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   12-AUG-2020, entry version 141.
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=3; 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; 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   SMR; Q9NP98; -.
DR   BioGRID; 121849; 15.
DR   IntAct; Q9NP98; 35.
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; 268 antibodies.
DR   DNASU; 58529; -.
DR   Ensembl; ENST00000359322; ENSP00000352272; ENSG00000177791.
DR   GeneID; 58529; -.
DR   KEGG; hsa:58529; -.
DR   UCSC; uc001jur.5; human.
DR   CTD; 58529; -.
DR   DisGeNET; 58529; -.
DR   EuPathDB; HostDB:ENSG00000177791.11; -.
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   eggNOG; ENOG502R4N9; Eukaryota.
DR   GeneTree; ENSGT00950000183027; -.
DR   HOGENOM; CLU_071316_0_0_1; -.
DR   InParanoid; Q9NP98; -.
DR   OMA; AMPYGGF; -.
DR   OrthoDB; 988464at2759; -.
DR   PhylomeDB; Q9NP98; -.
DR   TreeFam; TF331748; -.
DR   PathwayCommons; Q9NP98; -.
DR   BioGRID-ORCS; 58529; 1 hit in 870 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 quadriceps femoris and 148 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   InterPro; IPR008438; MYOZ.
DR   PANTHER; PTHR15941; PTHR15941; 1.
DR   Pfam; PF05556; Calsarcin; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..299
FT                   /note="Myozenin-1"
FT                   /id="PRO_0000111095"
FT   COMPBIAS        95..175
FT                   /note="Gly-rich"
FT                   /evidence="ECO:0000255"
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"
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
//