ID   CLD2_CANLF              Reviewed;         230 AA.
AC   Q95KM6;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Claudin-2;
GN   Name=CLDN2;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=11309408; DOI=10.1083/jcb.153.2.263;
RA   Furuse M., Furuse K., Sasaki H., Tsukita S.;
RT   "Conversion of zonulae occludentes from tight to leaky strand type by
RT   introducing claudin-2 into Madin-Darby canine kidney I cells.";
RL   J. Cell Biol. 153:263-272(2001).
CC   -!- FUNCTION: Plays a major role in tight junction-specific obliteration of
CC       the intercellular space, through calcium-independent cell-adhesion
CC       activity. {ECO:0000250|UniProtKB:O88552}.
CC   -!- SUBUNIT: Can form homo- and heteropolymers with other CLDN.
CC       Homopolymers interact with CLDN3, but not CLDN1, homopolymers. Directly
CC       interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC       {ECO:0000250|UniProtKB:O88552}. Cell membrane
CC       {ECO:0000250|UniProtKB:O88552}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:O88552}.
CC   -!- PTM: The disulfide bond is necessary for pore formation, but is not
CC       required for correct protein trafficking. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR   EMBL; AF358907; AAK51433.1; -; mRNA.
DR   RefSeq; NP_001003089.1; NM_001003089.1.
DR   AlphaFoldDB; Q95KM6; -.
DR   SMR; Q95KM6; -.
DR   BioGRID; 139573; 1.
DR   IntAct; Q95KM6; 1.
DR   MINT; Q95KM6; -.
DR   STRING; 9615.ENSCAFP00000044590; -.
DR   iPTMnet; Q95KM6; -.
DR   SwissPalm; Q95KM6; -.
DR   PaxDb; Q95KM6; -.
DR   Ensembl; ENSCAFT00030041176; ENSCAFP00030035927; ENSCAFG00030022406.
DR   GeneID; 403649; -.
DR   KEGG; cfa:403649; -.
DR   CTD; 9075; -.
DR   eggNOG; ENOG502R10A; Eukaryota.
DR   InParanoid; Q95KM6; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0070830; P:bicellular tight junction assembly; IBA:GO_Central.
DR   GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; ISS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR   InterPro; IPR006187; Claudin.
DR   InterPro; IPR005411; Claudin2.
DR   InterPro; IPR017974; Claudin_CS.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; PTHR12002; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01589; CLAUDIN2.
DR   PROSITE; PS01346; CLAUDIN; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Disulfide bond; Isopeptide bond; Membrane;
KW   Phosphoprotein; Reference proteome; Tight junction; Transmembrane;
KW   Transmembrane helix; Ubl conjugation.
FT   CHAIN           1..230
FT                   /note="Claudin-2"
FT                   /id="PRO_0000144733"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..81
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..116
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..162
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..230
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          205..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..230
FT                   /note="Interaction with TJP1, TJP2 and TJP3"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88552"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88552"
FT   DISULFID        54..64
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        218
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   230 AA;  24503 MW;  91B71C1E5CDC4BE9 CRC64;
     MASLGLQLVG YILGLLGLLG TLVAMLLPSW RTSSYVGTSI VTAVGFSKGL WMECATHSTG
     ITQCDIYSTL LGLPADIQAA QAMMVTSSAI SSLACIVSVV GMRCTVFCQD SRAKDRLAVV
     GGVFFIIGGL LGFIPVAWNL HGILRDFYSP LVPDSMKFEI GEALYLGIIS SLFSLVAGII
     LCFSCPLQGN RSDYYDSYQA QPLATRGSPR PGQPPKAKSE FNSYSLTGYV