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MYL3_PONAB
ID   MYL3_PONAB              Reviewed;         195 AA.
AC   Q5R887;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Myosin light chain 3;
DE   AltName: Full=Myosin light chain 1, slow-twitch muscle B/ventricular isoform;
DE            Short=MLC1SB {ECO:0000250|UniProtKB:P08590};
GN   Name=MYL3 {ECO:0000250|UniProtKB:P08590};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulatory light chain of myosin. Does not bind calcium (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC       {ECO:0000250}.
CC   -!- PTM: N-terminus is methylated by METTL11A/NTM1. {ECO:0000250}.
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DR   EMBL; CR859867; CAH92023.1; -; mRNA.
DR   RefSeq; NP_001127497.1; NM_001134025.1.
DR   RefSeq; XP_009237357.1; XM_009239082.1.
DR   AlphaFoldDB; Q5R887; -.
DR   SMR; Q5R887; -.
DR   STRING; 9601.ENSPPYP00000015580; -.
DR   Ensembl; ENSPPYT00000016200; ENSPPYP00000015580; ENSPPYG00000013927.
DR   GeneID; 100174572; -.
DR   KEGG; pon:100174572; -.
DR   CTD; 4634; -.
DR   eggNOG; KOG0030; Eukaryota.
DR   GeneTree; ENSGT01030000234570; -.
DR   HOGENOM; CLU_061288_13_0_1; -.
DR   InParanoid; Q5R887; -.
DR   OMA; YDRTPKC; -.
DR   OrthoDB; 1470794at2759; -.
DR   TreeFam; TF351553; -.
DR   Proteomes; UP000001595; Chromosome 3.
DR   GO; GO:0031672; C:A band; IEA:Ensembl.
DR   GO; GO:0031674; C:I band; IEA:Ensembl.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003785; F:actin monomer binding; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
DR   GO; GO:0006942; P:regulation of striated muscle contraction; IEA:Ensembl.
DR   GO; GO:0002026; P:regulation of the force of heart contraction; IEA:Ensembl.
DR   GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl.
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   2: Evidence at transcript 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..195
FT                   /note="Myosin light chain 3"
FT                   /id="PRO_0000240322"
FT   DOMAIN          49..86
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          128..163
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          163..195
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          1..37
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         88
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P16409"
FT   MOD_RES         127
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P09542"
FT   MOD_RES         129
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P16409"
FT   MOD_RES         130
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P16409"
FT   MOD_RES         179
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09542"
SQ   SEQUENCE   195 AA;  21932 MW;  306CF328841729DD CRC64;
     MAPKKPEPKK DDAKAAPKAA PAPAPPPEPE RPKEVEFDAS KIKIEFTPEQ IEEFKEAFML
     FDRTPKCEMK ITYGQCGDVL RALGQNPTQA EVLRVLGKPR QEELNTKMMD FETFLPMLQH
     ISKNKDTGTY EDFVEGLRVF DKEGNGTVMG AELRHVLATL GERLTEDEVE KLMAGQEDSN
     GCINYEAFVK HIMSS
 
 
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