CLD19_MOUSE
ID CLD19_MOUSE Reviewed; 224 AA.
AC Q9ET38; Q8R4B7;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Claudin-19;
GN Name=Cldn19;
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] (ISOFORM 1).
RA Luk J.M., Tong M.K., Mok B.W.;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-203.
RC STRAIN=ICR;
RA Kiuchi Y., Morita K., Furuse M., Tsukita S.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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).
RN [5] {ECO:0007744|PDB:3X29}
RP X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 1-185 IN COMPLEX WITH CLOSTRIDIUM
RP PERFRINGENS CPE, INTERACTION WITH CLOSTRIDIUM PERFRINGENS CPE, SUBCELLULAR
RP LOCATION, FUNCTION, MUTAGENESIS OF TYR-35; ASP-38; ALA-39; ILE-40; ILE-41;
RP THR-42; SER-53; GLN-146; GLU-147; ASN-150; PRO-151; SER-152; THR-153;
RP PRO-154; VAL-155; ASN-156 AND TYR-159, AND DISULFIDE BOND.
RX PubMed=25678664; DOI=10.1126/science.1261833;
RA Saitoh Y., Suzuki H., Tani K., Nishikawa K., Irie K., Ogura Y., Tamura A.,
RA Tsukita S., Fujiyoshi Y.;
RT "Tight junctions. Structural insight into tight junction disassembly by
RT Clostridium perfringens enterotoxin.";
RL Science 347:775-778(2015).
CC -!- FUNCTION: Plays a major role in tight junction-specific obliteration of
CC the intercellular space, through calcium-independent cell-adhesion
CC activity. {ECO:0000305|PubMed:25678664}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via both extracellular
CC domains) with Clostridium perfringens enterotoxin CPE; the interaction
CC disrupts claudin assembly in tight junctions.
CC {ECO:0000269|PubMed:25678664}.
CC -!- INTERACTION:
CC Q9ET38; P01558: cpe; Xeno; NbExp=2; IntAct=EBI-8036280, EBI-16142958;
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:25678664}. Cell membrane
CC {ECO:0000269|PubMed:25678664}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:25678664}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ET38-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ET38-2; Sequence=VSP_010343;
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR EMBL; AF486651; AAM12735.2; -; mRNA.
DR EMBL; AK032743; BAC28005.1; -; mRNA.
DR EMBL; AF249889; AAF98323.1; -; mRNA.
DR CCDS; CCDS18577.1; -. [Q9ET38-1]
DR CCDS; CCDS18578.1; -. [Q9ET38-2]
DR RefSeq; NP_001033679.1; NM_001038590.1. [Q9ET38-1]
DR RefSeq; NP_694745.1; NM_153105.7. [Q9ET38-2]
DR PDB; 3X29; X-ray; 3.70 A; A/C=1-185.
DR PDBsum; 3X29; -.
DR AlphaFoldDB; Q9ET38; -.
DR SMR; Q9ET38; -.
DR DIP; DIP-42881N; -.
DR IntAct; Q9ET38; 2.
DR MINT; Q9ET38; -.
DR STRING; 10090.ENSMUSP00000081334; -.
DR PhosphoSitePlus; Q9ET38; -.
DR PaxDb; Q9ET38; -.
DR PRIDE; Q9ET38; -.
DR ProteomicsDB; 285486; -. [Q9ET38-1]
DR ProteomicsDB; 285487; -. [Q9ET38-2]
DR Antibodypedia; 32237; 164 antibodies from 25 providers.
DR DNASU; 242653; -.
DR Ensembl; ENSMUST00000084309; ENSMUSP00000081334; ENSMUSG00000066058. [Q9ET38-1]
DR Ensembl; ENSMUST00000094823; ENSMUSP00000092418; ENSMUSG00000066058. [Q9ET38-2]
DR GeneID; 242653; -.
DR KEGG; mmu:242653; -.
DR UCSC; uc008uls.1; mouse. [Q9ET38-1]
DR CTD; 149461; -.
DR MGI; MGI:3033992; Cldn19.
DR VEuPathDB; HostDB:ENSMUSG00000066058; -.
DR eggNOG; ENOG502QTG5; Eukaryota.
DR GeneTree; ENSGT00940000158624; -.
DR HOGENOM; CLU_076370_2_0_1; -.
DR InParanoid; Q9ET38; -.
DR OMA; ARFEFGP; -.
DR OrthoDB; 1244077at2759; -.
DR PhylomeDB; Q9ET38; -.
DR TreeFam; TF331936; -.
DR BioGRID-ORCS; 242653; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q9ET38; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9ET38; protein.
DR Bgee; ENSMUSG00000066058; Expressed in sciatic nerve and 31 other tissues.
DR ExpressionAtlas; Q9ET38; baseline and differential.
DR Genevisible; Q9ET38; MM.
DR GO; GO:0043296; C:apical junction complex; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0030054; C:cell junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
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:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0043297; P:apical junction assembly; 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; IBA:GO_Central.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0061045; P:negative regulation of wound healing; ISO:MGI.
DR GO; GO:0019227; P:neuronal action potential propagation; IMP:MGI.
DR GO; GO:1901890; P:positive regulation of cell junction assembly; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0150111; P:regulation of transepithelial transport; ISO:MGI.
DR GO; GO:0120193; P:tight junction organization; IMP:MGI.
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 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Disulfide bond; Membrane; Reference proteome; Tight junction;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..224
FT /note="Claudin-19"
FT /id="PRO_0000144782"
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 DISULFID 54..64
FT /evidence="ECO:0000269|PubMed:25678664,
FT ECO:0007744|PDB:3X29"
FT VAR_SEQ 210..224
FT /note="PVVKLPASVKGPLGV -> YV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010343"
FT MUTAGEN 35
FT /note="Y->F: No effect on interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 35
FT /note="Y->S: Abolishes interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 38
FT /note="D->A: No effect on interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 39
FT /note="A->R: Abolishes interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 39
FT /note="A->S: Strongly reduces interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 40
FT /note="I->A,S,L: Abolishes interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 40
FT /note="I->V: Strongly reduces interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 41
FT /note="I->A,S,V: Abolishes interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 41
FT /note="I->L: No effect on interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 42
FT /note="T->A,V: No effect on interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 53
FT /note="S->A: No effect on interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 146
FT /note="Q->A: No effect on interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 147
FT /note="E->A,Q,R: No effect on interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 150
FT /note="N->A,D,Q,K: Abolishes interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 150
FT /note="N->S,L: Strongly inhibits interaction with
FT Clostridium perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 151
FT /note="P->A,G: Abolishes interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 152
FT /note="S->D: Abolishes interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 152
FT /note="S->L,M,F: No effect on interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 153
FT /note="T->V,L: No effect on interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 153
FT /note="T->Y: Abolishes interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 154
FT /note="P->A: Strongly inhibits interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 154
FT /note="P->D: Abolishes interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 155
FT /note="V->I: No effect on interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 156
FT /note="N->A,S: No effect on interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 156
FT /note="N->G: Strongly inhibits interaction with Clostridium
FT perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
FT MUTAGEN 159
FT /note="Y->S,F: Strongly inhibits interaction with
FT Clostridium perfringens CPE."
FT /evidence="ECO:0000269|PubMed:25678664"
SQ SEQUENCE 224 AA; 23343 MW; 4282BE63C4D8BCD2 CRC64;
MANSGLQLLG YFLALGGWVG IIASTALPQW KQSSYAGDAI ITAVGLYEGL WMSCASQSTG
QVQCKLYDSL LALDGHIQSA RALMVVAVLL GFVAMVLSVV GMKCTRVGDS NPTAKSRVAI
SGGALFLLAG LCTLTAVSWY ATLVTQEFFN PSTPVNARYE FGPALFVGWA SAGLAMLGGS
FLCCTCPEPE RANSIPQPYR SGPSTAAREP VVKLPASVKG PLGV
