CLD6_MOUSE
ID CLD6_MOUSE Reviewed; 219 AA.
AC Q9Z262;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Claudin-6;
DE AltName: Full=Skullin;
GN Name=Cldn6;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9892664; DOI=10.1073/pnas.96.2.511;
RA Morita K., Furuse M., Fujimoto K., Tsukita S.;
RT "Claudin multigene family encoding four-transmembrane domain protein
RT components of tight junction strands.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:511-516(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryonic stem cell;
RA Troy T., Wisco V., Turksen K.;
RT "Skullin: a novel membrane molecule marks formation of epithelium.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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].
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 INTERACTION WITH TJP1; TJP2 AND TJP3.
RX PubMed=10601346; DOI=10.1083/jcb.147.6.1351;
RA Itoh M., Furuse M., Morita K., Kubota K., Saitou M., Tsukita S.;
RT "Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and
RT ZO-3, with the COOH termini of claudins.";
RL J. Cell Biol. 147:1351-1363(1999).
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: Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3
CC (PubMed:10601346). Interacts with CLDN1, CD81 and OCLN (By similarity).
CC {ECO:0000250|UniProtKB:P56747, ECO:0000269|PubMed:10601346}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:9892664}. Cell membrane
CC {ECO:0000269|PubMed:9892664}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9892664}.
CC -!- TISSUE SPECIFICITY: Expressed mostly in embryonic tissues.
CC {ECO:0000269|PubMed:9892664}.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR EMBL; AF087824; AAD09759.1; -; mRNA.
DR EMBL; AF125305; AAK02012.1; -; mRNA.
DR EMBL; AK010560; BAB27028.1; -; mRNA.
DR EMBL; AK010682; BAB27114.1; -; mRNA.
DR EMBL; BC005718; AAH05718.1; -; mRNA.
DR CCDS; CCDS28457.1; -.
DR RefSeq; NP_061247.1; NM_018777.4.
DR RefSeq; XP_006524704.1; XM_006524641.1.
DR AlphaFoldDB; Q9Z262; -.
DR SMR; Q9Z262; -.
DR MINT; Q9Z262; -.
DR STRING; 10090.ENSMUSP00000024699; -.
DR iPTMnet; Q9Z262; -.
DR PhosphoSitePlus; Q9Z262; -.
DR PaxDb; Q9Z262; -.
DR PRIDE; Q9Z262; -.
DR ProteomicsDB; 283379; -.
DR Antibodypedia; 23973; 578 antibodies from 31 providers.
DR DNASU; 54419; -.
DR Ensembl; ENSMUST00000024699; ENSMUSP00000024699; ENSMUSG00000023906.
DR Ensembl; ENSMUST00000232719; ENSMUSP00000156498; ENSMUSG00000023906.
DR Ensembl; ENSMUST00000233364; ENSMUSP00000156806; ENSMUSG00000023906.
DR GeneID; 54419; -.
DR KEGG; mmu:54419; -.
DR UCSC; uc008asw.3; mouse.
DR CTD; 9074; -.
DR MGI; MGI:1859284; Cldn6.
DR VEuPathDB; HostDB:ENSMUSG00000023906; -.
DR eggNOG; ENOG502QSCN; Eukaryota.
DR GeneTree; ENSGT00940000163060; -.
DR HOGENOM; CLU_076370_1_2_1; -.
DR InParanoid; Q9Z262; -.
DR OMA; HYLARYS; -.
DR OrthoDB; 1231389at2759; -.
DR PhylomeDB; Q9Z262; -.
DR TreeFam; TF331936; -.
DR BioGRID-ORCS; 54419; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Cldn6; mouse.
DR PRO; PR:Q9Z262; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9Z262; protein.
DR Bgee; ENSMUSG00000023906; Expressed in yolk sac and 118 other tissues.
DR ExpressionAtlas; Q9Z262; baseline and differential.
DR Genevisible; Q9Z262; MM.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0001618; F:virus receptor activity; ISO: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; IBA:GO_Central.
DR GO; GO:0045216; P:cell-cell junction organization; IDA:MGI.
DR InterPro; IPR006187; Claudin.
DR InterPro; IPR003925; Claudin6.
DR InterPro; IPR017974; Claudin_CS.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR PANTHER; PTHR12002; PTHR12002; 1.
DR PANTHER; PTHR12002:SF41; PTHR12002:SF41; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01445; CLAUDIN6.
DR PROSITE; PS01346; CLAUDIN; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW Tight junction; Transmembrane; Transmembrane helix.
FT CHAIN 1..219
FT /note="Claudin-6"
FT /id="PRO_0000144749"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..163
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 218..219
FT /note="Interactions with TJP1, TJP2 and TJP3"
FT /evidence="ECO:0000250"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56747"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56747"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56747"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56747"
FT CONFLICT 34
FT /note="A -> T (in Ref. 2; AAK02012)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 219 AA; 23388 MW; 00CF687FAB687E1F CRC64;
MASTGLQILG IVLTLLGWVN ALVSCALPMW KVTAFIGNSI VVAQMVWEGL WMSCVVQSTG
QMQCKVYDSL LALPQDLQAA RALCVVTLLI VLLGLLVYLA GAKCTTCVED RNSKSRLVLI
SGIIFVISGV LTLIPVCWTA HSIIQDFYNP LVADAQKREL GASLYLGWAA SGLLLLGGGL
LCCACSSGGT QGPRHYMACY STSVPHSRGP SEYPTKNYV
