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Protein

Claudin-11

Gene

Cldn11

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

Functioni

Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.By similarity

GO - Molecular functioni

GO - Biological processi

  • axon ensheathment Source: MGI
  • calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules Source: UniProtKB
  • cell adhesion Source: MGI
  • spermatogenesis Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Claudin-11
Alternative name(s):
Oligodendrocyte transmembrane protein
Oligodendrocyte-specific protein
Gene namesi
Name:Cldn11
Synonyms:Osp, Otm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:106925. Cldn11.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 11CytoplasmicSequence analysis
Transmembranei2 – 2221HelicalSequence analysisAdd
BLAST
Topological domaini23 – 8260ExtracellularSequence analysisAdd
BLAST
Transmembranei83 – 10321HelicalSequence analysisAdd
BLAST
Topological domaini104 – 12219CytoplasmicSequence analysisAdd
BLAST
Transmembranei123 – 14321HelicalSequence analysisAdd
BLAST
Topological domaini144 – 15714ExtracellularSequence analysisAdd
BLAST
Transmembranei158 – 17821HelicalSequence analysisAdd
BLAST
Topological domaini179 – 20729CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • basal part of cell Source: MGI
  • bicellular tight junction Source: UniProtKB
  • extracellular exosome Source: MGI
  • integral component of plasma membrane Source: MGI
  • myelin sheath Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 207207Claudin-11PRO_0000144762Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei193 – 1931PhosphoserineBy similarity
Modified residuei194 – 1941PhosphoserineCombined sources
Modified residuei197 – 1971PhosphoserineCombined sources
Modified residuei198 – 1981PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ60771.
PaxDbiQ60771.
PRIDEiQ60771.

PTM databases

iPTMnetiQ60771.
PhosphoSiteiQ60771.
SwissPalmiQ60771.

Expressioni

Gene expression databases

BgeeiQ60771.
CleanExiMM_CLDN11.
GenevisibleiQ60771. MM.

Interactioni

Subunit structurei

Interacts with tetraspanin-3/TSPAN3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Csf1P071412EBI-309095,EBI-777188

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ60771. 2 interactions.
MINTiMINT-217520.
STRINGi10090.ENSMUSP00000042181.

Structurei

3D structure databases

ProteinModelPortaliQ60771.
SMRiQ60771. Positions 6-172.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the claudin family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IEXU. Eukaryota.
ENOG41101XN. LUCA.
GeneTreeiENSGT00730000111104.
HOGENOMiHOG000220937.
HOVERGENiHBG102313.
InParanoidiQ60771.
KOiK06087.
OMAiYSLYTGW.
OrthoDBiEOG76HQ2T.
PhylomeDBiQ60771.
TreeFamiTF331936.

Family and domain databases

InterProiIPR006187. Claudin.
IPR003555. Claudin11.
IPR017974. Claudin_CS.
IPR004031. PMP22/EMP/MP20/Claudin.
[Graphical view]
PANTHERiPTHR12002. PTHR12002. 1 hit.
PTHR12002:SF6. PTHR12002:SF6. 1 hit.
PfamiPF00822. PMP22_Claudin. 1 hit.
[Graphical view]
PRINTSiPR01384. CLAUDIN11.
PROSITEiPS01346. CLAUDIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60771-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVATCLQVVG FVTSFVGWIG IIVTTSTNDW VVTCSYTIPT CRKMDELGSK
60 70 80 90 100
GLWADCVMAT GLYHCKPLVD ILILPGYVQA CRALMIAASV LGLPAILLLL
110 120 130 140 150
TVLPCIRMGH EPGVAKYRRA QLAGVLLILL ALCAIVATIW FPVCAHREIT
160 170 180 190 200
IVSFGYSLYA GWIGAVMCLV GGCVIVCCSG DAQSFGENRF YYSSGSSSPT

HAKSAHV
Length:207
Mass (Da):22,114
Last modified:November 1, 1996 - v1
Checksum:iA3F936F15958F27B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti196 – 1961S → C in BAB23860 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19582 mRNA. Translation: AAB50270.1.
AF124426 mRNA. Translation: AAD17321.1.
AK005088 mRNA. Translation: BAB23810.1.
AK005171 mRNA. Translation: BAB23860.1.
AK161698 mRNA. Translation: BAE36538.1.
BC021659 mRNA. Translation: AAH21659.1.
CCDSiCCDS17290.1.
RefSeqiNP_032796.1. NM_008770.3.
UniGeneiMm.4425.

Genome annotation databases

EnsembliENSMUST00000046174; ENSMUSP00000042181; ENSMUSG00000037625.
GeneIDi18417.
KEGGimmu:18417.
UCSCiuc008ovw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19582 mRNA. Translation: AAB50270.1.
AF124426 mRNA. Translation: AAD17321.1.
AK005088 mRNA. Translation: BAB23810.1.
AK005171 mRNA. Translation: BAB23860.1.
AK161698 mRNA. Translation: BAE36538.1.
BC021659 mRNA. Translation: AAH21659.1.
CCDSiCCDS17290.1.
RefSeqiNP_032796.1. NM_008770.3.
UniGeneiMm.4425.

3D structure databases

ProteinModelPortaliQ60771.
SMRiQ60771. Positions 6-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ60771. 2 interactions.
MINTiMINT-217520.
STRINGi10090.ENSMUSP00000042181.

PTM databases

iPTMnetiQ60771.
PhosphoSiteiQ60771.
SwissPalmiQ60771.

Proteomic databases

MaxQBiQ60771.
PaxDbiQ60771.
PRIDEiQ60771.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000046174; ENSMUSP00000042181; ENSMUSG00000037625.
GeneIDi18417.
KEGGimmu:18417.
UCSCiuc008ovw.2. mouse.

Organism-specific databases

CTDi5010.
MGIiMGI:106925. Cldn11.

Phylogenomic databases

eggNOGiENOG410IEXU. Eukaryota.
ENOG41101XN. LUCA.
GeneTreeiENSGT00730000111104.
HOGENOMiHOG000220937.
HOVERGENiHBG102313.
InParanoidiQ60771.
KOiK06087.
OMAiYSLYTGW.
OrthoDBiEOG76HQ2T.
PhylomeDBiQ60771.
TreeFamiTF331936.

Miscellaneous databases

PROiQ60771.
SOURCEiSearch...

Gene expression databases

BgeeiQ60771.
CleanExiMM_CLDN11.
GenevisibleiQ60771. MM.

Family and domain databases

InterProiIPR006187. Claudin.
IPR003555. Claudin11.
IPR017974. Claudin_CS.
IPR004031. PMP22/EMP/MP20/Claudin.
[Graphical view]
PANTHERiPTHR12002. PTHR12002. 1 hit.
PTHR12002:SF6. PTHR12002:SF6. 1 hit.
PfamiPF00822. PMP22_Claudin. 1 hit.
[Graphical view]
PRINTSiPR01384. CLAUDIN11.
PROSITEiPS01346. CLAUDIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a novel oligodendrocyte-specific protein."
    Bronstein J.M., Popper P., Micevych P.E., Farber D.B.
    Neurology 47:772-778(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Claudin-11/OSP-based tight junctions of myelin sheaths in brain and Sertoli cells in testis."
    Morita K., Furuse M., Tsukita S.
    J. Cell Biol. 145:579-588(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  3. "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: Cerebellum.
  4. "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: Salivary gland.
  5. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 190-203, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  6. "OSP/claudin-11 forms a complex with a novel member of the tetraspanin super family and beta1 integrin and regulates proliferation and migration of oligodendrocytes."
    Tiwari-Woodruff S.K., Buznikov A.G., Vu T.Q., Micevych P.E., Chen K., Kornblum H.I., Bronstein J.M.
    J. Cell Biol. 153:295-306(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TSPAN3.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-197 AND SER-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Testis.

Entry informationi

Entry nameiCLD11_MOUSE
AccessioniPrimary (citable) accession number: Q60771
Secondary accession number(s): Q545N5, Q9DB65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: June 8, 2016
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

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.