ID   ML12A_PONAB             Reviewed;         171 AA.
AC   Q5RC34;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Myosin regulatory light chain 12A;
DE   AltName: Full=Myosin RLC;
DE   AltName: Full=Myosin regulatory light chain 2, nonsarcomeric;
DE   AltName: Full=Myosin regulatory light chain MRLC3;
GN   Name=MYL12A; Synonyms=MLCB, MRLC3;
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: Myosin regulatory subunit that plays an important role in
CC       regulation of both smooth muscle and nonmuscle cell contractile
CC       activity via its phosphorylation. Implicated in cytokinesis, receptor
CC       capping, and cell locomotion (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylation increases the actin-activated myosin ATPase
CC       activity and thereby regulates the contractile activity. It is required
CC       to generate the driving force in the migration of the cells but not
CC       necessary for localization of myosin-2 at the leading edge (By
CC       similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: This chain binds calcium. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH90676.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR858447; CAH90676.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001125368.1; NM_001131896.1.
DR   RefSeq; XP_009250543.1; XM_009252268.1.
DR   RefSeq; XP_009250544.1; XM_009252269.1.
DR   RefSeq; XP_009250545.1; XM_009252270.1.
DR   AlphaFoldDB; Q5RC34; -.
DR   SMR; Q5RC34; -.
DR   STRING; 9601.ENSPPYP00000010136; -.
DR   GeneID; 100172271; -.
DR   KEGG; pon:100172271; -.
DR   CTD; 10627; -.
DR   eggNOG; KOG0031; Eukaryota.
DR   HOGENOM; CLU_061288_9_3_1; -.
DR   InParanoid; Q5RC34; -.
DR   OrthoDB; 1435392at2759; -.
DR   TreeFam; TF314218; -.
DR   Proteomes; UP000001595; Chromosome 18.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd00051; EFh; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR015070; EF_hand_DJBP.
DR   InterPro; IPR002048; EF_hand_dom.
DR   Pfam; PF08976; EF-hand_11; 1.
DR   Pfam; PF13405; EF-hand_6; 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   Calcium; Metal-binding; Motor protein; Muscle protein; Myosin;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..171
FT                   /note="Myosin regulatory light chain 12A"
FT                   /id="PRO_0000198734"
FT   DOMAIN          28..63
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          97..132
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          133..168
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         41
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         43
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         45
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         52
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         18
FT                   /note="Phosphothreonine; by MLCK"
FT                   /evidence="ECO:0000250|UniProtKB:P19105"
FT   MOD_RES         19
FT                   /note="Phosphoserine; by MLCK"
FT                   /evidence="ECO:0000250|UniProtKB:P19105"
SQ   SEQUENCE   171 AA;  19794 MW;  C871AA881BF5C215 CRC64;
     MSSKRTKTKT KKRPQRATSN VFAMFDQSQI QEFKEAFNMI DQNRDGFIDK EDLHDMLASL
     GKNPTDEYLD AMMNEAPGPI NFTMFLTMFG EKLNGTDPED VIRNAFACFD EEATGTIQED
     YLRELLTTMG DRFTDEEVDE LYREAPIDKK GNFNYIEFTR ILKHGAKDKD D