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Database: UniProt
Entry: M4AGZ2_XIPMA
LinkDB: M4AGZ2_XIPMA
Original site: M4AGZ2_XIPMA 
ID   M4AGZ2_XIPMA            Unreviewed;       213 AA.
AC   M4AGZ2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000013736.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000013736.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000013736.1};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Plays a major role in tight junction-specific obliteration of
CC       the intercellular space, through calcium-independent cell-adhesion
CC       activity. {ECO:0000256|RuleBase:RU060637}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC       {ECO:0000256|RuleBase:RU060637}. Cell membrane
CC       {ECO:0000256|RuleBase:RU060637}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU060637}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the claudin family.
CC       {ECO:0000256|ARBA:ARBA00008295, ECO:0000256|RuleBase:RU060637}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU060637}.
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DR   RefSeq; XP_005810455.1; XM_005810398.2.
DR   AlphaFoldDB; M4AGZ2; -.
DR   STRING; 8083.ENSXMAP00000013736; -.
DR   Ensembl; ENSXMAT00000013752.2; ENSXMAP00000013736.1; ENSXMAG00000013711.2.
DR   GeneID; 102218729; -.
DR   KEGG; xma:102218729; -.
DR   CTD; 436612; -.
DR   eggNOG; ENOG502QPXX; Eukaryota.
DR   GeneTree; ENSGT00940000166258; -.
DR   HOGENOM; CLU_076370_1_2_1; -.
DR   InParanoid; M4AGZ2; -.
DR   OMA; EFGMAIF; -.
DR   OrthoDB; 4040914at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0060322; P:head development; IEA:Ensembl.
DR   Gene3D; 1.20.140.150; -; 1.
DR   InterPro; IPR006187; Claudin.
DR   InterPro; IPR017974; Claudin_CS.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; CLAUDIN; 1.
DR   PANTHER; PTHR12002:SF78; CLAUDIN-7; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01077; CLAUDIN.
DR   PRINTS; PR01385; CLAUDIN14.
DR   PROSITE; PS01346; CLAUDIN; 1.
PE   3: Inferred from homology;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949,
KW   ECO:0000256|RuleBase:RU060637};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU060637};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU060637};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW   Tight junction {ECO:0000256|ARBA:ARBA00022427,
KW   ECO:0000256|RuleBase:RU060637};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU060637};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU060637}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        79..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        118..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        161..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   REGION          191..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   213 AA;  22646 MW;  C93AA6B33BCA5E23 CRC64;
     MANSGIQLLG FFLSLVGIVG LIVGTVLPQW KMSAYIGDNI ITAVAMYQGL WMSCAFQSTG
     QLQCKIYDSI LQLDSSLQAT RALMIVGIIV SVAGLGVACM GMKCTTCGGS DKLRKSRIAM
     IGGIILLIGG LCAIVACSWF AHNVIRAFYN PYTPVNTKFE FGVAIFIAWG GALLDVLGGA
     MLAASCPRKK QVSRYPNMPG SRSSPPSSNK EYV
//
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