CLD15_RAT
ID CLD15_RAT Reviewed; 227 AA.
AC D3ZQJ0;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Claudin-15;
GN Name=Cldn15;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16505581; DOI=10.1679/aohc.68.349;
RA Inai T., Sengoku A., Guan X., Hirose E., Iida H., Shibata Y.;
RT "Heterogeneity in expression and subcellular localization of tight junction
RT proteins, claudin-10 and -15, examined by RT-PCR and immunofluorescence
RT microscopy.";
RL Arch. Histol. Cytol. 68:349-360(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; SER-214 AND SER-217, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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
CC {ECO:0000269|PubMed:16505581}. Cell membrane
CC {ECO:0000269|PubMed:16505581}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16505581}. Note=Tight junctions form continuous
CC circumferential cell-cell contacts at the borders of apical and lateral
CC cell membranes that seal the intercellular space and show up as strand-
CC like structures in electron microscopy. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in kidney, jejunum and colon (at protein
CC level). {ECO:0000269|PubMed:16505581}.
CC -!- PTM: Palmitoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR EMBL; AABR06071124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06071125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06071126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473973; EDM13299.1; -; Genomic_DNA.
DR RefSeq; NP_001100605.1; NM_001107135.2.
DR RefSeq; XP_006249217.1; XM_006249155.3.
DR AlphaFoldDB; D3ZQJ0; -.
DR SMR; D3ZQJ0; -.
DR STRING; 10116.ENSRNOP00000001923; -.
DR iPTMnet; D3ZQJ0; -.
DR PhosphoSitePlus; D3ZQJ0; -.
DR PaxDb; D3ZQJ0; -.
DR Ensembl; ENSRNOT00000001923; ENSRNOP00000001923; ENSRNOG00000001419.
DR GeneID; 304388; -.
DR KEGG; rno:304388; -.
DR UCSC; RGD:1310678; rat.
DR CTD; 24146; -.
DR RGD; 1310678; Cldn15.
DR eggNOG; ENOG502RYAR; Eukaryota.
DR GeneTree; ENSGT00940000157650; -.
DR HOGENOM; CLU_076370_0_0_1; -.
DR InParanoid; D3ZQJ0; -.
DR OMA; SNCWEFP; -.
DR OrthoDB; 1375597at2759; -.
DR PhylomeDB; D3ZQJ0; -.
DR TreeFam; TF331936; -.
DR PRO; PR:D3ZQJ0; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Proteomes; UP000234681; Chromosome 12.
DR Bgee; ENSRNOG00000001419; Expressed in duodenum and 18 other tissues.
DR Genevisible; D3ZQJ0; RN.
DR GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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 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 1: Evidence at protein 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..227
FT /note="Claudin-15"
FT /id="PRO_0000429588"
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..227
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 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT DISULFID 52..62
FT /evidence="ECO:0000250"
SQ SEQUENCE 227 AA; 24312 MW; 2FEE2CBA883D6F82 CRC64;
MSIAVETFGF FMSALGLLML GVTLPNSYWR VSTVHGNVIT TNTIFENLWY SCATDSLGVS
NCWDFPSMLA LSGYVQGCRA LMITAILLGF LGLFLGMVGL RCTNVGNIDL SRKAKLLAIA
GAFHILAGAC GMVAISWYAV NITTDFFNPL YVGTKYELGS ALYLGWSASL LSILGGICVF
STCCCDSKED PATRVGLPYK PSTVVTARAT SDESDVSFGK YGKNAYV
