MYL11_HUMAN
ID MYL11_HUMAN Reviewed; 169 AA.
AC Q96A32; A0A024QZG6; B2RA83; Q14843; Q6IB41;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Myosin regulatory light chain 11 {ECO:0000305};
DE AltName: Full=Fast skeletal myosin light chain 2 {ECO:0000303|PubMed:14756420};
DE AltName: Full=MLC2B;
DE AltName: Full=Myosin light chain 11 {ECO:0000312|HGNC:HGNC:29824};
DE AltName: Full=Myosin regulatory light chain 2, skeletal muscle isoform;
GN Name=MYL11 {ECO:0000312|HGNC:HGNC:29824};
GN Synonyms=HSRLC {ECO:0000303|PubMed:14756420}, MYLPF;
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] {ECO:0000305, ECO:0000312|EMBL:CAA40762.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle {ECO:0000312|EMBL:CAA40762.1};
RX PubMed=14756420; DOI=10.1080/1042517031000154952;
RA Sachdev S., Raychowdhury M.K., Sarkar S.;
RT "Human fast skeletal myosin light chain 2 cDNA: isolation, tissue specific
RT expression of the single copy gene, comparative sequence analysis of
RT isoforms and evolutionary relationships.";
RL DNA Seq. 14:339-350(2003).
RN [2] {ECO:0000312|EMBL:AAA91848.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle {ECO:0000312|EMBL:AAA91848.1};
RA Wu Q.L.;
RT "Characterization of a full length human skeletal fast light chain 2
RT cDNA.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:AAA91848.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta {ECO:0000312|EMBL:AAK52797.1};
RA Gong L., Wang Y.-G., Li T., Wu K.;
RT "Cloning and characterization of a human MRLC2 gene encoding a myosin
RT regulatory light chain.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAA91848.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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 [6] {ECO:0000312|EMBL:AAA91848.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000312|EMBL:AAH12571.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle {ECO:0000312|EMBL:AAH12571.1};
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 [8]
RP INVOLVEMENT IN DA1C, AND VARIANTS DA1C VAL-33; ARG-157; PHE-157 AND
RP SER-163.
RX PubMed=32707087; DOI=10.1016/j.ajhg.2020.06.014;
RG University of Washington Center for Mendelian Genomics;
RA Chong J.X., Talbot J.C., Teets E.M., Previs S., Martin B.L., Shively K.M.,
RA Marvin C.T., Aylsworth A.S., Saadeh-Haddad R., Schatz U.A., Inzana F.,
RA Ben-Omran T., Almusafri F., Al-Mulla M., Buckingham K.J., Harel T.,
RA Mor-Shaked H., Radhakrishnan P., Girisha K.M., Nayak S.S., Shukla A.,
RA Dieterich K., Faure J., Rendu J., Capri Y., Latypova X., Nickerson D.A.,
RA Warshaw D.M., Janssen P.M.L., Amacher S.L., Bamshad M.J.;
RT "Mutations in MYLPF Cause a Novel Segmental Amyoplasia that Manifests as
RT Distal Arthrogryposis.";
RL Am. J. Hum. Genet. 107:293-310(2020).
CC -!- FUNCTION: Myosin regulatory subunit that plays an essential role to
CC maintain muscle integrity during early development (By similarity).
CC Plays a role in muscle contraction (By similarity).
CC {ECO:0000250|UniProtKB:O93409}.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC {ECO:0000305}.
CC -!- INTERACTION:
CC Q96A32; P14136: GFAP; NbExp=3; IntAct=EBI-1390771, EBI-744302;
CC Q96A32; P28799: GRN; NbExp=3; IntAct=EBI-1390771, EBI-747754;
CC Q96A32; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-1390771, EBI-1055254;
CC Q96A32; O43933: PEX1; NbExp=3; IntAct=EBI-1390771, EBI-988601;
CC Q96A32; O76024: WFS1; NbExp=3; IntAct=EBI-1390771, EBI-720609;
CC -!- TISSUE SPECIFICITY: Expressed in fetal and adult skeletal muscle.
CC {ECO:0000269|PubMed:14756420}.
CC -!- DISEASE: Arthrogryposis, distal, 1C (DA1C) [MIM:619110]: A form of
CC distal arthrogryposis, a disease characterized by congenital joint
CC contractures that mainly involve two or more distal parts of the limbs,
CC in the absence of a primary neurological or muscle disease. DA1C
CC patients show multiple congenital contractures, scoliosis, short
CC stature, and segmental amyoplasia. DA1C inheritance can be autosomal
CC recessive or autosomal dominant. {ECO:0000269|PubMed:32707087}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
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DR EMBL; X57543; CAA40762.1; -; mRNA.
DR EMBL; M21812; AAA91848.1; -; mRNA.
DR EMBL; AF363061; AAK52797.1; -; mRNA.
DR EMBL; CR456963; CAG33244.1; -; mRNA.
DR EMBL; AK314082; BAG36780.1; -; mRNA.
DR EMBL; CH471192; EAW52254.1; -; Genomic_DNA.
DR EMBL; CH471192; EAW52255.1; -; Genomic_DNA.
DR EMBL; BC012571; AAH12571.1; -; mRNA.
DR CCDS; CCDS10677.1; -.
DR RefSeq; NP_001311387.1; NM_001324458.1.
DR RefSeq; NP_001311388.1; NM_001324459.1.
DR RefSeq; NP_037424.2; NM_013292.4.
DR AlphaFoldDB; Q96A32; -.
DR SMR; Q96A32; -.
DR BioGRID; 118947; 20.
DR IntAct; Q96A32; 8.
DR STRING; 9606.ENSP00000325239; -.
DR iPTMnet; Q96A32; -.
DR PhosphoSitePlus; Q96A32; -.
DR BioMuta; MYLPF; -.
DR DMDM; 74760696; -.
DR MassIVE; Q96A32; -.
DR PaxDb; Q96A32; -.
DR PeptideAtlas; Q96A32; -.
DR PRIDE; Q96A32; -.
DR ProteomicsDB; 75901; -.
DR Antibodypedia; 13671; 182 antibodies from 29 providers.
DR DNASU; 29895; -.
DR Ensembl; ENST00000322861.12; ENSP00000325239.7; ENSG00000180209.12.
DR GeneID; 29895; -.
DR KEGG; hsa:29895; -.
DR MANE-Select; ENST00000322861.12; ENSP00000325239.7; NM_013292.5; NP_037424.2.
DR UCSC; uc002dxv.2; human.
DR CTD; 29895; -.
DR DisGeNET; 29895; -.
DR GeneCards; MYLPF; -.
DR HGNC; HGNC:29824; MYL11.
DR HPA; ENSG00000180209; Group enriched (skeletal muscle, tongue).
DR MalaCards; MYLPF; -.
DR MIM; 617378; gene.
DR MIM; 619110; phenotype.
DR neXtProt; NX_Q96A32; -.
DR OpenTargets; ENSG00000180209; -.
DR PharmGKB; PA164723287; -.
DR VEuPathDB; HostDB:ENSG00000180209; -.
DR eggNOG; KOG0031; Eukaryota.
DR GeneTree; ENSGT00940000159038; -.
DR InParanoid; Q96A32; -.
DR OMA; EDVKNMW; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; Q96A32; -.
DR TreeFam; TF314218; -.
DR PathwayCommons; Q96A32; -.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR SignaLink; Q96A32; -.
DR SIGNOR; Q96A32; -.
DR BioGRID-ORCS; 29895; 10 hits in 1068 CRISPR screens.
DR ChiTaRS; MYLPF; human.
DR GenomeRNAi; 29895; -.
DR Pharos; Q96A32; Tbio.
DR PRO; PR:Q96A32; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96A32; protein.
DR Bgee; ENSG00000180209; Expressed in biceps brachii and 114 other tissues.
DR ExpressionAtlas; Q96A32; baseline and differential.
DR Genevisible; Q96A32; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005859; C:muscle myosin complex; TAS:ProtInc.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0008307; F:structural constituent of muscle; ISS:BHF-UCL.
DR GO; GO:0033275; P:actin-myosin filament sliding; ISS:UniProtKB.
DR GO; GO:0006955; P:immune response; IEA:Ensembl.
DR GO; GO:0006936; P:muscle contraction; IMP:UniProtKB.
DR GO; GO:0060415; P:muscle tissue morphogenesis; ISS:UniProtKB.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISS:BHF-UCL.
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 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; Disease variant; Metal-binding; Methylation; Motor protein;
KW Muscle protein; Myosin; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02608"
FT CHAIN 2..169
FT /note="Myosin regulatory light chain 11"
FT /evidence="ECO:0000250|UniProtKB:P02608"
FT /id="PRO_0000283746"
FT DOMAIN 25..60
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 95..130
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 131..166
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N,N,N-trimethylalanine"
FT /evidence="ECO:0000250|UniProtKB:P02608"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97457"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97457"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04466"
FT MOD_RES 35
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04466"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04466"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04466"
FT VARIANT 33
FT /note="A -> V (in DA1C; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:32707087"
FT /id="VAR_085167"
FT VARIANT 157
FT /note="C -> F (in DA1C; dbSNP:rs756765686)"
FT /evidence="ECO:0000269|PubMed:32707087"
FT /id="VAR_085168"
FT VARIANT 157
FT /note="C -> R (in DA1C; dbSNP:rs748809300)"
FT /evidence="ECO:0000269|PubMed:32707087"
FT /id="VAR_085169"
FT VARIANT 163
FT /note="G -> S (in DA1C; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:32707087"
FT /id="VAR_085170"
FT CONFLICT 11
FT /note="V -> VA (in Ref. 1; CAA40762 and 2; AAA91848)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="E -> D (in Ref. 4; CAG33244)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 169 AA; 19015 MW; 2CE585D6B1F8769D CRC64;
MAPKRAKRRT VEGGSSSVFS MFDQTQIQEF KEAFTVIDQN RDGIIDKEDL RDTFAAMGRL
NVKNEELDAM MKEASGPINF TVFLTMFGEK LKGADPEDVI TGAFKVLDPE GKGTIKKKFL
EELLTTQCDR FSQEEIKNMW AAFPPDVGGN VDYKNICYVI THGDAKDQE
