ID   CLD17_PIG               Reviewed;         225 AA.
AC   C3VMW3;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Claudin-17;
GN   Name=CLDN17;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Xie J.-X., Wang Y.-L., Yang G.-Y., Wang W.-J., Zhang Z.-Q., Chen F.-W.,
RA   Li W.-L., Chang L., Yan W., Sun Y.-L., Gao J.-W., Niu H., Wu Y.-X.,
RA   Wang J., Zang M.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc;
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=22402829; DOI=10.1007/s00018-012-0949-x;
RA   Krug S.M., Guenzel D., Conrad M.P., Rosenthal R., Fromm A., Amasheh S.,
RA   Schulzke J.D., Fromm M.;
RT   "Claudin-17 forms tight junction channels with distinct anion
RT   selectivity.";
RL   Cell. Mol. Life Sci. 69:2765-2778(2012).
CC   -!- FUNCTION: Channel-forming tight junction protein with selectivity for
CC       anions, including chloride and bicarbonate, and for solutes smaller
CC       than 9 Angstrom in diameter. In the kidney proximal tubule, may be
CC       involved in quantitative reabsorption of filtered anions. Does not
CC       affect water permeability. {ECO:0000269|PubMed:22402829}.
CC   -!- SUBUNIT: Interacts with OCLN. {ECO:0000250|UniProtKB:P56750}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC       {ECO:0000250|UniProtKB:P56750}. Cell membrane
CC       {ECO:0000250|UniProtKB:P56750}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P56750}.
CC   -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR   EMBL; FJ875102; ACP19320.1; -; mRNA.
DR   EMBL; CU855716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001153555.1; NM_001160083.1.
DR   AlphaFoldDB; C3VMW3; -.
DR   SMR; C3VMW3; -.
DR   STRING; 9823.ENSSSCP00000012813; -.
DR   PaxDb; C3VMW3; -.
DR   Ensembl; ENSSSCT00000013163; ENSSSCP00000012813; ENSSSCG00000012031.
DR   Ensembl; ENSSSCT00035105358; ENSSSCP00035045236; ENSSSCG00035077377.
DR   Ensembl; ENSSSCT00045003004; ENSSSCP00045001895; ENSSSCG00045001927.
DR   Ensembl; ENSSSCT00055031144; ENSSSCP00055024800; ENSSSCG00055015813.
DR   Ensembl; ENSSSCT00065067091; ENSSSCP00065029147; ENSSSCG00065049022.
DR   GeneID; 100294681; -.
DR   KEGG; ssc:100294681; -.
DR   CTD; 26285; -.
DR   VGNC; VGNC:86734; CLDN17.
DR   eggNOG; ENOG502RTNJ; Eukaryota.
DR   GeneTree; ENSGT00940000162550; -.
DR   HOGENOM; CLU_076370_1_2_1; -.
DR   InParanoid; C3VMW3; -.
DR   OMA; VCWTANI; -.
DR   OrthoDB; 1314055at2759; -.
DR   TreeFam; TF331936; -.
DR   Proteomes; UP000008227; Chromosome 13.
DR   Proteomes; UP000314985; Unplaced.
DR   Bgee; ENSSSCG00000012031; Expressed in tonsil and 1 other tissue.
DR   GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
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:0007155; P:cell adhesion; IBA:GO_Central.
DR   InterPro; IPR006187; Claudin.
DR   InterPro; IPR017974; Claudin_CS.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; PTHR12002; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PROSITE; PS01346; CLAUDIN; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Chloride; Chloride channel; Ion channel;
KW   Ion transport; Membrane; Reference proteome; Tight junction; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..225
FT                   /note="Claudin-17"
FT                   /id="PRO_0000437543"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..81
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..124
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        146..164
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        186..225
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          194..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   225 AA;  24747 MW;  851EC84AF1E83983 CRC64;
     MAFYPLQIAG LVLGFLGMVG TLATTLLPQW RVSAFIGSNI IVFERIWEGL WMNCVRQAKA
     RLQCKFYSSM LALSPALEAA RALMCVAVAL SLIALIIGIC GMKKIQCTGS NERAKAYLLG
     TSGVLFILTG IFVLIPVCWT ANIIIRDFYN PAVHVGQKRE LGAALFLGWA SVAVLFIAGG
     LLCGFCCCNR KKQRDGYPAP RPSMPRTDER RRNMTRQSET PTSYV