ID   VEZA_PONAB              Reviewed;         731 AA.
AC   Q5RFL7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Vezatin;
GN   Name=VEZT;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR857138; CAH89440.1; -; mRNA.
DR   RefSeq; NP_001124614.1; NM_001131142.1.
DR   AlphaFoldDB; Q5RFL7; -.
DR   SMR; Q5RFL7; -.
DR   STRING; 9601.ENSPPYP00000005524; -.
DR   GeneID; 100171451; -.
DR   KEGG; pon:100171451; -.
DR   CTD; 55591; -.
DR   eggNOG; ENOG502QTQW; Eukaryota.
DR   InParanoid; Q5RFL7; -.
DR   OrthoDB; 1379096at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
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..731
FT                   /note="Vezatin"
FT                   /id="PRO_0000349249"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          570..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          710..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          382..414
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        573..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..605
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..671
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   731 AA;  83356 MW;  7878E02014F6DDE5 CRC64;
     MLKEWAIKQG ILLKVAETIK SWIFFSQCNK KDDLLHKLDI GFRLDSLHTI LQQEVLLQED
     VELIELLDPS ILSAGQSQQQ ENGHLPTLCS LATPNIWDLS MLFAFISLLV MLPTWWIVSS
     WLVWGVILFV YLVIRALRLW RTAKLQVTLK KYSVHLEDMA TNSRAFTNLV RKALRLIQET
     EVISRGFTLV SAACPFNKAG QHPSQHLIGL RKAVYRTLRA NFQAARLATL YMLKNYPLNS
     ESDNVTNYIC VVPFKELGLG LSEEQISEEE AHNFTDGFSL PALKVLFQLW VAQSSEFFRR
     LALLLSTTNS PPGPLLTPAL LPHRILSDVT QGLPHAHSAC LEELKRSYEF YRYFETQHQS
     VPQCLSKTQQ KSRELNNVHT AVRSLQLHLK ALLNEVIILE DELEKLVCTK ETQELVSEAY
     PILEQKLKLI QPHVQASNNC WEEAISQVDK LLRRNTDKKG KPEIACENPH CTVVPLKQPT
     LHIADKDPIP EEQELEAYVD DIDIDSDFRK DDFYYLSQED KERQKLEHEE SKRVLQELKS
     VLGFKASEAE RQKWKQLLFS DHAVLKSLSP VDPVEPISNS EPSMNSDMGK VSKNDTEEES
     SKSTTTDNEI SRTEYLCENS LEGKNKDNSS NEVFRQGAEE RMCYQCESED EPQADGSGLT
     TAPPTPRDSL QPSIKQRLAR LQLSPDFTFT AGLAAEVAAR SLSFTTMQEQ TFGDEEEEQI
     IEENKNKIEE K