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MYL3_RAT
ID   MYL3_RAT                Reviewed;         200 AA.
AC   P16409;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Myosin light chain 3 {ECO:0000305};
DE   AltName: Full=Myosin alkali light chain 1, ventricular {ECO:0000305|PubMed:2798124};
DE            Short=MLClV {ECO:0000303|PubMed:2798124};
DE   AltName: Full=Myosin light chain 1, slow-twitch muscle B/ventricular isoform {ECO:0000250|UniProtKB:P08590};
DE            Short=MLC1SB {ECO:0000250|UniProtKB:P08590};
DE   AltName: Full=Ventricular myosin light chain 1 {ECO:0000303|PubMed:2717409};
DE            Short=rVMLC1 {ECO:0000303|PubMed:2717409};
GN   Name=Myl3 {ECO:0000312|RGD:3142}; Synonyms=Mlc1v {ECO:0000312|RGD:3142};
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 [MRNA].
RC   TISSUE=Heart ventricle;
RX   PubMed=2717409; DOI=10.1093/nar/17.7.2753;
RA   McNally E., Buttrick P., Leinwand L.;
RT   "Ventricular myosin light chain 1 is developmentally regulated and does not
RT   change in hypertension.";
RL   Nucleic Acids Res. 17:2753-2767(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Wistar; TISSUE=Heart ventricle;
RX   PubMed=2798124; DOI=10.1093/nar/17.19.7723;
RA   Periasamy M., Wodgaonkar R., Kumar C., Martin B.J., Siddiqui M.A.Q.;
RT   "Characterization of a rat myosin alkali light chain gene expressed in
RT   ventricular and slow twitch skeletal muscles.";
RL   Nucleic Acids Res. 17:7723-7734(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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 THR-93; THR-134; TYR-135 AND
RP   SER-184, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Regulatory light chain of myosin. Does not bind calcium.
CC   -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC   -!- TISSUE SPECIFICITY: Expressed only in ventricular and slow twitch
CC       skeletal muscle tissues. {ECO:0000269|PubMed:2798124}.
CC   -!- PTM: N-terminus is methylated by METTL11A/NTM1. {ECO:0000250}.
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DR   EMBL; X14812; CAA32917.1; -; mRNA.
DR   EMBL; X16325; CAA34388.1; -; Genomic_DNA.
DR   EMBL; X16326; CAA34388.1; JOINED; Genomic_DNA.
DR   EMBL; X16327; CAA34388.1; JOINED; Genomic_DNA.
DR   EMBL; X16329; CAA34388.1; JOINED; Genomic_DNA.
DR   EMBL; X16330; CAA34388.1; JOINED; Genomic_DNA.
DR   EMBL; BC081832; AAH81832.1; -; mRNA.
DR   PIR; S09573; MORT3V.
DR   RefSeq; NP_036738.1; NM_012606.2.
DR   RefSeq; XP_006243979.3; XM_006243917.3.
DR   AlphaFoldDB; P16409; -.
DR   SMR; P16409; -.
DR   BioGRID; 246728; 2.
DR   IntAct; P16409; 1.
DR   MINT; P16409; -.
DR   STRING; 10116.ENSRNOP00000028458; -.
DR   iPTMnet; P16409; -.
DR   PhosphoSitePlus; P16409; -.
DR   jPOST; P16409; -.
DR   PaxDb; P16409; -.
DR   PRIDE; P16409; -.
DR   Ensembl; ENSRNOT00000028458; ENSRNOP00000028458; ENSRNOG00000020955.
DR   GeneID; 24585; -.
DR   KEGG; rno:24585; -.
DR   CTD; 4634; -.
DR   RGD; 3142; Myl3.
DR   eggNOG; KOG0030; Eukaryota.
DR   GeneTree; ENSGT01030000234570; -.
DR   HOGENOM; CLU_061288_13_0_1; -.
DR   InParanoid; P16409; -.
DR   OMA; YDRTPKC; -.
DR   OrthoDB; 1470794at2759; -.
DR   PhylomeDB; P16409; -.
DR   TreeFam; TF351553; -.
DR   Reactome; R-RNO-390522; Striated Muscle Contraction.
DR   PRO; PR:P16409; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000020955; Expressed in heart and 17 other tissues.
DR   Genevisible; P16409; RN.
DR   GO; GO:0031672; C:A band; ISO:RGD.
DR   GO; GO:0031674; C:I band; ISO:RGD.
DR   GO; GO:0016459; C:myosin complex; IDA:RGD.
DR   GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR   GO; GO:0003785; F:actin monomer binding; ISO:RGD.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IDA:RGD.
DR   GO; GO:0060048; P:cardiac muscle contraction; IDA:RGD.
DR   GO; GO:0006936; P:muscle contraction; TAS:RGD.
DR   GO; GO:0006942; P:regulation of striated muscle contraction; ISO:RGD.
DR   GO; GO:0002026; P:regulation of the force of heart contraction; ISO:RGD.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD.
DR   GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:RGD.
DR   CDD; cd00051; EFh; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   1: Evidence at protein level;
KW   Methylation; Motor protein; Muscle protein; Myosin; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P09542"
FT   CHAIN           2..200
FT                   /note="Myosin light chain 3"
FT                   /id="PRO_0000198698"
FT   DOMAIN          54..91
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          133..168
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          168..200
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N,N,N-trimethylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P09542"
FT   MOD_RES         93
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         132
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P09542"
FT   MOD_RES         134
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         135
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   200 AA;  22156 MW;  2B8C832A9D364253 CRC64;
     MAPKKPEPKK DDAKTAAPKA APAPAAAPAA APEPERPKEA EFDASKIKIE FTPEQIEEFK
     EAFQLFDRTP KGEMKITYGQ CGDVLRALGQ NPTQAEVLRV LGKPKQEELN SKMMDFETFL
     PMLQHISKNK DTGTYEDFVE GLRVFDKEGN GTVMGAELRH VLATLGERLT EDEVEKLMAG
     QEDSNGCINY EAFVKHIMAS
 
 
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