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P56746 (CLD15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Claudin-15
Gene names
Name:CLDN15
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members function as impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN15 forms tight junctions that mediate the paracellular transport of small monovalent cations along a concentration gradient, due to selective permeability for Na+, Li+ and K+ ions, but selects against Cl- ions. Plays an important role in paracellular Na+ transport in the intestine and in Na+ homeostasis. Required for normal Na+-dependent intestinal nutrient uptake. Ref.4 Ref.5

Subunit structure

Can form linear homooligomers in the membrane, giving rise to tight junction strand-like structures.

Subcellular location

Cell junctiontight junction. Cell membrane; Multi-pass membrane protein. Note: Tight junctions form continuous circumferential cell-cell contacts at the borders of apical and lateral cell membranes that seal the intercellular space and show up as strand-like structures in electron microscopy. Ref.4 Ref.5

Tissue specificity

Detected in colon (at protein level). Ref.4

Post-translational modification

Palmitoylated By similarity.

Sequence similarities

Belongs to the claudin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 228228Claudin-15
PRO_0000144771

Regions

Topological domain11Cytoplasmic By similarity
Transmembrane2 – 2423Helical; By similarity
Topological domain25 – 7450Extracellular By similarity
Transmembrane75 – 9925Helical; By similarity
Topological domain100 – 11516Cytoplasmic By similarity
Transmembrane116 – 14025Helical; By similarity
Topological domain141 – 15919Extracellular By similarity
Transmembrane160 – 18223Helical; By similarity
Topological domain183 – 22846Cytoplasmic By similarity
Region146 – 1472Important for the formation of tight-junction strand-like structures By similarity

Sites

Site551Important for Na(+)-selective paracellular ion transport
Site641Important for Na(+)-selective paracellular ion transport
Site681Important for the formation of tight-junction strand-like structures By similarity

Amino acid modifications

Disulfide bond52 ↔ 62 By similarity

Experimental info

Mutagenesis461E → K: No effect on charge selectivity for paracellular ion transport. Ref.4
Mutagenesis551D → R: Reverses the charge selectivity for paracellular ion transport, favoring Cl(-) transport. Ref.4
Mutagenesis641E → K: Impairs the charge selectivity for paracellular ion transport, favoring Cl(-) transport. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P56746 [UniParc].

Last modified May 30, 2000. Version 1.
Checksum: D502E2CD9116F4B1

FASTA22824,356
        10         20         30         40         50         60 
MSMAVETFGF FMATVGLLML GVTLPNSYWR VSTVHGNVIT TNTIFENLWF SCATDSLGVY 

        70         80         90        100        110        120 
NCWEFPSMLA LSGYIQACRA LMITAILLGF LGLLLGIAGL RCTNIGGLEL SRKAKLAATA 

       130        140        150        160        170        180 
GALHILAGIC GMVAISWYAF NITRDFFDPL YPGTKYELGP ALYLGWSASL ISILGGLCLC 

       190        200        210        220 
SACCCGSDED PAASARRPYQ APVSVMPVAT SDQEGDSSFG KYGRNAYV 

« Hide

References

« Hide 'large scale' references
[1]Keen T.J., Inglehearn C.F.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"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. expand/collapse author list , 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].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Claudins create charge-selective channels in the paracellular pathway between epithelial cells."
Colegio O.R., Van Itallie C.M., McCrea H.J., Rahner C., Anderson J.M.
Am. J. Physiol. 283:C142-C142(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLU-46; ASP-55 AND GLU-64.
[5]"Reversal of charge selectivity in cation or anion-selective epithelial lines by expression of different claudins."
Van Itallie C.M., Fanning A.S., Anderson J.M.
Am. J. Physiol. 285:F1078-F1078(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ245738 mRNA. Translation: CAB52587.1.
AK056103 mRNA. Translation: BAG51627.1.
CH471197 Genomic DNA. Translation: EAW50211.1.
CCDSCCDS5717.1.
RefSeqNP_001172009.1. NM_001185080.1.
NP_055158.1. NM_014343.2.
UniGeneHs.38738.

3D structure databases

ProteinModelPortalP56746.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117296. 1 interaction.
IntActP56746. 1 interaction.
STRING9606.ENSP00000308870.

Protein family/group databases

TCDB1.H.1.1.9. the claudin tight junction (claudin) family.

PTM databases

PhosphoSiteP56746.

Polymorphism databases

DMDM6685306.

Proteomic databases

PaxDbP56746.
PRIDEP56746.

Protocols and materials databases

DNASU24146.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308344; ENSP00000308870; ENSG00000106404.
ENST00000401528; ENSP00000385300; ENSG00000106404.
GeneID24146.
KEGGhsa:24146.
UCSCuc003uyg.2. human.

Organism-specific databases

CTD24146.
GeneCardsGC07M100875.
HGNCHGNC:2036. CLDN15.
HPAHPA053199.
neXtProtNX_P56746.
PharmGKBPA26562.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46136.
HOGENOMHOG000220937.
HOVERGENHBG000643.
InParanoidP56746.
KOK06087.
OMAIFENLWY.
OrthoDBEOG76HQ2T.
PhylomeDBP56746.
TreeFamTF331936.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpressP56746.
BgeeP56746.
CleanExHS_CLDN15.
GenevestigatorP56746.

Family and domain databases

InterProIPR006187. Claudin.
IPR008094. Claudin15.
IPR017974. Claudin_CS.
IPR004031. PMP22/EMP/MP20/Claudin.
[Graphical view]
PANTHERPTHR12002. PTHR12002. 1 hit.
PfamPF00822. PMP22_Claudin. 1 hit.
[Graphical view]
PRINTSPR01077. CLAUDIN.
PR01718. CLAUDIN15.
PROSITEPS01346. CLAUDIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCLDN15.
GenomeRNAi24146.
NextBio46839.
PROP56746.

Entry information

Entry nameCLD15_HUMAN
AccessionPrimary (citable) accession number: P56746
Secondary accession number(s): B3KPB5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM