ML12A_HUMAN
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 03-AUG-2022, entry version 200.
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; 137.
DR CORUM; P19105; -.
DR IntAct; P19105; 50.
DR MINT; P19105; -.
DR STRING; 9606.ENSP00000217652; -.
DR DrugBank; DB08378; 4-[4-(2,5-DIOXO-PYRROLIDIN-1-YL)-PHENYLAMINO]-4-HYDROXY-BUTYRIC ACID.
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 SWISS-2DPAGE; P19105; -.
DR EPD; P19105; -.
DR jPOST; P19105; -.
DR MassIVE; P19105; -.
DR PaxDb; P19105; -.
DR PeptideAtlas; P19105; -.
DR PRIDE; P19105; -.
DR ProteomicsDB; 53633; -.
DR TopDownProteomics; P19105; -.
DR Antibodypedia; 3856; 169 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 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; WEAPINK; -.
DR OrthoDB; 1435392at2759; -.
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 1019 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 161 other tissues.
DR ExpressionAtlas; P19105; baseline and differential.
DR Genevisible; P19105; HS.
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; IBA:GO_Central.
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; IEA:InterPro.
DR GO; GO:0035254; F:glutamate receptor binding; IEA:Ensembl.
DR GO; GO:0032036; F:myosin heavy chain binding; IBA:GO_Central.
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 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 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
