MLRM_CHICK
ID MLRM_CHICK Reviewed; 172 AA.
AC P02612;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Myosin regulatory light chain 2, smooth muscle major isoform;
DE Short=MLC-2;
DE AltName: Full=DTNB;
DE AltName: Full=G1;
DE AltName: Full=Isoform L20-A;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3344215; DOI=10.1093/nar/16.3.1214;
RA Zavodny P.J., Petro M.E., Kumar C.C., Dailey S.H., Lonial H.K.,
RA Narula S.K., Leibowitz P.J.;
RT "The nucleotide sequence of chicken smooth muscle myosin light chain two.";
RL Nucleic Acids Res. 16:1214-1214(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3391271; DOI=10.1016/0014-5793(88)81300-0;
RA Messer N.G., Kendrick-Jones J.;
RT "Molecular cloning and sequencing of the chicken smooth muscle myosin
RT regulatory light chain.";
RL FEBS Lett. 234:49-52(1988).
RN [3]
RP PROTEIN SEQUENCE OF 2-172, AND ACETYLATION AT SER-2.
RX PubMed=7274219; DOI=10.1111/j.1432-1033.1981.tb06354.x;
RA Maita T., Chen J., Matsuda G.;
RT "Amino-acid sequence of the 20 000-molecular-weight light chain of chicken
RT gizzard-muscle myosin.";
RL Eur. J. Biochem. 117:417-424(1981).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=6546724; DOI=10.1016/0014-5793(84)80216-1;
RA Pearson R.B., Jakes R., John M., Kendrick-Jones J., Kemp B.;
RT "Phosphorylation site sequence of smooth muscle myosin light chain (Mr = 20
RT 000).";
RL FEBS Lett. 168:108-112(1984).
RN [5]
RP PROTEIN SEQUENCE OF 64-73.
RC TISSUE=Embryonic gizzard;
RX PubMed=2776758; DOI=10.1111/j.1432-1033.1989.tb21094.x;
RA Inoue A., Yanagisawa M., Takano-Ohmuro H., Masaki T.;
RT "Two isoforms of smooth muscle myosin regulatory light chain in chicken
RT gizzard.";
RL Eur. J. Biochem. 183:645-651(1989).
CC -!- FUNCTION: Myosin regulatory subunit that plays an important role in
CC regulation of both smooth muscle and nonmuscle cell contractile
CC activity. Implicated in cytokinesis, receptor capping, and cell
CC locomotion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC -!- MISCELLANEOUS: This chain binds calcium.
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DR EMBL; X06387; CAA29684.1; -; mRNA.
DR EMBL; Y00983; CAB46269.1; -; mRNA.
DR PIR; S03184; MOCHG1.
DR RefSeq; NP_990609.1; NM_205278.1.
DR RefSeq; XP_015151726.1; XM_015296240.1.
DR RefSeq; XP_015151727.1; XM_015296241.1.
DR PDB; 3J04; EM; -; B/E=26-168.
DR PDB; 7MF3; EM; 3.40 A; D/E=2-172.
DR PDBsum; 3J04; -.
DR PDBsum; 7MF3; -.
DR AlphaFoldDB; P02612; -.
DR SMR; P02612; -.
DR IntAct; P02612; 1.
DR STRING; 9031.ENSGALP00000041913; -.
DR iPTMnet; P02612; -.
DR PaxDb; P02612; -.
DR Ensembl; ENSGALT00000074687; ENSGALP00000053584; ENSGALG00000028567.
DR Ensembl; ENSGALT00000086483; ENSGALP00000063190; ENSGALG00000028567.
DR GeneID; 396215; -.
DR KEGG; gga:396215; -.
DR CTD; 10398; -.
DR VEuPathDB; HostDB:geneid_396215; -.
DR eggNOG; KOG0031; Eukaryota.
DR GeneTree; ENSGT00940000155458; -.
DR HOGENOM; CLU_061288_9_3_1; -.
DR InParanoid; P02612; -.
DR OMA; FECFDEN; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; P02612; -.
DR TreeFam; TF314218; -.
DR Reactome; R-GGA-445355; Smooth Muscle Contraction.
DR Reactome; R-GGA-5627123; RHO GTPases activate PAKs.
DR PRO; PR:P02612; -.
DR Proteomes; UP000000539; Chromosome 20.
DR Bgee; ENSGALG00000028567; Expressed in colon and 11 other tissues.
DR ExpressionAtlas; P02612; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005859; C:muscle myosin complex; IMP:CAFA.
DR GO; GO:0030016; C:myofibril; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0032036; F:myosin heavy chain binding; IBA:GO_Central.
DR GO; GO:0045159; F:myosin II binding; IPI:CAFA.
DR GO; GO:0008307; F:structural constituent of muscle; IMP:CAFA.
DR GO; GO:0030239; P:myofibril assembly; IMP:CAFA.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13405; EF-hand_6; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Direct protein sequencing;
KW Metal-binding; Motor protein; Muscle protein; Myosin; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7274219"
FT CHAIN 2..172
FT /note="Myosin regulatory light chain 2, smooth muscle major
FT isoform"
FT /id="PRO_0000198731"
FT DOMAIN 29..64
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 98..133
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 134..169
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:6546724,
FT ECO:0000269|PubMed:7274219"
FT CONFLICT 6..17
FT /note="AKAKTTKKRPQR -> KRPQRAKAKTTK (in Ref. 3; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 29..41
FT /evidence="ECO:0007829|PDB:7MF3"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:7MF3"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:7MF3"
SQ SEQUENCE 172 AA; 19845 MW; 3B858F333CE3D1D9 CRC64;
MSSKRAKAKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS
MGKNPTDEYL EGMMSEAPGP INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEASGFIHE
DHLRELLTTM GDRFTDEEVD EMYREAPIDK KGNFNYVEFT RILKHGAKDK DD
