VEZA_XENLA
ID VEZA_XENLA Reviewed; 774 AA.
AC Q6PCG6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Vezatin;
GN Name=vezt;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) 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; BC059333; AAH59333.1; -; mRNA.
DR RefSeq; NP_001083222.1; NM_001089753.1.
DR AlphaFoldDB; Q6PCG6; -.
DR DNASU; 398809; -.
DR GeneID; 398809; -.
DR KEGG; xla:398809; -.
DR CTD; 398809; -.
DR Xenbase; XB-GENE-1015459; vezt.L.
DR OrthoDB; 1379096at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 398809; Expressed in egg cell and 19 other tissues.
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; IEA:UniProtKB-SubCell.
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; 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; Coiled coil; Membrane; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..774
FT /note="Vezatin"
FT /id="PRO_0000349251"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 746..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 430..457
FT /evidence="ECO:0000255"
FT COMPBIAS 759..774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 774 AA; 88334 MW; 83148767328C95AA CRC64;
MTAEFDEEVV FENSPLFQYL QDLGHTDFEI CPLSKEEERL AENGQGKQDV HTTEKKSIIS
RTVEFLKSWS PFLSKKKKDE KIHLLEIGFR LESLRTILQQ EVLIQEDVEL IELLDPGILS
AGQTQNQQND HLPTLWSIAT PNIWETSILF VFLSAVAAFQ SWSISSSLIW GPSLILFAAF
TVLKTLHTWR SARLRIILRK YCTQVEGTVS NSRAFTNLVR KALRLIQETE VISRGFTLVS
AACPYGKAGQ HASQHLLGLR KAVYRTVRTN FRISRLATLY MLKHYPLNSE IDNVTNYICV
VPLKDLGLGL CEEHVSEEDA HNLTDAFSLP ALKVLFQLWI GQSSEFFRRL ALLLSPENAS
QGPSTSPEQL PHFIWSDVVQ DLPHTQAACM AELKRSYEFY RYFETQHQSG LERTAKRKEV
GELNNLHGAV RSLQLHLKAL LNEVIVLEDE LDKLSSCKEM QAVTPEASLM LEEKLRIIQP
HVQASNTCWE EALCQVERMV RKPTTKKDTG KYSCENLNYP VVSNVPPAMR IEDRDPVPEE
QILEAYVEEA VTDQEFNSEE IYLFSPEERE RQKREREESR RVLQELKAVL GLKASEAERQ
KWKQLLFSEH AVITPLLPEE PVGHFEPLLS IYPEEPHKNL GFYGEIPSEI NGTEHVKDAP
IQVDHGNMNH EDEAKICPVS EEVEPASCKE EEDETPCPAP RTVLPPAIKE RLARIHQSSD
LNFTSGLATQ VAARSLTFTF LQEQTFGDEW DDDDDNEDHD HDKERNNDSS QLEG