CLD15_BOVIN
ID CLD15_BOVIN Reviewed; 235 AA.
AC Q2KIY2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Claudin-15;
GN Name=CLDN15;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Claudins function as major constituents of the tight junction
CC complexes that regulate the permeability of epithelia. While some
CC claudin family members function as impermeable barriers, others mediate
CC the permeability to ions and small molecules. Often, several claudin
CC family members are coexpressed and interact with each other, and this
CC determines the overall permeability. CLDN15 forms tight junctions that
CC mediate the paracellular transport of small monovalent cations along a
CC concentration gradient, due to selective permeability for Na(+), Li(+)
CC and K(+) ions, but selects against Cl(-) ions. Plays an important role
CC in paracellular Na(+) transport in the intestine and in Na(+)
CC homeostasis. Required for normal Na(+)-dependent intestinal nutrient
CC uptake (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Can form linear homooligomers in the membrane, giving rise to
CC tight junction strand-like structures. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}. Cell
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC Note=Tight junctions form continuous circumferential cell-cell contacts
CC at the borders of apical and lateral cell membranes that seal the
CC intercellular space and show up as strand-like structures in electron
CC microscopy. {ECO:0000250}.
CC -!- PTM: Palmitoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR EMBL; BC112464; AAI12465.1; -; mRNA.
DR RefSeq; NP_001039651.1; NM_001046186.2.
DR AlphaFoldDB; Q2KIY2; -.
DR SMR; Q2KIY2; -.
DR STRING; 9913.ENSBTAP00000000450; -.
DR PaxDb; Q2KIY2; -.
DR GeneID; 514998; -.
DR KEGG; bta:514998; -.
DR CTD; 24146; -.
DR eggNOG; ENOG502RYAR; Eukaryota.
DR InParanoid; Q2KIY2; -.
DR OrthoDB; 1375597at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
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:0006811; P:ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR006187; Claudin.
DR InterPro; IPR008094; Claudin15.
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; PR01718; CLAUDIN15.
DR PROSITE; PS01346; CLAUDIN; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Disulfide bond; Ion transport; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome; Tight junction;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..235
FT /note="Claudin-15"
FT /id="PRO_0000244419"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 2..24
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 25..74
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 75..99
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 100..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 116..140
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 141..159
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 160..182
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 183..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 146..147
FT /note="Important for the formation of tight-junction
FT strand-like structures"
FT /evidence="ECO:0000250"
FT SITE 55
FT /note="Important for Na(+)-selective paracellular ion
FT transport"
FT /evidence="ECO:0000250"
FT SITE 64
FT /note="Important for Na(+)-selective paracellular ion
FT transport"
FT /evidence="ECO:0000250"
FT SITE 68
FT /note="Important for the formation of tight-junction
FT strand-like structures"
FT /evidence="ECO:0000250"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56746"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZQJ0"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0S5"
FT DISULFID 52..62
FT /evidence="ECO:0000250"
SQ SEQUENCE 235 AA; 25074 MW; 85D4F22C51553539 CRC64;
MLVAVEIFGF FLTAVGLLML GVTLAHSSWR VSTVHGNVIT TNTIFENLWY SCATDSMGVH
NCWEFPSMLA LSGYIQACRA LMITAILLGF LGLFLGMVGL RCTNIGGLEL SRKTKLAATA
GALHILAGIC GMVAVSWYAF NITRDFFNPL YAGTKYELGP ALYLGWSACL LAILGGICLF
SNCCCSRDRD PATGVQLPYK APVIPAASLA ARLPAAASDE EGDSSFGKYG KNAYV
