MYOZ1_HUMAN
ID MYOZ1_HUMAN Reviewed; 299 AA.
AC Q9NP98; Q9H1I7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Myozenin-1;
DE AltName: Full=Calsarcin-2;
DE AltName: Full=Filamin-, actinin- and telethonin-binding protein;
DE AltName: Full=Protein FATZ;
GN Name=MYOZ1 {ECO:0000312|HGNC:HGNC:13752};
GN Synonyms=MYOZ {ECO:0000312|EMBL:AAG24509.1};
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:CAB92967.1}
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ACTN2; FLNC AND TCAP,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle {ECO:0000312|EMBL:CAB92967.1};
RX PubMed=10984498; DOI=10.1074/jbc.m007493200;
RA Faulkner G., Pallavicini A., Comelli A., Salamon M., Bortoletto G.,
RA Ievolella C., Trevisan S., Kojic' S., Dalla Vecchia F., Laveder P.,
RA Valle G., Lanfranchi G.;
RT "FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc
RT of skeletal muscle.";
RL J. Biol. Chem. 275:41234-41242(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAG38940.1}
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ACTN2 AND PPP3CA, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Heart {ECO:0000269|PubMed:11114196};
RX PubMed=11114196; DOI=10.1073/pnas.260501097;
RA Frey N., Richardson J.A., Olson E.N.;
RT "Calsarcins, a novel family of sarcomeric calcineurin-binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14632-14637(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAG24509.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INTERACTION WITH ACTN2; ACTN3 AND
RP FLNC, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle {ECO:0000312|EMBL:AAG24509.1};
RX PubMed=11171996; DOI=10.1073/pnas.98.4.1595;
RA Takada F., Vander Woude D.L., Tong H.-Q., Thompson T.G., Watkins S.C.,
RA Kunkel L.M., Beggs A.H.;
RT "Myozenin: an alpha-actinin- and gamma-filamin-binding protein of skeletal
RT muscle Z lines.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1595-1600(2001).
RN [4] {ECO:0000312|EMBL:CAB94568.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG The European IMAGE consortium;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAH25753.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung {ECO:0000312|EMBL:AAH25753.1};
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 [6] {ECO:0000305}
RP INTERACTION WITH LDB3.
RX PubMed=11842093; DOI=10.1074/jbc.m200712200;
RA Frey N., Olson E.N.;
RT "Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin
RT family, interacts with multiple Z-disc proteins.";
RL J. Biol. Chem. 277:13998-14004(2002).
RN [7] {ECO:0000305}
RP INTERACTION WITH FLNA; FLNB; FLNC AND MYOT, AND SUBCELLULAR LOCATION.
RX PubMed=16076904; DOI=10.1242/jcs.02484;
RA Gontier Y., Taivainen A., Fontao L., Sonnenberg A., van der Flier A.,
RA Carpen O., Faulkner G., Borradori L.;
RT "The Z-disc proteins myotilin and FATZ-1 interact with each other and are
RT connected to the sarcolemma via muscle-specific filamins.";
RL J. Cell Sci. 118:3739-3749(2005).
CC -!- FUNCTION: Myozenins may serve as intracellular binding proteins
CC involved in linking Z-disk proteins such as alpha-actinin, gamma-
CC filamin, TCAP/telethonin, LDB3/ZASP and localizing calcineurin
CC signaling to the sarcomere. Plays an important role in the modulation
CC of calcineurin signaling. May play a role in myofibrillogenesis.
CC -!- SUBUNIT: Interacts with ACTN2, ACTN3, FLNA, FLNB, FLNC, LDB3, PPP3CA
CC and TCAP. Interacts via its C-terminal region with MYOT.
CC {ECO:0000269|PubMed:10984498, ECO:0000269|PubMed:11114196,
CC ECO:0000269|PubMed:11171996, ECO:0000269|PubMed:11842093,
CC ECO:0000269|PubMed:16076904}.
CC -!- INTERACTION:
CC Q9NP98; P12814: ACTN1; NbExp=4; IntAct=EBI-744402, EBI-351710;
CC Q9NP98; Q08043: ACTN3; NbExp=3; IntAct=EBI-744402, EBI-2880652;
CC Q9NP98; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-744402, EBI-357530;
CC Q9NP98; O95429: BAG4; NbExp=3; IntAct=EBI-744402, EBI-2949658;
CC Q9NP98; P40199: CEACAM6; NbExp=3; IntAct=EBI-744402, EBI-4314501;
CC Q9NP98; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-744402, EBI-742887;
CC Q9NP98; O43186: CRX; NbExp=3; IntAct=EBI-744402, EBI-748171;
CC Q9NP98; O00303: EIF3F; NbExp=3; IntAct=EBI-744402, EBI-711990;
CC Q9NP98; Q96B26: EXOSC8; NbExp=3; IntAct=EBI-744402, EBI-371922;
CC Q9NP98; P21333-2: FLNA; NbExp=6; IntAct=EBI-744402, EBI-9641086;
CC Q9NP98; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-744402, EBI-11163335;
CC Q9NP98; O76011: KRT34; NbExp=3; IntAct=EBI-744402, EBI-1047093;
CC Q9NP98; O76013-2: KRT36; NbExp=3; IntAct=EBI-744402, EBI-11958506;
CC Q9NP98; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-744402, EBI-10176379;
CC Q9NP98; Q969G2: LHX4; NbExp=3; IntAct=EBI-744402, EBI-2865388;
CC Q9NP98; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-744402, EBI-741037;
CC Q9NP98; Q99471: PFDN5; NbExp=3; IntAct=EBI-744402, EBI-357275;
CC Q9NP98; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-744402, EBI-473160;
CC Q9NP98; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-744402, EBI-949255;
CC Q9NP98; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-744402, EBI-302345;
CC Q9NP98; Q13077: TRAF1; NbExp=3; IntAct=EBI-744402, EBI-359224;
CC Q9NP98; P36406: TRIM23; NbExp=3; IntAct=EBI-744402, EBI-740098;
CC Q9NP98; Q969Q1: TRIM63; NbExp=2; IntAct=EBI-744402, EBI-5661333;
CC Q9NP98; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-744402, EBI-739895;
CC Q9NP98; Q08AM6: VAC14; NbExp=3; IntAct=EBI-744402, EBI-2107455;
CC Q9NP98; P61758: VBP1; NbExp=3; IntAct=EBI-744402, EBI-357430;
CC Q9NP98; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-744402, EBI-712969;
CC Q9NP98; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-744402, EBI-12040603;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cell projection, pseudopodium.
CC Note=Localized to the nucleus and pseudopodia of undifferentiated cells
CC and detected throughout the myotubes of differentiated cells.
CC Colocalizes with ACTN2, FLNC and MYOT at the Z-lines of skeletal
CC muscle.
CC -!- TISSUE SPECIFICITY: Expressed primarily in skeletal muscle. Detected at
CC lower levels in heart, prostate and pancreas.
CC {ECO:0000269|PubMed:10984498, ECO:0000269|PubMed:11114196,
CC ECO:0000269|PubMed:11171996}.
CC -!- SIMILARITY: Belongs to the myozenin family. {ECO:0000305}.
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DR EMBL; AJ278124; CAB92967.1; -; mRNA.
DR EMBL; AY013297; AAG38940.1; -; mRNA.
DR EMBL; AF240633; AAG24509.1; -; mRNA.
DR EMBL; AF243390; AAG27296.1; -; Genomic_DNA.
DR EMBL; AF243387; AAG27296.1; JOINED; Genomic_DNA.
DR EMBL; AF243388; AAG27296.1; JOINED; Genomic_DNA.
DR EMBL; AF243389; AAG27296.1; JOINED; Genomic_DNA.
DR EMBL; AL359210; CAB94568.1; -; mRNA.
DR EMBL; BC025753; AAH25753.1; -; mRNA.
DR CCDS; CCDS7330.1; -.
DR RefSeq; NP_067068.1; NM_021245.3.
DR PDB; 7A8T; X-ray; 2.69 A; B=176-263.
DR PDB; 7A8U; X-ray; 3.80 A; B=92-299.
DR PDB; 7ANK; X-ray; 3.20 A; C=92-299.
DR PDBsum; 7A8T; -.
DR PDBsum; 7A8U; -.
DR PDBsum; 7ANK; -.
DR AlphaFoldDB; Q9NP98; -.
DR SASBDB; Q9NP98; -.
DR SMR; Q9NP98; -.
DR BioGRID; 121849; 42.
DR IntAct; Q9NP98; 36.
DR MINT; Q9NP98; -.
DR STRING; 9606.ENSP00000352272; -.
DR iPTMnet; Q9NP98; -.
DR PhosphoSitePlus; Q9NP98; -.
DR BioMuta; MYOZ1; -.
DR DMDM; 74734300; -.
DR MassIVE; Q9NP98; -.
DR PaxDb; Q9NP98; -.
DR PeptideAtlas; Q9NP98; -.
DR PRIDE; Q9NP98; -.
DR ProteomicsDB; 81941; -.
DR Antibodypedia; 29468; 296 antibodies from 27 providers.
DR DNASU; 58529; -.
DR Ensembl; ENST00000359322.5; ENSP00000352272.4; ENSG00000177791.12.
DR GeneID; 58529; -.
DR KEGG; hsa:58529; -.
DR MANE-Select; ENST00000359322.5; ENSP00000352272.4; NM_021245.4; NP_067068.1.
DR UCSC; uc001jur.5; human.
DR CTD; 58529; -.
DR DisGeNET; 58529; -.
DR GeneCards; MYOZ1; -.
DR HGNC; HGNC:13752; MYOZ1.
DR HPA; ENSG00000177791; Group enriched (skeletal muscle, tongue).
DR MIM; 605603; gene.
DR neXtProt; NX_Q9NP98; -.
DR OpenTargets; ENSG00000177791; -.
DR PharmGKB; PA31420; -.
DR VEuPathDB; HostDB:ENSG00000177791; -.
DR eggNOG; ENOG502R4N9; Eukaryota.
DR GeneTree; ENSGT00950000183027; -.
DR HOGENOM; CLU_071316_0_0_1; -.
DR InParanoid; Q9NP98; -.
DR OMA; DIGCRPS; -.
DR OrthoDB; 988464at2759; -.
DR PhylomeDB; Q9NP98; -.
DR TreeFam; TF331748; -.
DR PathwayCommons; Q9NP98; -.
DR SignaLink; Q9NP98; -.
DR BioGRID-ORCS; 58529; 4 hits in 1067 CRISPR screens.
DR ChiTaRS; MYOZ1; human.
DR GeneWiki; MYOZ1; -.
DR GenomeRNAi; 58529; -.
DR Pharos; Q9NP98; Tbio.
DR PRO; PR:Q9NP98; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NP98; protein.
DR Bgee; ENSG00000177791; Expressed in hindlimb stylopod muscle and 122 other tissues.
DR Genevisible; Q9NP98; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0051373; F:FATZ binding; IDA:UniProtKB.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; ISS:BHF-UCL.
DR GO; GO:0031433; F:telethonin binding; IBA:GO_Central.
DR GO; GO:0030239; P:myofibril assembly; TAS:UniProtKB.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; ISS:BHF-UCL.
DR GO; GO:0043417; P:negative regulation of skeletal muscle tissue regeneration; ISS:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0045214; P:sarcomere organization; ISS:BHF-UCL.
DR GO; GO:0043503; P:skeletal muscle fiber adaptation; ISS:BHF-UCL.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISS:BHF-UCL.
DR GO; GO:0042060; P:wound healing; ISS:BHF-UCL.
DR InterPro; IPR008438; MYOZ.
DR PANTHER; PTHR15941; PTHR15941; 1.
DR Pfam; PF05556; Calsarcin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..299
FT /note="Myozenin-1"
FT /id="PRO_0000111095"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JK37"
FT CONFLICT 153
FT /note="R -> K (in Ref. 2; AAG38940)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="A -> T (in Ref. 2; AAG38940)"
FT /evidence="ECO:0000305"
FT HELIX 187..191
FT /evidence="ECO:0007829|PDB:7A8T"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:7A8T"
SQ SEQUENCE 299 AA; 31745 MW; AADEB488C66B5E27 CRC64;
MPLSGTPAPN KKRKSSKLIM ELTGGGQESS GLNLGKKISV PRDVMLEELS LLTNRGSKMF
KLRQMRVEKF IYENHPDVFS DSSMDHFQKF LPTVGGQLGT AGQGFSYSKS NGRGGSQAGG
SGSAGQYGSD QQHHLGSGSG AGGTGGPAGQ AGRGGAAGTA GVGETGSGDQ AGGEGKHITV
FKTYISPWER AMGVDPQQKM ELGIDLLAYG AKAELPKYKS FNRTAMPYGG YEKASKRMTF
QMPKFDLGPL LSEPLVLYNQ NLSNRPSFNR TPIPWLSSGE PVDYNVDIGI PLDGETEEL
