CLD11_MOUSE
ID CLD11_MOUSE Reviewed; 207 AA.
AC Q60771; Q545N5; Q9DB65;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Claudin-11;
DE AltName: Full=Oligodendrocyte transmembrane protein;
DE AltName: Full=Oligodendrocyte-specific protein;
GN Name=Cldn11; Synonyms=Osp, Otm;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8797478; DOI=10.1212/wnl.47.3.772;
RA Bronstein J.M., Popper P., Micevych P.E., Farber D.B.;
RT "Isolation and characterization of a novel oligodendrocyte-specific
RT protein.";
RL Neurology 47:772-778(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=10225958; DOI=10.1083/jcb.145.3.579;
RA Morita K., Furuse M., Tsukita S.;
RT "Claudin-11/OSP-based tight junctions of myelin sheaths in brain and
RT Sertoli cells in testis.";
RL J. Cell Biol. 145:579-588(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 190-203, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP INTERACTION WITH TSPAN3.
RX PubMed=11309411; DOI=10.1083/jcb.153.2.295;
RA Tiwari-Woodruff S.K., Buznikov A.G., Vu T.Q., Micevych P.E., Chen K.,
RA Kornblum H.I., Bronstein J.M.;
RT "OSP/claudin-11 forms a complex with a novel member of the tetraspanin
RT super family and beta1 integrin and regulates proliferation and migration
RT of oligodendrocytes.";
RL J. Cell Biol. 153:295-306(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-197 AND SER-198, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a major role in tight junction-specific obliteration of
CC the intercellular space, through calcium-independent cell-adhesion
CC activity. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with tetraspanin-3/TSPAN3 (PubMed:11309411).
CC Interacts with OCLN (By similarity). {ECO:0000250|UniProtKB:O75508,
CC ECO:0000269|PubMed:11309411}.
CC -!- INTERACTION:
CC Q60771; P07141: Csf1; NbExp=2; IntAct=EBI-309095, EBI-777188;
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane
CC {ECO:0000250|UniProtKB:O75508}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR EMBL; U19582; AAB50270.1; -; mRNA.
DR EMBL; AF124426; AAD17321.1; -; mRNA.
DR EMBL; AK005088; BAB23810.1; -; mRNA.
DR EMBL; AK005171; BAB23860.1; -; mRNA.
DR EMBL; AK161698; BAE36538.1; -; mRNA.
DR EMBL; BC021659; AAH21659.1; -; mRNA.
DR CCDS; CCDS17290.1; -.
DR RefSeq; NP_032796.1; NM_008770.3.
DR AlphaFoldDB; Q60771; -.
DR SMR; Q60771; -.
DR BioGRID; 201987; 4.
DR CORUM; Q60771; -.
DR IntAct; Q60771; 4.
DR MINT; Q60771; -.
DR STRING; 10090.ENSMUSP00000042181; -.
DR iPTMnet; Q60771; -.
DR PhosphoSitePlus; Q60771; -.
DR SwissPalm; Q60771; -.
DR MaxQB; Q60771; -.
DR PaxDb; Q60771; -.
DR PeptideAtlas; Q60771; -.
DR PRIDE; Q60771; -.
DR ProteomicsDB; 283289; -.
DR Antibodypedia; 2785; 361 antibodies from 38 providers.
DR DNASU; 18417; -.
DR Ensembl; ENSMUST00000046174; ENSMUSP00000042181; ENSMUSG00000037625.
DR GeneID; 18417; -.
DR KEGG; mmu:18417; -.
DR UCSC; uc008ovw.2; mouse.
DR CTD; 5010; -.
DR MGI; MGI:106925; Cldn11.
DR VEuPathDB; HostDB:ENSMUSG00000037625; -.
DR eggNOG; ENOG502QSDJ; Eukaryota.
DR GeneTree; ENSGT00890000139496; -.
DR HOGENOM; CLU_094997_0_0_1; -.
DR InParanoid; Q60771; -.
DR OMA; AHRETMI; -.
DR OrthoDB; 1223820at2759; -.
DR PhylomeDB; Q60771; -.
DR TreeFam; TF331936; -.
DR BioGRID-ORCS; 18417; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q60771; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q60771; protein.
DR Bgee; ENSMUSG00000037625; Expressed in ventral tegmental area and 165 other tissues.
DR Genevisible; Q60771; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0045178; C:basal part of cell; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005883; C:neurofilament; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0070160; C:tight junction; IDA:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0008366; P:axon ensheathment; IMP:MGI.
DR GO; GO:0070830; P:bicellular tight junction assembly; IBA:GO_Central.
DR GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0120192; P:tight junction assembly; ISO:MGI.
DR InterPro; IPR006187; Claudin.
DR InterPro; IPR003555; Claudin11.
DR InterPro; IPR017974; Claudin_CS.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR PANTHER; PTHR12002; PTHR12002; 1.
DR PANTHER; PTHR12002:SF6; PTHR12002:SF6; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01384; CLAUDIN11.
DR PROSITE; PS01346; CLAUDIN; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Direct protein sequencing; Membrane;
KW Phosphoprotein; Reference proteome; Tight junction; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..207
FT /note="Claudin-11"
FT /id="PRO_0000144762"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..82
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..157
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99P82"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 196
FT /note="S -> C (in Ref. 3; BAB23860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 207 AA; 22114 MW; A3F936F15958F27B CRC64;
MVATCLQVVG FVTSFVGWIG IIVTTSTNDW VVTCSYTIPT CRKMDELGSK GLWADCVMAT
GLYHCKPLVD ILILPGYVQA CRALMIAASV LGLPAILLLL TVLPCIRMGH EPGVAKYRRA
QLAGVLLILL ALCAIVATIW FPVCAHREIT IVSFGYSLYA GWIGAVMCLV GGCVIVCCSG
DAQSFGENRF YYSSGSSSPT HAKSAHV
