MYZAP_MOUSE
ID MYZAP_MOUSE Reviewed; 466 AA.
AC Q3UIJ9; B2RT00;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Myocardial zonula adherens protein;
DE Flags: Precursor;
GN Name=Myzap; Synonyms=Myozap;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [4]
RP INTERACTION WITH GRIN1.
RX PubMed=18849881; DOI=10.1097/wnr.0b013e328317f05f;
RA Roginski R.S., Goubaeva F., Mikami M., Fried-Cassorla E., Nair M.R.,
RA Yang J.;
RT "GRINL1A colocalizes with N-methyl D-aspartate receptor NR1 subunit and
RT reduces N-methyl D-aspartate toxicity.";
RL NeuroReport 19:1721-1726(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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).
RN [6]
RP FUNCTION, INTERACTION WITH DSP; MPRIP AND TJP1, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20093627; DOI=10.1161/circresaha.109.213256;
RA Seeger T.S., Frank D., Rohr C., Will R., Just S., Grund C., Lyon R.,
RA Luedde M., Koegl M., Sheikh F., Rottbauer W., Franke W.W., Katus H.A.,
RA Olson E.N., Frey N.;
RT "Myozap, a novel intercalated disc protein, activates serum response
RT factor-dependent signaling and is required to maintain cardiac function in
RT vivo.";
RL Circ. Res. 106:880-890(2010).
CC -!- FUNCTION: Plays a role in cellular signaling via Rho-related GTP-
CC binding proteins and activation of transcription factor SRF. Targets
CC TJP1 to cell junctions (By similarity). In cortical neurons, may play a
CC role in glutaminergic signal transduction through interaction with the
CC NMDA receptor subunit GRIN1 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:20093627}.
CC -!- SUBUNIT: Interacts with DSP, MPRIP and TJP1/ZO1. Interaction with MPRIP
CC inhibits the activation of transcription factor SRF. Interacts with
CC GRIN1. Interacts with DYNLL1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:20093627}. Cell membrane
CC {ECO:0000269|PubMed:20093627}; Peripheral membrane protein
CC {ECO:0000269|PubMed:20093627}; Cytoplasmic side
CC {ECO:0000269|PubMed:20093627}. Cytoplasm, myofibril, sarcomere, I band
CC {ECO:0000269|PubMed:20093627}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:20093627}. Cell junction
CC {ECO:0000250|UniProtKB:P0CAP1}. Note=Detected predominantly at the
CC intercalated disk in cardiomyocytes, and at low levels on sarcomeric Z
CC disks. Colocalizes with F-actin. Colocalizes with cortical actin.
CC -!- TISSUE SPECIFICITY: Detected in heart myocardium and lung.
CC {ECO:0000269|PubMed:20093627}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryonic vasculature at 8 dpc.
CC Detected in endocardium and the primitive ventricle at 9 dpc. First
CC detected in myocardium at 11.5 dpc. Highly expressed in heart and lung
CC at 15.5 dpc and in neonates, wherease expression in vasculature is no
CC longer detectable. {ECO:0000269|PubMed:20093627}.
CC -!- SIMILARITY: Belongs to the MYZAP family. {ECO:0000305}.
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DR EMBL; AK146889; BAE27507.1; -; mRNA.
DR EMBL; CH466522; EDL26227.1; -; Genomic_DNA.
DR EMBL; BC139077; AAI39078.1; -; mRNA.
DR EMBL; BC139078; AAI39079.1; -; mRNA.
DR CCDS; CCDS23327.1; -.
DR RefSeq; NP_001028380.1; NM_001033208.4.
DR AlphaFoldDB; Q3UIJ9; -.
DR SMR; Q3UIJ9; -.
DR STRING; 10090.ENSMUSP00000091342; -.
DR iPTMnet; Q3UIJ9; -.
DR PhosphoSitePlus; Q3UIJ9; -.
DR MaxQB; Q3UIJ9; -.
DR PaxDb; Q3UIJ9; -.
DR PRIDE; Q3UIJ9; -.
DR ProteomicsDB; 287551; -.
DR Ensembl; ENSMUST00000093823; ENSMUSP00000091342; ENSMUSG00000041361.
DR GeneID; 102371; -.
DR KEGG; mmu:102371; -.
DR UCSC; uc009qpa.1; mouse.
DR CTD; 100820829; -.
DR MGI; MGI:2142908; Myzap.
DR VEuPathDB; HostDB:ENSMUSG00000041361; -.
DR eggNOG; ENOG502QSEE; Eukaryota.
DR GeneTree; ENSGT00950000183065; -.
DR HOGENOM; CLU_022112_0_0_1; -.
DR InParanoid; Q3UIJ9; -.
DR OMA; RKEQHPD; -.
DR OrthoDB; 639997at2759; -.
DR PhylomeDB; Q3UIJ9; -.
DR TreeFam; TF331627; -.
DR BioGRID-ORCS; 102371; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Myzap; mouse.
DR PRO; PR:Q3UIJ9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3UIJ9; protein.
DR Bgee; ENSMUSG00000041361; Expressed in myocardium of ventricle and 194 other tissues.
DR ExpressionAtlas; Q3UIJ9; baseline and differential.
DR Genevisible; Q3UIJ9; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0031674; C:I band; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005665; C:RNA polymerase II, core complex; ISO:MGI.
DR GO; GO:0016591; C:RNA polymerase II, holoenzyme; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR InterPro; IPR028273; Myozap.
DR PANTHER; PTHR23171:SF2; PTHR23171:SF2; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..466
FT /note="Myocardial zonula adherens protein"
FT /id="PRO_0000326226"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 95..137
FT /evidence="ECO:0000255"
FT COILED 187..415
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 466 AA; 53897 MW; FF6F99C1E486B717 CRC64;
MLRSTSTVTL FSGGGAKSPG TPSRRANVCR LRLTVPPENP VPQQTEKKIE RKDQPPELSN
GESTKRLPQG VVYGVVRRSD PNQQKEMVVY GWSTNQLKEE MNYIKDVRAT LEKVRKRMYG
DYDEMRQKIR QLTQDLSVSH AQQDYLDSHI QAQASALDSF NAMNAALASD SVGLQKTLVD
VTLENSHIKD QIRHLQQTYE ASMDKLREKQ RQLEAAQMEN QLLKMRVESS QEANAEVMRE
MTRKLYSQYE EKLQEAQRKH SAEKEVLLEE TNSFLKAIEE ANKKMEAAEL SLEEKDQKIG
ELDRLIERME KERHQLQLQL LEHETEMSGE MADSDKNRYQ QLEEASASLR ERIRHLDDMV
HCQQKKVKQM VEEIESLKKK VQQKQLLILQ LLEKISFLEG ENNELQSRLD YLTETQPKTE
VETREIGVGC DLLPSPTGRT REITMPSRSY TPYTRVLELS SKKTLT
