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   24-JAN-2024, entry version 167.
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; 12.
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; 9606-ENSP00000335247; -.
DR   PeptideAtlas; Q9Y365; -.
DR   ProteomicsDB; 85976; -.
DR   Pumba; Q9Y365; -.
DR   Antibodypedia; 7866; 166 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   AGR; HGNC:10666; -.
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; CRMECKD; -.
DR   OrthoDB; 1064073at2759; -.
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; 14 hits in 1157 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 180 other cell types or tissues.
DR   ExpressionAtlas; Q9Y365; baseline and differential.
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   PANTHER; PTHR19308; PHOSPHATIDYLCHOLINE TRANSFER PROTEIN; 1.
DR   PANTHER; PTHR19308:SF7; START DOMAIN-CONTAINING PROTEIN 10; 1.
DR   Pfam; PF01852; START; 1.
DR   SMART; SM00234; START; 1.
DR   SUPFAM; SSF55961; Bet v1-like; 1.
DR   PROSITE; PS50848; START; 1.
DR   Genevisible; Q9Y365; HS.
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
//