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Database: UniProt
Entry: A0A672UH67_STRHB
LinkDB: A0A672UH67_STRHB
Original site: A0A672UH67_STRHB 
ID   A0A672UH67_STRHB        Unreviewed;       214 AA.
AC   A0A672UH67;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
GN   Name=CLDN3 {ECO:0000313|Ensembl:ENSSHBP00005014530.1};
OS   Strigops habroptila (Kakapo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Strigops.
OX   NCBI_TaxID=2489341 {ECO:0000313|Ensembl:ENSSHBP00005014530.1, ECO:0000313|Proteomes:UP000472266};
RN   [1] {ECO:0000313|Ensembl:ENSSHBP00005014530.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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|ARBA:ARBA00002246,
CC       ECO:0000256|RuleBase:RU060637}.
CC   -!- SUBUNIT: Can form homo- and heteropolymers with other CLDN.
CC       Homopolymers interact with CLDN1 and CLDN2 homopolymers. Directly
CC       interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3.
CC       {ECO:0000256|ARBA:ARBA00025914}.
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}.
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DR   AlphaFoldDB; A0A672UH67; -.
DR   Ensembl; ENSSHBT00005017453.1; ENSSHBP00005014530.1; ENSSHBG00005012737.1.
DR   GeneTree; ENSGT00940000162095; -.
DR   InParanoid; A0A672UH67; -.
DR   OMA; LCSIICC; -.
DR   OrthoDB; 4040914at2759; -.
DR   Proteomes; UP000472266; 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; IPR003549; Claudin3.
DR   InterPro; IPR017974; Claudin_CS.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; CLAUDIN; 1.
DR   PANTHER; PTHR12002:SF112; CLAUDIN-3; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01077; CLAUDIN.
DR   PRINTS; PR01378; CLAUDIN3.
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:UP000472266};
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        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        78..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        116..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        159..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
SQ   SEQUENCE   214 AA;  22905 MW;  DDA6CF3937239954 CRC64;
     MSMGLEIGGV ALSVLGWLCS IICCALPMWR VTAFIGNNIV TAQIIWEGLW MNCVVQSTGQ
     MQCKVYDSML ALPQDLQAAR ALLVVAIVLA ALGLMVAIVG AQCTRCIEDE STKAKITIAS
     GVIFILSGIL TLIPASWSAN TIIRDFYNPL VLDAQKRELG ASLYVGWAAS ALLLLGGSLL
     CCSCPPKEDS YTTSKVAYSA PRSAVTSYDK RNYV
//
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