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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}.
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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
 
 
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