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Database: UniProt
Entry: A0A1U7TQK8_CARSF
LinkDB: A0A1U7TQK8_CARSF
Original site: A0A1U7TQK8_CARSF 
ID   A0A1U7TQK8_CARSF        Unreviewed;       224 AA.
AC   A0A1U7TQK8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
GN   Name=CLDN17 {ECO:0000313|RefSeq:XP_008060060.1};
OS   Carlito syrichta (Philippine tarsier) (Tarsius syrichta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Tarsiiformes; Tarsiidae;
OC   Carlito.
OX   NCBI_TaxID=1868482 {ECO:0000313|Proteomes:UP000189704, ECO:0000313|RefSeq:XP_008060060.1};
RN   [1] {ECO:0000313|RefSeq:XP_008060060.1}
RP   IDENTIFICATION.
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_008060060.1; XM_008061869.1.
DR   AlphaFoldDB; A0A1U7TQK8; -.
DR   GeneID; 103264225; -.
DR   KEGG; csyr:103264225; -.
DR   CTD; 26285; -.
DR   OrthoDB; 4040914at2759; -.
DR   Proteomes; UP000189704; Unplaced.
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:SF75; CLAUDIN-17; 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|RuleBase:RU060637};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU060637};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189704};
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        79..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        123..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        165..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
SQ   SEQUENCE   224 AA;  24690 MW;  7CBDB84FBF5F23C7 CRC64;
     MAFYPLQIAG LVLGFLGMAG TLATTLLPQW RVSAFVGSNI IVFERLWEGL WMNCIRQAKV
     RLQCKFYNSL LALPPALEAA RALMCVAVSL SLIALLIGIC GMKQLKCTGS NERTKAYLLG
     TSGVLFILTG IFVLIPVCWT ANIIIRDFYN PAIHIGQKRE LGAALFLGWA STAVLFIGGG
     LLLGFCCCNR KKQRHRYPVP RYCVPHTDKR RNVTVASKSS TSYV
//
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