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SCAI_MOUSE
ID   SCAI_MOUSE              Reviewed;         606 AA.
AC   Q8C8N2; A2RTF5; A3KGQ2; Q8C409; Q8C8K2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Protein SCAI;
DE   AltName: Full=Suppressor of cancer cell invasion protein;
GN   Name=Scai;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Hippocampus, Medulla oblongata, and Retina;
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 GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-64, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   FUNCTION, INTERACTION WITH DIAPH1; MRTFA AND SRF, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=19350017; DOI=10.1038/ncb1862;
RA   Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J., Nollau P.,
RA   Grosse R.;
RT   "SCAI acts as a suppressor of cancer cell invasion through the
RT   transcriptional control of beta1-integrin.";
RL   Nat. Cell Biol. 11:557-568(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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: Tumor suppressor which functions to suppress MRTFA-induced
CC       SRF transcriptional activity. May function in the RHOA-DIAPH1 signal
CC       transduction pathway and regulate cell migration through
CC       transcriptional regulation of ITGB1. {ECO:0000269|PubMed:19350017}.
CC   -!- SUBUNIT: Interacts with DIAPH1. Forms a nuclear ternary complex with
CC       MRTFA and SRF. {ECO:0000269|PubMed:19350017}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:19350017}. Cytoplasm
CC       {ECO:0000269|PubMed:19350017}. Note=Nuclear localization is required
CC       for inhibition of MRTFA.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C8N2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C8N2-2; Sequence=VSP_015121, VSP_015122;
CC   -!- TISSUE SPECIFICITY: Expressed in most tissues tested with higher
CC       expression levels in brain, spleen and thymus.
CC       {ECO:0000269|PubMed:19350017}.
CC   -!- SIMILARITY: Belongs to the SCAI family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32904.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK044772; BAC32081.1; -; mRNA.
DR   EMBL; AK046875; BAC32904.1; ALT_INIT; mRNA.
DR   EMBL; AK083280; BAC38841.1; -; mRNA.
DR   EMBL; AL844588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL845350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL928639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466519; EDL26843.1; -; Genomic_DNA.
DR   EMBL; BC132485; AAI32486.1; -; mRNA.
DR   CCDS; CCDS38121.1; -. [Q8C8N2-1]
DR   RefSeq; NP_848893.2; NM_178778.3. [Q8C8N2-1]
DR   AlphaFoldDB; Q8C8N2; -.
DR   BioGRID; 235895; 17.
DR   IntAct; Q8C8N2; 15.
DR   MINT; Q8C8N2; -.
DR   STRING; 10090.ENSMUSP00000037194; -.
DR   iPTMnet; Q8C8N2; -.
DR   PhosphoSitePlus; Q8C8N2; -.
DR   SwissPalm; Q8C8N2; -.
DR   EPD; Q8C8N2; -.
DR   MaxQB; Q8C8N2; -.
DR   PaxDb; Q8C8N2; -.
DR   PeptideAtlas; Q8C8N2; -.
DR   PRIDE; Q8C8N2; -.
DR   ProteomicsDB; 256925; -. [Q8C8N2-1]
DR   ProteomicsDB; 256926; -. [Q8C8N2-2]
DR   Antibodypedia; 7729; 37 antibodies from 16 providers.
DR   Ensembl; ENSMUST00000038874; ENSMUSP00000037194; ENSMUSG00000035236. [Q8C8N2-1]
DR   GeneID; 320271; -.
DR   KEGG; mmu:320271; -.
DR   UCSC; uc008jof.1; mouse. [Q8C8N2-1]
DR   UCSC; uc008joh.1; mouse. [Q8C8N2-2]
DR   CTD; 286205; -.
DR   MGI; MGI:2443716; Scai.
DR   VEuPathDB; HostDB:ENSMUSG00000035236; -.
DR   eggNOG; ENOG502QPT4; Eukaryota.
DR   GeneTree; ENSGT00390000009566; -.
DR   HOGENOM; CLU_020095_2_1_1; -.
DR   InParanoid; Q8C8N2; -.
DR   OMA; MGYDLGG; -.
DR   PhylomeDB; Q8C8N2; -.
DR   TreeFam; TF324872; -.
DR   Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR   BioGRID-ORCS; 320271; 3 hits in 71 CRISPR screens.
DR   ChiTaRS; Scai; mouse.
DR   PRO; PR:Q8C8N2; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8C8N2; protein.
DR   Bgee; ENSMUSG00000035236; Expressed in manus and 223 other tissues.
DR   ExpressionAtlas; Q8C8N2; baseline and differential.
DR   Genevisible; Q8C8N2; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR   GO; GO:0030336; P:negative regulation of cell migration; IGI:UniProtKB.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IDA:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR022709; SCAI.
DR   InterPro; IPR016607; SCAI_metazoan/Viridiplantae.
DR   Pfam; PF12070; SCAI; 1.
DR   PIRSF; PIRSF013022; UCP013022; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Membrane; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Signal transduction inhibitor;
KW   Transcription; Transcription regulation; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..606
FT                   /note="Protein SCAI"
FT                   /id="PRO_0000089736"
FT   TRANSMEM        472..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..212
FT                   /note="Necessary to inhibit MRTFA-induced SRF
FT                   transcriptional activity"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          71..173
FT                   /note="Required for interaction with MRTFA"
FT                   /evidence="ECO:0000269|PubMed:19350017"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         64
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455"
FT   VAR_SEQ         322..325
FT                   /note="EPAD -> VIIA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_015121"
FT   VAR_SEQ         326..606
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_015122"
FT   CONFLICT        58
FT                   /note="T -> A (in Ref. 1; BAC32081)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   606 AA;  70275 MW;  09CBEDC06FDC573F CRC64;
     MVRGARQSQQ PRSRLAPRLS GTVEKPPRKR KSRTEFTLKE TMSSGGAEDD IPQGERKTVT
     DFCYLLDKSK QLFNGLRDLP QYGQKQWQSY FGRTFDVYTK LWKFQQQHRQ VLDNRYGLKR
     WQIGEIASKI GQLYYHYYLR TSETSYLNEA FSFYSAIRQR SYYSQVNKED RPELVVKKLR
     YYARFIVVCL LLNKMDVVKD LVKELSDEIE DYTHRFNTED QVEWNLVLQE VAAFIEADPV
     MVLNDDNTIV ITSNRLAETG APLLEQGMIV GQLSLADALI IGNCNNQVKF SELTVDMFRM
     LQALEREPMN LASQMNKPGI QEPADKPTRR ENPHKYLLYK PTFSQLYTFL AASFKELPAN
     SVLLIYLSAT GVFPTGRSDG EGPYDFGGVL TNSNRDIING DAIHKRNQSH KEMHCLHPGD
     LYPFTRKPLF IVVDSSNSVA YKNFTNLFGQ PLVCLLSPTA YPKALQDQSQ RGSLFTLFLN
     NPLMAFLFVS GLSSMRRGLW EKCQEYLRKI NRDIAQLLTH SRSIDQAFLQ FFGDEFLRLL
     LTRFVFCSAT MRMHKAFRET RNYPESYPQL PRDETVENPH LQKHILELAS ILDVRNIFFE
     NSMDDY
 
 
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