ID   CLD2_BOVIN              Reviewed;         230 AA.
AC   Q765P1; A5D7D2;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Claudin-2;
GN   Name=CLDN2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Ohta H., Takiguchi M., Inaba M.;
RT   "Localization of claudin proteins in bovine kidneys.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; AB115779; BAD01111.1; -; mRNA.
DR   EMBL; BC140513; AAI40514.1; -; mRNA.
DR   RefSeq; NP_991350.1; NM_205781.2.
DR   AlphaFoldDB; Q765P1; -.
DR   SMR; Q765P1; -.
DR   STRING; 9913.ENSBTAP00000006960; -.
DR   PaxDb; Q765P1; -.
DR   PRIDE; Q765P1; -.
DR   GeneID; 404089; -.
DR   KEGG; bta:404089; -.
DR   CTD; 9075; -.
DR   eggNOG; ENOG502R10A; Eukaryota.
DR   HOGENOM; CLU_076370_1_1_1; -.
DR   InParanoid; Q765P1; -.
DR   OrthoDB; 1209440at2759; -.
DR   TreeFam; TF331936; -.
DR   Proteomes; UP000009136; 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; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
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_0000144732"
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;  24534 MW;  ED241778B0E541CA CRC64;
     MASLGLQLVG YVLGLLGLLG TVIAMLLPSW RTSSYVGASI VTAVGFSKGL WMECATHSTG
     ITQCDIYSTM LGLPADIQAA QAMMVTSSAM SSLACIVSVV GMRCTVFFQE SRAKDRVAVV
     GGVFFILGGL LGFIPVAWNL HGILRDFYSP LVPDSMKFEI GEALYLGIIS SLFSLIAGIF
     LCFSCSPQGN RSNYYDAYQA QPLATRSSPR PGQAPKGKSE FNSYSLTGYV