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SIMC1_MOUSE
ID   SIMC1_MOUSE             Reviewed;        1354 AA.
AC   E9Q6E9; Q3TM32; Q8C747; Q8CE66;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=SUMO-interacting motif-containing protein 1;
DE   AltName: Full=Platform element for inhibition of autolytic degradation {ECO:0000303|PubMed:23707407};
GN   Name=Simc1; Synonyms=Pleiad {ECO:0000303|PubMed:23707407};
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 713-1354 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland, Skin, and Stomach;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [4]
RP   IDENTIFICATION, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX   PubMed=23707407; DOI=10.1016/j.jmb.2013.05.009;
RA   Ono Y., Iemura S., Novak S.M., Doi N., Kitamura F., Natsume T.,
RA   Gregorio C.C., Sorimachi H.;
RT   "PLEIAD/SIMC1/C5orf25, a novel autolysis regulator for a skeletal-muscle-
RT   specific calpain, CAPN3, scaffolds a CAPN3 substrate, CTBP1.";
RL   J. Mol. Biol. 425:2955-2972(2013).
CC   -!- FUNCTION: Inhibits the protease activity of CAPN3.
CC       {ECO:0000250|UniProtKB:Q8NDZ2}.
CC   -!- SUBUNIT: Interacts (via SIM domains) with SUMO1 and SUMO2. Interacts
CC       with CAPN3 and CTBP1. {ECO:0000250|UniProtKB:Q8NDZ2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms may exist. {ECO:0000305|PubMed:23707407};
CC       Name=1; Synonyms=PLEIADa {ECO:0000303|PubMed:23707407};
CC         IsoId=E9Q6E9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=E9Q6E9-2; Sequence=VSP_060887, VSP_060888;
CC   -!- TISSUE SPECIFICITY: Skeletal muscle. {ECO:0000269|PubMed:23707407}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC35039.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAE38610.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK052561; BAC35039.1; ALT_INIT; mRNA.
DR   EMBL; AK028926; BAC26197.1; -; mRNA.
DR   EMBL; AK166176; BAE38610.1; ALT_INIT; mRNA.
DR   EMBL; AC155262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC165145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS26528.2; -. [E9Q6E9-1]
DR   RefSeq; NP_795961.3; NM_176987.4. [E9Q6E9-1]
DR   AlphaFoldDB; E9Q6E9; -.
DR   STRING; 10090.ENSMUSP00000113676; -.
DR   iPTMnet; E9Q6E9; -.
DR   PhosphoSitePlus; E9Q6E9; -.
DR   EPD; E9Q6E9; -.
DR   MaxQB; E9Q6E9; -.
DR   PaxDb; E9Q6E9; -.
DR   PRIDE; E9Q6E9; -.
DR   ProteomicsDB; 351391; -. [E9Q6E9-1]
DR   Antibodypedia; 60845; 52 antibodies from 12 providers.
DR   DNASU; 319719; -.
DR   Ensembl; ENSMUST00000121401; ENSMUSP00000113676; ENSMUSG00000043183. [E9Q6E9-1]
DR   GeneID; 319719; -.
DR   KEGG; mmu:319719; -.
DR   UCSC; uc007qoe.2; mouse. [E9Q6E9-1]
DR   CTD; 375484; -.
DR   MGI; MGI:2442599; Simc1.
DR   VEuPathDB; HostDB:ENSMUSG00000043183; -.
DR   eggNOG; ENOG502RR6K; Eukaryota.
DR   GeneTree; ENSGT00940000153451; -.
DR   HOGENOM; CLU_264356_0_0_1; -.
DR   InParanoid; E9Q6E9; -.
DR   OMA; GDAIQSP; -.
DR   OrthoDB; 117288at2759; -.
DR   TreeFam; TF332523; -.
DR   BioGRID-ORCS; 319719; 1 hit in 58 CRISPR screens.
DR   ChiTaRS; Simc1; mouse.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; E9Q6E9; protein.
DR   Bgee; ENSMUSG00000043183; Expressed in undifferentiated genital tubercle and 248 other tissues.
DR   ExpressionAtlas; E9Q6E9; baseline and differential.
DR   Genevisible; E9Q6E9; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030017; C:sarcomere; ISS:UniProtKB.
DR   GO; GO:0030414; F:peptidase inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0032184; F:SUMO polymer binding; ISO:MGI.
DR   GO; GO:0010466; P:negative regulation of peptidase activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Alternative splicing; Protease inhibitor; Reference proteome.
FT   CHAIN           1..1354
FT                   /note="SUMO-interacting motif-containing protein 1"
FT                   /id="PRO_0000451959"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          783..870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          945..1354
FT                   /note="Required for inhibition of CAPN3 protease activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NDZ2"
FT   REGION          1111..1142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           45..49
FT                   /note="SUMO interaction motif 1 (SIM); mediates the binding
FT                   to polysumoylated substrates"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NDZ2"
FT   MOTIF           64..68
FT                   /note="SUMO interaction motif 2 (SIM); mediates the binding
FT                   to polysumoylated substrates"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NDZ2"
FT   COMPBIAS        432..461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..580
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..697
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..726
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        744..758
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..824
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        841..869
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1112..1142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..858
FT                   /note="MEDFIVISDDSGSESSAGTRSGRARRLRRALSRTPGALPRRTVDFIDLTREN
FT                   RARTKDRNGLCVIDLTRNEEENRPIATLDLTLEPVASSQKEPTSLQTCTSLSGKEVMEA
FT                   HEDRGSQPAAQRIINNDPVDLDLLEENLFEGSRPPTSISQDSVYPPEPNCSSITYKGDL
FT                   SFLTSLQLSSDVSSFSSTSNQRASLPCPQQDVPCQSQGLLCPLQALSCPQTASPCPPRA
FT                   SSCPPQALSCPPQALSCPSQTLQCQLQALPQPPQEVPCSTQNVPCPQQNMPSTPQGLSW
FT                   HPRHTLYPYQDTLGLPQDVPGRPQNMSYPQDVTQLQDMPWSLHDMPLSLQDVLQSLQDV
FT                   PPLLGDVPPSPEVMQLPGYVTQTSRDVIQSPAGVTQSLGSMMQSPGSVTQSLRSVMQSS
FT                   GSVTQSLRSVMQSSGSVTQSLRSVMQSSGSVMQSPGGVTQSLRSVTQSPGGVMQSPGGV
FT                   MQSPRDVMQSPRDVMQSPRDVMQSPRGVTQSLGSMMQSPGGVMQSLRSVMQSSGGVTQS
FT                   LRSVMQSPGGVMQSPGGVTQSPRGMIKSPGMMLSPGDVIQSLNSVPQSSRDRMQSAGHV
FT                   PSASGDAIQSPGGMSPTSRDRMQSPGGVSLATEDSIQLPGGVPLSSDVIQSQGGVPLSS
FT                   KDRMQSPGGVPPSSGDMIQSQGGVPQSLGDAIQSAGGVPQSSGDAIQSPGGVSLATGDS
FT                   IQLPGGVPLSSGDVIQSQGGVPRSSRDRMQSPGGVPPSSGGVIQSPGGVSPASGDAIQS
FT                   PGSVLPASGDAIQSAGGVLLASGDAIQSPRSVPQSPSGTLRSPGNMSESLGDTPNLSGD
FT                   VSNSPQALLDLARDRPKSSPNDVQNRDTPMDISASSSSS -> MQYSHQEVCYRHQEMQ
FT                   YSQQEVCYWHQEMQ (in isoform 2)"
FT                   /id="VSP_060887"
FT   VAR_SEQ         1022
FT                   /note="Q -> QYEPLQ (in isoform 2)"
FT                   /id="VSP_060888"
FT   CONFLICT        814
FT                   /note="P -> L (in Ref. 1; BAE38610)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        887
FT                   /note="R -> K (in Ref. 1; BAE38610)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1354 AA;  146618 MW;  D9B2573C7AA23360 CRC64;
     MEDFIVISDD SGSESSAGTR SGRARRLRRA LSRTPGALPR RTVDFIDLTR ENRARTKDRN
     GLCVIDLTRN EEENRPIATL DLTLEPVASS QKEPTSLQTC TSLSGKEVME AHEDRGSQPA
     AQRIINNDPV DLDLLEENLF EGSRPPTSIS QDSVYPPEPN CSSITYKGDL SFLTSLQLSS
     DVSSFSSTSN QRASLPCPQQ DVPCQSQGLL CPLQALSCPQ TASPCPPRAS SCPPQALSCP
     PQALSCPSQT LQCQLQALPQ PPQEVPCSTQ NVPCPQQNMP STPQGLSWHP RHTLYPYQDT
     LGLPQDVPGR PQNMSYPQDV TQLQDMPWSL HDMPLSLQDV LQSLQDVPPL LGDVPPSPEV
     MQLPGYVTQT SRDVIQSPAG VTQSLGSMMQ SPGSVTQSLR SVMQSSGSVT QSLRSVMQSS
     GSVTQSLRSV MQSSGSVMQS PGGVTQSLRS VTQSPGGVMQ SPGGVMQSPR DVMQSPRDVM
     QSPRDVMQSP RGVTQSLGSM MQSPGGVMQS LRSVMQSSGG VTQSLRSVMQ SPGGVMQSPG
     GVTQSPRGMI KSPGMMLSPG DVIQSLNSVP QSSRDRMQSA GHVPSASGDA IQSPGGMSPT
     SRDRMQSPGG VSLATEDSIQ LPGGVPLSSD VIQSQGGVPL SSKDRMQSPG GVPPSSGDMI
     QSQGGVPQSL GDAIQSAGGV PQSSGDAIQS PGGVSLATGD SIQLPGGVPL SSGDVIQSQG
     GVPRSSRDRM QSPGGVPPSS GGVIQSPGGV SPASGDAIQS PGSVLPASGD AIQSAGGVLL
     ASGDAIQSPR SVPQSPSGTL RSPGNMSESL GDTPNLSGDV SNSPQALLDL ARDRPKSSPN
     DVQNRDTPMD ISASSSSSCS ANPQSRQSEF KLDKVPWLTI TDSSARREKS LPQLANPGSA
     QIQGQIPQVG VYNRPCLHRL KYFLRPPVHH LFFQTLIPDK DTRESKGQKL EPIPHRRLRM
     VTNTIEENFP LGTVQFLMDF VSPQHYPPRE IVAHIVQKIL LSGSETVDVL KEAYMLLMKI
     QQLHPANAKT VEWDWKLLTY VMEEEGQTLP GRVLFLRYVV QTLEDDFQQI LRRQRQHLQQ
     SIANTVLSCD KQPHNVRDVI KWLVKAVTEN ELTPPQDETQ TSPRTGVLKT SSDHLSPRPN
     QNKNTNQLIV CQLQRMLSIA VEVDRTPTCS SNKIAEMMFG FVLDIPERSQ REMFFTTMES
     HLLRCKVLEI IFLHSCETPT RLPLSLAQTL YFLNNSTSLL KCQSDKTQWQ TWDELVEHLQ
     FLLSSYQHVL REHLRSSVID RKDLIIKRIK PKPQQGDDIT VLDVEKQIEA FRSRLVHILG
     EPLVPQLQDK VHLLKLLLFY AADLNPDTEP ASEH
 
 
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