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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)DescriptionActionsGraphical viewLength
Sitei55Important for Na(+)-selective paracellular ion transportBy similarity1
Sitei64Important for Na(+)-selective paracellular ion transportBy similarity1
Sitei68Important for the formation of tight-junction strand-like structures1

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)DescriptionActionsGraphical viewLength
Topological domaini1Cytoplasmic1 Publication1
Transmembranei2 – 24HelicalAdd BLAST23
Topological domaini25 – 74Extracellular1 PublicationAdd BLAST50
Transmembranei75 – 99HelicalAdd BLAST25
Topological domaini100 – 115Cytoplasmic1 PublicationAdd BLAST16
Transmembranei116 – 140HelicalAdd BLAST25
Topological domaini141 – 159Extracellular1 PublicationAdd BLAST19
Transmembranei160 – 182HelicalAdd BLAST23
Topological domaini183 – 227Cytoplasmic1 PublicationAdd BLAST45

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)DescriptionActionsGraphical viewLength
Mutagenesisi68M → A or E: Abolishes formation of tight-junction strand-like structures. 1 Publication1
Mutagenesisi68M → I or L: No effect on formation of tight-junction strand-like structures. 1 Publication1
Mutagenesisi102C → A: Abolishes palmitoylation; when associated with 183-A--A-185. 1 Publication1
Mutagenesisi146 – 147FF → AA: Abolishes formation of tight-junction strand-like structures. 1 Publication2
Mutagenesisi183 – 185CCC → AAA: Abolishes palmitoylation; when associated with A-102. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001447721 – 227Claudin-15Add BLAST227

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi52 ↔ 621 Publication
Modified residuei111PhosphoserineBy similarity1
Modified residuei211PhosphoserineBy similarity1
Modified residuei214PhosphoserineCombined sources1
Modified residuei217PhosphoserineCombined sources1

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.
PhosphoSitePlusiQ9Z0S5.

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

BgeeiENSMUSG00000001739.
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

1227
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 24Combined sources23
Beta strandi29 – 32Combined sources4
Beta strandi43 – 46Combined sources4
Beta strandi48 – 54Combined sources7
Beta strandi60 – 64Combined sources5
Helixi67 – 72Combined sources6
Helixi75 – 99Combined sources25
Beta strandi100 – 102Combined sources3
Helixi110 – 146Combined sources37
Beta strandi156 – 158Combined sources3
Helixi160 – 184Combined sources25

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni146 – 147Important for the formation of tight-junction strand-like structures2

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.
OrthoDBiEOG091G0MX2.
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)DescriptionActionsGraphical viewLength
Sequence conflicti2S → L in BAB25544 (PubMed:16141072).Curated1
Sequence conflicti212D → N in BAB25544 (PubMed:16141072).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4P79X-ray2.40A2-194[»]
ProteinModelPortaliQ9Z0S5.
SMRiQ9Z0S5.
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.
PhosphoSitePlusiQ9Z0S5.

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.
OrthoDBiEOG091G0MX2.
PhylomeDBiQ9Z0S5.
TreeFamiTF331936.

Miscellaneous databases

PROiQ9Z0S5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000001739.
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...

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: November 2, 2016
This is version 120 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.