VEZA_XENTR
ID VEZA_XENTR Reviewed; 791 AA.
AC Q28C41;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Vezatin;
GN Name=vezt; ORFNames=TEgg004g23.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) 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. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with myosin VIIa and the cadherin-catenins complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell
CC junction, adherens junction. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the vezatin family. {ECO:0000305}.
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DR EMBL; CR942466; CAJ81723.1; -; mRNA.
DR EMBL; BC136189; AAI36190.1; -; mRNA.
DR RefSeq; NP_001039208.1; NM_001045743.1.
DR AlphaFoldDB; Q28C41; -.
DR SMR; Q28C41; -.
DR STRING; 8364.ENSXETP00000051413; -.
DR PaxDb; Q28C41; -.
DR Ensembl; ENSXETT00000051413; ENSXETP00000051413; ENSXETG00000023853.
DR GeneID; 734067; -.
DR KEGG; xtr:734067; -.
DR CTD; 55591; -.
DR Xenbase; XB-GENE-1015453; vezt.
DR eggNOG; ENOG502QTQW; Eukaryota.
DR InParanoid; Q28C41; -.
DR OrthoDB; 1379096at2759; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000023853; Expressed in brain and 13 other tissues.
DR ExpressionAtlas; Q28C41; differential.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0002142; C:stereocilia ankle link complex; ISS:UniProtKB.
DR GO; GO:0017022; F:myosin binding; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
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; Coiled coil; Membrane; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..791
FT /note="Vezatin"
FT /id="PRO_0000349252"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 752..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 435..464
FT /evidence="ECO:0000255"
FT COMPBIAS 752..767
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 90155 MW; 06A139409E6A038E CRC64;
MTAEFDEEVV FENSPLFQYL QDLGQTDFEI CPLSKEEEHL AGNGHGEQDV HTTEKKSNIS
RTVEFLKSWS PLFSKKKRDE KICLLENGFR LESLRTILQQ EVLIQEDVEL IELLDPGILS
AGQTQNQQNG HLPTLWSIAT PNIWEMSVLF AFLSALAALQ SWSISSSLVW GPSLILFAAF
TVLRALHTWR SATLRMILRK YCNQVEGTVL NSRAFTNLVR KALRLIQETE VISRGFTLLL
DRVSAACPYG KAGQHASQHL LGLRKAVYRT VRTNFRISRL ATLYMLKHYP LNSEIDNVTN
YICVVPLKDL GLGLCEEHVS EEEAHNLTDA FSLPALKVLF QLWIGQSSEF FRRLALLLSP
ENAAQGHLAS PEQLPHLIWS DVVQDLPHTQ AACLAELKRS YEFYRYFETQ HQSGFERTAK
RKKEVGELSN LHGAVRSLQL HLKALLNEVI ILEDELEKLS SCKEMQAMTQ EASLMLEEKL
RIIQPHVQAS NTCWEEALCQ VGRMVRRPAA KKDIEKSSCE NLNFPVVSNM PPALRIEDRD
PVPEEQILEA YVEEAVTDQE FNSEDIYLFS PEERERQKRE REESKRVLQE LKAVLGLKAS
EAERQKWKQL LFSEHAVITP FLPEEPVGHF EPPDSVYPED PCKNLGFYGE FTSEINGTEH
AKDTPNQGDL QMNMNHEDEA KICPLSEEAE PESGKDENES PCPVPRTVLP PAIKERLARI
HQTSDLNFTS GLAAQVAARS LTFTFLQEQT FGDEWDDDDD DNDNDDDNYD QVKNVESHEK
ERNNVSLQLE E