CLD19_HUMAN
ID CLD19_HUMAN Reviewed; 224 AA.
AC Q8N6F1; B7Z5I2; F5H5P9; Q5QT57; Q8N8X0;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Claudin-19;
GN Name=CLDN19;
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] (ISOFORM 2).
RA Morita K.;
RT "Human claudin-19.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Spleen;
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 [6]
RP VARIANTS HOMG5 ASP-20; GLU-57 AND PRO-90.
RX PubMed=17033971; DOI=10.1086/508617;
RA Konrad M., Schaller A., Seelow D., Pandey A.V., Waldegger S., Lesslauer A.,
RA Vitzthum H., Suzuki Y., Luk J.M., Becker C., Schlingmann K.P., Schmid M.,
RA Rodriguez-Soriano J., Ariceta G., Cano F., Enriquez R., Jueppner H.,
RA Bakkaloglu S.A., Hediger M.A., Gallati S., Neuhauss S.C.F., Nuernberg P.,
RA Weber S.;
RT "Mutations in the tight-junction gene claudin 19 (CLDN19) are associated
RT with renal magnesium wasting, renal failure, and severe ocular
RT involvement.";
RL Am. J. Hum. Genet. 79:949-957(2006).
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|UniProtKB:Q9ET38}.
CC -!- INTERACTION:
CC Q8N6F1-2; Q13520: AQP6; NbExp=3; IntAct=EBI-12256978, EBI-13059134;
CC Q8N6F1-2; O43315: AQP9; NbExp=3; IntAct=EBI-12256978, EBI-17444777;
CC Q8N6F1-2; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-12256978, EBI-747430;
CC Q8N6F1-2; Q13323: BIK; NbExp=3; IntAct=EBI-12256978, EBI-700794;
CC Q8N6F1-2; J3KQ12: BSCL2; NbExp=3; IntAct=EBI-12256978, EBI-11532900;
CC Q8N6F1-2; Q7KYR7-4: BTN2A1; NbExp=3; IntAct=EBI-12256978, EBI-17841208;
CC Q8N6F1-2; Q8TD46-4: CD200R1; NbExp=3; IntAct=EBI-12256978, EBI-12824513;
CC Q8N6F1-2; P19397: CD53; NbExp=3; IntAct=EBI-12256978, EBI-6657396;
CC Q8N6F1-2; P04233-2: CD74; NbExp=3; IntAct=EBI-12256978, EBI-12222807;
CC Q8N6F1-2; Q86T13: CLEC14A; NbExp=3; IntAct=EBI-12256978, EBI-17710733;
CC Q8N6F1-2; Q9UHP7-3: CLEC2D; NbExp=3; IntAct=EBI-12256978, EBI-11749983;
CC Q8N6F1-2; P58418: CLRN1; NbExp=3; IntAct=EBI-12256978, EBI-17274839;
CC Q8N6F1-2; O43889-2: CREB3; NbExp=3; IntAct=EBI-12256978, EBI-625022;
CC Q8N6F1-2; P49682: CXCR3; NbExp=3; IntAct=EBI-12256978, EBI-12836456;
CC Q8N6F1-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12256978, EBI-3867333;
CC Q8N6F1-2; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12256978, EBI-781551;
CC Q8N6F1-2; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-12256978, EBI-18304435;
CC Q8N6F1-2; P12314: FCGR1A; NbExp=3; IntAct=EBI-12256978, EBI-2869867;
CC Q8N6F1-2; P55899: FCGRT; NbExp=3; IntAct=EBI-12256978, EBI-2833934;
CC Q8N6F1-2; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-12256978, EBI-3918971;
CC Q8N6F1-2; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-12256978, EBI-12142257;
CC Q8N6F1-2; Q9UJ14: GGT7; NbExp=3; IntAct=EBI-12256978, EBI-1058791;
CC Q8N6F1-2; P48165: GJA8; NbExp=3; IntAct=EBI-12256978, EBI-17458373;
CC Q8N6F1-2; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-12256978, EBI-3917143;
CC Q8N6F1-2; Q8N6U8: GPR161; NbExp=3; IntAct=EBI-12256978, EBI-6255622;
CC Q8N6F1-2; Q8TED1: GPX8; NbExp=3; IntAct=EBI-12256978, EBI-11721746;
CC Q8N6F1-2; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-12256978, EBI-18053395;
CC Q8N6F1-2; P32942: ICAM3; NbExp=3; IntAct=EBI-12256978, EBI-725421;
CC Q8N6F1-2; P38484: IFNGR2; NbExp=3; IntAct=EBI-12256978, EBI-3905457;
CC Q8N6F1-2; P26951: IL3RA; NbExp=3; IntAct=EBI-12256978, EBI-1757512;
CC Q8N6F1-2; P23276: KEL; NbExp=3; IntAct=EBI-12256978, EBI-746662;
CC Q8N6F1-2; P43628: KIR2DL3; NbExp=3; IntAct=EBI-12256978, EBI-8632435;
CC Q8N6F1-2; Q15323: KRT31; NbExp=3; IntAct=EBI-12256978, EBI-948001;
CC Q8N6F1-2; O76011: KRT34; NbExp=3; IntAct=EBI-12256978, EBI-1047093;
CC Q8N6F1-2; Q13571: LAPTM5; NbExp=3; IntAct=EBI-12256978, EBI-2865663;
CC Q8N6F1-2; Q8N386: LRRC25; NbExp=3; IntAct=EBI-12256978, EBI-11304917;
CC Q8N6F1-2; Q9HCJ2: LRRC4C; NbExp=3; IntAct=EBI-12256978, EBI-3925442;
CC Q8N6F1-2; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-12256978, EBI-11956541;
CC Q8N6F1-2; Q96JA4: MS4A14; NbExp=3; IntAct=EBI-12256978, EBI-12839612;
CC Q8N6F1-2; Q96JQ5: MS4A4A; NbExp=3; IntAct=EBI-12256978, EBI-12820341;
CC Q8N6F1-2; P15941-11: MUC1; NbExp=3; IntAct=EBI-12256978, EBI-17263240;
CC Q8N6F1-2; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-12256978, EBI-716063;
CC Q8N6F1-2; Q9P0L9: PKD2L1; NbExp=3; IntAct=EBI-12256978, EBI-7956847;
CC Q8N6F1-2; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-12256978, EBI-373552;
CC Q8N6F1-2; P15151: PVR; NbExp=3; IntAct=EBI-12256978, EBI-3919694;
CC Q8N6F1-2; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-12256978, EBI-3920694;
CC Q8N6F1-2; Q14108: SCARB2; NbExp=3; IntAct=EBI-12256978, EBI-1564650;
CC Q8N6F1-2; O95470: SGPL1; NbExp=3; IntAct=EBI-12256978, EBI-1046170;
CC Q8N6F1-2; Q96DU3: SLAMF6; NbExp=3; IntAct=EBI-12256978, EBI-14058448;
CC Q8N6F1-2; Q14973: SLC10A1; NbExp=3; IntAct=EBI-12256978, EBI-3923031;
CC Q8N6F1-2; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-12256978, EBI-17295964;
CC Q8N6F1-2; Q9HBV2: SPACA1; NbExp=3; IntAct=EBI-12256978, EBI-17498703;
CC Q8N6F1-2; P27105: STOM; NbExp=3; IntAct=EBI-12256978, EBI-1211440;
CC Q8N6F1-2; Q8TAV4: STOML3; NbExp=3; IntAct=EBI-12256978, EBI-12900395;
CC Q8N6F1-2; Q96L08: SUSD3; NbExp=3; IntAct=EBI-12256978, EBI-18194029;
CC Q8N6F1-2; Q8N205-2: SYNE4; NbExp=3; IntAct=EBI-12256978, EBI-12099160;
CC Q8N6F1-2; Q96CE8: TM4SF18; NbExp=3; IntAct=EBI-12256978, EBI-13351685;
CC Q8N6F1-2; Q9BVX2: TMEM106C; NbExp=3; IntAct=EBI-12256978, EBI-2821497;
CC Q8N6F1-2; Q9NWD8: TMEM248; NbExp=3; IntAct=EBI-12256978, EBI-10314986;
CC Q8N6F1-2; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-12256978, EBI-18178701;
CC Q8N6F1-2; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-12256978, EBI-11742770;
CC Q8N6F1-2; O43557: TNFSF14; NbExp=3; IntAct=EBI-12256978, EBI-524131;
CC Q8N6F1-2; Q9Z0S6: Cldn10; Xeno; NbExp=2; IntAct=EBI-12256978, EBI-15799971;
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane;
CC Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N6F1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N6F1-2; Sequence=VSP_010342;
CC Name=3;
CC IsoId=Q8N6F1-3; Sequence=VSP_044839;
CC -!- DISEASE: Hypomagnesemia 5, renal, with or without ocular involvement
CC (HOMG5) [MIM:248190]: A progressive renal disease characterized by
CC primary renal magnesium wasting with hypomagnesemia, hypercalciuria and
CC nephrocalcinosis associated with severe ocular abnormalities such as
CC bilateral chorioretinal scars, macular colobomata, significant myopia
CC and nystagmus. The renal phenotype is virtually undistinguishable from
CC that of patients with HOMG3. {ECO:0000269|PubMed:17033971}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR EMBL; AF497644; AAQ07256.1; -; mRNA.
DR EMBL; AK096063; BAC04691.1; -; mRNA.
DR EMBL; AK298992; BAH12918.1; -; mRNA.
DR EMBL; AC098484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07147.1; -; Genomic_DNA.
DR EMBL; BC030524; AAH30524.1; -; mRNA.
DR CCDS; CCDS44125.1; -. [Q8N6F1-2]
DR CCDS; CCDS471.1; -. [Q8N6F1-1]
DR CCDS; CCDS53306.1; -. [Q8N6F1-3]
DR RefSeq; NP_001116867.1; NM_001123395.1. [Q8N6F1-2]
DR RefSeq; NP_001172046.1; NM_001185117.1. [Q8N6F1-3]
DR RefSeq; NP_683763.2; NM_148960.2. [Q8N6F1-1]
DR AlphaFoldDB; Q8N6F1; -.
DR SMR; Q8N6F1; -.
DR BioGRID; 127213; 68.
DR DIP; DIP-48953N; -.
DR IntAct; Q8N6F1; 68.
DR MINT; Q8N6F1; -.
DR STRING; 9606.ENSP00000296387; -.
DR TCDB; 1.H.1.1.5; the claudin tight junction (claudin1) family.
DR PhosphoSitePlus; Q8N6F1; -.
DR BioMuta; CLDN19; -.
DR DMDM; 47606757; -.
DR MassIVE; Q8N6F1; -.
DR PaxDb; Q8N6F1; -.
DR PeptideAtlas; Q8N6F1; -.
DR PRIDE; Q8N6F1; -.
DR ProteomicsDB; 26945; -.
DR ProteomicsDB; 72162; -. [Q8N6F1-1]
DR ProteomicsDB; 72163; -. [Q8N6F1-2]
DR Antibodypedia; 32237; 164 antibodies from 25 providers.
DR DNASU; 149461; -.
DR Ensembl; ENST00000296387.6; ENSP00000296387.1; ENSG00000164007.11. [Q8N6F1-1]
DR Ensembl; ENST00000372539.3; ENSP00000361617.3; ENSG00000164007.11. [Q8N6F1-2]
DR Ensembl; ENST00000539749.5; ENSP00000443229.1; ENSG00000164007.11. [Q8N6F1-3]
DR GeneID; 149461; -.
DR KEGG; hsa:149461; -.
DR MANE-Select; ENST00000296387.6; ENSP00000296387.1; NM_148960.3; NP_683763.2.
DR UCSC; uc001cht.1; human. [Q8N6F1-1]
DR CTD; 149461; -.
DR DisGeNET; 149461; -.
DR GeneCards; CLDN19; -.
DR HGNC; HGNC:2040; CLDN19.
DR HPA; ENSG00000164007; Group enriched (choroid plexus, kidney, placenta).
DR MalaCards; CLDN19; -.
DR MIM; 248190; phenotype.
DR MIM; 610036; gene.
DR neXtProt; NX_Q8N6F1; -.
DR OpenTargets; ENSG00000164007; -.
DR Orphanet; 2196; Primary hypomagnesemia with hypercalciuria and nephrocalcinosis with severe ocular involvement.
DR PharmGKB; PA26566; -.
DR VEuPathDB; HostDB:ENSG00000164007; -.
DR eggNOG; ENOG502QTG5; Eukaryota.
DR GeneTree; ENSGT00940000158624; -.
DR HOGENOM; CLU_076370_2_0_1; -.
DR InParanoid; Q8N6F1; -.
DR OMA; ARFEFGP; -.
DR OrthoDB; 1244077at2759; -.
DR PhylomeDB; Q8N6F1; -.
DR TreeFam; TF331936; -.
DR PathwayCommons; Q8N6F1; -.
DR Reactome; R-HSA-420029; Tight junction interactions.
DR SignaLink; Q8N6F1; -.
DR BioGRID-ORCS; 149461; 20 hits in 1064 CRISPR screens.
DR GeneWiki; CLDN19; -.
DR GenomeRNAi; 149461; -.
DR Pharos; Q8N6F1; Tbio.
DR PRO; PR:Q8N6F1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8N6F1; protein.
DR Bgee; ENSG00000164007; Expressed in trigeminal ganglion and 115 other tissues.
DR Genevisible; Q8N6F1; HS.
DR GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:ARUK-UCL.
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:0030336; P:negative regulation of cell migration; IMP:ARUK-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:ARUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0061045; P:negative regulation of wound healing; IMP:ARUK-UCL.
DR GO; GO:0019227; P:neuronal action potential propagation; IEA:Ensembl.
DR GO; GO:1901890; P:positive regulation of cell junction assembly; IMP:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:ARUK-UCL.
DR GO; GO:0150111; P:regulation of transepithelial transport; IMP:ARUK-UCL.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR InterPro; IPR006187; Claudin.
DR InterPro; IPR017974; Claudin_CS.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR PANTHER; PTHR12002; PTHR12002; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PROSITE; PS01346; CLAUDIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Disease variant;
KW Disulfide bond; Magnesium; Membrane; Primary hypomagnesemia;
KW Reference proteome; Sensory transduction; Tight junction; Transmembrane;
KW Transmembrane helix; Vision.
FT CHAIN 1..224
FT /note="Claudin-19"
FT /id="PRO_0000144781"
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..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..160
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 191..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 54..64
FT /evidence="ECO:0000250|UniProtKB:Q9ET38"
FT VAR_SEQ 131..224
FT /note="LCTLTAVSWYATLVTQEFFNPSTPVNARYEFGPALFVGWASAGLAVLGGSFL
FT CCTCPEPERPNSSPQPYRPGPSAAAREPVVKLPASAKGPLGV -> MNLAQPCSWAGPQ
FT LAWPCWAAPSSAAHARSQRDPTAAHSPIGLDPLLLPESTSELRLPWPAPHPVAPLPSIQ
FT PASQHPGQGHWGIGWA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044839"
FT VAR_SEQ 210..224
FT /note="PVVKLPASAKGPLGV -> YV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_010342"
FT VARIANT 13
FT /note="L -> F (in dbSNP:rs12065961)"
FT /id="VAR_031238"
FT VARIANT 20
FT /note="G -> D (in HOMG5; perinuclear retention of the
FT mutant protein; dbSNP:rs118203979)"
FT /evidence="ECO:0000269|PubMed:17033971"
FT /id="VAR_031239"
FT VARIANT 57
FT /note="Q -> E (in HOMG5; the mutant protein inserts
FT correctly into the cell membrane although subsequent
FT analyses suggested that dimer formation was disrupted;
FT dbSNP:rs118203980)"
FT /evidence="ECO:0000269|PubMed:17033971"
FT /id="VAR_031240"
FT VARIANT 90
FT /note="L -> P (in HOMG5; dbSNP:rs118203981)"
FT /evidence="ECO:0000269|PubMed:17033971"
FT /id="VAR_031241"
FT CONFLICT 46
FT /note="L -> P (in Ref. 2; BAC04691)"
FT /evidence="ECO:0000305"
FT CONFLICT Q8N6F1-3:186
FT /note="R -> C (in Ref. 2; BAH12918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 23229 MW; 60E1A21902415219 CRC64;
MANSGLQLLG YFLALGGWVG IIASTALPQW KQSSYAGDAI ITAVGLYEGL WMSCASQSTG
QVQCKLYDSL LALDGHIQSA RALMVVAVLL GFVAMVLSVV GMKCTRVGDS NPIAKGRVAI
AGGALFILAG LCTLTAVSWY ATLVTQEFFN PSTPVNARYE FGPALFVGWA SAGLAVLGGS
FLCCTCPEPE RPNSSPQPYR PGPSAAAREP VVKLPASAKG PLGV
