wanglab/gogpt-training-data huggingface dataset:
Protein: PEP-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL (EC 2.7.1.121) (P76014)
Organism: Escherichia coli (strain K12)
Function: ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL-ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone bound to DhaK. DhaL acts also as coactivator of the transcription activator DhaR by binding to the sensor domain of DhaR. In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity. In the absence of dihydroxyacetone, DhaL-ADP is converted by the PTS to DhaL-ATP, which does not bind to DhaR.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- PEP-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit DhaK
- PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM
- PTS-dependent dihydroxyacetone kinase operon regulatory protein
- Glycerol dehydrogenase
- Anaerobic glycerol-3-phosphate dehydrogenase subunit A
- Aerobic glycerol-3-phosphate dehydrogenase
- Glycerol-3-phosphate dehydrogenase [NAD
- Anaerobic glycerol-3-phosphate dehydrogenase subunit B
- Anaerobic glycerol-3-phosphate dehydrogenase subunit C
Sequence:
MSLSRTQIVNWLTRCGDIFSTESEYLTGLDREIGDADHGLNMNRGFSKVVEKLPAIADKDIGFILKNTGMTLLSSVGGASGPLFGTFFIRAAQATQARQSLTLEELYQMFRDGADGVISRGKAEPGDKTMCDVWVPVVESLRQSSEQNLSVPVALEAASSIAESAAQSTITMQARKGRASYLGERSIGHQDPGATSVMFMMQMLALAAKE
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q9VJ14)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin
- GH17761p
- Ubiquitin-ribosomal protein eL40 fusion protein
- Autophagy-related 8b, isoform A
- Autophagy-related 8a, isoform A
- ubiquitinyl hydrolase 1
- Caspase-8
- Ubiquitin-like domain-containing protein
- RE23139p1
Sequence:
MRASIPPGIRVVRGPNWIWSNQDDGEGHVGTVCEIGRCGSTHSPENTVVVNWDSGHRTNYRVGYQNQYDLIIVDNAQVGVRHSNVVCDGCSKAGIAGIVFKCAQCPNYHLCAYCYAEDLHDIEHPFIRYTTPNSLGVRLPMRKGAKRIQLRGIFVGSKVVRGPDWEWNEQDGGEGRTGRVMEIRGWDNESCRSVANVAWVTGSTNVYRLGHKGNVDLKYITATCGGHYYKDHMPVLGQTEELQPVAPMVKPSFSVGDRVKVCLEVDALMKLQQGHGGWNPRMVEHLSKLGTVHRITDKGDIRVQYENCPNRWTFHPAALVKVVSFRVGDLVTIINDANKVQQLQKGHGEWIEIMRHALGKICKVVKVYSDGDLRIQQLDDGFEWTLNPKCVKLERSPLATAAERSNSMMDLSHRRADHVMTPLSGLSGSSVADKLVREAAQGHLDFVRQYLDVNPSQVDVMSGGKACIQVASHQGYVDLVSYLISKGANVNAVDKEGDSALHYAAFGNQPATMRVLLQHGAEVNFLNSSHCSALHICAHKKTPHCVRELLQHNANVNIQDSYGDTALHDAIGKENTEVVELLCNAPNLDFTVKNNRGFNVLHHAALKGNVVAARRILLLSRQLVNVRKDDGFAALHLAALNGHAQVVETLVTEGQAELDIRNNRQQTPFLLAVSQGHAGVIERLVRLSCDVNAKDEDGDNAMHLCVIKKSNLQSAAEPQPEEAPEIHKFYLSLVHSSIRPEDRLMYSILIYLSRAGCRVELNNANASIFEWITDRHIRQLIFGQQGEAESLPRNLQALEVSAGSADGEESSASAGAESNGAGPGSVAAPPPPQRQTFELMPKPNDIPAIGVGASPSTPSASPGVKKLNSDATPQNVSPQVAPRKKAPKPPVTTSSSSTALEAGAAGPSTSPVIVPGPHECIVCNEILPMVRFEPCQHQIACEECGIRMKKCLRCAVAIERRLTVSGRVVALPTSTSSPSDPTRLPSGDLLRYLENKVLEFEESHFCGICMERKRDVAFLCGHGACSHCAETLRTCHMCRKTILKKINLY
Protein: Xanthotoxin 5-hydroxylase CYP82C2 (8-methoxypsoralen 5-hydroxylase CYP82C2) (EC 1.14.14.-) (Cytochrome P450 82C2) (Indole-3-carbonyl nitrile 4-hydroxylase CYP82C2) (EC 1.14.14.165) (O49394)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthetic pathway to 4-hydroxyindole-3-carbonyl nitrile (4-OH-ICN), a cyanogenic metabolite required for inducible pathogen defense. Converts indole-3-carbonyl nitrile (ICN) into 4-OH-ICN. Can hydroxylate xanthotoxin (8-methoxypsoralen) to form 5-hydroxyxanthotoxin (5-hydroxy-8-methoxypsoralen) in vivo and in vitro.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Berberine bridge enzyme-like 3
- Berberine bridge enzyme-like 4
- Transmembrane protein
- At3g62990
- Peroxidase 62
- Uncharacterized protein
- Uncharacterized protein At4g36500
- Glutaredoxin family protein
- Hyperosmolality-gated Ca2+ permeable channel 2.1
- Putative pectinesterase
Sequence:
MDTSLFSLFVPILVFVFIALFKKSKKPKHVKAPAPSGAWPIIGHLHLLSGKEQLLYRTLGKMADQYGPAMSLRLGSSETFVVSSFEVAKDCFTVNDKALASRPITAAAKHMGYDCAVFGFAPYSAFWREMRKIATLELLSNRRLQMLKHVRVSEISMVMQDLYSLWVKKGGSEPVMVDLKSWLEDMSLNMMVRMVAGKRYFGGGSLSPEDAEEARQCRKGVANFFHLVGIFTVSDAFPKLGWFDFQGHEKEMKQTGRELDVILERWIENHRQQRKVSGTKHNDSDFVDVMLSLAEQGKFSHLQHDAITSIKSTCLALILGGSETSPSTLTWAISLLLNNKDMLKKAQDEIDIHVGRDRNVEDSDIENLVYIQAIIKETLRLYPAGPLLGHREAIEDCTVAGYNVRRGTRMLVNVWKIQRDPRVYMEPNEFRPERFITGEAKEFDVRGQNFELMPFGSGRRSCPGSSLAMQVLHLGLARFLQSFDVKTVMDMPVDMTESPGLTIPKATPLEILISPRLKEGLYV
Protein: Neuropeptide Y receptor type 4 (NPY4-R) (NPYR-D) (Pancreatic polypeptide receptor 1) (PP1) (Q61041)
Organism: Mus musculus (Mouse)
Function: Receptor for neuropeptide Y and peptide YY. The rank order of affinity of this receptor for pancreatic polypeptides is PP >> PYY >= NPY.
Subcellular location: Cell membrane {ECO:0000269|PubMed:8641440}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pro-neuropeptide Y
- Peptide YY
- Pancreatic polypeptide prohormone
Sequence:
MNTSHFLAPLFPGSLQGKNGTNPLDSPYNFSDGCQDSAELLAFIITTYSIETILGVLGNLCLIFVTTRQKEKSNVTNLLIANLAFSDFLMCLICQPLTVTYTIMDYWIFGEVLCKMLTFIQCMSVTVSILSLVLVALERHQLIINPTGWKPSIFQAYLGIVVIWFVSCFLSLPFLANSTLNDLFHYNHSKVVEFLEDKVVCFVSWSSDHHRLIYTTFLLLFQYCIPLAFILVCYIRIYQRLQRQKHVFHAHACSSRAGQMKRINSMLMTMVTAFAVLWLPLHVFNTLEDWYQEAIPACHGNLIFLMCHLLAMASTCVNPFIYGFLNINFKKDIKALVLTCHCRSPRGESEHLPLSTVHTDLSKGSMRMGSKSNFI
Protein: Polyprenyl transferase mpaA (EC 2.5.1.-) (Mycophenolic acid biosynthesis cluster protein A) (W6QIT8)
Organism: Penicillium roqueforti (strain FM164)
Function: Polyprenyl transferase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893. MpaA is a Golgi apparatus-associated enzyme that catalyzes the prenylation of 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) to yield farnesyl-DHMP (FDHMP). The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (Probable).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:A0A0B5L778}; Multi-pass membrane protein {ECO:0000255}. Note=Membrane association is functionally relevant because mpaA must ostensibly interact with its membrane-embedded substrate FPP. {ECO:0000305}.
Interaction partners:
- Probable hexaprenyl pyrophosphate synthase
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Flavin prenyltransferase PAD1, mitochondrial
- isopentenyl-diphosphate Delta-isomerase
- Phosphatidate cytidylyltransferase
- Ferulic acid decarboxylase 1
- Flavin prenyltransferase PAD1, mitochondrial
- Ferulic acid decarboxylase 1
- Ferrochelatase
Sequence:
MVGSMENPGSWGLACLLISTSRFNRYMPYYTMMAAVWSTLIAGALKLQEDPASLSVEYILFKAGLCFVHCLLLCGAGNTWNDLIDRDIDARVERTKMRPLASGKVSTVEALVWMVGQYFLSVKMLDLILDNRSIWGLMLPLTASIMLYPYLKRPVFSRVFIYPQYILGLAVAYPSITGWASINGQEQSMSEIFTHCTPICLLIFFWCLYFNTAYSHQDSVDDRKMNINSAYVVAGQRIRLFLAFLGALPLAVIPYVVLKINSPWLWFSWMAVWTVSIVMQIVRFDSKKLESGGRIHWDNFLLGLWTTVACIVEVGLQKVEFWNLI
Protein: Intraflagellar transport 88 (D4ACI9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MMENVHLAPETDEDDLYSGFNDYNPAYDTEELENDTGFQQAVRTSHGRRPPVTAKIPSTAVSRPIATGYGSKTSLTSSMGRPMTGTIQDGVARPMTAVRAAGFSKAALRGSAFDPLGQSRGPAPPLEAKNEDSPEEKIRQLEKKVNELVEESCIANSCGDLKLALEKAKDAGRKERVLVRQREQVTSPENINLDLTYSVLFNLASQYSANEMYAEALNTYQVIVKNKMFSNAGRLKVNMGNIYLKQRNYSKAIKFYRMALDQIPSVHKEMRIKIMQNIGITFIKTGQYSDAINSFEHIMSMAPSLKAGFNLILSCFAIGDREKMKKAFQKLIAVPLEIDEDDKYISPSDDPHTNLLIEAIKNDHLRQMERERKAMAEKYIMTAAKLIAPVIEASFAVGYNWCVEVVKASQYVELANDLEINKAITYLRQKDFNQAVDTLKMFEKKDSRVKSAAATNLSFLYYLENEFAQASSYADLAVSSDRYNPSALTNKGNTVFANGDYEKAAEFYKEALRNDSSCTEALYNIGLTYKKLNRLDEALDSFLKLHAILRNSAQVLCQIANVYELMEDPNQAIEWLMQLISVVPTDSQALSKLGELYDSEGDKSQAFQYYYESYRYFPSNIEVIEWLGAYYIDTQFCEKAIQYFERASLIQPTQVKWQLMVASCFRRSGNYQKALDTYKEIHRKFPENVECLRFLVRLCTDIGLKEVQEYATKLKRLEKMKEMREQRIKSGRDSGGGSRSKREGSAGSDASYVDPLGPQIERPKTAARKRIDEDDFADEELGDDLLPE
Protein: Modulator of FtsH protease YccA (P0AAC6)
Organism: Escherichia coli (strain K12)
Function: Negatively modulates the activity of the FtsH protease for membrane substrates. Overexpression or stabilizing YccA counteracts the FtsH-mediated degradation of SecY when the SecYEG preprotein translocator is jammed.
Subcellular location: Cell inner membrane; Multi-pass membrane protein. Note=There are conflicting results regarding the localization of the C-terminus of this protein: According to a report, the C-terminus localizes in the periplasm (PubMed:10357810). Another report gives the C-terminus in the cytoplasm (PubMed:15919996). We show the periplasmic location. {ECO:0000269|PubMed:10357810, ECO:0000269|PubMed:15919996}.
Interaction partners:
- Sulfurtransferase TusE
- Protease HtpX
- ATP-dependent zinc metalloprotease FtsH
- Uncharacterized protein YbhM
Sequence:
MDRIVSSSHDRTSLLSTHKVLRNTYFLLSLTLAFSAITATASTVLMLPSPGLILTLVGMYGLMFLTYKTANKPTGIISAFAFTGFLGYILGPILNTYLSAGMGDVIAMALGGTALVFFCCSAYVLTTRKDMSFLGGMLMAGIVVVLIGMVANIFLQLPALHLAISAVFILISSGAILFETSNIIHGGETNYIRATVSLYVSLYNIFVSLLSILGFASRD
Protein: Synaptotagmin-11 (Synaptotagmin XI) (SytXI) (Q9BT88)
Organism: Homo sapiens (Human)
Function: Synaptotagmin family member involved in vesicular and membrane trafficking which does not bind Ca(2+). Inhibits clathrin-mediated and bulk endocytosis, functions to ensure precision in vesicle retrieval. Plays an important role in dopamine transmission by regulating endocytosis and the vesicle-recycling process. Essential component of a neuronal vesicular trafficking pathway that differs from the synaptic vesicle trafficking pathway but is crucial for development and synaptic plasticity. In macrophages and microglia, inhibits the conventional cytokine secretion, of at least IL6 and TNF, and phagocytosis. In astrocytes, regulates lysosome exocytosis, mechanism required for the repair of injured astrocyte cell membrane (By similarity). Required for the ATP13A2-mediated regulation of the autophagy-lysosome pathway.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000305|PubMed:12925569}; Single-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:Q9R0N3}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9R0N3}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9R0N3}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q9R0N3}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9R0N3}. Lysosome membrane {ECO:0000250|UniProtKB:Q9R0N3}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9R0N3}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q9R0N3}. Cell projection, axon {ECO:0000269|PubMed:12925569}. Cell projection, dendrite {ECO:0000269|PubMed:12925569}. Postsynaptic density {ECO:0000250|UniProtKB:Q9R0N3}. Recycling endosome membrane {ECO:0000250|UniProtKB:O08835}; Single-pass membrane protein {ECO:0000250|UniProtKB:O08835}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:O08835}; Single-pass membrane protein {ECO:0000250|UniProtKB:O08835}. Perikaryon {ECO:0000269|PubMed:12925569}. Note=Localized in vesicles that travels in axonal and dendritic shafts in both anterograde and retrograde directions. In macrophages and microglia, recruited in phagosomes at early stages of phagocytosis (By similarity). Found in the core of the Lewy bodies in the brain of sporadic Parkinson disease patients (PubMed:12925569). {ECO:0000250|UniProtKB:Q9R0N3, ECO:0000269|PubMed:12925569}.
Interaction partners:
- E3 ubiquitin-protein ligase parkin
- Synaptotagmin-1
- Vesicle-associated membrane protein 2
- Synaptotagmin-2
- Coiled-coil domain-containing protein 62
- Clathrin coat assembly protein AP180
Sequence:
MAEITNIRPSFDVSPVVAGLIGASVLVVCVSVTVFVWSCCHQQAEKKQKNPPYKFIHMLKGISIYPETLSNKKKIIKVRRDKDGPGREGGRRNLLVDAAEAGLLSRDKDPRGPSSGSCIDQLPIKMDYGEELRSPITSLTPGESKTTSPSSPEEDVMLGSLTFSVDYNFPKKALVVTIQEAHGLPVMDDQTQGSDPYIKMTILPDKRHRVKTRVLRKTLDPVFDETFTFYGIPYSQLQDLVLHFLVLSFDRFSRDDVIGEVMVPLAGVDPSTGKVQLTRDIIKRNIQKCISRGELQVSLSYQPVAQRMTVVVLKARHLPKMDITGLSGNPYVKVNVYYGRKRIAKKKTHVKKCTLNPIFNESFIYDIPTDLLPDISIEFLVIDFDRTTKNEVVGRLILGAHSVTASGAEHWREVCESPRKPVAKWHSLSEY
Protein: Protocadherin gamma subfamily A, 8 (Q6PHX8)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MAASKNQHRHGRLVLLCTLMGTLCKISVGQIRYSVPEETDKGTVVGNISKDLGLEPRELAERGVRIVSRGRSQLFSLNPRGGSLVTAGRIDREELCAQSTPCLVNINILVEEKGKLFGVEIEITDINDNNPKFHVGDLEVKINEIAAPGARYPLPEAVDPDVGINSLQSYQLSPNRHFSLHLQTGDDGTINPELVLERTLDREEEPTHHLVLTASDGGEPRRSSTALIQITVLDTNDNAPVFDQPVYRVKVLENVAPGTLLLTVRASDPDEGVNGKVTYKFRKINEKQSLLFHLHGNTGEMTVAKNLDYEECSLYEMEIQAEDVGALLGRSKVIIMVEDVNDNRPEVTITSLFNPVLENSLPGTVIAFLNVHDQDSGKNGQVVCYTHDNLPFKLEKSIDNYYRLVTWKYLDREKVSTYNITVIASDLGAPPLSTETYIALTVADTNDNPPRFSHTSYTAYLPENNLRGASIFSLTAHDPDSQENAQVTYSVSEDTIQGVPLSSYISINSDTGILYALQSFDFEKIQDLQLLVIATDSGSPPLSSNVSLSLFVLDQNDNAPEILYPSFPTDGSTGVELAPRSAEPGYLVTKVVAVDKDSGQNAWLSYRLLKASEPGLFSVGLHTGEVRTARALLDRDALKQNLVMAVQDHGQPPLSATVTLTVAVANSIPEVLADLSSIMTPEVPEDSDLTLHLVVAVAVVSCVFLVFVIVLLALRLQRWQKSRQLQGSRSGLAPAPPSHFVGIDGVQAFLQTYSHEVSLTSGSQTSHIIFPQPNYADMLINQESCEKNDSLLTSIDFHENKDEDACAPQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: Uncharacterized protein (Q38B16)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLQSKVVGAQARGAGAQPYQAVNGNLDKHNNPMSLSLKEHKRRLRSLLHPSHSGSSDSSYPAASKFSLPDRSAQASVRPSPRIRSYRMQTGNTVSPVNSSTPSAVRRQRSNISSTCLTPGRCSPRRALGGKRRPPEDTFNTFATYDRVLQFTLLHSGRFHSKTTNGDSAEQESTATRSQQDSQQLSAISKTPKDQATPPEQPVLHRARSVFVDRPLNGTEDAAVPGLRSFISTMATPRPEGGQAPLFSARGRYFKSPVRTRGGNAPKSGDAAETEDVVPATIVFKLDAALAKLCESKEAEVMREENGAPMGQEGTSLNGVDGEFCQKHSYHDSRSEDLSCSAVGGALRPGENGVAFDGKLGAVERNSLRKVVSSGSHLKSALKPPKADITRSQVLSSDGSCLTPANSLADIPSAAKNLPSPTTVRPRPRQLKLPSTLVDSKASVSEEANNVSSDRPVGKLVRFSDAENIGHAIMKESPRTPLRRGVGRSTLPATPSQKMTPKTRRRDKLLPTQDYTEGQLICVSSSRRKKSGHTVQKGGLVSSTEASAVTKVKTLPSGNGEVKPTEDVTSKVVSDFNQVEKVTPDGGKGSNITSSRKSASLDSSVTAKSSIQLGVAPTNEQAPTES
Protein: Serine palmitoyltransferase 1 (EC 2.3.1.50) (Long chain base biosynthesis protein 1) (LCB 1) (Serine-palmitoyl-CoA transferase 1) (SPT 1) (SPT1) (O35704)
Organism: Mus musculus (Mouse)
Function: Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates. The SPTLC1-SPTLC2-SPTSSB complex displays a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme has the ability to use a broader range of acyl-CoAs (By similarity). Required for adipocyte cell viability and metabolic homeostasis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:1317856, ECO:0000269|PubMed:26301690}; Single-pass membrane protein {ECO:0000269|PubMed:1317856}.
Interaction partners:
- Serine palmitoyltransferase 2
- Serine palmitoyltransferase 3
- Serine palmitoyltransferase small subunit A
- 3-ketodihydrosphingosine reductase
- ORM1-like protein 3
- Serine palmitoyltransferase small subunit B
- ORM1-like protein 1
- ORM1-like protein 2
- Ceramide glucosyltransferase
- Ceramide kinase
Sequence:
MATVAEQWVLVEMVQALYEAPAYHLILEGILILWIIRLVFSKTYKLQERSDLTAKEKEELIEEWQPEPLVPPVSKNHPALNYNIVSGPPTHNIVVNGKECVNFASFNFLGLLANPRVKATAFSSLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMKTEEAIIYSYGFSTIASAIPAYSKRGDIIFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDQKNPRKARVTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISIDDIDLISANMENALASVGGFCCGRSFVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPDIFAVLKKKCQNIHKSLQGVSGLKVVGESLSPALHLQLEESTGSREKDVKLLQAIVDQCMDKGIALTQARYLDKEEKCLPPPSIRVVVTVEQTEEELQRAASTIREAAQAVLL
Protein: Peptide chain release factor 2 (RF-2) (P9WHG1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein bL27
- Large ribosomal subunit protein bL12
- Large ribosomal subunit protein uL16
- Small ribosomal subunit protein bS16
- Large ribosomal subunit protein bL20
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein bS6
- Small ribosomal subunit protein uS12
Sequence:
MDPDRQADIAALDCTLTTVERVLDVEGLRSRIEKLEHEASDPHLWDDQTRAQRVTSELSHTQGELRRVEELRRRLDDLPVLYELAAEEAGAAAADAVAEADAELKSLRADIEATEVRTLLSGEYDEREALVTIRSGAGGVDAADWAEMLMRMYIRWAEQHKYPVEVFDTSYAEEAGIKSATFAVHAPFAYGTLSVEQGTHRLVRISPFDNQSRRQTSFAEVEVLPVVETTDHIDIPEGDVRVDVYRSSGPGGQSVNTTDSAVRLTHIPSGIVVTCQNEKSQLQNKIAAMRVLQAKLLERKRLEERAELDALKADGGSSWGNQMRSYVLHPYQMVKDLRTEYEVGNPAAVLDGDLDGFLEAGIRWRNRRNDD
Protein: Xylanase inhibitor protein XIP (OsXIP) (Class III chitinase homolog XIP) (Q5WMW5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Fungal xylanase inhibitor. Possesses competitive inhibiting activity against several fungal endo-1,4-beta-D-xylanases belonging to glycoside hydrolase family 10 (GH10) and family 11 (GH11). May function in plant defense against secreted fungal pathogen xylanases. Is similar to class III chitinases, but does not exhibit chitinase activity.
Subcellular location: Secreted {ECO:0000269|PubMed:18511458}.
Interaction partners:
Sequence:
MALRRLAALLSLAVLLSAGLAAVSATSQNTGDTVIIWGRNKDEGSLREACDAGRYTTVIISFLSAFGYIPGTYKLDISGHQVSAVGPDIKYCQSKGKLILLAIGGQGGEYSLPSSQAAVDLHDHLWYSYLGGRRNGVYRPFGDANVNGIDFFIDQGAREHYNELAKMLYDHNKDYRATVGVMVTATTRCGYPDHRLDEALATGLFHRIHVKMFSDGRCPAWSRRQSFEKWAKTYPQSRVLIGVVASPDVDKDAYMPPEALNNLLQFINKQPNFGGVMVWDRFYDKKTGFTAHL
Protein: Small ribosomal subunit protein uS4 (40S ribosomal protein S9) (Q6ZWN5)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P46781}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P46781}.
Interaction partners:
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS8
- Large ribosomal subunit protein eL14
- Small ribosomal subunit protein eS26
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein eS24
- Small ribosomal subunit protein eS12
Sequence:
MPVARSWVCRKTYVTPRRPFEKSRLDQELKLIGEYGLRNKREVWRVKFTLAKIRKAARELLTLDEKDPRRLFEGNALLRRLVRIGVLDEGKMKLDYILGLKIEDFLERRLQTQVFKLGLAKSIHHARVLIRQRHIRVRKQVVNIPSFIVRLDSQKHIDFSLRSPYGGGRPGRVKRKNAKKGQGGAGAGDDEEED
Protein: Glutathione transferase omega-1 (EC 2.5.1.18) (Glutathione-dependent dehydroascorbate reductase) (EC 1.8.5.1) (Monomethylarsonic acid reductase) (MMA(V) reductase) (EC 1.20.4.2) (P34345)
Organism: Caenorhabditis elegans
Function: Exhibits glutathione-dependent thiol transferase activity (By similarity). Has dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid (By similarity). Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) (By similarity). Protects against environmental stress and oxidative stress.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Glutathione S-transferase kappa 1
- glutathione-specific gamma-glutamylcyclotransferase
- Glutathione S-transferase P 10
- Glutathione S-transferase P
- Glutathione reductase, mitochondrial
- Probable glutathione S-transferase 6
- Glutathione peroxidase 3
- Probable glutathione S-transferase 8
- Probable glutathione S-transferase 5
- Glutathione synthetase
Sequence:
MVLTGVTSKAIRKGDAEPPLSKGSFRVYNMRFCPWAERAMLYVAAKGIEAEVVNLNVTDKLEWYWTKHYQGKAPAVEHNGKVVIESGFIPEYLDDAFPETRILPTDPYEKVQQKLLADRLTAVAHAVPLLFAVMRDRTLKDEKQRKVFEVLKQAENLLANDFYAGSQPGYPDYLSFPFFEKIWWSASLDGVVDLPTIEFPGEEEYPKLTKWFQKMISSDVVQSVTQSLEHGAAFMNAYATHQELNYDLGL
Protein: Trace amine-associated receptor 1 (Q5QNP6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDDHINISQTESWEKPLLCYEFSNRSCQKFVYPLDTRILLYMLFSISSIITIIGNLLVIITVVHFRQLHTPTNYLILSLAVADLLVGGVVMPPSMLRSIETCWYLGDLFCKIHSSLDVTLCTASILNLCIISLDRYYAICHPFQYHSKMTSLATLIMIIICWTVSAVLGFGMIFMELNILGVEDFYYENIRCDGGCFVFQSKTGGTVFSLICFYIPAFVMLGVYLKILHEAQRQVQAIQSVNSELKKEGKATKTLAIIMGVFLTFWIPFFLCNLIDPLIGYSVPSLVFDLFLWVGYYNSTCNPIVYAFFYSWFRHAFRVILSKRVFQTNSSRTILM
Protein: Nodulin-like domain-containing protein (Q381C3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MACSLRQCLLSYGVAESAMLREQVEEDVTTPVSEHEEEEEAAPTTHLLSPRGTVRLIDGYESTGHRDTHCLSPDSRERGSWIYHRPPIYGLQALSEPKRFWQLVVGALCCFVVSSSFTFNLYSGQLQAKFNFTQNDITSIFTGSDVAGILMLPLGAVYDKYGARPVFILALLTQPVGAILQALTYDDFIKGNLYLFIFYSALQAVGTWLLDTAAVMTLLSIFPSDKGPVVALSKVITGIGYGVIGAIHSAFFYGGEAKDTRNFFIFLASIGVVATVLGYMYLEDPPYVVKGSEVDTITRKERVTRRRLRRIYLRQRPSGLRFAIGFGIVAVLMVYLPVQAIVSMYFNLGHRYRVSFACTTVAILALYPVMALPLQCLERSQSLILPMTSTRCSERSSCVSRAASESVGSVACVDDLDYMAPQFHIKLADNIKTLRFWALMWTMFSLSGAEVLVLANMRFLLAAFDGGLLADTYVGYLLVLTSVGSGFGRIILSLFEMVSQNRSAEERIPITAALFVPAVVQVVALSLFFVLPAPLLAIPCFLVSFAGGCSAAASVIVVRTIFASDVGKYYNCITVATVVSSLLINRGLYGEVYTHEAMKEGKTICLGRQCVILPIIVVLVACVSSLLAVGYIHRDYSQHCEHMFELHKQRHASNEAPVKADHIGFNFKRSGKQSPAGGSAANI