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Database: UniProt
Entry: A0A2Y9HK19_NEOSC
LinkDB: A0A2Y9HK19_NEOSC
Original site: A0A2Y9HK19_NEOSC 
ID   A0A2Y9HK19_NEOSC        Unreviewed;       217 AA.
AC   A0A2Y9HK19;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
GN   Name=LOC110584232 {ECO:0000313|RefSeq:XP_021549935.1};
OS   Neomonachus schauinslandi (Hawaiian monk seal) (Monachus schauinslandi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC   Neomonachus.
OX   NCBI_TaxID=29088 {ECO:0000313|Proteomes:UP000248481, ECO:0000313|RefSeq:XP_021549935.1};
RN   [1] {ECO:0000313|RefSeq:XP_021549935.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_021549935.1};
RG   RefSeq;
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|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_021549935.1; XM_021694260.1.
DR   AlphaFoldDB; A0A2Y9HK19; -.
DR   STRING; 29088.A0A2Y9HK19; -.
DR   KEGG; nsu:110584232; -.
DR   InParanoid; A0A2Y9HK19; -.
DR   OrthoDB; 4058939at2759; -.
DR   Proteomes; UP000248481; Chromosome 2.
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:SF84; CLAUDIN-22; 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:UP000248481};
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..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        118..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        162..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
SQ   SEQUENCE   217 AA;  23967 MW;  BEF33E4C2C1EA13A CRC64;
     MALVFRSVAQ FAGISLSLLG RVLSCLTNYL PQWKNLNLDL NEMENWTMGL WQACVIQEEV
     GRQCKDFDSF LALPAELRIS RILMFLSNGL GLLGLLLSGS GLDCLRIGET RRGRKKGLLI
     LGGILFWSAG ISALTPVSWV AYKTVQEFWD ETVPEIVPRW EFGEALFLGW FAGFFLLVGG
     CLLNCAACST RAAPASGHHA VTETHITIST RRCTKPI
//
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