CLD5_HUMAN
ID CLD5_HUMAN Reviewed; 218 AA.
AC O00501; B3KS11; Q53XW2; Q8WUW3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Claudin-5;
DE AltName: Full=Transmembrane protein deleted in VCFS;
DE Short=TMDVCF;
GN Name=CLDN5; Synonyms=AWAL, TMVCF;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9192844; DOI=10.1006/geno.1997.4734;
RA Sirotkin H., Morrow B., St Jore B., Puech A., Das Gupta R., Patanjali S.,
RA Skoultchi A., Weissman S.M., Kucherlapati R.;
RT "Identification, characterization, and precise mapping of a human gene
RT encoding a novel membrane-spanning protein from the 22q11 region deleted in
RT velo-cardio-facial syndrome.";
RL Genomics 42:245-251(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
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).
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.
CC Interacts with MPDZ (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O00501; P29972: AQP1; NbExp=3; IntAct=EBI-18400628, EBI-745213;
CC O00501; Q6UX41-6: BTNL8; NbExp=3; IntAct=EBI-18400628, EBI-17442596;
CC O00501; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-18400628, EBI-9083477;
CC O00501; A0PK11: CLRN2; NbExp=3; IntAct=EBI-18400628, EBI-12813623;
CC O00501; Q9BT09: CNPY3; NbExp=3; IntAct=EBI-18400628, EBI-2835965;
CC O00501; Q9Y5Q5: CORIN; NbExp=3; IntAct=EBI-18400628, EBI-17876114;
CC O00501; P40313: CTRL; NbExp=3; IntAct=EBI-18400628, EBI-7883667;
CC O00501; Q07325: CXCL9; NbExp=3; IntAct=EBI-18400628, EBI-3911467;
CC O00501; Q8NBI2: CYB561A3; NbExp=3; IntAct=EBI-18400628, EBI-10269179;
CC O00501; P52803: EFNA5; NbExp=3; IntAct=EBI-18400628, EBI-1753674;
CC O00501; Q08426: EHHADH; NbExp=3; IntAct=EBI-18400628, EBI-2339219;
CC O00501; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-18400628, EBI-711490;
CC O00501; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-18400628, EBI-10976398;
CC O00501; P02724: GYPA; NbExp=3; IntAct=EBI-18400628, EBI-702665;
CC O00501; O43561-2: LAT; NbExp=3; IntAct=EBI-18400628, EBI-8070286;
CC O00501; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-18400628, EBI-2820517;
CC O00501; P30301: MIP; NbExp=3; IntAct=EBI-18400628, EBI-8449636;
CC O00501; Q04941: PLP2; NbExp=3; IntAct=EBI-18400628, EBI-608347;
CC O00501; Q96GM1: PLPPR2; NbExp=3; IntAct=EBI-18400628, EBI-12955265;
CC O00501; Q01453: PMP22; NbExp=3; IntAct=EBI-18400628, EBI-2845982;
CC O00501; Q9NS64: RPRM; NbExp=3; IntAct=EBI-18400628, EBI-1052363;
CC O00501; P11686: SFTPC; NbExp=3; IntAct=EBI-18400628, EBI-10197617;
CC O00501; Q13326: SGCG; NbExp=3; IntAct=EBI-18400628, EBI-5357343;
CC O00501; Q969S0: SLC35B4; NbExp=3; IntAct=EBI-18400628, EBI-10281213;
CC O00501; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-18400628, EBI-741850;
CC O00501; Q9NZ01: TECR; NbExp=3; IntAct=EBI-18400628, EBI-2877718;
CC O00501; P02787: TF; NbExp=3; IntAct=EBI-18400628, EBI-714319;
CC O00501; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-18400628, EBI-10694905;
CC O00501; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-18400628, EBI-2844246;
CC O00501; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-18400628, EBI-2339195;
CC O00501; Q6ZP80: TMEM182; NbExp=3; IntAct=EBI-18400628, EBI-10255122;
CC O00501; Q8WZ59: TMEM190; NbExp=3; IntAct=EBI-18400628, EBI-10278423;
CC O00501; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-18400628, EBI-347385;
CC O00501; O60636: TSPAN2; NbExp=3; IntAct=EBI-18400628, EBI-3914288;
CC O00501; O95183: VAMP5; NbExp=3; IntAct=EBI-18400628, EBI-10191195;
CC O00501; Q9Y548: YIPF1; NbExp=3; IntAct=EBI-18400628, EBI-7850136;
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane;
CC Multi-pass membrane protein.
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; AF000959; AAC51364.1; -; mRNA.
DR EMBL; CR456420; CAG30306.1; -; mRNA.
DR EMBL; AK092561; BAG52573.1; -; mRNA.
DR EMBL; BT007254; AAP35918.1; -; mRNA.
DR EMBL; AC000082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002404; AAH02404.1; -; mRNA.
DR EMBL; BC019290; AAH19290.2; -; mRNA.
DR EMBL; BC032363; AAH32363.1; -; mRNA.
DR RefSeq; NP_001124333.1; NM_001130861.1.
DR RefSeq; NP_003268.2; NM_003277.3.
DR AlphaFoldDB; O00501; -.
DR SMR; O00501; -.
DR BioGRID; 112977; 49.
DR IntAct; O00501; 36.
DR STRING; 9606.ENSP00000385477; -.
DR TCDB; 1.H.1.1.16; the claudin tight junction (claudin1) family.
DR iPTMnet; O00501; -.
DR PhosphoSitePlus; O00501; -.
DR SwissPalm; O00501; -.
DR BioMuta; CLDN5; -.
DR jPOST; O00501; -.
DR MassIVE; O00501; -.
DR PaxDb; O00501; -.
DR PeptideAtlas; O00501; -.
DR PRIDE; O00501; -.
DR ProteomicsDB; 47945; -.
DR ABCD; O00501; 13 sequenced antibodies.
DR Antibodypedia; 3615; 484 antibodies from 38 providers.
DR DNASU; 7122; -.
DR Ensembl; ENST00000618236.2; ENSP00000480623.1; ENSG00000184113.10.
DR GeneID; 7122; -.
DR KEGG; hsa:7122; -.
DR MANE-Select; ENST00000618236.2; ENSP00000480623.1; NM_001363066.2; NP_001349995.1.
DR UCSC; uc062bmp.1; human.
DR CTD; 7122; -.
DR DisGeNET; 7122; -.
DR GeneCards; CLDN5; -.
DR HGNC; HGNC:2047; CLDN5.
DR HPA; ENSG00000184113; Tissue enhanced (adipose tissue, breast, lung).
DR MIM; 602101; gene.
DR neXtProt; NX_O00501; -.
DR OpenTargets; ENSG00000184113; -.
DR PharmGKB; PA26573; -.
DR VEuPathDB; HostDB:ENSG00000184113; -.
DR eggNOG; ENOG502QW5D; Eukaryota.
DR GeneTree; ENSGT00940000161769; -.
DR HOGENOM; CLU_076370_1_2_1; -.
DR InParanoid; O00501; -.
DR PhylomeDB; O00501; -.
DR TreeFam; TF331936; -.
DR PathwayCommons; O00501; -.
DR Reactome; R-HSA-420029; Tight junction interactions.
DR Reactome; R-HSA-8935964; RUNX1 regulates expression of components of tight junctions.
DR SignaLink; O00501; -.
DR SIGNOR; O00501; -.
DR BioGRID-ORCS; 7122; 10 hits in 1067 CRISPR screens.
DR ChiTaRS; CLDN5; human.
DR GeneWiki; CLDN5; -.
DR GenomeRNAi; 7122; -.
DR Pharos; O00501; Tbio.
DR PRO; PR:O00501; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O00501; protein.
DR Bgee; ENSG00000184113; Expressed in right lung and 191 other tissues.
DR ExpressionAtlas; O00501; baseline and differential.
DR Genevisible; O00501; HS.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; TAS:Reactome.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0033270; C:paranode region of axon; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
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:0007043; P:cell-cell junction assembly; IMP:UniProtKB.
DR GO; GO:1990963; P:establishment of blood-retinal barrier; IMP:ARUK-UCL.
DR GO; GO:0060325; P:face morphogenesis; TAS:UniProtKB.
DR GO; GO:0007612; P:learning; TAS:UniProtKB.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; IMP:ARUK-UCL.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:ARUK-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:ARUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0043116; P:negative regulation of vascular permeability; IMP:ARUK-UCL.
DR GO; GO:0003151; P:outflow tract morphogenesis; TAS:UniProtKB.
DR GO; GO:1903348; P:positive regulation of bicellular tight junction assembly; IMP:ARUK-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:ARUK-UCL.
DR GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0032092; P:positive regulation of protein binding; IMP:ARUK-UCL.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0060021; P:roof of mouth development; TAS:UniProtKB.
DR GO; GO:0120192; P:tight junction assembly; ISS:ARUK-UCL.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
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_0000144745"
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..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..159
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 217..218
FT /note="Interactions with TJP1, TJP2 and TJP3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 218 AA; 23147 MW; 9F7F9E194D25425F CRC64;
MGSAALEILG LVLCLVGWGG LILACGLPMW QVTAFLDHNI VTAQTTWKGL WMSCVVQSTG
HMQCKVYDSV LALSTEVQAA RALTVSAVLL AFVALFVTLA GAQCTTCVAP GPAKARVALT
GGVLYLFCGL LALVPLCWFA NIVVREFYDP SVPVSQKYEL GAALYIGWAA TALLMVGGCL
LCCGAWVCTG RPDLSFPVKY SAPRRPTATG DYDKKNYV
