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Database: UniProt
Entry: A0A6I8RV10_XENTR
LinkDB: A0A6I8RV10_XENTR
Original site: A0A6I8RV10_XENTR 
ID   A0A6I8RV10_XENTR        Unreviewed;       229 AA.
AC   A0A6I8RV10;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
GN   Name=cldn10 {ECO:0000313|Ensembl:ENSXETP00000085070,
GN   ECO:0000313|RefSeq:XP_004912411.2,
GN   ECO:0000313|Xenbase:XB-GENE-940691};
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 {ECO:0000313|Ensembl:ENSXETP00000085070};
RN   [1] {ECO:0000313|Ensembl:ENSXETP00000085070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000085070};
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2] {ECO:0000313|Ensembl:ENSXETP00000085070}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAY-2020) to UniProtKB.
RN   [3] {ECO:0000313|RefSeq:XP_004912411.2}
RP   IDENTIFICATION.
RC   STRAIN=Nigerian {ECO:0000313|RefSeq:XP_004912411.2};
RC   TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_004912411.2};
RG   RefSeq;
RL   Submitted (NOV-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_004912411.2; XM_004912354.4.
DR   Ensembl; ENSXETT00000076942; ENSXETP00000085070; ENSXETG00000035018.
DR   GeneID; 101733407; -.
DR   KEGG; xtr:101733407; -.
DR   CTD; 9071; -.
DR   Xenbase; XB-GENE-940691; cldn10.
DR   OMA; CKEFISM; -.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Bgee; ENSXETG00000035018; Expressed in mesonephros and 4 other cell types or tissues.
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   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:SF13; CLAUDIN-10; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01077; CLAUDIN.
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|RuleBase:RU060637};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU060637};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008143};
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..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        37..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        79..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        158..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   REGION          206..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   229 AA;  24682 MW;  0CF9B6A583ED2018 CRC64;
     MFGMQILAMV LCVSGIGAIV VAITSNEWKV TTRASSVITA TWVFQGLWMN CAGNALGSYH
     CRPHLTIFRV EGFLQACRAL MISAVVIGFF GTVLGFLGMK CTKIGGSDQM KSKMACAAGI
     LFILSGLCTL SGCSLYAHKT TTEFFDPSFV SQKYELGTAL FVGWSGAAVC LLGGCIFCCS
     FAAECNRSRP GYSHAKARSL MSLRSREPKA ERDPMAQGFS KDFKTNSYV
//
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