CLD5_MOUSE
ID CLD5_MOUSE Reviewed; 218 AA.
AC O54942; O88789;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Claudin-5;
DE AltName: Full=Brain endothelial cell clone 1 protein;
DE AltName: Full=Lung-specific membrane protein;
GN Name=Cldn5; Synonyms=Bec1;
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].
RC TISSUE=Brain;
RX PubMed=9520948;
RA Chen Z., Zandonatti M., Jakubowski D., Fox H.S.;
RT "Brain capillary endothelial cells express MBEC1, a protein that is related
RT to the Clostridium perfringens enterotoxin receptors.";
RL Lab. Invest. 78:353-363(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim K.K., Baek D.H., Kwon B.S.;
RT "A mouse lung-specific membrane protein.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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: Interacts with MPDZ (By similarity). Directly interacts with
CC TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3. {ECO:0000250,
CC ECO:0000269|PubMed:10601346}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:9892664}. Cell membrane
CC {ECO:0000269|PubMed:9892664}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9892664}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in the lung.
CC {ECO:0000269|PubMed:9892664}.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR EMBL; AF035814; AAB96653.1; -; mRNA.
DR EMBL; U82758; AAC27545.1; -; mRNA.
DR EMBL; AF087823; AAD09758.1; -; mRNA.
DR EMBL; AK077282; BAC36728.1; -; mRNA.
DR EMBL; BC002016; AAH02016.1; -; mRNA.
DR EMBL; BC083341; AAH83341.1; -; mRNA.
DR CCDS; CCDS28026.1; -.
DR RefSeq; NP_038833.2; NM_013805.4.
DR AlphaFoldDB; O54942; -.
DR SMR; O54942; -.
DR MINT; O54942; -.
DR STRING; 10090.ENSMUSP00000041925; -.
DR iPTMnet; O54942; -.
DR PhosphoSitePlus; O54942; -.
DR MaxQB; O54942; -.
DR PaxDb; O54942; -.
DR PRIDE; O54942; -.
DR ProteomicsDB; 285490; -.
DR ABCD; O54942; 1 sequenced antibody.
DR Antibodypedia; 3615; 484 antibodies from 38 providers.
DR DNASU; 12741; -.
DR Ensembl; ENSMUST00000043577; ENSMUSP00000041925; ENSMUSG00000041378.
DR GeneID; 12741; -.
DR KEGG; mmu:12741; -.
DR UCSC; uc007yok.2; mouse.
DR CTD; 7122; -.
DR MGI; MGI:1276112; Cldn5.
DR VEuPathDB; HostDB:ENSMUSG00000041378; -.
DR eggNOG; ENOG502QW5D; Eukaryota.
DR GeneTree; ENSGT00940000161769; -.
DR HOGENOM; CLU_076370_1_2_1; -.
DR InParanoid; O54942; -.
DR OMA; IPLCWFA; -.
DR OrthoDB; 1400747at2759; -.
DR PhylomeDB; O54942; -.
DR TreeFam; TF331936; -.
DR BioGRID-ORCS; 12741; 3 hits in 73 CRISPR screens.
DR PRO; PR:O54942; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; O54942; protein.
DR Bgee; ENSMUSG00000041378; Expressed in brain blood vessel and 241 other tissues.
DR Genevisible; O54942; MM.
DR GO; GO:0016327; C:apicolateral plasma membrane; ISO:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0033270; C:paranode region of axon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:CAFA.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; ISO:MGI.
DR GO; GO:0070160; C:tight junction; IDA:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
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:0098609; P:cell-cell adhesion; IC:MGI.
DR GO; GO:0007043; P:cell-cell junction assembly; ISO:MGI.
DR GO; GO:1990963; P:establishment of blood-retinal barrier; ISO:MGI.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; ISO:MGI.
DR GO; GO:0042552; P:myelination; ISO:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0043116; P:negative regulation of vascular permeability; ISO:MGI.
DR GO; GO:1903348; P:positive regulation of bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0120192; P:tight junction assembly; IMP:ARUK-UCL.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR InterPro; IPR006187; Claudin.
DR InterPro; IPR003551; Claudin5.
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; PR01380; CLAUDIN5.
DR PROSITE; PS01346; CLAUDIN; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Membrane; Reference proteome; Tight junction;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..218
FT /note="Claudin-5"
FT /id="PRO_0000144746"
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..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..160
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 217..218
FT /note="Interactions with TJP1, TJP2 and TJP3"
FT /evidence="ECO:0000250"
FT CONFLICT 58
FT /note="S -> N (in Ref. 1; AAB96653)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 23054 MW; 8708F69AE282DE87 CRC64;
MGSAALEILG LVLCLVGWVG LILACGLPMW QVTAFLDHNI VTAQTTWKGL WMSCVVQSTG
HMQCKVYESV LALSAEVQAA RALTVGAVLL ALVALFVTLT GAQCTTCVAP GPVKARVALT
GGALYAVCGL LALVPLCWFA NIVVREFYDP TVPVSQKYEL GAALYIGWAA SALLMCGGGL
VCCGAWVCTG RPEFSFPVKY SAPRRPTANG DYDKKNYV
