SPTSA_HUMAN
ID SPTSA_HUMAN Reviewed; 71 AA.
AC Q969W0; B2RD54; D3DS93; Q8WTZ7;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Serine palmitoyltransferase small subunit A {ECO:0000305};
DE AltName: Full=Small subunit of serine palmitoyltransferase A;
DE Short=ssSPTa;
GN Name=SPTSSA {ECO:0000312|HGNC:HGNC:20361}; Synonyms=C14orf147, SSSPTA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Brain, and Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, TOPOLOGY, IDENTIFICATION IN THE SPT COMPLEX, AND INTERACTION WITH
RP SPTLC1.
RX PubMed=19416851; DOI=10.1073/pnas.0811269106;
RA Han G., Gupta S.D., Gable K., Niranjanakumari S., Moitra P., Eichler F.,
RA Brown R.H. Jr., Harmon J.M., Dunn T.M.;
RT "Identification of small subunits of mammalian serine palmitoyltransferase
RT that confer distinct acyl-CoA substrate specificities.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8186-8191(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MBOAT7.
RX PubMed=23510452; DOI=10.1111/gtc.12046;
RA Hirata Y., Yamamori N., Kono N., Lee H.C., Inoue T., Arai H.;
RT "Identification of small subunit of serine palmitoyltransferase a as a
RT lysophosphatidylinositol acyltransferase 1-interacting protein.";
RL Genes Cells 18:397-409(2013).
CC -!- FUNCTION: Stimulates the activity of serine palmitoyltransferase (SPT).
CC The composition of the serine palmitoyltransferase (SPT) complex
CC determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex
CC shows a strong preference for C16-CoA substrate, while the SPTLC1-
CC SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with
CC a slight preference for C14-CoA (PubMed:19416851). Plays a role in
CC MBOAT7 location to mitochondria-associated membranes (MAMs), may me
CC involved in fatty acid remodeling phosphatidylinositol (PI)
CC (PubMed:23510452). {ECO:0000269|PubMed:19416851,
CC ECO:0000269|PubMed:23510452}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBUNIT: Interacts with SPTLC1; the interaction is direct. Component of
CC the serine palmitoyltransferase (SPT) complex, composed of SPTLC1,
CC either SPTLC2 or SPTLC3, and either SPTSSA or SPTSSB (PubMed:19416851).
CC Interacts with MBOAT7; the interaction facilitates MBOAT7 location to
CC mitochondria-associated membranes (MAMs) (PubMed:23510452).
CC {ECO:0000269|PubMed:19416851, ECO:0000269|PubMed:23510452}.
CC -!- INTERACTION:
CC Q969W0; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-723396, EBI-3867333;
CC Q969W0; O00258: GET1; NbExp=3; IntAct=EBI-723396, EBI-18908258;
CC Q969W0; Q9BSE4: HERPUD2; NbExp=3; IntAct=EBI-723396, EBI-2868124;
CC Q969W0; O75783: RHBDL1; NbExp=3; IntAct=EBI-723396, EBI-12104986;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23510452}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the SPTSS family. SPTSSA subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16805.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH16808.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH21701.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH68480.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG37801.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK315409; BAG37801.1; ALT_INIT; mRNA.
DR EMBL; CH471078; EAW65923.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65924.1; -; Genomic_DNA.
DR EMBL; BC016805; AAH16805.1; ALT_INIT; mRNA.
DR EMBL; BC016808; AAH16808.1; ALT_INIT; mRNA.
DR EMBL; BC021701; AAH21701.1; ALT_INIT; mRNA.
DR EMBL; BC068480; AAH68480.1; ALT_INIT; mRNA.
DR CCDS; CCDS9647.2; -.
DR RefSeq; NP_612145.2; NM_138288.3.
DR PDB; 6M4N; EM; 3.80 A; D/H=1-71.
DR PDB; 6M4O; EM; 3.40 A; E=1-71.
DR PDB; 7CQI; EM; 3.20 A; E=1-71.
DR PDB; 7CQK; EM; 3.30 A; E=1-71.
DR PDB; 7K0I; EM; 3.30 A; C/F=1-71.
DR PDB; 7K0J; EM; 3.10 A; C=1-71.
DR PDB; 7K0K; EM; 2.60 A; C=1-71.
DR PDB; 7K0L; EM; 3.40 A; C=1-71.
DR PDB; 7K0M; EM; 2.90 A; C/G=1-71.
DR PDB; 7K0N; EM; 3.10 A; C/G=1-71.
DR PDB; 7K0O; EM; 3.10 A; C/G=1-71.
DR PDB; 7K0P; EM; 3.10 A; C/G=1-71.
DR PDB; 7K0Q; EM; 3.30 A; C=1-71.
DR PDBsum; 6M4N; -.
DR PDBsum; 6M4O; -.
DR PDBsum; 7CQI; -.
DR PDBsum; 7CQK; -.
DR PDBsum; 7K0I; -.
DR PDBsum; 7K0J; -.
DR PDBsum; 7K0K; -.
DR PDBsum; 7K0L; -.
DR PDBsum; 7K0M; -.
DR PDBsum; 7K0N; -.
DR PDBsum; 7K0O; -.
DR PDBsum; 7K0P; -.
DR PDBsum; 7K0Q; -.
DR AlphaFoldDB; Q969W0; -.
DR SMR; Q969W0; -.
DR BioGRID; 128143; 14.
DR ComplexPortal; CPX-6663; Serine palmitoyltransferase complex, SPTLC1-SPTLC2-SPTSSA variant.
DR ComplexPortal; CPX-6665; Serine palmitoyltransferase complex, SPTLC1-SPTLC3-SPTSSA variant.
DR CORUM; Q969W0; -.
DR DIP; DIP-60754N; -.
DR IntAct; Q969W0; 9.
DR STRING; 9606.ENSP00000298130; -.
DR BioMuta; SPTSSA; -.
DR DMDM; 238054261; -.
DR PaxDb; Q969W0; -.
DR PeptideAtlas; Q969W0; -.
DR PRIDE; Q969W0; -.
DR ProteomicsDB; 75855; -.
DR TopDownProteomics; Q969W0; -.
DR DNASU; 171546; -.
DR Ensembl; ENST00000298130.5; ENSP00000298130.4; ENSG00000165389.7.
DR GeneID; 171546; -.
DR KEGG; hsa:171546; -.
DR MANE-Select; ENST00000298130.5; ENSP00000298130.4; NM_138288.4; NP_612145.2.
DR UCSC; uc001wsc.4; human.
DR CTD; 171546; -.
DR GeneCards; SPTSSA; -.
DR HGNC; HGNC:20361; SPTSSA.
DR HPA; ENSG00000165389; Low tissue specificity.
DR MIM; 613540; gene.
DR neXtProt; NX_Q969W0; -.
DR OpenTargets; ENSG00000165389; -.
DR PharmGKB; PA128394765; -.
DR VEuPathDB; HostDB:ENSG00000165389; -.
DR eggNOG; ENOG502S4Q3; Eukaryota.
DR GeneTree; ENSGT00390000002766; -.
DR HOGENOM; CLU_187811_1_0_1; -.
DR InParanoid; Q969W0; -.
DR OMA; AWKQISW; -.
DR OrthoDB; 1627882at2759; -.
DR PhylomeDB; Q969W0; -.
DR TreeFam; TF328418; -.
DR BioCyc; MetaCyc:MON66-34371; -.
DR BRENDA; 2.3.1.50; 2681.
DR PathwayCommons; Q969W0; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR SABIO-RK; Q969W0; -.
DR SignaLink; Q969W0; -.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 171546; 212 hits in 1080 CRISPR screens.
DR ChiTaRS; SPTSSA; human.
DR GenomeRNAi; 171546; -.
DR Pharos; Q969W0; Tbio.
DR PRO; PR:Q969W0; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q969W0; protein.
DR Bgee; ENSG00000165389; Expressed in mucosa of sigmoid colon and 211 other tissues.
DR Genevisible; Q969W0; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017059; C:serine C-palmitoyltransferase complex; IDA:UniProtKB.
DR GO; GO:0004758; F:serine C-palmitoyltransferase activity; IDA:MGI.
DR GO; GO:0046513; P:ceramide biosynthetic process; IDA:MGI.
DR GO; GO:0008104; P:protein localization; IDA:UniProtKB.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:UniProtKB.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IDA:ComplexPortal.
DR InterPro; IPR024512; Ser_palmitoyltrfase_ssu-like.
DR Pfam; PF11779; SPT_ssu-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW Reference proteome; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..71
FT /note="Serine palmitoyltransferase small subunit A"
FT /id="PRO_0000089949"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..34
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 56
FT /note="M -> V (in Ref. 3; AAH21701)"
FT /evidence="ECO:0000305"
FT HELIX 9..23
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 31..55
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 59..68
FT /evidence="ECO:0007829|PDB:7K0M"
SQ SEQUENCE 71 AA; 8466 MW; ED4F188040EE703C CRC64;
MAGMALARAW KQMSWFYYQY LLVTALYMLE PWERTVFNSM LVSIVGMALY TGYVFMPQHI
MAILHYFEIV Q
