CLD10_HUMAN
ID CLD10_HUMAN Reviewed; 228 AA.
AC P78369; Q6IBF9; Q96N78;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Claudin-10;
DE AltName: Full=Oligodendrocyte-specific protein-like;
DE Short=OSP-like;
GN Name=CLDN10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, SUBCELLULAR
RP LOCATION, AND ALTERNATIVE SPLICING.
RC TISSUE=Kidney;
RX PubMed=19383724; DOI=10.1242/jcs.040113;
RA Gunzel D., Stuiver M., Kausalya P.J., Haisch L., Krug S.M., Rosenthal R.,
RA Meij I.C., Hunziker W., Fromm M., Muller D.;
RT "Claudin-10 exists in six alternatively spliced isoforms that exhibit
RT distinct localization and function.";
RL J. Cell Sci. 122:1507-1517(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Keen T.J.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
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 [8]
RP INVOLVEMENT IN HELIX, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP VARIANT HELIX LEU-131, AND CHARACTERIZATION OF VARIANT HELIX LEU-131.
RX PubMed=28771254; DOI=10.1038/gim.2017.71;
RA Hadj-Rabia S., Brideau G., Al-Sarraj Y., Maroun R.C., Figueres M.L.,
RA Leclerc-Mercier S., Olinger E., Baron S., Chaussain C., Nochy D.,
RA Taha R.Z., Knebelmann B., Joshi V., Curmi P.A., Kambouris M.,
RA Vargas-Poussou R., Bodemer C., Devuyst O., Houillier P., El-Shanti H.;
RT "Multiplex epithelium dysfunction due to CLDN10 mutation: the HELIX
RT syndrome.";
RL Genet. Med. 20:190-201(2018).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, SUBUNIT, INVOLVEMENT IN
RP HELIX, VARIANT HELIX LYS-48, AND CHARACTERIZATION OF VARIANT HELIX LYS-48.
RX PubMed=28686597; DOI=10.1371/journal.pgen.1006897;
RA Klar J., Piontek J., Milatz S., Tariq M., Jameel M., Breiderhoff T.,
RA Schuster J., Fatima A., Asif M., Sher M., Maebert K., Fromm A., Baig S.M.,
RA Guenzel D., Dahl N.;
RT "Altered paracellular cation permeability due to a rare CLDN10B variant
RT causes anhidrosis and kidney damage.";
RL PLoS Genet. 13:E1006897-E1006897(2017).
CC -!- FUNCTION: Plays a major role in tight junction-specific obliteration of
CC the intercellular space, through calcium-independent cell-adhesion
CC activity. Involved in the regulation of paracellular epithelia
CC permeability to ions in multiple organs. It acts as a paracellular ion
CC channel probably forming permselective pores; isoform 1 appears to
CC create pores preferentially permeable to cations and isoform 2 for
CC anions. In sweat glands and in the thick ascending limb (TAL) of
CC Henle's loop in kidney, it controls paracellular sodium permeability
CC which is essential for proper sweat production and renal function
CC (PubMed:19383724, PubMed:28771254, PubMed:28686597).
CC {ECO:0000269|PubMed:19383724, ECO:0000269|PubMed:28686597,
CC ECO:0000269|PubMed:28771254}.
CC -!- SUBUNIT: Can form homodimers both in trans (interaction between CLDN10
CC molecules in opposing membranes) and in cis (interaction between CLDN10
CC molecules within one membrane). {ECO:0000269|PubMed:28686597}.
CC -!- INTERACTION:
CC P78369; Q8NFU1: BEST2; NbExp=3; IntAct=EBI-13372810, EBI-19947314;
CC P78369; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-13372810, EBI-1045797;
CC P78369; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-13372810, EBI-18053395;
CC P78369; P35372-10: OPRM1; NbExp=3; IntAct=EBI-13372810, EBI-12807478;
CC P78369; O00623: PEX12; NbExp=3; IntAct=EBI-13372810, EBI-594836;
CC P78369; Q9H902: REEP1; NbExp=3; IntAct=EBI-13372810, EBI-1644241;
CC P78369; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-13372810, EBI-8638294;
CC P78369; Q9P0T7: TMEM9; NbExp=3; IntAct=EBI-13372810, EBI-723976;
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:19383724}. Cell membrane
CC {ECO:0000269|PubMed:19383724, ECO:0000269|PubMed:28686597,
CC ECO:0000269|PubMed:28771254}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Cldn10b;
CC IsoId=P78369-1; Sequence=Displayed;
CC Name=2; Synonyms=Cldn10a;
CC IsoId=P78369-2; Sequence=VSP_042898;
CC Name=3; Synonyms=Cldn10a_i1;
CC IsoId=P78369-3; Sequence=VSP_053550;
CC -!- TISSUE SPECIFICITY: Expressed in the kidney, eccrine sweat glands and
CC in all layers of the epidermis. In the kidney, it is detected in the
CC thick ascending limb of Henle's loop (TAL) (PubMed:28771254,
CC PubMed:28686597). In the sweat glands, it is expressed in cells from
CC secretory portions, corresponding to the clear cells (PubMed:28686597).
CC {ECO:0000269|PubMed:28686597, ECO:0000269|PubMed:28771254}.
CC -!- DOMAIN: The fourth transmembrane region (161-181) is necessary for
CC integration into tight junctions. {ECO:0000250}.
CC -!- DISEASE: HELIX syndrome (HELIX) [MIM:617671]: An autosomal recessive
CC disease characterized by congenital heat intolerance, generalized
CC anhidrosis, inability to produce tears, dry mouth, electrolyte
CC imbalance, and ichthyosis. {ECO:0000269|PubMed:28686597,
CC ECO:0000269|PubMed:28771254}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform
CC 2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CLDN10ID45827ch13q32.html";
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DR EMBL; U89916; AAC79506.1; -; mRNA.
DR EMBL; AK055855; BAB71030.1; -; mRNA.
DR EMBL; AK315737; BAG38092.1; -; mRNA.
DR EMBL; CR456845; CAG33126.1; -; mRNA.
DR EMBL; AL139376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471085; EAX08955.1; -; Genomic_DNA.
DR EMBL; BC010920; AAH10920.1; -; mRNA.
DR CCDS; CCDS9475.1; -. [P78369-2]
DR CCDS; CCDS9476.1; -. [P78369-1]
DR RefSeq; NP_001153572.1; NM_001160100.1. [P78369-3]
DR RefSeq; NP_008915.1; NM_006984.4. [P78369-1]
DR RefSeq; NP_878268.1; NM_182848.3. [P78369-2]
DR AlphaFoldDB; P78369; -.
DR SMR; P78369; -.
DR BioGRID; 114529; 27.
DR IntAct; P78369; 12.
DR MINT; P78369; -.
DR STRING; 9606.ENSP00000299339; -.
DR iPTMnet; P78369; -.
DR PhosphoSitePlus; P78369; -.
DR BioMuta; CLDN10; -.
DR DMDM; 6685311; -.
DR EPD; P78369; -.
DR MassIVE; P78369; -.
DR PaxDb; P78369; -.
DR PeptideAtlas; P78369; -.
DR PRIDE; P78369; -.
DR ProteomicsDB; 57597; -. [P78369-1]
DR ProteomicsDB; 57598; -. [P78369-2]
DR Antibodypedia; 4562; 274 antibodies from 32 providers.
DR DNASU; 9071; -.
DR Ensembl; ENST00000299339.3; ENSP00000299339.2; ENSG00000134873.10. [P78369-1]
DR Ensembl; ENST00000376873.7; ENSP00000366069.2; ENSG00000134873.10. [P78369-2]
DR GeneID; 9071; -.
DR KEGG; hsa:9071; -.
DR MANE-Select; ENST00000299339.3; ENSP00000299339.2; NM_006984.5; NP_008915.1.
DR UCSC; uc001vmg.3; human. [P78369-1]
DR CTD; 9071; -.
DR DisGeNET; 9071; -.
DR GeneCards; CLDN10; -.
DR HGNC; HGNC:2033; CLDN10.
DR HPA; ENSG00000134873; Tissue enhanced (kidney, pancreas, salivary gland).
DR MalaCards; CLDN10; -.
DR MIM; 617579; gene.
DR MIM; 617671; phenotype.
DR neXtProt; NX_P78369; -.
DR OpenTargets; ENSG00000134873; -.
DR Orphanet; 528105; Hypohidrosis-electrolyte imbalance-lacrimal gland dysfunction-ichthyosis-xerostomia syndrome.
DR PharmGKB; PA26558; -.
DR VEuPathDB; HostDB:ENSG00000134873; -.
DR eggNOG; ENOG502QPNP; Eukaryota.
DR GeneTree; ENSGT00940000155232; -.
DR HOGENOM; CLU_076370_0_0_1; -.
DR InParanoid; P78369; -.
DR OMA; CKEFISM; -.
DR OrthoDB; 1164514at2759; -.
DR PhylomeDB; P78369; -.
DR TreeFam; TF331936; -.
DR PathwayCommons; P78369; -.
DR Reactome; R-HSA-420029; Tight junction interactions.
DR SignaLink; P78369; -.
DR BioGRID-ORCS; 9071; 11 hits in 1062 CRISPR screens.
DR ChiTaRS; CLDN10; human.
DR GeneWiki; CLDN10; -.
DR GenomeRNAi; 9071; -.
DR Pharos; P78369; Tbio.
DR PRO; PR:P78369; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P78369; protein.
DR Bgee; ENSG00000134873; Expressed in parotid gland and 152 other tissues.
DR ExpressionAtlas; P78369; baseline and differential.
DR Genevisible; P78369; HS.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
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:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0043269; P:regulation of ion transport; IMP:UniProtKB.
DR InterPro; IPR006187; Claudin.
DR InterPro; IPR003554; Claudin10.
DR InterPro; IPR017974; Claudin_CS.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR PANTHER; PTHR12002; PTHR12002; 1.
DR PANTHER; PTHR12002:SF13; PTHR12002:SF13; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01383; CLAUDIN10.
DR PROSITE; PS01346; CLAUDIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Disease variant;
KW Ichthyosis; Ion transport; Membrane; Reference proteome; Tight junction;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..228
FT /note="Claudin-10"
FT /id="PRO_0000144757"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..80
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..160
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..73
FT /note="MASTASEIIAFMVSISGWVLVSSTLPTDYWKVSTIDGTVITTATYWANLWKA
FT CVTDSTGVSNCKDFPSMLALD -> MSRAQIWALVSGVGGFGALVAATTSNEWKVTTRA
FT SSVITATWVYQGLWMNCAGNALGSFHCRPHFTIFKVA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:19383724"
FT /id="VSP_042898"
FT VAR_SEQ 1..73
FT /note="MASTASEIIAFMVSISGWVLVSSTLPTDYWKVSTIDGTVITTATYWANLWKA
FT CVTDSTGVSNCKDFPSMLALD -> MSRAQIWALVSGVGGFGALVAATTSNEWKVTTRA
FT SSVITATWVYQGLWMNCA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19383724"
FT /id="VSP_053550"
FT VARIANT 48
FT /note="N -> K (in HELIX; decreased function in regulation
FT of paracellular ion transport as shown by reduced sodium
FT permeability of cell layers expressing the mutant; affects
FT self-interaction by inhibiting homodimerization in trans
FT and promoting homodimerization in cis; no effect on
FT localization to plasma membrane; dbSNP:rs759408749)"
FT /evidence="ECO:0000269|PubMed:28686597"
FT /id="VAR_080053"
FT VARIANT 131
FT /note="S -> L (in HELIX; strongly reduced localization at
FT the plasma membrane; dbSNP:rs1555299783)"
FT /evidence="ECO:0000269|PubMed:28771254"
FT /id="VAR_080054"
SQ SEQUENCE 228 AA; 24488 MW; 11E66F9F10BCC87B CRC64;
MASTASEIIA FMVSISGWVL VSSTLPTDYW KVSTIDGTVI TTATYWANLW KACVTDSTGV
SNCKDFPSML ALDGYIQACR GLMIAAVSLG FFGSIFALFG MKCTKVGGSD KAKAKIACLA
GIVFILSGLC SMTGCSLYAN KITTEFFDPL FVEQKYELGA ALFIGWAGAS LCIIGGVIFC
FSISDNNKTP RYTYNGATSV MSSRTKYHGG EDFKTTNPSK QFDKNAYV
