STAR8_MOUSE
ID STAR8_MOUSE Reviewed; 1019 AA.
AC Q8K031; B1AZJ2; Q3UZC7; Q6A0A8; Q6P5E0; Q8R3X8;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=StAR-related lipid transfer protein 8;
DE AltName: Full=START domain-containing protein 8;
DE Short=StARD8;
GN Name=Stard8; Synonyms=Kiaa0189;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, Kidney, and 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 736-1019.
RC TISSUE=Spleen;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=17976533; DOI=10.1016/j.bbrc.2007.10.052;
RA Kawai K., Kiyota M., Seike J., Deki Y., Yagisawa H.;
RT "START-GAP3/DLC3 is a GAP for RhoA and Cdc42 and is localized in focal
RT adhesions regulating cell morphology.";
RL Biochem. Biophys. Res. Commun. 364:783-789(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-494 AND SER-502, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, and Lung;
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 [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-168, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Accelerates GTPase activity of RHOA and CDC42, but not RAC1.
CC Stimulates the hydrolysis of phosphatidylinositol 4,5-bisphosphate by
CC PLCD1 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds both the SH2 and PTB domains of TNS1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000269|PubMed:17976533}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK133927; BAE21930.1; -; mRNA.
DR EMBL; AK149830; BAE29110.1; -; mRNA.
DR EMBL; AK150259; BAE29418.1; -; mRNA.
DR EMBL; AL954636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023434; AAH23434.1; -; mRNA.
DR EMBL; BC034186; AAH34186.1; -; mRNA.
DR EMBL; BC062944; AAH62944.1; -; mRNA.
DR EMBL; AK172910; BAD32188.1; -; mRNA.
DR CCDS; CCDS30297.1; -.
DR RefSeq; NP_950183.1; NM_199018.2.
DR RefSeq; XP_006528067.1; XM_006528004.2.
DR RefSeq; XP_006528070.1; XM_006528007.1.
DR AlphaFoldDB; Q8K031; -.
DR SMR; Q8K031; -.
DR STRING; 10090.ENSMUSP00000044491; -.
DR iPTMnet; Q8K031; -.
DR PhosphoSitePlus; Q8K031; -.
DR jPOST; Q8K031; -.
DR MaxQB; Q8K031; -.
DR PaxDb; Q8K031; -.
DR PRIDE; Q8K031; -.
DR ProteomicsDB; 257366; -.
DR Antibodypedia; 27311; 130 antibodies from 21 providers.
DR DNASU; 236920; -.
DR Ensembl; ENSMUST00000036606; ENSMUSP00000044491; ENSMUSG00000031216.
DR GeneID; 236920; -.
DR KEGG; mmu:236920; -.
DR UCSC; uc009tvg.2; mouse.
DR CTD; 9754; -.
DR MGI; MGI:2448556; Stard8.
DR VEuPathDB; HostDB:ENSMUSG00000031216; -.
DR eggNOG; KOG2200; Eukaryota.
DR GeneTree; ENSGT00950000183061; -.
DR HOGENOM; CLU_004367_0_1_1; -.
DR InParanoid; Q8K031; -.
DR OMA; EQCTISN; -.
DR OrthoDB; 218349at2759; -.
DR PhylomeDB; Q8K031; -.
DR TreeFam; TF314044; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR BioGRID-ORCS; 236920; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q8K031; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8K031; protein.
DR Bgee; ENSMUSG00000031216; Expressed in placenta labyrinth and 203 other tissues.
DR ExpressionAtlas; Q8K031; baseline and differential.
DR Genevisible; Q8K031; MM.
DR GO; GO:0005925; C:focal adhesion; 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: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; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00234; START; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW Cell junction; GTPase activation; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1019
FT /note="StAR-related lipid transfer protein 8"
FT /id="PRO_0000220677"
FT DOMAIN 569..773
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 805..1013
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT REGION 92..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..350
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92502"
FT MOD_RES 168
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92502"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 170..171
FT /note="FL -> IR (in Ref. 3; AAH23434/AAH34186)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="E -> EE (in Ref. 3; AAH23434/AAH34186)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="T -> A (in Ref. 3; AAH23434/AAH34186)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="F -> L (in Ref. 1; BAE21930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1019 AA; 113021 MW; B270E6C2E4F597C1 CRC64;
MTLNNCASMK LEVHFQCKQD DDSEEEEQCT ISSHWAFEQE SKCGSLMGSS ALLAPPSPSL
LGTSSCESVL TELSAASLPA ISASLSPESA DQPLLGLVPS PSNQPFLSPP QGQEGSQDKV
KKHYSRSFLK HLESLRRKEK GDSRQTEPEQ CLATSEKATK ASSFRTCRGF LSAGFHRAKN
RVTTSARVRD GETQKAWEAW PVATFRHPQP IRRRDYLVHV PGDHKPGTFP RSLSIESLCP
DEGRHLADWQ SSRCWGYEGR RGSCGSTGSH ASTYDNLPEL YPAEPIQAEA EAEAEEGEGS
YAHLDDILEH VWGLQQRVEL WSQTMYPDLR PGDKEEEEEE EEEEEEATSS VEVATVEVEG
QDEDLAQAES QAHRGFPTQV KEEVPLIVLD QAPNVVEPLV QAEAEAPAQA QDLEQEANST
AEPISASSLS VEEGHSISDT AVSSSELDSS GNSMNEADAA DAPAGLQASV PRERRDSGVG
ASLTRPCRKL RWHSFQNSHR PSLNSESLEI NRQFAGQINL LHKGSLLRLT GFMEKYTVPH
KQAWVWSMPK FMKRNKTPDY RGHHVFGVPP LIHVQRTGQP LPQSIQQAMR YLRSQCLDQV
GIFRKSGVKS RIQSLRQMNE NSPDNVCYEG QSAYDVADLL KQYFRDLPEP IFTSKLTTTF
LQIYQLLPKE QWLAAAQAAT LLLPDENREV LQTLLYFLSD IASAEENQMT AGNLAVCLAP
SIFHLNVSKK DSSSPRIKSK RSLVGRPGPR DLSENMAATQ GLSHMISDCK KLFQVPQDMV
VQLCGSYSAA ELSPPGPALA ELRQAQAAGV SLSLYMEESV QELLRDAAER FKGWTNVPGP
QHTELACRKA PDGHPLRMWK ASTEVAAPPA VVLHRVLRER ALWDEDLLRA QVLEALMPGV
ELYHYVTDSM APHPCRDFVV LRMWRSDLPR GGCLLVSQSL DPEQPVPESG VRALMLTSQY
LMEPCGLGRS RLTHICRADL RGRSPDWYNK VFGHLCAMEV AKIRDSFPTL QAAGPETKL