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SIMC1_RAT
ID   SIMC1_RAT               Reviewed;        1266 AA.
AC   F1LWT0;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2015, sequence version 3.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=SUMO-interacting motif-containing protein 1;
DE   AltName: Full=Platform element for inhibition of autolytic degradation {ECO:0000250|UniProtKB:Q8NDZ2};
GN   Name=Simc1; Synonyms=Pleiad {ECO:0000250|UniProtKB:Q8NDZ2};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
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}.
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DR   EMBL; AABR07027009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07027010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F1LWT0; -.
DR   STRING; 10116.ENSRNOP00000060156; -.
DR   PaxDb; F1LWT0; -.
DR   RGD; 2319689; Simc1.
DR   VEuPathDB; HostDB:ENSRNOG00000016932; -.
DR   eggNOG; ENOG502RR6K; Eukaryota.
DR   HOGENOM; CLU_264356_0_0_1; -.
DR   InParanoid; F1LWT0; -.
DR   OMA; GDAIQSP; -.
DR   TreeFam; TF332523; -.
DR   Proteomes; UP000002494; Chromosome 17.
DR   Bgee; ENSRNOG00000016932; Expressed in testis and 19 other tissues.
DR   ExpressionAtlas; F1LWT0; baseline and differential.
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:RGD.
DR   GO; GO:0010466; P:negative regulation of peptidase activity; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Protease inhibitor; Reference proteome.
FT   CHAIN           1..1266
FT                   /note="SUMO-interacting motif-containing protein 1"
FT                   /id="PRO_0000451960"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          756..812
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          857..1266
FT                   /note="Required for inhibition of CAPN3 protease activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NDZ2"
FT   REGION          1024..1052
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        532..575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..617
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..673
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        698..732
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1266 AA;  136789 MW;  D41D7F60905C4BF5 CRC64;
     MEDFIVISDD SGSESSAGTR SGRARRLRRA LSRTPGALPR RTVDFIDLTR ETRTRAKDRN
     GLCVIDLTRS EEENRPIATL DLTLEPVASS QKEPPSLQTC TNLSGKEMIE AQGDRGTQPA
     AQRVINNDPV DLDLLEENMF EGSRPPTSIS QDSVYPPEPN CSSITYKGDL SFLTSLQLSS
     DVSPFSSTSN NSSSSSNQRT SLPCPQQDVP CQSQGLLCSL QALSYPLRGS PCPPRASSCP
     PQALSCPPQA LSSLSCPSQT VQCQLQALPQ PPQEVPCSTQ NVPCPQQNIP STPQDLPWHP
     RHPLYPSQDT LGLPQDVPGR PQNVSYPQDM TQLQDMPWSL QDMPLSLQDV LQSLQDVPPL
     LGDVPQSPEV MQLPGYMTQS SRNVIQSSAG VIRSSGGVMQ PSGCMMQPSG GVTQSLRSAI
     QSSGGVMQSS GVTQSLRSVM QSSGGVMQSS GVTQSSGGVT WSLRSVMQSS GCMMQSPGGV
     MLSAGDMMQS SGGATRSLRS MMQSSGCMMQ SPGGVTQSSG SVMQSLRNVI QSSGGVTQSS
     GGVIQSSSGV PQSLRDRMQS PGSVSQSSGD VIQSPRGASP ASGDVIKSQG GMPRSLRDRM
     QSPGGVPQSS EDVIQSAGGV SPASGDAIQS PGGVSPASGD AMQSSGGVTP SLGDVPQSSG
     GVSPASGDAM QSPGGVTPSL GDAMQSPGGV SPASGDAMQS PGGVSPSLGD VPQSPGNMLE
     SLGNTPNLSG DVSHVPQELL DLAKGRPKLS LNAVQNRHSP MTISAPSSPS CSANPLSQQS
     EFSSEKRPWL TVSNSSAREE RSLPQSATPG SAQIQGQIAQ AGVYNRPCLH RLKYFLRPPV
     HHLFFQTLIP DKDTRESKGQ KLEPIPHRRL RMVTNTIEEN FPLGTVQFLM DFVSPQHYPP
     REIVAHIIQK ILLSGSETVD VLKEAYMLLM KIQQLHPANA KTVEWDWKLL TYVMEEEGQT
     LPGRVLFLRY VVQTLEDDFQ QILRRQRQHL QQSIANTVLS CDKQPHNVRD VIKWLVKAVT
     ENALTPPQDE TQTSPGPGVL KTSSDHLSPQ PNLARNTNQL IVCQLQRMLS IAVEVDRTPT
     CSSNKIAEMM FGFVLDIPER SQREMFFTTM ESHLLRCKVL EIIFLHSCET PTRLPLSLAQ
     ALYFLNNSTS LLKCQSDKSQ WQTWDELVEH LQFLLSSYQH VLREHLRSSV IDRKDLIIKR
     IKPKPQQGDD ITVVDVEKQI EAFRSRLVHI LGEPLVPQLQ DKVHLLKLLL FYAADLNPDT
     EPASER
 
 
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