VEZA_MOUSE
ID VEZA_MOUSE Reviewed; 780 AA.
AC Q3ZK22; A0M8X3; Q3ZK21; Q8BY12; Q8BYB4; Q8BZB5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Vezatin {ECO:0000305};
GN Name=Vezt {ECO:0000312|MGI:MGI:2143698};
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 [MRNA] (ISOFORMS 1 AND 3), DEVELOPMENTAL STAGE,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RC STRAIN=129S2/SvPas;
RX PubMed=16199027; DOI=10.1016/j.ydbio.2005.09.004;
RA Hyenne V., Louvet-Vallee S., El-Amraoui A., Petit C., Maro B.,
RA Simmler M.-C.;
RT "Vezatin, an ubiquitous adherens junction protein, is required for mouse
RT blastocyst morphogenesis.";
RL Dev. Biol. 287:180-191(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), DISRUPTION PHENOTYPE, AND FUNCTION.
RC STRAIN=129S2/SvPas;
RX PubMed=17452094; DOI=10.1016/j.mod.2007.03.004;
RA Hyenne V., Souilhol C., Cohen-Tannoudji M., Cereghini S., Petit C.,
RA Langa F., Maro B., Simmler M.-C.;
RT "Conditional knock-out reveals that zygotic vezatin-null mouse embryos die
RT at implantation.";
RL Mech. Dev. 124:449-462(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Thymus;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH USH2A.
RX PubMed=17567809; DOI=10.1523/jneurosci.0342-07.2007;
RA Michalski N., Michel V., Bahloul A., Lefevre G., Barral J., Yagi H.,
RA Chardenoux S., Weil D., Martin P., Hardelin J.P., Sato M., Petit C.;
RT "Molecular characterization of the ankle-link complex in cochlear hair
RT cells and its role in the hair bundle functioning.";
RL J. Neurosci. 27:6478-6488(2007).
RN [6]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17379651; DOI=10.1530/rep-06-0271;
RA Hyenne V., Harf J.C., Latz M., Maro B., Wolfrum U., Simmler M.-C.;
RT "Vezatin, a ubiquitous protein of adherens cell-cell junctions, is
RT exclusively expressed in germ cells in mouse testis.";
RL Reproduction 133:563-574(2007).
CC -!- FUNCTION: Plays a pivotal role in the establishment of adherens
CC junctions and their maintenance in adult life. Required for
CC morphogenesis of the preimplantation embryo, and for the implantation
CC process. {ECO:0000269|PubMed:16199027, ECO:0000269|PubMed:17452094}.
CC -!- SUBUNIT: Interacts with USH2A (via the cytoplasmic region); the
CC interaction associates VEZT with the USH2 complex at the stereocilia
CC base (PubMed:17567809). Interacts with myosin MYO7A and the cadherin-
CC catenins complex (By similarity). {ECO:0000250|UniProtKB:Q9HBM0,
CC ECO:0000269|PubMed:17567809}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16199027};
CC Multi-pass membrane protein {ECO:0000305}. Cell projection,
CC stereocilium membrane {ECO:0000269|PubMed:17567809}. Cell junction,
CC adherens junction {ECO:0000269|PubMed:16199027}. Nucleus
CC {ECO:0000269|PubMed:16199027}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000269|PubMed:17379651}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=2.4;
CC IsoId=Q3ZK22-1; Sequence=Displayed;
CC Name=2; Synonyms=0.8;
CC IsoId=Q3ZK22-2; Sequence=VSP_035268, VSP_035269, VSP_035270;
CC Name=3; Synonyms=1.9;
CC IsoId=Q3ZK22-3; Sequence=VSP_035272, VSP_035273;
CC Name=4;
CC IsoId=Q3ZK22-4; Sequence=VSP_035271, VSP_035274;
CC -!- TISSUE SPECIFICITY: Expressed in developing cochlear hair cells
CC (PubMed:17567809). Isoform 1, isoform 2 and isoform 3 are expressed in
CC testis. In the seminiferous epithelium, present exclusively in the
CC acrosome of spermatids (at protein level).
CC {ECO:0000269|PubMed:17379651, ECO:0000269|PubMed:17567809}.
CC -!- DEVELOPMENTAL STAGE: Present in oocytes and at every embryonic stage
CC (at protein level). {ECO:0000269|PubMed:16199027}.
CC -!- DISRUPTION PHENOTYPE: Embryos die at the time of implantation because
CC of a defect in intercellular adhesion. {ECO:0000269|PubMed:17452094}.
CC -!- SIMILARITY: Belongs to the vezatin family. {ECO:0000305}.
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DR EMBL; AY753561; AAX12551.1; -; mRNA.
DR EMBL; AY753562; AAX12552.1; -; mRNA.
DR EMBL; DQ025533; AAY87458.1; -; mRNA.
DR EMBL; AK036017; BAC29277.1; -; mRNA.
DR EMBL; AK041354; BAC30915.1; -; mRNA.
DR EMBL; AK042540; BAC31287.1; -; mRNA.
DR EMBL; BC056428; AAH56428.1; -; mRNA.
DR CCDS; CCDS36038.1; -. [Q3ZK22-1]
DR CCDS; CCDS78886.1; -. [Q3ZK22-3]
DR CCDS; CCDS83750.1; -. [Q3ZK22-4]
DR RefSeq; NP_001291501.1; NM_001304572.1. [Q3ZK22-3]
DR RefSeq; NP_001291504.1; NM_001304575.1.
DR RefSeq; NP_001291649.1; NM_001304720.1. [Q3ZK22-4]
DR RefSeq; NP_766126.2; NM_172538.5. [Q3ZK22-1]
DR AlphaFoldDB; Q3ZK22; -.
DR SMR; Q3ZK22; -.
DR BioGRID; 229587; 1.
DR STRING; 10090.ENSMUSP00000037955; -.
DR iPTMnet; Q3ZK22; -.
DR PhosphoSitePlus; Q3ZK22; -.
DR SwissPalm; Q3ZK22; -.
DR EPD; Q3ZK22; -.
DR MaxQB; Q3ZK22; -.
DR PaxDb; Q3ZK22; -.
DR PeptideAtlas; Q3ZK22; -.
DR PRIDE; Q3ZK22; -.
DR ProteomicsDB; 297976; -. [Q3ZK22-1]
DR ProteomicsDB; 297977; -. [Q3ZK22-2]
DR ProteomicsDB; 297978; -. [Q3ZK22-3]
DR ProteomicsDB; 297979; -. [Q3ZK22-4]
DR Antibodypedia; 1345; 64 antibodies from 23 providers.
DR DNASU; 215008; -.
DR Ensembl; ENSMUST00000047711; ENSMUSP00000037955; ENSMUSG00000036099. [Q3ZK22-1]
DR Ensembl; ENSMUST00000118077; ENSMUSP00000113983; ENSMUSG00000036099. [Q3ZK22-3]
DR Ensembl; ENSMUST00000118205; ENSMUSP00000113321; ENSMUSG00000036099. [Q3ZK22-4]
DR Ensembl; ENSMUST00000150704; ENSMUSP00000121727; ENSMUSG00000036099. [Q3ZK22-2]
DR GeneID; 215008; -.
DR KEGG; mmu:215008; -.
DR UCSC; uc007gvh.2; mouse. [Q3ZK22-1]
DR UCSC; uc007gvi.2; mouse. [Q3ZK22-3]
DR UCSC; uc007gvj.2; mouse. [Q3ZK22-2]
DR UCSC; uc056yhx.1; mouse. [Q3ZK22-4]
DR CTD; 55591; -.
DR MGI; MGI:2143698; Vezt.
DR VEuPathDB; HostDB:ENSMUSG00000036099; -.
DR eggNOG; ENOG502QTQW; Eukaryota.
DR GeneTree; ENSGT00390000003290; -.
DR HOGENOM; CLU_019876_2_0_1; -.
DR InParanoid; Q3ZK22; -.
DR OMA; IVCENPR; -.
DR OrthoDB; 1379096at2759; -.
DR PhylomeDB; Q3ZK22; -.
DR TreeFam; TF332269; -.
DR BioGRID-ORCS; 215008; 14 hits in 61 CRISPR screens.
DR ChiTaRS; Vezt; mouse.
DR PRO; PR:Q3ZK22; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q3ZK22; protein.
DR Bgee; ENSMUSG00000036099; Expressed in superior cervical ganglion and 236 other tissues.
DR ExpressionAtlas; Q3ZK22; baseline and differential.
DR Genevisible; Q3ZK22; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0002142; C:stereocilia ankle link complex; IDA:MGI.
DR GO; GO:0060171; C:stereocilium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017022; F:myosin binding; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0043009; P:chordate embryonic development; IMP:MGI.
DR InterPro; IPR026859; Myosin-bd.
DR InterPro; IPR026858; Vezatin.
DR PANTHER; PTHR15989; PTHR15989; 1.
DR Pfam; PF12632; Vezatin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW Coiled coil; Cytoplasmic vesicle; Developmental protein; Membrane; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..780
FT /note="Vezatin"
FT /id="PRO_0000349248"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 620..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 430..467
FT /evidence="ECO:0000255"
FT COMPBIAS 620..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..780
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 239..307
FT /note="SAACSFNKAAQHPGQHLIGLRKAVYRTVRANFQAARLATLYMLKNYPLNSES
FT DNVTNYICVVPFKELGL -> LLR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17452094"
FT /id="VSP_035268"
FT VAR_SEQ 311..342
FT /note="EDQISEEEARNLTDGFSLPALKVLFQLWVAQS -> DEWLCAQPVLRQVYQM
FT LGLVSFLTFTHIMDLT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17452094"
FT /id="VSP_035269"
FT VAR_SEQ 343..780
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17452094"
FT /id="VSP_035270"
FT VAR_SEQ 611..639
FT /note="AVLTSLSPVDPVESVSNSEPPMNSDTEKV -> EWTFNWIHHAGHGGTVIPA
FT RWLRQGGSGV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035271"
FT VAR_SEQ 611..617
FT /note="AVLTSLS -> GVKAEWN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16199027"
FT /id="VSP_035272"
FT VAR_SEQ 618..780
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16199027"
FT /id="VSP_035273"
FT VAR_SEQ 640..780
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035274"
FT CONFLICT 57
FT /note="R -> K (in Ref. 1; AAX12552/AAX12551 and 2;
FT AAY87458)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="S -> P (in Ref. 1; AAX12552/AAX12551 and 2;
FT AAY87458)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="F -> L (in Ref. 1; AAX12552/AAX12551 and 2;
FT AAY87458)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="S -> T (in Ref. 1; AAX12552)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="D -> E (in Ref. 1; AAX12552/AAX12551)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 780 AA; 87987 MW; AB8D244A6EDBDCEE CRC64;
MTPEFDEEVV FENSPLYQYL QDLGHTDFEI CSSSSPKPEK CLTTEGPQPP PTRVLQRQGI
LLKLTETIKS WTFSSQHSKK DDLLHKLDTG FRLDSLHTIL QQEVLLQEDV ELLELLDASI
LSAGQPQQES GHLPTLCSLA TPNTWDVSLL FAFISLLIMF PTCWIVSSWL VWGIILFLYL
IIRVLKLWRT AKLQMTLKKY RVRLEDMAAN SRAFTNLVRK SLRLIQETEV ISRGFTLVSA
ACSFNKAAQH PGQHLIGLRK AVYRTVRANF QAARLATLYM LKNYPLNSES DNVTNYICVV
PFKELGLGLS EDQISEEEAR NLTDGFSLPA LKVLFQLWVA QSSEFFRRLA LLLSTANSPS
GPLLTAALLP HHILCDVTQG LPHAHSACLD ELKRSYEFFR YFETQHQSVP QRLSKTPQKS
RELSNVHTAV RSLQLHLKAL LNEVIILEDE LEKLVCTKET QELLSEAYPI LEQKLKLIEP
HVQASNSCWE EAISQVDKLL RRNTDKKGKP GVACENPHCT AEPLVRPALH IEDRDPIPEE
QELEAYVDDI DIESEFRKDD FYHLSQEDRE RQKREQEESR RVLQELKSVL GFKASEAERQ
KWKQLLFSDH AVLTSLSPVD PVESVSNSEP PMNSDTEKVN SNATEEETSK PCAGDKEDSR
TEYVCDSPTE GPSKDTSADT GLLLPGAEET MCHQHESEAK SPQAAAAGAT APPTPRDTLQ
LSIKQRLARL QLPPEFTFSA GLAAEVAARS LSFTTMQEQT FGDEEEEQLV EGGENEVEEK
