ID   ML12A_HUMAN             Reviewed;         171 AA.
AC   P19105; Q53X45;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 209.
DE   RecName: Full=Myosin regulatory light chain 12A;
DE   AltName: Full=Epididymis secretory protein Li 24;
DE            Short=HEL-S-24;
DE   AltName: Full=MLC-2B;
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, RLC;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Placenta;
RX   PubMed=2216787; DOI=10.1093/nar/18.19.5892;
RA   Grant J.W., Zhong R.Q., McEwen P., Church S.L.;
RT   "Human nonsarcomeric 20,000 Da myosin regulatory light chain cDNA.";
RL   Nucleic Acids Res. 18:5892-5892(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION AT THR-18 AND SER-19.
RX   PubMed=11942626; DOI=10.1247/csf.26.677;
RA   Iwasaki T., Murata-Hori M., Ishitobi S., Hosoya H.;
RT   "Diphosphorylated MRLC is required for organization of stress fibers in
RT   interphase cells and the contractile ring in dividing cells.";
RL   Cell Struct. Funct. 26:677-683(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Li J.Y., Wang H.Y., Liu F.J., Liu J.;
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skeletal muscle, Skin, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
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   -!- INTERACTION:
CC       P19105; Q62868: Rock2; Xeno; NbExp=2; IntAct=EBI-354418, EBI-1569209;
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.
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DR   EMBL; X54304; CAA38201.1; -; mRNA.
DR   EMBL; D82059; BAB88919.1; -; mRNA.
DR   EMBL; EU794621; ACJ13675.1; -; mRNA.
DR   EMBL; AK291145; BAF83834.1; -; mRNA.
DR   EMBL; CH471113; EAX01678.1; -; Genomic_DNA.
DR   EMBL; CH471113; EAX01680.1; -; Genomic_DNA.
DR   EMBL; CH471113; EAX01681.1; -; Genomic_DNA.
DR   EMBL; BC016372; AAH16372.1; -; mRNA.
DR   EMBL; BC031972; AAH31972.1; -; mRNA.
DR   EMBL; BC032748; AAH32748.1; -; mRNA.
DR   CCDS; CCDS11830.1; -.
DR   PIR; S11493; MOHULP.
DR   RefSeq; NP_001289976.1; NM_001303047.1.
DR   RefSeq; NP_001289977.1; NM_001303048.1.
DR   RefSeq; NP_001289978.1; NM_001303049.1.
DR   RefSeq; NP_006462.1; NM_006471.3.
DR   AlphaFoldDB; P19105; -.
DR   SMR; P19105; -.
DR   BioGRID; 115871; 189.
DR   CORUM; P19105; -.
DR   IntAct; P19105; 54.
DR   MINT; P19105; -.
DR   STRING; 9606.ENSP00000464359; -.
DR   DrugBank; DB08378; 4-[4-(2,5-DIOXO-PYRROLIDIN-1-YL)-PHENYLAMINO]-4-HYDROXY-BUTYRIC ACID.
DR   GlyCosmos; P19105; 1 site, 1 glycan.
DR   GlyGen; P19105; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P19105; -.
DR   MetOSite; P19105; -.
DR   PhosphoSitePlus; P19105; -.
DR   SwissPalm; P19105; -.
DR   BioMuta; MYL12A; -.
DR   DMDM; 127169; -.
DR   OGP; P19105; -.
DR   EPD; P19105; -.
DR   jPOST; P19105; -.
DR   MassIVE; P19105; -.
DR   PaxDb; 9606-ENSP00000217652; -.
DR   PeptideAtlas; P19105; -.
DR   ProteomicsDB; 53633; -.
DR   Pumba; P19105; -.
DR   TopDownProteomics; P19105; -.
DR   Antibodypedia; 3856; 198 antibodies from 31 providers.
DR   DNASU; 10627; -.
DR   Ensembl; ENST00000217652.8; ENSP00000217652.3; ENSG00000101608.13.
DR   Ensembl; ENST00000536605.1; ENSP00000441231.1; ENSG00000101608.13.
DR   Ensembl; ENST00000578611.5; ENSP00000463614.1; ENSG00000101608.13.
DR   Ensembl; ENST00000579226.5; ENSP00000462171.1; ENSG00000101608.13.
DR   GeneID; 10627; -.
DR   KEGG; hsa:10627; -.
DR   MANE-Select; ENST00000217652.8; ENSP00000217652.3; NM_006471.4; NP_006462.1.
DR   UCSC; uc002klr.3; human.
DR   AGR; HGNC:16701; -.
DR   CTD; 10627; -.
DR   DisGeNET; 10627; -.
DR   GeneCards; MYL12A; -.
DR   HGNC; HGNC:16701; MYL12A.
DR   HPA; ENSG00000101608; Group enriched (heart muscle, skeletal muscle, tongue).
DR   MIM; 609211; gene.
DR   neXtProt; NX_P19105; -.
DR   OpenTargets; ENSG00000101608; -.
DR   PharmGKB; PA164723273; -.
DR   VEuPathDB; HostDB:ENSG00000101608; -.
DR   eggNOG; KOG0031; Eukaryota.
DR   GeneTree; ENSGT00940000153607; -.
DR   InParanoid; P19105; -.
DR   OMA; ETFNMID; -.
DR   OrthoDB; 312751at2759; -.
DR   PhylomeDB; P19105; -.
DR   TreeFam; TF314218; -.
DR   PathwayCommons; P19105; -.
DR   Reactome; R-HSA-3928664; Ephrin signaling.
DR   Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR   SignaLink; P19105; -.
DR   SIGNOR; P19105; -.
DR   BioGRID-ORCS; 10627; 89 hits in 1078 CRISPR screens.
DR   ChiTaRS; MYL12A; human.
DR   GeneWiki; MRCL3; -.
DR   GenomeRNAi; 10627; -.
DR   Pharos; P19105; Tbio.
DR   PRO; PR:P19105; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; P19105; Protein.
DR   Bgee; ENSG00000101608; Expressed in apex of heart and 163 other cell types or tissues.
DR   ExpressionAtlas; P19105; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016460; C:myosin II complex; IEA:Ensembl.
DR   GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0035254; F:glutamate receptor binding; IEA:Ensembl.
DR   GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
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   PANTHER; PTHR23049:SF57; MYOSIN REGULATORY LIGHT CHAIN 12A; 1.
DR   PANTHER; PTHR23049; MYOSIN REGULATORY LIGHT CHAIN 2; 1.
DR   Pfam; PF08976; EF-hand_11; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 3.
DR   SWISS-2DPAGE; P19105; -.
DR   Genevisible; P19105; HS.
PE   1: Evidence at protein 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_0000198733"
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:0000269|PubMed:11942626"
FT   MOD_RES         19
FT                   /note="Phosphoserine; by MLCK"
FT                   /evidence="ECO:0000269|PubMed:11942626"
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
//