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STA10_MOUSE
ID   STA10_MOUSE             Reviewed;         291 AA.
AC   Q9JMD3;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=START domain-containing protein 10;
DE            Short=StARD10;
DE   AltName: Full=PCTP-like protein;
DE            Short=PCTP-L;
DE   AltName: Full=Serologically defined colon cancer antigen 28 homolog;
DE   AltName: Full=StAR-related lipid transfer protein 10;
GN   Name=Stard10; Synonyms=Pctpl, Sdccag28, Sdccagg28;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Testis;
RX   PubMed=10819773; DOI=10.1095/biolreprod62.6.1694;
RA   Yamanaka M., Koga M., Tanaka H., Nakamura Y., Ohta H., Yomogida K.,
RA   Tsuchida J., Iguchi N., Nojima H., Nozaki M., Matsumiya K., Okuyama A.,
RA   Toshimori K., Nishimune Y.;
RT   "Molecular cloning and characterization of phosphatidylcholine transfer
RT   protein-like protein gene expressed in murine haploid germ cells.";
RL   Biol. Reprod. 62:1694-1701(2000).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284 AND SER-289, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-94; LYS-197 AND LYS-202, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Phospholipid transfer protein that preferentially selects
CC       lipid species containing a palmitoyl or stearoyl chain on the sn-1 and
CC       an unsaturated fatty acyl chain (18:1 or 18:2) on the sn-2 position.
CC       Able to transfer phosphatidylcholine (PC) and phosphatidyetanolamline
CC       (PE) between membranes (By similarity). May play metabolic roles in
CC       sperm maturation or fertilization. {ECO:0000250,
CC       ECO:0000269|PubMed:10819773}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC       {ECO:0000269|PubMed:10819773}. Cytoplasm {ECO:0000250}. Membrane
CC       {ECO:0000250}. Note=Mainly cytosolic (By similarity). In testis was
CC       predominantly detected at the flagella of elongated spermatids, with a
CC       strong signal also found at the tail of epididymal sperm.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Testis, kidney, liver, and intestine with the
CC       highest level in the testis.
CC   -!- DEVELOPMENTAL STAGE: During male germ cell development, it was detected
CC       first in the 23-day-old mouse testis, and the signal increased with
CC       age.
CC   -!- PTM: Phosphorylation at Ser-284 by CK2 negatively regulates lipid
CC       transfer activity, possibly by decreasing membrane association.
CC       {ECO:0000250}.
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DR   EMBL; AB031550; BAA92233.1; -; mRNA.
DR   CCDS; CCDS21509.1; -.
DR   RefSeq; NP_064374.1; NM_019990.4.
DR   AlphaFoldDB; Q9JMD3; -.
DR   SMR; Q9JMD3; -.
DR   BioGRID; 207773; 1.
DR   STRING; 10090.ENSMUSP00000032927; -.
DR   iPTMnet; Q9JMD3; -.
DR   PhosphoSitePlus; Q9JMD3; -.
DR   jPOST; Q9JMD3; -.
DR   MaxQB; Q9JMD3; -.
DR   PaxDb; Q9JMD3; -.
DR   PRIDE; Q9JMD3; -.
DR   ProteomicsDB; 257442; -.
DR   Antibodypedia; 7866; 150 antibodies from 26 providers.
DR   DNASU; 56018; -.
DR   Ensembl; ENSMUST00000032927; ENSMUSP00000032927; ENSMUSG00000030688.
DR   Ensembl; ENSMUST00000164479; ENSMUSP00000133002; ENSMUSG00000030688.
DR   Ensembl; ENSMUST00000210192; ENSMUSP00000148114; ENSMUSG00000030688.
DR   GeneID; 56018; -.
DR   KEGG; mmu:56018; -.
DR   UCSC; uc009ioi.1; mouse.
DR   CTD; 10809; -.
DR   MGI; MGI:1860093; Stard10.
DR   VEuPathDB; HostDB:ENSMUSG00000030688; -.
DR   eggNOG; KOG2761; Eukaryota.
DR   GeneTree; ENSGT00510000047611; -.
DR   InParanoid; Q9JMD3; -.
DR   OMA; ITVWTQV; -.
DR   PhylomeDB; Q9JMD3; -.
DR   TreeFam; TF354285; -.
DR   Reactome; R-MMU-1483191; Synthesis of PC.
DR   BioGRID-ORCS; 56018; 3 hits in 75 CRISPR screens.
DR   ChiTaRS; Stard10; mouse.
DR   PRO; PR:Q9JMD3; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9JMD3; protein.
DR   Bgee; ENSMUSG00000030688; Expressed in left lobe of liver and 258 other tissues.
DR   ExpressionAtlas; Q9JMD3; baseline and differential.
DR   Genevisible; Q9JMD3; MM.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0046581; C:intercellular canaliculus; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005902; C:microvillus; IDA:MGI.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0032782; P:bile acid secretion; IMP:MGI.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; IMP:MGI.
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   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_0000220662"
FT   DOMAIN          14..224
FT                   /note="START"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT   REGION          1..23
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:0000250|UniProtKB:Q9Y365"
FT   MOD_RES         94
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         197
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         202
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         253
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y365"
FT   MOD_RES         259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y365"
FT   MOD_RES         284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         289
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   291 AA;  32951 MW;  598467C430D97080 CRC64;
     MEKPAASTEP QGSRPALGRE SVQVPDDQDF RSFRSECEAE VGWNLTYSKA GVSVWVQAVE
     MDRTLHKIKC RMECCDVPAE TLYDVLHDIE YRKKWDSNVI ETFDIARLTV NADVGYYSWR
     CPKPLKNRDV ITLRSWLPMG ADYIIMNYSV KHPKYPPRKD LVRAVSIQTG YLIQSTGPKS
     CVITYLAQVD PKGSLPKWVV NKSSQFLAPK AMKKMYKACI KYPEWKQKHQ PHFKPWLHPE
     QSPLPSLALS ELSVQHADSL ENIDESAVTE SREERAGGAG GEGSDDDTSL T
 
 
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