GET /api/protein/UniProt/A0A6P5KHM7/?format=api
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{
"metadata": {
"accession": "A0A6P5KHM7",
"id": "A0A6P5KHM7_PHACI",
"source_organism": {
"taxId": "38626",
"scientificName": "Phascolarctos cinereus",
"fullName": "Phascolarctos cinereus (Koala)"
},
"name": "Serine palmitoyltransferase small subunit B",
"description": [
"Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases. The SPT complex is composed of SPTLC1, SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer consisting of SPTLC1 and SPTLC2/SPTLC3 forms the catalytic core. Within the SPT complex, SPTSSB stimulates the catalytic activity and plays a role in substrate specificity. SPT complexes with this subunit showing a preference for longer acyl-CoAs. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference"
],
"length": 84,
"sequence": "MPLADMMNLRYVKDYFAWLYYQYTLISCCAVLEPWERSMFNTILLTIVGMVVYTAYVFIPIHIRLAWEFFSEIFGDQSTASVSN",
"proteome": "UP000515140",
"gene": "SPTSSB",
"go_terms": null,
"protein_evidence": 3,
"source_database": "unreviewed",
"is_fragment": false,
"in_alphafold": true,
"in_bfvd": false,
"ida_accession": "23b61e0842cf0cb55f7e7f68da666ccdbb4943b7",
"counters": {
"domain_architectures": 4302,
"entries": 3,
"isoforms": 0,
"proteomes": 1,
"sets": 0,
"structures": 0,
"taxa": 1,
"dbEntries": {
"panther": 1,
"pfam": 1,
"interpro": 1
},
"proteome": 1,
"taxonomy": 1,
"similar_proteins": 4302
}
}
}