STA10_HUMAN
ID STA10_HUMAN Reviewed; 291 AA.
AC Q9Y365; O60532;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=START domain-containing protein 10;
DE Short=StARD10;
DE AltName: Full=Antigen NY-CO-28;
DE AltName: Full=PCTP-like protein;
DE Short=PCTP-L;
DE AltName: Full=Serologically defined colon cancer antigen 28;
DE AltName: Full=StAR-related lipid transfer protein 10;
GN Name=STARD10; Synonyms=SDCCAG28; ORFNames=CGI-52;
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].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [3]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon carcinoma;
RX PubMed=9610721;
RX DOI=10.1002/(sici)1097-0215(19980529)76:5<652::aid-ijc7>3.0.co;2-p;
RA Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E.,
RA Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
RT "Characterization of human colon cancer antigens recognized by autologous
RT antibodies.";
RL Int. J. Cancer 76:652-658(1998).
RN [4]
RP FUNCTION, AND LIPID-BINDING.
RX PubMed=15911624; DOI=10.1074/jbc.m413330200;
RA Olayioye M.A., Vehring S., Muller P., Herrmann A., Schiller J., Thiele C.,
RA Lindeman G.J., Visvader J.E., Pomorski T.;
RT "StarD10, a START domain protein overexpressed in breast cancer, functions
RT as a phospholipid transfer protein.";
RL J. Biol. Chem. 280:27436-27442(2005).
RN [5]
RP PHOSPHORYLATION AT SER-284, AND SUBCELLULAR LOCATION.
RX PubMed=17561512; DOI=10.1074/jbc.m701990200;
RA Olayioye M.A., Buchholz M., Schmid S., Schoffler P., Hoffmann P.,
RA Pomorski T.;
RT "Phosphorylation of StarD10 on serine 284 by casein kinase II modulates its
RT lipid transfer activity.";
RL J. Biol. Chem. 282:22492-22498(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253; SER-259 AND SER-284, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May play metabolic roles in sperm maturation or fertilization
CC (By similarity). Phospholipid transfer protein that preferentially
CC selects lipid species containing a palmitoyl or stearoyl chain on the
CC sn-1 and an unsaturated fatty acyl chain (18:1 or 18:2) on the sn-2
CC position. Able to transfer phosphatidylcholine (PC) and
CC phosphatidyetanolamline (PE) between membranes. {ECO:0000250,
CC ECO:0000269|PubMed:15911624}.
CC -!- INTERACTION:
CC Q9Y365; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-4289836, EBI-912440;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000250}.
CC Cytoplasm {ECO:0000269|PubMed:17561512}. Membrane
CC {ECO:0000269|PubMed:17561512}. Note=In testis was predominantly
CC detected at the flagella of elongated spermatids, with a strong signal
CC also found at the tail of epididymal sperm (By similarity). Mainly
CC cytosolic. {ECO:0000250}.
CC -!- PTM: Phosphorylation at Ser-284 by CK2 negatively regulates lipid
CC transfer activity, possibly by decreasing membrane association.
CC {ECO:0000269|PubMed:17561512}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC18045.1; Type=Miscellaneous discrepancy; Note=Various sequencing problems as well as a translation in a wrong frame.; Evidence={ECO:0000305};
CC Sequence=AAD34047.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF151810; AAD34047.1; ALT_INIT; mRNA.
DR EMBL; BC007919; AAH07919.1; -; mRNA.
DR EMBL; BC014033; AAH14033.1; -; mRNA.
DR EMBL; AF039696; AAC18045.1; ALT_SEQ; mRNA.
DR CCDS; CCDS41688.1; -.
DR RefSeq; NP_006636.2; NM_006645.2.
DR PDB; 6SER; X-ray; 2.30 A; A=1-291.
DR PDBsum; 6SER; -.
DR AlphaFoldDB; Q9Y365; -.
DR SMR; Q9Y365; -.
DR BioGRID; 116023; 7.
DR IntAct; Q9Y365; 3.
DR MINT; Q9Y365; -.
DR STRING; 9606.ENSP00000335247; -.
DR ChEMBL; CHEMBL4523506; -.
DR iPTMnet; Q9Y365; -.
DR PhosphoSitePlus; Q9Y365; -.
DR BioMuta; STARD10; -.
DR DMDM; 25090873; -.
DR EPD; Q9Y365; -.
DR jPOST; Q9Y365; -.
DR MassIVE; Q9Y365; -.
DR MaxQB; Q9Y365; -.
DR PaxDb; Q9Y365; -.
DR PeptideAtlas; Q9Y365; -.
DR PRIDE; Q9Y365; -.
DR ProteomicsDB; 85976; -.
DR Antibodypedia; 7866; 150 antibodies from 26 providers.
DR DNASU; 10809; -.
DR Ensembl; ENST00000334805.11; ENSP00000335247.6; ENSG00000214530.10.
DR Ensembl; ENST00000543304.5; ENSP00000438792.1; ENSG00000214530.10.
DR GeneID; 10809; -.
DR KEGG; hsa:10809; -.
DR MANE-Select; ENST00000334805.11; ENSP00000335247.6; NM_006645.3; NP_006636.2.
DR UCSC; uc001osz.4; human.
DR CTD; 10809; -.
DR DisGeNET; 10809; -.
DR GeneCards; STARD10; -.
DR HGNC; HGNC:10666; STARD10.
DR HPA; ENSG00000214530; Tissue enhanced (liver).
DR MIM; 617382; gene.
DR neXtProt; NX_Q9Y365; -.
DR OpenTargets; ENSG00000214530; -.
DR PharmGKB; PA35596; -.
DR VEuPathDB; HostDB:ENSG00000214530; -.
DR eggNOG; KOG2761; Eukaryota.
DR GeneTree; ENSGT00510000047611; -.
DR InParanoid; Q9Y365; -.
DR OMA; ITVWTQV; -.
DR OrthoDB; 902242at2759; -.
DR PhylomeDB; Q9Y365; -.
DR TreeFam; TF354285; -.
DR PathwayCommons; Q9Y365; -.
DR Reactome; R-HSA-1483191; Synthesis of PC.
DR SignaLink; Q9Y365; -.
DR SIGNOR; Q9Y365; -.
DR BioGRID-ORCS; 10809; 13 hits in 1079 CRISPR screens.
DR ChiTaRS; STARD10; human.
DR GeneWiki; STARD10; -.
DR GenomeRNAi; 10809; -.
DR Pharos; Q9Y365; Tbio.
DR PRO; PR:Q9Y365; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9Y365; protein.
DR Bgee; ENSG00000214530; Expressed in right lobe of liver and 178 other tissues.
DR ExpressionAtlas; Q9Y365; baseline and differential.
DR Genevisible; Q9Y365; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0046581; C:intercellular canaliculus; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd08871; START_STARD10-like; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR041951; STARD10_START.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR Pfam; PF01852; START; 1.
DR SMART; SM00234; START; 1.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell projection; Cilium; Cytoplasm; Flagellum;
KW Lipid transport; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..291
FT /note="START domain-containing protein 10"
FT /id="PRO_0000220661"
FT DOMAIN 14..224
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 94
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMD3"
FT MOD_RES 197
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMD3"
FT MOD_RES 202
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMD3"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 284
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:17561512,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMD3"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:6SER"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:6SER"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:6SER"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:6SER"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:6SER"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:6SER"
FT STRAND 97..109
FT /evidence="ECO:0007829|PDB:6SER"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:6SER"
FT STRAND 127..139
FT /evidence="ECO:0007829|PDB:6SER"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:6SER"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6SER"
FT STRAND 165..175
FT /evidence="ECO:0007829|PDB:6SER"
FT STRAND 181..190
FT /evidence="ECO:0007829|PDB:6SER"
FT HELIX 197..227
FT /evidence="ECO:0007829|PDB:6SER"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:6SER"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:6SER"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:6SER"
SQ SEQUENCE 291 AA; 33049 MW; 26D6D3AF8C300EA6 CRC64;
MEKLAASTEP QGPRPVLGRE SVQVPDDQDF RSFRSECEAE VGWNLTYSRA GVSVWVQAVE
MDRTLHKIKC RMECCDVPAE TLYDVLHDIE YRKKWDSNVI ETFDIARLTV NADVGYYSWR
CPKPLKNRDV ITLRSWLPMG ADYIIMNYSV KHPKYPPRKD LVRAVSIQTG YLIQSTGPKS
CVITYLAQVD PKGSLPKWVV NKSSQFLAPK AMKKMYKACL KYPEWKQKHL PHFKPWLHPE
QSPLPSLALS ELSVQHADSL ENIDESAVAE SREERMGGAG GEGSDDDTSL T
