAELDARRAEVLSSAAKKIQRRIRTHQAQKRFIVLRKATISLQAICRGRLSCKHYDNLRREAAAVKIQKNGRRHYSRKSYKKLHVASLVVQTGLRAMAARKQFRFRKQTKAATIVQAQWRCHRAISYYKKLKNGVVLSQTRWRGRLAKRELRKLKMAARETGALKEAKDMLEKKVEELTYRVQLEKRSRGDLEEAKTQEILKLKSSFEEMRKKVDETNALLLKEREAAKKAAEEAPPVIKETQILVEDTKKIELMTEELESVKVTLENEKQRADDAVRKFEEAQESLEDKKKKLEETEKKGQQLQESLTRMEEKCSNLESENKVLRQQAVSMAPNKFLSGRSRSILQRGSESGHLAVDARSNLDLHSHSINHRDPSEVEDKPQKSLNEKQQENQDLLIRSIVQHLGFQGNRPITACIIYKCLLQWRSFEVERTSVFDRIIQTIGHAIETQDNNNTLAYWLSNTSTLLLLLQRTLKASGAAGMAPQRRRSSSATLFGRMSQSFRGAPPGVNLAMINGAAGGGADTFRQVEAKYPALLFKQQLTAYVEKIYGMIRDNLKKEISPLLGLCIQAPRTSRASLVKGASRSVGNTAAQQALIAHWQGIVKSLTNFLNTLKSNNVPSFLVRKVFTQIFSFINVQLFNSLLLRRECCSFSNGEYVKAGLSELEHWCFKATNEYAGSSWDELKHIRQAIGFLVVHQKPKKTLDEISHDLCPVLSIQQLYRISTMYWDDKYGTHSVSPDVIANMRVLMTEDSNNAVSNSFLLDDDSSIPFSVDDLSKSMEKFEIADIEPPPLIRENSGFSFLLPVSE
Protein: Virus-induced 1 (Virus-induced RNA 1, isoform D) (Virus-induced RNA 1, isoform E) (Q3YBY4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDQLQQMMEPLREEIRHEEDLEQEHEDKEYLERKEKKEREEFDSSDDEDGEATTPVVMSETFNDEWAEFDQDQDREHDRNEDQDHDLDFENDLNNEIDIEENFVPIDLSNDIAVNDLAAADPNFPINEDAEFIVHPAVIRTMPMFEKLSLGEPAK
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q9M1Q0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDDSCAVCADNLEWVAYGSCGHREVCSTCVVRLRFVLDDPRCCICKTESPIVFVTKALGDYTRTINDFSTFPSAPREGRVGAFWYHEDTQAFFDDLDQYRMIKAMCRLSCGVCDKTEDKPREGGPRHHRQRIKSVEQLKGHLYHKHKLHMCGLCLEGRKIFICEQKLYTRAQLNQHIQTGDSEVDGSESERGGFAGHPMCEFCRNPFYGDNELYTHMSTEHYTCHLCQRSQPGQYEYYKNYDDLEIHFRRDHFLCEDDSCLAKKFTVFQNESELKRHNAIEHGGKMSRSQRSAALQIPTSFRYSRGNDQENRRGRPRSFRREPGDEEYNLAVHAALRLSESEYSRQEPAPPPSSAPPGFSENNNIHVDDTDPLIQPMESLSTTDMEPSSRYLQAVGSFGGGGSRLGESAFPPLSGQQSSGQNVESLPTNTMAARLRRQTNRTSTASAIASPSQGWPVINRGPGQASITSGGNHSSSGWPAIGRTPVQASSSSVQSRSHNRVSQPRPLASAVPQAARNANRIPHSSSAPNLSDTRSLQPSHSDFPPVSSAVVQNRKTSSTTTQGSSNTQPPPDVQSANKSLIEKMRSALGHDEDVFVAFRNISGQYRQGSIDAKTYLEYVQGYGLSHLVIDLARLCPDPKRQKELIDTHNASLREEDSKDNGRSAAQSSSQPKESQSSKKNKGKAVKVVDPKETLADNFMDTVRRLQSSQNPQEEEEEAISKDKNTYRSDKGKSQVVGTDSSSTGSKQQRKKTSKFHRVRLGDGSMAALLDLNNSTRESEQESKDSNSNSNQNQTGGLPVRGVWRKGGANLFS
Protein: Ionotropic receptor 31a, isoform C (M9PCT4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Ionotropic receptor 8a
- Ionotropic receptor 40a
- IP13856p
- Ionotropic receptor 41a
- Ionotropic receptor 92a
- Ionotropic receptor 60a
- Ionotropic receptor 21a
- Ionotropic receptor 93a
- Ionotropic receptor 25a
Sequence:
MNLLISMFILILAAGEGEIIPSMEESVVTNFVKSLVKTKQAIVFSCLFKDFKEISLALMRINQFVSVVNLNQSYSLTSILTRENYARTSVMVNARCSGSSELLFEASENRYFNKTYQWFLWGVDLEVQSLFPLNLNYVGPNAQITYVNETADGYAYWDIHSKGRHLKSNLEINLIATLINDTLNIARDIFHLQSIDFRGQFNGLTLRGASVIDKEDIISNEQIESILSRPTKDAGVAAFIKYHYELLGLLRERFNFTVNFRNSRGWAGRLGNTTFRLGLLGIVMRNEADIAASGAFNRINRFAEFDTIHQSWKFETAFLYRYTSDLDTHGKSGNFLSPFSDRVWLFCLLTLGAFSIIWVLFEIIDYKILRIRVNSQKLEHLNQKSSVICIKTTCIERILQTFGACCQQGLDPNPVDRSVRFLVMTLFLFSLVMYNYYTSSVVGGLLSSSDQGPSTVDEITASPLKISFEDIGYYKVLFRESQNRSITRLIEKKLSSSRSLNELPIFSHIEDAVPYLKAGGFAFHCEVVDAYPVISEYFDANEICDLREVSGLMEVEILNWILHKNSQYTEIFKTAMCNAQEKGFVERILRRRQIKKPACQSLYTVYPVSLSGVLPGFVILICGFGASLLLLCLEKVYAHFGPRKFCGF
Protein: Cholecystokinin (CCK8) [Cleaved into: Cholecystokinin-8 (CCK8); Cholecystokinin-12 (CCK12); Cholecystokinin-26 (CCK26); Cholecystokinin-36 (CCK36); Cholecystokinin-69 (CCK69)] (O93464)
Organism: Carassius auratus (Goldfish)
Function: This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut (By similarity). Induces the secretion of gonadotropin and growth hormone from the pituitary. Suppresses food intake and decreases the expression of preprosomatostatin genes in the forebrain.
Subcellular location: Secreted {ECO:0000303|PubMed:9493851, ECO:0000305}.
Interaction partners:
Sequence:
MNAGICVCVLLAALSTSSCLSLPAVSEDGGQSDLGIVMEHTRHTRAAPSSGQLSLLSKAEDDEEPRSSLTELLARIISTKGTYRRSPSPKSKSMGNNHRIKDRDYLGWMDFGRRSAEEYEYSS
Protein: Cytochrome p450 CYP199A2 (EC 1.14.99.15) (4-methoxybenzoate O-demethylase CYP199A2) (4-methoxybenzoate monooxygenase (O-demethylating)) (Q6N8N2)
Organism: Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Function: The oxidative demethylation of 4-methoxybenzoate requires the participation of the monooxygenase CYP199A2, the ferredoxin-like protein ThcC/RPA1872 and a ferredoxin reductase to mediate the transfer of electrons from NADH to CYP199A2. It is also active with 4-ethylbenzoate.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- PDR/VanB family oxidoreductase
- Condensation domain-containing protein
- 2Fe-2S iron-sulfur cluster-binding protein
- 4-hydroxybenzoate 3-monooxygenase)
- 2Fe-2S iron-sulfur cluster-binding protein
- 4-hydroxybenzoate--CoA/benzoate--CoA ligase
- Possible 4-hydroxybenzoyl-CoA thioesterase
- Hybrid non-ribosomal peptide synthetase/type I polyketide synthase)
- DNA polymerase I
- Small ribosomal subunit protein uS12
Sequence:
MTTAPSLVPVTTPSQHGAGVPHLGIDPFALDYFADPYPEQETLREAGPVVYLDKWNVYGVARYAEVYAVLNDPLTFCSSRGVGLSDFKKEKPWRPPSLILEADPPAHTRTRAVLSKVLSPATMKRLRDGFAAAADAKIDELLARGGNIDAIADLAEAYPLSVFPDAMGLKQEGRENLLPYAGLVFNAFGPPNELRQSAIERSAPHQAYVAEQCQRPNLAPGGFGACIHAFSDTGEITPEEAPLLVRSLLSAGLDTTVNGIAAAVYCLARFPDEFARLRADPSLARNAFEEAVRFESPVQTFFRTTTRDVELAGATIGEGEKVLMFLGSANRDPRRWDDPDRYDITRKTSGHVGFGSGVHMCVGQLVARLEGEVVLAALARKVAAIEIAGPLKRRFNNTLRGLESLPIQLTPA
Protein: 2-oxoisovalerate dehydrogenase subunit beta 1, mitochondrial (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component beta chain) (BCKDE1B) (BCKDH E1-beta) (Q9SAV3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: 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) (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P21953}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha 2, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha 1, mitochondrial
- Putative 2-dehydropantoate 2-reductase
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase 2, mitochondrial
- Dihydrolipoyl dehydrogenase 1, mitochondrial
- Dihydrolipoyl dehydrogenase 1, chloroplastic
- Dihydrolipoyl dehydrogenase 2, chloroplastic
- Pyruvate dehydrogenase E1 component subunit alpha-3, chloroplastic
- Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial
Sequence:
MAALLGRSCRKLSFPSLSHGARRVSTETGKPLNLYSAINQALHIALDTDPRSYVFGEDVGFGGVFRCTTGLAERFGKNRVFNTPLCEQGIVGFGIGLAAMGNRAIVEIQFADYIYPAFDQIVNEAAKFRYRSGNQFNCGGLTIRAPYGAVGHGGHYHSQSPEAFFCHVPGIKVVIPRSPREAKGLLLSCIRDPNPVVFFEPKWLYRQAVEEVPEHDYMIPLSEAEVIREGNDITLVGWGAQLTVMEQACLDAEKEGISCELIDLKTLLPWDKETVEASVKKTGRLLISHEAPVTGGFGAEISATILERCFLKLEAPVSRVCGLDTPFPLVFEPFYMPTKNKILDAIKSTVNY
Protein: Ubiquitin-like-conjugating enzyme ATG10 (EC 2.3.2.-) (Autophagy-related protein 10) (APG10-like) (Q9H0Y0)
Organism: Homo sapiens (Human)
Function: E2-like enzyme involved in autophagy. Acts as an E2-like enzyme that catalyzes the conjugation of ATG12 to ATG5. ATG12 conjugation to ATG5 is required for autophagy. Likely serves as an ATG5-recognition molecule. Not involved in ATG12 conjugation to ATG3 (By similarity). Plays a role in adenovirus-mediated cell lysis.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Ubiquitin-like protein ATG12
- Ubiquitin-like modifier-activating enzyme ATG7
- Autophagy protein 5
- Immunity-related GTPase family M protein
- Autophagy-related protein 13
- Autophagy-related protein 16-1
- Ubiquitin-like-conjugating enzyme ATG3
- RB1-inducible coiled-coil protein 1
- Microtubule-associated protein 1 light chain 3 alpha
- Gamma-aminobutyric acid receptor-associated protein-like 2
Sequence:
MEEDEFIGEKTFQRYCAEFIKHSQQIGDSWEWRPSKDCSDGYMCKIHFQIKNGSVMSHLGASTHGQTCLPMEEAFELPLDDCEVIETAAASEVIKYEYHVLYSCSYQVPVLYFRASFLDGRPLTLKDIWEGVHECYKMRLLQGPWDTITQQEHPILGQPFFVLHPCKTNEFMTPVLKNSQKINKNVNYITSWLSIVGPVVGLNLPLSYAKATSQDERNVP