VEZA_RAT
ID VEZA_RAT Reviewed; 782 AA.
AC Q5XI52;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Vezatin;
GN Name=Vezt;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
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).
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:0000250|UniProtKB:Q3ZK22}.
CC -!- SUBUNIT: Interacts with USH2A (via the cytoplasmic region); the
CC interaction associates VEZT with the USH2 complex at the stereocilia
CC base (By similarity). Interacts with myosin MYO7A and the cadherin-
CC catenins complex (By similarity). {ECO:0000250|UniProtKB:Q3ZK22,
CC ECO:0000250|UniProtKB:Q9HBM0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q3ZK22};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q3ZK22}. Cell
CC projection, stereocilium membrane {ECO:0000250|UniProtKB:Q3ZK22}. Cell
CC junction, adherens junction {ECO:0000250|UniProtKB:Q3ZK22}. Nucleus
CC {ECO:0000250|UniProtKB:Q3ZK22}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000250|UniProtKB:Q3ZK22}.
CC -!- SIMILARITY: Belongs to the vezatin family. {ECO:0000305}.
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DR EMBL; BC083840; AAH83840.1; -; mRNA.
DR RefSeq; NP_001006985.1; NM_001006984.1.
DR AlphaFoldDB; Q5XI52; -.
DR SMR; Q5XI52; -.
DR STRING; 10116.ENSRNOP00000038458; -.
DR PhosphoSitePlus; Q5XI52; -.
DR SwissPalm; Q5XI52; -.
DR PaxDb; Q5XI52; -.
DR PRIDE; Q5XI52; -.
DR GeneID; 299738; -.
DR KEGG; rno:299738; -.
DR UCSC; RGD:1359117; rat.
DR CTD; 55591; -.
DR RGD; 1359117; Vezt.
DR VEuPathDB; HostDB:ENSRNOG00000006514; -.
DR eggNOG; ENOG502QTQW; Eukaryota.
DR HOGENOM; CLU_019876_1_0_1; -.
DR InParanoid; Q5XI52; -.
DR OMA; IVCENPR; -.
DR OrthoDB; 1379096at2759; -.
DR PhylomeDB; Q5XI52; -.
DR TreeFam; TF332269; -.
DR PRO; PR:Q5XI52; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000006514; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q5XI52; RN.
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; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0002142; C:stereocilia ankle link complex; ISS:UniProtKB.
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; ISO:RGD.
DR GO; GO:0043009; P:chordate embryonic development; ISO:RGD.
DR InterPro; IPR026859; Myosin-bd.
DR InterPro; IPR026858; Vezatin.
DR PANTHER; PTHR15989; PTHR15989; 1.
DR Pfam; PF12632; Vezatin; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Cell projection; Coiled coil;
KW Cytoplasmic vesicle; Membrane; Nucleus; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..782
FT /note="Vezatin"
FT /id="PRO_0000349250"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 565..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 434..471
FT /evidence="ECO:0000255"
FT COMPBIAS 624..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 88694 MW; 12633F8A239C46C7 CRC64;
MTPEFDEEVV FENSPLYQYL QDLGHTDFEI CSSLSPKTET CLTTEEPQTP PTRVLQKQGI
LLKLTETIKS WTLSSQYSKK DDLLHKLDTG FRLDALDAIL QQEVLLQEDV ELIELLDPSI
LSAGHPQQEN GHLPTLCSLA TPNIWDVSML FAFISLLIML PTWWIVSSWL VWGIILFLYL
IIRVLKFWRT AKLQMTLKKY RVRLEDMAAN SRAFTNLVRK SLRLIQETEV ISRGFTLLLD
RVSAACSFNK AAQHPSQHLI GLRKAVYRTV RANFQAARLA TLYMLKNYPL NSESDNVTNY
ICVVPFKELG LGLSEDQISE EEARNLTDGF SLPALKVLFQ LWVAQSSEFF RRLALLLSTA
NSPSGPLLTA ALLPHRILSD VTQGLPHAHT ACLDELKRSY EFFRYFETQH QSVPQRLPKT
QPKWRELNNV HTAVRSLQLH LKALLNEVII LEDELEKLVC TKETQELLSE AYPVLEQRLK
LIEPHVQASN SCWEEAISQV DRLLRRNTDQ KGKPGVACEN PHCTAAPLLR PTLHIEDRDP
IPEEQELEAY VDGIDIESEF RKDSLYHVSQ EDRERQKREQ EESKRVLQEL KSVLGFKASE
AERQKWKQLL FSDHAVLKSL SPVEPVESVS NSETPMNSDT EQAHSEATEE ETSKPCASDK
EDTRTEYMCD GPPKGQSKDT SGDQGHLLQG AHQCESEAKP PQAAAAGATA PPTPRDSPRL
SIKQRLARLQ LSPEYTFTAG LAAEVAARSL SFTTMQEQTF GDEEDEDKEQ LVEGGERELE
EK
