ID   MLRN_CHICK              Reviewed;         172 AA.
AC   P24032;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Myosin regulatory light chain 2, smooth muscle minor isoform;
DE            Short=MLC-2;
DE   AltName: Full=DTNB;
DE   AltName: Full=G1;
DE   AltName: Full=Isoform L20-B1;
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].
RC   TISSUE=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   -!- PTM: Phosphorylation increases the actin-activated myosin ATPase
CC       activity and thereby regulates the contractile activity. {ECO:0000250}.
CC   -!- MISCELLANEOUS: This chain binds calcium.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X16532; CAA34535.1; -; mRNA.
DR   PIR; A61034; A61034.
DR   PIR; S05530; MOCH2G.
DR   RefSeq; NP_990672.1; NM_205341.3.
DR   RefSeq; XP_015133434.1; XM_015277948.1.
DR   AlphaFoldDB; P24032; -.
DR   SMR; P24032; -.
DR   IntAct; P24032; 1.
DR   STRING; 9031.ENSGALP00000030296; -.
DR   PaxDb; P24032; -.
DR   PRIDE; P24032; -.
DR   Ensembl; ENSGALT00000030933; ENSGALP00000030296; ENSGALG00000014854.
DR   GeneID; 396284; -.
DR   KEGG; gga:396284; -.
DR   CTD; 10627; -.
DR   VEuPathDB; HostDB:geneid_396284; -.
DR   eggNOG; KOG0031; Eukaryota.
DR   GeneTree; ENSGT00940000153607; -.
DR   HOGENOM; CLU_061288_9_3_1; -.
DR   InParanoid; P24032; -.
DR   OMA; GFVDHED; -.
DR   OrthoDB; 1435392at2759; -.
DR   PhylomeDB; P24032; -.
DR   Reactome; R-GGA-3928664; Ephrin signaling.
DR   Reactome; R-GGA-445355; Smooth Muscle Contraction.
DR   PRO; PR:P24032; -.
DR   Proteomes; UP000000539; Chromosome 2.
DR   Bgee; ENSGALG00000014854; Expressed in colon and 14 other tissues.
DR   ExpressionAtlas; P24032; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016460; C:myosin II complex; 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   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   2: Evidence at transcript level;
KW   Acetylation; Calcium; Metal-binding; Motor protein; Muscle protein; Myosin;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..172
FT                   /note="Myosin regulatory light chain 2, smooth muscle minor
FT                   isoform"
FT                   /id="PRO_0000198732"
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   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:0000250"
FT   MOD_RES         19
FT                   /note="Phosphothreonine; by MLCK"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         20
FT                   /note="Phosphoserine; by MLCK"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   172 AA;  19911 MW;  A5DB388DC9BC0874 CRC64;
     MSSKRAKTKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS
     LGKNPTDEYL DAMMNEAPGP INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEATGFIQE
     DYLRELLTTM GDRFTDEEVD ELYREAPIDK KGNFNYIEFT RILKHGAKDK DD