STA13_MOUSE
ID STA13_MOUSE Reviewed; 1113 AA.
AC Q923Q2; E9PUB5; Q8K369;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 5.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=StAR-related lipid transfer protein 13;
DE AltName: Full=START domain-containing protein 13;
DE Short=StARD13;
GN Name=Stard13;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, and Pancreas;
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).
CC -!- FUNCTION: May function as a GTPase-activating protein.
CC -!- SUBUNIT: Homodimer. Interacts with TAX1BP1 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q923Q2; Q96QB1: DLC1; Xeno; NbExp=2; IntAct=EBI-8393503, EBI-2608428;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein;
CC Cytoplasmic side. Mitochondrion membrane; Peripheral membrane protein;
CC Cytoplasmic side. Lipid droplet {ECO:0000250}.
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DR EMBL; AC109614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC163219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027830; AAH27830.2; -; mRNA.
DR CCDS; CCDS19890.1; -.
DR RefSeq; NP_666370.3; NM_146258.2.
DR AlphaFoldDB; Q923Q2; -.
DR BMRB; Q923Q2; -.
DR SMR; Q923Q2; -.
DR BioGRID; 232505; 38.
DR IntAct; Q923Q2; 10.
DR STRING; 10090.ENSMUSP00000053232; -.
DR iPTMnet; Q923Q2; -.
DR PhosphoSitePlus; Q923Q2; -.
DR jPOST; Q923Q2; -.
DR MaxQB; Q923Q2; -.
DR PaxDb; Q923Q2; -.
DR PRIDE; Q923Q2; -.
DR ProteomicsDB; 258651; -.
DR Antibodypedia; 35333; 123 antibodies from 25 providers.
DR DNASU; 243362; -.
DR Ensembl; ENSMUST00000110483; ENSMUSP00000106109; ENSMUSG00000016128.
DR GeneID; 243362; -.
DR KEGG; mmu:243362; -.
DR UCSC; uc009aum.2; mouse.
DR CTD; 90627; -.
DR MGI; MGI:2385331; Stard13.
DR VEuPathDB; HostDB:ENSMUSG00000016128; -.
DR eggNOG; KOG2200; Eukaryota.
DR GeneTree; ENSGT00950000183061; -.
DR HOGENOM; CLU_004367_0_0_1; -.
DR InParanoid; Q923Q2; -.
DR PhylomeDB; Q923Q2; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR BioGRID-ORCS; 243362; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Stard13; mouse.
DR PRO; PR:Q923Q2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q923Q2; protein.
DR Bgee; ENSMUSG00000016128; Expressed in animal zygote and 200 other tissues.
DR ExpressionAtlas; Q923Q2; baseline and differential.
DR Genevisible; Q923Q2; MM.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0043542; P:endothelial cell migration; ISO:MGI.
DR GO; GO:0097498; P:endothelial tube lumen extension; ISO:MGI.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; IMP:MGI.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00234; START; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cytoplasm; GTPase activation; Lipid droplet;
KW Membrane; Mitochondrion; Phosphoprotein; Reference proteome.
FT CHAIN 1..1113
FT /note="StAR-related lipid transfer protein 13"
FT /id="PRO_0000220680"
FT DOMAIN 55..122
FT /note="SAM"
FT DOMAIN 663..868
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 899..1109
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT REGION 164..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..569
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:Q9Y3M8"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 384
FT /note="M -> V (in Ref. 2; AAH27830)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="A -> V (in Ref. 2; AAH27830)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1113 AA; 125060 MW; A516D16FFA327E74 CRC64;
MFSQVPRTPA AGCYYLNPLT PESQEMYLRF DQTARRSPYR MSRILARHHL VTKIQQEIEA
KEACDWLRAA GFPQYAQLYE DSQFPINIAA VKKDHDFLER DLVEPLCRRL NTLNKCASMR
LDVNFQRKKG DDSDEEDLCI SNKWTFQRTS RRWSRVDDLH TLFPVADRNG SPGGPRMRNT
ASSESVLTDL SEPEVCSIHS ESSGGSDSRS QSGHHSADST HALEATLVSS SLPQSTREGL
NQSFHPKNEK PTRTRAKSFL KRMDTLRVKG ALGRHKGPGR TGGLVISRPV LQQEPESFKT
MQCVQIPNGD LQTSPPAACR KGLPCSSKSS GESSPLENSS TVSTPCMKER KCHHEANKRG
GMYLEDLDVL AGTALPDTSD QNHMHGFHSQ ENLVVHIPKD HKPGTFPKAL SIESLSPTDN
SNGVNWRTGS ISLGRQQGPG MREPRLMSSC HRASRVSIYD NVPSSHLYAS TGDLLDLEKD
GLLPQLDDIL QHVNGIQEVV DDWSKNILPE LQSHSTLAGD PGLSPFPSPN QVTLDFEGNS
VSEGRTTPSD VERDRTSLNE SEATGVRERR DSGVGASLTR PNRRLRWSSF QLSHQPQPSP
ATPHISSQTA AQLNLLQRFS LLRLTAIMEK YSMSNKHGWT WSVPKFMKRI KAPDYRDKAV
FGVPLIVHVQ RTGQPLPQSI QQALRYLRSN CLDQVGLFRK SGVKSRIHAL RQMNENFPDN
VSYEDQSAYD VADMVKQFFR DLPEPLFTNK LSETFLHIYQ YVPKEQRLQA VQAAILLLAD
ENREALQTLL CFLHDVVNLV DENQMTPMNL AVCLAPSLFH LNLLKKESSP KVIQKKYATG
KPDQKDLNEN LAAAQGLAHM ITECNRLFEV PHEMVAQSRD SYLEAEIHVP SLEDLGAQLA
ESGATFHTYL EHLVQGLQKE AKEKFKGWVT CSSPDNTDLA FKKVGDGHPL KLWKASVEVE
APPSVVLNRV LRERHLWDED FVQWKVVERL DKQTEIYQYV LNSMVPHPSR DFLVLRTWKT
DLPKGMCTLV SLSVEYEEAQ LMGGVRAVVM DSQYLIEPCG SGKSRLTHIC RIDLKGHSPE
WYSKGFGHLC AAEVTRIRNS FQPLVAEGPE TKI
