CLD7_RAT
ID CLD7_RAT Reviewed; 211 AA.
AC Q9Z1L1; Q3T1J0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Claudin-7;
GN Name=Cldn7;
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 MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-211.
RC TISSUE=Pheochromocytoma;
RA Keen T.J., Inglehearn C.F.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH
RP EPCAM, AND PHOSPHORYLATION.
RX PubMed=16054130; DOI=10.1016/j.yexcr.2005.06.013;
RA Ladwein M., Pape U.F., Schmidt D.S., Schnoelzer M., Fiedler S.,
RA Langbein L., Franke W.W., Moldenhauer G., Zoeller M.;
RT "The cell-cell adhesion molecule EpCAM interacts directly with the tight
RT junction protein claudin-7.";
RL Exp. Cell Res. 309:345-357(2005).
CC -!- FUNCTION: Plays a major role in tight junction-specific obliteration of
CC the intercellular space. {ECO:0000250}.
CC -!- SUBUNIT: Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3 (By
CC similarity). The phosphorylated form interacts with EPCAM
CC (PubMed:16054130). {ECO:0000250|UniProtKB:Q9Z261,
CC ECO:0000269|PubMed:16054130}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95471};
CC Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000269|PubMed:16054130}. Cell junction, tight junction
CC {ECO:0000269|PubMed:16054130}. Note=Colocalizes with EPCAM at the
CC basolateral cell membrane and tight junction.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:16054130}.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABR03074542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101892; AAI01893.1; -; mRNA.
DR EMBL; AJ011811; CAA09790.1; -; mRNA.
DR RefSeq; NP_113890.1; NM_031702.1.
DR RefSeq; XP_006246867.1; XM_006246805.3.
DR AlphaFoldDB; Q9Z1L1; -.
DR SMR; Q9Z1L1; -.
DR STRING; 10116.ENSRNOP00000023291; -.
DR iPTMnet; Q9Z1L1; -.
DR PhosphoSitePlus; Q9Z1L1; -.
DR SwissPalm; Q9Z1L1; -.
DR jPOST; Q9Z1L1; -.
DR PaxDb; Q9Z1L1; -.
DR Ensembl; ENSRNOT00000023291; ENSRNOP00000023291; ENSRNOG00000017325.
DR GeneID; 65132; -.
DR KEGG; rno:65132; -.
DR UCSC; RGD:68432; rat.
DR CTD; 1366; -.
DR RGD; 68432; Cldn7.
DR eggNOG; ENOG502QPXX; Eukaryota.
DR GeneTree; ENSGT00940000160672; -.
DR InParanoid; Q9Z1L1; -.
DR OMA; ACAWCTH; -.
DR OrthoDB; 1244077at2759; -.
DR PhylomeDB; Q9Z1L1; -.
DR TreeFam; TF331936; -.
DR PRO; PR:Q9Z1L1; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000017325; Expressed in jejunum and 17 other tissues.
DR ExpressionAtlas; Q9Z1L1; baseline and differential.
DR Genevisible; Q9Z1L1; RN.
DR GO; GO:0016327; C:apicolateral plasma membrane; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
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:0016328; C:lateral plasma membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
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:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IDA:RGD.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:RGD.
DR GO; GO:2000147; P:positive regulation of cell motility; IDA:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR InterPro; IPR006187; Claudin.
DR InterPro; IPR003552; Claudin7.
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; PR01381; CLAUDIN7.
DR PROSITE; PS01346; CLAUDIN; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW Tight junction; Transmembrane; Transmembrane helix.
FT CHAIN 1..211
FT /note="Claudin-7"
FT /id="PRO_0000144752"
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..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..160
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 210..211
FT /note="Interactions with TJP1, TJP2 and TJP3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 211 AA; 22432 MW; 7F90B644BAA472A0 CRC64;
MANSGLQLLG FSMAMLGWVG LIASTAIPQW QMSSYAGDNI ITAQAMYKGL WMECVTQSTG
MMSCKMYDSV LALPAATQAT RALMIVSLVL GFLAMFVATM GMKCTRCGGD DKVKKARIAM
TGGIIFIVAG LAALVACSWI GHQIVTDFYN PLTPMNIKYE FGPAIFIGWA GSALVLLGGA
LLSCSCPGSE SKAAYRAPRS YPKSNSSKEY V
