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Protein

Claudin-5

Gene

CLDN5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Plays a major role in tight junction-specific obliteration of the intercellular space.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_19373. Tight junction interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Claudin-5
Alternative name(s):
Transmembrane protein deleted in VCFS
Short name:
TMDVCF
Gene namesi
Name:CLDN5
Synonyms:AWAL, TMVCF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:2047. CLDN5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicSequence Analysis
Transmembranei8 – 2821HelicalSequence AnalysisAdd
BLAST
Topological domaini29 – 8153ExtracellularSequence AnalysisAdd
BLAST
Transmembranei82 – 10221HelicalSequence AnalysisAdd
BLAST
Topological domaini103 – 12220CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei123 – 14321HelicalSequence AnalysisAdd
BLAST
Topological domaini144 – 15916ExtracellularSequence AnalysisAdd
BLAST
Transmembranei160 – 18021HelicalSequence AnalysisAdd
BLAST
Topological domaini181 – 21838CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell-cell junction Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: ProtInc
  • plasma membrane Source: UniProtKB-SubCell
  • tight junction Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Tight junction

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26573.

Polymorphism and mutation databases

BioMutaiCLDN5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218Claudin-5PRO_0000144745Add
BLAST

Proteomic databases

PaxDbiO00501.
PRIDEiO00501.

PTM databases

PhosphoSiteiO00501.

Expressioni

Gene expression databases

BgeeiO00501.
CleanExiHS_CLDN5.
ExpressionAtlasiO00501. baseline and differential.
GenevestigatoriO00501.

Organism-specific databases

HPAiCAB002607.

Interactioni

Subunit structurei

Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3. Interacts with MPDZ (By similarity).By similarity

Protein-protein interaction databases

BioGridi112977. 4 interactions.
STRINGi9606.ENSP00000384554.

Structurei

3D structure databases

ProteinModelPortaliO00501.
SMRiO00501. Positions 4-181.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni217 – 2182Interactions with TJP1, TJP2 and TJP3By similarity

Sequence similaritiesi

Belongs to the claudin family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG43495.
GeneTreeiENSGT00760000118928.
HOGENOMiHOG000220937.
HOVERGENiHBG000643.
InParanoidiO00501.
KOiK06087.
OrthoDBiEOG76HQ2T.
PhylomeDBiO00501.
TreeFamiTF331936.

Family and domain databases

InterProiIPR006187. Claudin.
IPR003551. Claudin5.
IPR017974. Claudin_CS.
IPR004031. PMP22/EMP/MP20/Claudin.
[Graphical view]
PANTHERiPTHR12002. PTHR12002. 1 hit.
PfamiPF00822. PMP22_Claudin. 1 hit.
[Graphical view]
PRINTSiPR01077. CLAUDIN.
PR01380. CLAUDIN5.
PROSITEiPS01346. CLAUDIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O00501-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSAALEILG LVLCLVGWGG LILACGLPMW QVTAFLDHNI VTAQTTWKGL
60 70 80 90 100
WMSCVVQSTG HMQCKVYDSV LALSTEVQAA RALTVSAVLL AFVALFVTLA
110 120 130 140 150
GAQCTTCVAP GPAKARVALT GGVLYLFCGL LALVPLCWFA NIVVREFYDP
160 170 180 190 200
SVPVSQKYEL GAALYIGWAA TALLMVGGCL LCCGAWVCTG RPDLSFPVKY
210
SAPRRPTATG DYDKKNYV
Length:218
Mass (Da):23,147
Last modified:July 1, 1997 - v1
Checksum:i9F7F9E194D25425F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF000959 mRNA. Translation: AAC51364.1.
CR456420 mRNA. Translation: CAG30306.1.
AK092561 mRNA. Translation: BAG52573.1.
BT007254 mRNA. Translation: AAP35918.1.
AC000082 Genomic DNA. No translation available.
BC002404 mRNA. Translation: AAH02404.1.
BC019290 mRNA. Translation: AAH19290.2.
BC032363 mRNA. Translation: AAH32363.1.
RefSeqiNP_001124333.1. NM_001130861.1.
NP_003268.2. NM_003277.3.
UniGeneiHs.505337.

Genome annotation databases

EnsembliENST00000618236; ENSP00000480623; ENSG00000184113.
GeneIDi7122.
KEGGihsa:7122.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF000959 mRNA. Translation: AAC51364.1.
CR456420 mRNA. Translation: CAG30306.1.
AK092561 mRNA. Translation: BAG52573.1.
BT007254 mRNA. Translation: AAP35918.1.
AC000082 Genomic DNA. No translation available.
BC002404 mRNA. Translation: AAH02404.1.
BC019290 mRNA. Translation: AAH19290.2.
BC032363 mRNA. Translation: AAH32363.1.
RefSeqiNP_001124333.1. NM_001130861.1.
NP_003268.2. NM_003277.3.
UniGeneiHs.505337.

3D structure databases

ProteinModelPortaliO00501.
SMRiO00501. Positions 4-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112977. 4 interactions.
STRINGi9606.ENSP00000384554.

PTM databases

PhosphoSiteiO00501.

Polymorphism and mutation databases

BioMutaiCLDN5.

Proteomic databases

PaxDbiO00501.
PRIDEiO00501.

Protocols and materials databases

DNASUi7122.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000618236; ENSP00000480623; ENSG00000184113.
GeneIDi7122.
KEGGihsa:7122.

Organism-specific databases

CTDi7122.
GeneCardsiGC22M019510.
HGNCiHGNC:2047. CLDN5.
HPAiCAB002607.
MIMi602101. gene.
neXtProtiNX_O00501.
PharmGKBiPA26573.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG43495.
GeneTreeiENSGT00760000118928.
HOGENOMiHOG000220937.
HOVERGENiHBG000643.
InParanoidiO00501.
KOiK06087.
OrthoDBiEOG76HQ2T.
PhylomeDBiO00501.
TreeFamiTF331936.

Enzyme and pathway databases

ReactomeiREACT_19373. Tight junction interactions.

Miscellaneous databases

ChiTaRSiCLDN5. human.
GeneWikiiCLDN5.
GenomeRNAii7122.
NextBioi27871.
PROiO00501.
SOURCEiSearch...

Gene expression databases

BgeeiO00501.
CleanExiHS_CLDN5.
ExpressionAtlasiO00501. baseline and differential.
GenevestigatoriO00501.

Family and domain databases

InterProiIPR006187. Claudin.
IPR003551. Claudin5.
IPR017974. Claudin_CS.
IPR004031. PMP22/EMP/MP20/Claudin.
[Graphical view]
PANTHERiPTHR12002. PTHR12002. 1 hit.
PfamiPF00822. PMP22_Claudin. 1 hit.
[Graphical view]
PRINTSiPR01077. CLAUDIN.
PR01380. CLAUDIN5.
PROSITEiPS01346. CLAUDIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, characterization, and precise mapping of a human gene encoding a novel membrane-spanning protein from the 22q11 region deleted in velo-cardio-facial syndrome."
    Sirotkin H., Morrow B., St Jore B., Puech A., Das Gupta R., Patanjali S., Skoultchi A., Weissman S.M., Kucherlapati R.
    Genomics 42:245-251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Lung.

Entry informationi

Entry nameiCLD5_HUMAN
AccessioniPrimary (citable) accession number: O00501
Secondary accession number(s): B3KS11, Q53XW2, Q8WUW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: May 27, 2015
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.