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Protein

Claudin-15

Gene

Cldn15

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei55 – 551Important for Na(+)-selective paracellular ion transportBy similarity
Sitei64 – 641Important for Na(+)-selective paracellular ion transportBy similarity
Sitei68 – 681Important for the formation of tight-junction strand-like structures

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ion transport, Transport

Protein family/group databases

TCDBi1.H.1.1.12. the claudin tight junction (claudin1) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Claudin-15
Gene namesi
Name:Cldn15
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1913103. Cldn15.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 11Cytoplasmic1 Publication
Transmembranei2 – 2423HelicalAdd
BLAST
Topological domaini25 – 7450Extracellular1 PublicationAdd
BLAST
Transmembranei75 – 9925HelicalAdd
BLAST
Topological domaini100 – 11516Cytoplasmic1 PublicationAdd
BLAST
Transmembranei116 – 14025HelicalAdd
BLAST
Topological domaini141 – 15919Extracellular1 PublicationAdd
BLAST
Transmembranei160 – 18223HelicalAdd
BLAST
Topological domaini183 – 22745Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Tight junction

Pathology & Biotechi

Disruption phenotypei

No visible phenotype at birth and during the first four weeks after birth. After about eight weeks, the upper part of the small intestine is abnormally increased both in length and in thickness with enlarged villi and crypts. The villi are about two times larger than normal, and each is associated with about forty abnormally large crypts instead of the normally observed ratio of ten crypts per villus. In contrast, there is no difference in the size of the lower part of the small intestine. The body weight of mutant mice does not differ from that of wild-type littermates (PubMed:18242218). According to PubMed:20727355, the intestinal mucosa from newborn and adult mutant mice displays strongly decreased transepithelial conductance with strongly reduced paracellular Na+ permeability, but no major changes in paracellular permeability to Cl-. Adults show strongly decreased Na+ levels in the lumen of the small intestine. Mutant mice also display decreased intestinal glucose uptake, probably due to decreased Na+ levels. According to PubMed:23089202, mutant mice lacking both Cldn2 and Cldn15 display no visible phenotype at birth, but show decreased growth after about 10 days, severe developmental retardation about 14 days after birth, and then die from malnutrition. None survive more than 25 days after birth. Mice lacking both Cldn2 and Cldn15 show abnormally low Na+ levels in the intestine, leading to decreased intestinal glucose uptake; glucose uptake can be restored to normal levels by addition of Na+. Likewise, mice lacking both Cldn2 and Cldn15 show decreased intestinal uptake of milk fat, fatty acids, bile acids and amino acids; again, normal bile acid and amino acid uptake can be restored by the addition of Na+.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi68 – 681M → A or E: Abolishes formation of tight-junction strand-like structures. 1 Publication
Mutagenesisi68 – 681M → I or L: No effect on formation of tight-junction strand-like structures. 1 Publication
Mutagenesisi102 – 1021C → A: Abolishes palmitoylation; when associated with 183-A--A-185. 1 Publication
Mutagenesisi146 – 1472FF → AA: Abolishes formation of tight-junction strand-like structures. 1 Publication
Mutagenesisi183 – 1853CCC → AAA: Abolishes palmitoylation; when associated with A-102. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 227227Claudin-15PRO_0000144772Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 621 Publication
Modified residuei111 – 1111PhosphoserineBy similarity
Modified residuei211 – 2111PhosphoserineBy similarity
Modified residuei214 – 2141PhosphoserineCombined sources
Modified residuei217 – 2171PhosphoserineCombined sources

Post-translational modificationi

Palmitoylated when heterogeneously expressed in S.frugiperda cells.1 Publication

Keywords - PTMi

Disulfide bond, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ9Z0S5.
PaxDbiQ9Z0S5.
PeptideAtlasiQ9Z0S5.
PRIDEiQ9Z0S5.

PTM databases

iPTMnetiQ9Z0S5.
PhosphoSiteiQ9Z0S5.

Expressioni

Tissue specificityi

Detected in duodenum, jejunum and ileum. Detected on intestinal villi and crypts (at protein level). Ubiquitous. Detected in small intestine, colon, jejunum, heart, kidney and lung.4 Publications

Gene expression databases

BgeeiQ9Z0S5.
CleanExiMM_CLDN15.
GenevisibleiQ9Z0S5. MM.

Interactioni

Subunit structurei

Can form linear homooligomers in the membrane, giving rise to tight junction strand-like structures.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000001790.

Structurei

Secondary structure

1
227
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 2423Combined sources
Beta strandi29 – 324Combined sources
Beta strandi43 – 464Combined sources
Beta strandi48 – 547Combined sources
Beta strandi60 – 645Combined sources
Helixi67 – 726Combined sources
Helixi75 – 9925Combined sources
Beta strandi100 – 1023Combined sources
Helixi110 – 14637Combined sources
Beta strandi156 – 1583Combined sources
Helixi160 – 18425Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4P79X-ray2.40A2-194[»]
ProteinModelPortaliQ9Z0S5.
SMRiQ9Z0S5. Positions 1-186.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni146 – 1472Important for the formation of tight-junction strand-like structures

Sequence similaritiesi

Belongs to the claudin family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IKVT. Eukaryota.
ENOG410YHAD. LUCA.
GeneTreeiENSGT00760000119222.
HOGENOMiHOG000220937.
HOVERGENiHBG000643.
InParanoidiQ9Z0S5.
KOiK06087.
OMAiIFENLWY.
OrthoDBiEOG76HQ2T.
PhylomeDBiQ9Z0S5.
TreeFamiTF331936.

Family and domain databases

InterProiIPR006187. Claudin.
IPR008094. Claudin15.
IPR017974. Claudin_CS.
IPR004031. PMP22/EMP/MP20/Claudin.
[Graphical view]
PANTHERiPTHR12002. PTHR12002. 1 hit.
PfamiPF00822. PMP22_Claudin. 1 hit.
[Graphical view]
PRINTSiPR01718. CLAUDIN15.
PROSITEiPS01346. CLAUDIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z0S5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVAVETFGF FMSALGLLML GLTLSNSYWR VSTVHGNVIT TNTIFENLWY
60 70 80 90 100
SCATDSLGVS NCWDFPSMLA LSGYVQGCRA LMITAILLGF LGLFLGMVGL
110 120 130 140 150
RCTNVGNMDL SKKAKLLAIA GTLHILAGAC GMVAISWYAV NITTDFFNPL
160 170 180 190 200
YAGTKYELGP ALYLGWSASL LSILGGICVF STCCCSSKEE PATRAGLPYK
210 220
PSTVVIPRAT SDESDISFGK YGKNAYV
Length:227
Mass (Da):24,280
Last modified:May 10, 2002 - v2
Checksum:i7112FE8A6EEF2941
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → L in BAB25544 (PubMed:16141072).Curated
Sequence conflicti212 – 2121D → N in BAB25544 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008227 mRNA. Translation: BAB25544.1.
AK008683 mRNA. Translation: BAB25831.1.
BC023428 mRNA. Translation: AAH23428.1.
AF124427 mRNA. Translation: AAD17331.1.
CCDSiCCDS19758.1.
RefSeqiNP_068365.1. NM_021719.4.
UniGeneiMm.87202.

Genome annotation databases

EnsembliENSMUST00000001790; ENSMUSP00000001790; ENSMUSG00000001739.
ENSMUST00000111093; ENSMUSP00000106722; ENSMUSG00000001739.
GeneIDi60363.
KEGGimmu:60363.
UCSCiuc009abg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008227 mRNA. Translation: BAB25544.1.
AK008683 mRNA. Translation: BAB25831.1.
BC023428 mRNA. Translation: AAH23428.1.
AF124427 mRNA. Translation: AAD17331.1.
CCDSiCCDS19758.1.
RefSeqiNP_068365.1. NM_021719.4.
UniGeneiMm.87202.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4P79X-ray2.40A2-194[»]
ProteinModelPortaliQ9Z0S5.
SMRiQ9Z0S5. Positions 1-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000001790.

Protein family/group databases

TCDBi1.H.1.1.12. the claudin tight junction (claudin1) family.

PTM databases

iPTMnetiQ9Z0S5.
PhosphoSiteiQ9Z0S5.

Proteomic databases

MaxQBiQ9Z0S5.
PaxDbiQ9Z0S5.
PeptideAtlasiQ9Z0S5.
PRIDEiQ9Z0S5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001790; ENSMUSP00000001790; ENSMUSG00000001739.
ENSMUST00000111093; ENSMUSP00000106722; ENSMUSG00000001739.
GeneIDi60363.
KEGGimmu:60363.
UCSCiuc009abg.2. mouse.

Organism-specific databases

CTDi24146.
MGIiMGI:1913103. Cldn15.

Phylogenomic databases

eggNOGiENOG410IKVT. Eukaryota.
ENOG410YHAD. LUCA.
GeneTreeiENSGT00760000119222.
HOGENOMiHOG000220937.
HOVERGENiHBG000643.
InParanoidiQ9Z0S5.
KOiK06087.
OMAiIFENLWY.
OrthoDBiEOG76HQ2T.
PhylomeDBiQ9Z0S5.
TreeFamiTF331936.

Miscellaneous databases

PROiQ9Z0S5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z0S5.
CleanExiMM_CLDN15.
GenevisibleiQ9Z0S5. MM.

Family and domain databases

InterProiIPR006187. Claudin.
IPR008094. Claudin15.
IPR017974. Claudin_CS.
IPR004031. PMP22/EMP/MP20/Claudin.
[Graphical view]
PANTHERiPTHR12002. PTHR12002. 1 hit.
PfamiPF00822. PMP22_Claudin. 1 hit.
[Graphical view]
PRINTSiPR01718. CLAUDIN15.
PROSITEiPS01346. CLAUDIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Small intestine and Stomach.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  3. Morita K., Furuse M., Tsukita S.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-122.
    Tissue: Lung.
  4. "Heterogeneity in expression and subcellular localization of tight junction proteins, claudin-10 and -15, examined by RT-PCR and immunofluorescence microscopy."
    Inai T., Sengoku A., Guan X., Hirose E., Iida H., Shibata Y.
    Arch. Histol. Cytol. 68:349-360(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. Cited for: DISRUPTION, FUNCTION, TISSUE SPECIFICITY.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 AND SER-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue and Kidney.
  7. "Loss of claudin-15, but not claudin-2, causes Na+ deficiency and glucose malabsorption in mouse small intestine."
    Tamura A., Hayashi H., Imasato M., Yamazaki Y., Hagiwara A., Wada M., Noda T., Watanabe M., Suzuki Y., Tsukita S.
    Gastroenterology 140:913-923(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Loss of claudins 2 and 15 from mice causes defects in paracellular Na+ flow and nutrient transport in gut and leads to death from malnutrition."
    Wada M., Tamura A., Takahashi N., Tsukita S.
    Gastroenterology 144:369-380(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
  9. "Crystal structure of a claudin provides insight into the architecture of tight junctions."
    Suzuki H., Nishizawa T., Tani K., Yamazaki Y., Tamura A., Ishitani R., Dohmae N., Tsukita S., Nureki O., Fujiyoshi Y.
    Science 344:304-307(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-194 OF MUTANT ALA-102/ALA-183/ALA-184/ALA-185, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF MET-68; CYS-102; 146-PHE-PHE-147 AND 183-CYS--CYS-185, TOPOLOGY, DISULFIDE BOND, PALMITOYLATION.

Entry informationi

Entry nameiCLD15_MOUSE
AccessioniPrimary (citable) accession number: Q9Z0S5
Secondary accession number(s): Q9D7Z0, Q9D8A6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 10, 2002
Last modified: July 6, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.