MYOZ1_MOUSE
ID MYOZ1_MOUSE Reviewed; 296 AA.
AC Q9JK37; Q8C9L3; Q9D7N4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
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|MGI:MGI:1929471};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAB76836.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Diaphragm {ECO:0000312|EMBL:CAB76836.1};
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:AAG38941.1}
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PPP3CA, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
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:0000312|EMBL:BAB26059.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB26059.1};
RC TISSUE=Thymus {ECO:0000312|EMBL:BAC31092.1}, and
RC Tongue {ECO:0000312|EMBL:BAB26059.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4] {ECO:0000312|EMBL:AAH24660.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH24660.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH24660.1};
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 {ECO:0000303|PubMed:10984498, ECO:0000303|PubMed:11114196,
CC ECO:0000305}.
CC -!- SUBUNIT: Interacts with ACTN2, ACTN3, FLNA, FLNB, FLNC, LDB3, PPP3CA
CC and TCAP. Interacts via its C-terminal region with MYOT.
CC {ECO:0000250|UniProtKB:Q9NP98, ECO:0000269|PubMed:11114196}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cell projection,
CC pseudopodium {ECO:0000250}. Note=Localized to the nucleus and
CC pseudopodia of undifferentiated cells and detected throughout the
CC myotubes of differentiated cells. Colocalizes with ACTN2, FLNC and MYOT
CC at the Z-lines of skeletal muscle (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed primarily in skeletal muscle and
CC specifically enriched in the gastrocnemius, which is composed
CC predominantly of fast-twitch muscle fibers. Detected at lower levels in
CC heart. {ECO:0000269|PubMed:10984498, ECO:0000269|PubMed:11114196}.
CC -!- DEVELOPMENTAL STAGE: At 9.5 dpc, expressed at significant levels in
CC cardiac muscle with lower levels detected in skeletal muscle of tongue.
CC At 15.5 dpc, cardiac expression is down-regulated and only weakly
CC detected in atria, whereas skeletal muscle expression is more robust.
CC {ECO:0000269|PubMed:11114196}.
CC -!- SIMILARITY: Belongs to the myozenin family. {ECO:0000305}.
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DR EMBL; AJ005620; CAB76836.1; -; mRNA.
DR EMBL; AY013298; AAG38941.1; -; mRNA.
DR EMBL; AK009077; BAB26059.1; -; mRNA.
DR EMBL; AK041896; BAC31092.1; -; mRNA.
DR EMBL; BC024660; AAH24660.1; -; mRNA.
DR CCDS; CCDS36819.1; -.
DR RefSeq; NP_067483.1; NM_021508.3.
DR AlphaFoldDB; Q9JK37; -.
DR BioGRID; 208482; 1.
DR STRING; 10090.ENSMUSP00000087955; -.
DR iPTMnet; Q9JK37; -.
DR PhosphoSitePlus; Q9JK37; -.
DR MaxQB; Q9JK37; -.
DR PaxDb; Q9JK37; -.
DR PRIDE; Q9JK37; -.
DR ProteomicsDB; 287339; -.
DR Antibodypedia; 29468; 296 antibodies from 27 providers.
DR DNASU; 59011; -.
DR Ensembl; ENSMUST00000090469; ENSMUSP00000087955; ENSMUSG00000068697.
DR GeneID; 59011; -.
DR KEGG; mmu:59011; -.
DR UCSC; uc007skd.1; mouse.
DR CTD; 58529; -.
DR MGI; MGI:1929471; Myoz1.
DR VEuPathDB; HostDB:ENSMUSG00000068697; -.
DR eggNOG; ENOG502R4N9; Eukaryota.
DR GeneTree; ENSGT00950000183027; -.
DR HOGENOM; CLU_071316_0_0_1; -.
DR InParanoid; Q9JK37; -.
DR OMA; DIGCRPS; -.
DR OrthoDB; 988464at2759; -.
DR PhylomeDB; Q9JK37; -.
DR TreeFam; TF331748; -.
DR BioGRID-ORCS; 59011; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Myoz1; mouse.
DR PRO; PR:Q9JK37; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9JK37; protein.
DR Bgee; ENSMUSG00000068697; Expressed in temporalis muscle and 98 other tissues.
DR Genevisible; Q9JK37; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IMP:BHF-UCL.
DR GO; GO:0031433; F:telethonin binding; IBA:GO_Central.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IMP:BHF-UCL.
DR GO; GO:0043417; P:negative regulation of skeletal muscle tissue regeneration; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045214; P:sarcomere organization; IMP:BHF-UCL.
DR GO; GO:0043503; P:skeletal muscle fiber adaptation; IMP:BHF-UCL.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:BHF-UCL.
DR GO; GO:0042060; P:wound healing; IMP: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..296
FT /note="Myozenin-1"
FT /id="PRO_0000111096"
FT REGION 105..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 100
FT /note="T -> A (in Ref. 3; BAB26059)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="Q -> H (in Ref. 3; BAC31092)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 31457 MW; E9D16F4723B1EE83 CRC64;
MPLSGTPAPN KRRKSSKLIM ELTGGGRESS GLNLGKKISV PRDVMLEELS LLTNRGSKMF
KLRQMRVEKF IYENHPDVFS DSSMDHFQKF LPTVGGQLET AGQGFSYGKG SSGGQAGSSG
SAGQYGSDRH QQGSGFGAGG SGGPGGQAGG GGAPGTVGLG EPGSGDQAGG DGKHVTVFKT
YISPWDRAMG VDPQQKVELG IDLLAYGAKA ELPKYKSFNR TAMPYGGYEK ASKRMTFQMP
KFDLGPLLSE PLVLYNQNLS NRPSFNRTPI PWLSSGEHVD YNVDVGIPLD GETEEL
