CLD7_MOUSE
ID CLD7_MOUSE Reviewed; 211 AA.
AC Q9Z261; Q3TJX4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Claudin-7;
GN Name=Cldn7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9892664; DOI=10.1073/pnas.96.2.511;
RA Morita K., Furuse M., Fujimoto K., Tsukita S.;
RT "Claudin multigene family encoding four-transmembrane domain protein
RT components of tight junction strands.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:511-516(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary gland;
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 [5]
RP INTERACTION WITH TJP1; TJP2 AND TJP3.
RX PubMed=10601346; DOI=10.1083/jcb.147.6.1351;
RA Itoh M., Furuse M., Morita K., Kubota K., Saitou M., Tsukita S.;
RT "Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and
RT ZO-3, with the COOH termini of claudins.";
RL J. Cell Biol. 147:1351-1363(1999).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC -!- SUBUNIT: Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3
CC (PubMed:10601346). The phosphorylated form interacts with EPCAM (By
CC similarity). {ECO:0000250|UniProtKB:O95471,
CC ECO:0000269|PubMed:10601346}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95471};
CC Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:O95471}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:O95471}. Note=Colocalizes with EPCAM at the
CC basolateral cell membrane and tight junction.
CC {ECO:0000250|UniProtKB:O95471}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in lung and kidney.
CC {ECO:0000269|PubMed:9892664}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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; AF087825; AAD09760.1; -; mRNA.
DR EMBL; AK002924; BAB22460.1; -; mRNA.
DR EMBL; AK087296; BAC39839.1; -; mRNA.
DR EMBL; AK145504; BAE26475.1; -; mRNA.
DR EMBL; AK167250; BAE39371.1; -; mRNA.
DR EMBL; AL596185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008104; AAH08104.1; -; mRNA.
DR EMBL; BC050007; AAH50007.1; -; mRNA.
DR CCDS; CCDS24925.1; -.
DR RefSeq; NP_001180548.1; NM_001193619.1.
DR RefSeq; NP_058583.1; NM_016887.6.
DR AlphaFoldDB; Q9Z261; -.
DR SMR; Q9Z261; -.
DR IntAct; Q9Z261; 1.
DR MINT; Q9Z261; -.
DR STRING; 10090.ENSMUSP00000018713; -.
DR iPTMnet; Q9Z261; -.
DR PhosphoSitePlus; Q9Z261; -.
DR MaxQB; Q9Z261; -.
DR PaxDb; Q9Z261; -.
DR PRIDE; Q9Z261; -.
DR ProteomicsDB; 283295; -.
DR Antibodypedia; 4583; 519 antibodies from 37 providers.
DR DNASU; 53624; -.
DR Ensembl; ENSMUST00000018713; ENSMUSP00000018713; ENSMUSG00000018569.
DR Ensembl; ENSMUST00000108597; ENSMUSP00000104238; ENSMUSG00000018569.
DR GeneID; 53624; -.
DR KEGG; mmu:53624; -.
DR UCSC; uc007jtb.2; mouse.
DR CTD; 1366; -.
DR MGI; MGI:1859285; Cldn7.
DR VEuPathDB; HostDB:ENSMUSG00000018569; -.
DR eggNOG; ENOG502QPXX; Eukaryota.
DR GeneTree; ENSGT00940000160672; -.
DR HOGENOM; CLU_076370_1_2_1; -.
DR InParanoid; Q9Z261; -.
DR OMA; ACAWCTH; -.
DR OrthoDB; 1244077at2759; -.
DR PhylomeDB; Q9Z261; -.
DR TreeFam; TF331936; -.
DR BioGRID-ORCS; 53624; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Cldn7; mouse.
DR PRO; PR:Q9Z261; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9Z261; protein.
DR Bgee; ENSMUSG00000018569; Expressed in crypt of Lieberkuhn of small intestine and 150 other tissues.
DR ExpressionAtlas; Q9Z261; baseline and differential.
DR Genevisible; Q9Z261; MM.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:2000147; P:positive regulation of cell motility; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
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_0000144751"
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; 22359 MW; 4FE87F3A57AC9F29 CRC64;
MANSGLQLLG FSMAMLGWVG LIASTAIPQW QMSSYAGDNI ITAQAMYKGL WMECVTQSTG
MMSCKMYDSV LALPGALQAT RALMVVSLVL GFLAMFVATM GMKCTRCGGD DKAKKARIAM
TGGIVFIVAG LAALVACSWI GHQIVTDFYN PLTPMNVKYE FGPAIFIGWA GSALVLLGGA
LLSCSCPGSE SKAAYRAPRS YPKSNSSKEY V
