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TELT_MOUSE
ID   TELT_MOUSE              Reviewed;         167 AA.
AC   O70548;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Telethonin;
DE   AltName: Full=Titin cap protein;
GN   Name=Tcap;
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 [MRNA].
RC   TISSUE=Diaphragm;
RA   Ievolella C., Formentin E., Valle G., Lanfranchi G.;
RT   "Skeletal muscle transcripts characterization in Homo sapiens and Mus
RT   musculus.";
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RA   Kolmerer B.;
RT   "The titin cap protein - a novel protein essential for sarcomere
RT   formation.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart;
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: Muscle assembly regulating factor. Mediates the antiparallel
CC       assembly of titin (TTN) molecules at the sarcomeric Z-disk (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with MYOZ1, MYOZ2 and MYOZ3. Interacts with CSRP3.
CC       Interacts directly with the N-terminal Ig-like domains of 2 titin (TTN)
CC       molecules. Interacts with ANKRD2; the interaction is direct (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere.
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DR   EMBL; AJ223854; CAA11585.1; -; mRNA.
DR   EMBL; Y15845; CAB38077.1; -; mRNA.
DR   EMBL; BC027631; AAH27631.1; -; mRNA.
DR   CCDS; CCDS25346.1; -.
DR   RefSeq; NP_035670.2; NM_011540.2.
DR   AlphaFoldDB; O70548; -.
DR   SMR; O70548; -.
DR   BioGRID; 203994; 1.
DR   ComplexPortal; CPX-127; Titin-Telethonin complex.
DR   STRING; 10090.ENSMUSP00000008021; -.
DR   iPTMnet; O70548; -.
DR   PhosphoSitePlus; O70548; -.
DR   PaxDb; O70548; -.
DR   PRIDE; O70548; -.
DR   ProteomicsDB; 263033; -.
DR   Antibodypedia; 3888; 221 antibodies from 29 providers.
DR   DNASU; 21393; -.
DR   Ensembl; ENSMUST00000008021; ENSMUSP00000008021; ENSMUSG00000007877.
DR   GeneID; 21393; -.
DR   KEGG; mmu:21393; -.
DR   UCSC; uc007lgf.1; mouse.
DR   CTD; 8557; -.
DR   MGI; MGI:1330233; Tcap.
DR   VEuPathDB; HostDB:ENSMUSG00000007877; -.
DR   eggNOG; ENOG502S21D; Eukaryota.
DR   GeneTree; ENSGT00390000012014; -.
DR   HOGENOM; CLU_128806_0_0_1; -.
DR   InParanoid; O70548; -.
DR   OMA; PWLLMRM; -.
DR   OrthoDB; 1270613at2759; -.
DR   PhylomeDB; O70548; -.
DR   TreeFam; TF333228; -.
DR   Reactome; R-MMU-390522; Striated Muscle Contraction.
DR   BioGRID-ORCS; 21393; 5 hits in 72 CRISPR screens.
DR   ChiTaRS; Tcap; mouse.
DR   PRO; PR:O70548; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; O70548; protein.
DR   Bgee; ENSMUSG00000007877; Expressed in hindlimb stylopod muscle and 99 other tissues.
DR   ExpressionAtlas; O70548; baseline and differential.
DR   Genevisible; O70548; MM.
DR   GO; GO:0031674; C:I band; IDA:BHF-UCL.
DR   GO; GO:1990733; C:titin-telethonin complex; ISO:MGI.
DR   GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR   GO; GO:0036122; F:BMP binding; ISO:MGI.
DR   GO; GO:0051373; F:FATZ binding; ISO:MGI.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR   GO; GO:0008307; F:structural constituent of muscle; ISO:MGI.
DR   GO; GO:0031432; F:titin binding; ISO:MGI.
DR   GO; GO:0070080; F:titin Z domain binding; ISO:MGI.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR   GO; GO:0007512; P:adult heart development; IEP:BHF-UCL.
DR   GO; GO:0055013; P:cardiac muscle cell development; ISO:MGI.
DR   GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
DR   GO; GO:0003300; P:cardiac muscle hypertrophy; ISO:MGI.
DR   GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; ISO:MGI.
DR   GO; GO:0055008; P:cardiac muscle tissue morphogenesis; ISO:MGI.
DR   GO; GO:0055003; P:cardiac myofibril assembly; ISO:MGI.
DR   GO; GO:0035995; P:detection of muscle stretch; ISO:MGI.
DR   GO; GO:0030916; P:otic vesicle formation; IEP:BHF-UCL.
DR   GO; GO:0045214; P:sarcomere organization; ISO:MGI.
DR   GO; GO:0048769; P:sarcomerogenesis; ISO:MGI.
DR   GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
DR   GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; ISO:MGI.
DR   GO; GO:0030240; P:skeletal muscle thin filament assembly; ISO:MGI.
DR   GO; GO:0001756; P:somitogenesis; IEP:BHF-UCL.
DR   Gene3D; 2.20.160.10; -; 1.
DR   InterPro; IPR015667; Telethonin.
DR   InterPro; IPR023111; Titin-like_dom_sf.
DR   PANTHER; PTHR15143; PTHR15143; 1.
DR   Pfam; PF09470; Telethonin; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..167
FT                   /note="Telethonin"
FT                   /id="PRO_0000072484"
FT   REGION          142..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   167 AA;  19078 MW;  2CB1F6F5415B4DC1 CRC64;
     MATSELSCQV SEENQERREA FWAEWKDLTL STRPEEGCSL HEEDTQRHET YHRQGQCQAV
     VQRSPWLVMR LGILGRGLQE YQLPYQRVLP LPIFTPTKVG ASKEEREETP IQLRELLALE
     TALGGQCVER QDVAEITKQL PPVVPVSKPG PLRRTLSRSM SQEAQRG
 
 
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