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MYL3_BOVIN
ID   MYL3_BOVIN              Reviewed;         199 AA.
AC   P85100;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Myosin light chain 3 {ECO:0000305};
DE   AltName: Full=Myosin light chain 1, slow-twitch muscle B/ventricular isoform {ECO:0000250|UniProtKB:P08590};
DE            Short=MLC1SB {ECO:0000250|UniProtKB:P08590};
GN   Name=MYL3 {ECO:0000250|UniProtKB:P08590};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
RN   [2] {ECO:0000305}
RP   METHYLATION AT ALA-2.
RX   PubMed=3979397; DOI=10.1111/j.1432-1033.1985.tb08809.x;
RA   Henry G.D., Trayer I.P., Brewer S., Levine B.A.;
RT   "The widespread distribution of alpha-N-trimethylalanine as the N-terminal
RT   amino acid of light chains from vertebrate striated muscle myosins.";
RL   Eur. J. Biochem. 148:75-82(1985).
CC   -!- FUNCTION: Regulatory light chain of myosin. Does not bind calcium.
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC   -!- PTM: N-terminus is methylated by METTL11A/NTM1. {ECO:0000250}.
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DR   EMBL; AAFC03056301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001069969.2; NM_001076501.2.
DR   PDB; 5N69; X-ray; 2.45 A; G/H=1-199.
DR   PDB; 6FSA; X-ray; 2.33 A; D/H=1-199.
DR   PDBsum; 5N69; -.
DR   PDBsum; 6FSA; -.
DR   AlphaFoldDB; P85100; -.
DR   SMR; P85100; -.
DR   STRING; 9913.ENSBTAP00000011047; -.
DR   iPTMnet; P85100; -.
DR   PaxDb; P85100; -.
DR   PRIDE; P85100; -.
DR   GeneID; 618352; -.
DR   KEGG; bta:618352; -.
DR   CTD; 4634; -.
DR   eggNOG; KOG0030; Eukaryota.
DR   HOGENOM; CLU_061288_13_0_1; -.
DR   InParanoid; P85100; -.
DR   OrthoDB; 1470794at2759; -.
DR   TreeFam; TF351553; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0031672; C:A band; IBA:GO_Central.
DR   GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR   GO; GO:0003785; F:actin monomer binding; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0060048; P:cardiac muscle contraction; IBA:GO_Central.
DR   GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IBA:GO_Central.
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; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Methylation; Motor protein; Muscle protein; Myosin;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P09542"
FT   CHAIN           2..199
FT                   /note="Myosin light chain 3"
FT                   /id="PRO_0000283743"
FT   DOMAIN          53..90
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          132..167
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          167..199
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000305"
FT   REGION          1..44
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   COMPBIAS        23..37
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N,N,N-trimethylalanine"
FT                   /evidence="ECO:0000269|PubMed:3979397"
FT   MOD_RES         92
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P16409"
FT   MOD_RES         131
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P09542"
FT   MOD_RES         133
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P16409"
FT   MOD_RES         134
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P16409"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09542"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:5N69"
FT   HELIX           52..64
FT                   /evidence="ECO:0007829|PDB:6FSA"
FT   STRAND          73..76
FT                   /evidence="ECO:0007829|PDB:5N69"
FT   TURN            77..79
FT                   /evidence="ECO:0007829|PDB:6FSA"
FT   HELIX           80..86
FT                   /evidence="ECO:0007829|PDB:6FSA"
FT   HELIX           93..99
FT                   /evidence="ECO:0007829|PDB:6FSA"
FT   TURN            105..109
FT                   /evidence="ECO:0007829|PDB:6FSA"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:5N69"
FT   HELIX           115..126
FT                   /evidence="ECO:0007829|PDB:6FSA"
FT   HELIX           134..142
FT                   /evidence="ECO:0007829|PDB:6FSA"
FT   STRAND          146..150
FT                   /evidence="ECO:0007829|PDB:6FSA"
FT   HELIX           154..163
FT                   /evidence="ECO:0007829|PDB:6FSA"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:6FSA"
FT   HELIX           170..176
FT                   /evidence="ECO:0007829|PDB:6FSA"
FT   TURN            177..179
FT                   /evidence="ECO:0007829|PDB:6FSA"
FT   HELIX           191..196
FT                   /evidence="ECO:0007829|PDB:6FSA"
SQ   SEQUENCE   199 AA;  21939 MW;  BC05C19146FD964C CRC64;
     MAPKKPDPKK DEAKAGAKAA AAPAPAPAPP PAPEPSKEPE FDPSKIKIEF TPEQIEEFKE
     AFTLFDRTPK CEMKITYGQC GDVLRALGQN PTQAEVLRVL GKPKQEELNS KMMDFDTFLP
     MLQHISKNKD TGTYEDFVEG LRVFDKEGNG TVMGAELRHV LATLGEKLTE DEVEKLMAGQ
     EDSNGCINYE AFVKHIMAG
 
 
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