CLD9_HUMAN
ID CLD9_HUMAN Reviewed; 217 AA.
AC O95484;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Claudin-9;
GN Name=CLDN9;
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 [GENOMIC DNA].
RA Keen T.J., Inglehearn C.F.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Pituitary;
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 [3]
RP TISSUE SPECIFICITY, FUNCTION (MICROBIAL INFECTION), AND MUTAGENESIS OF
RP ASN-38; ALA-43; VAL-45 AND SER-53.
RX PubMed=17804490; DOI=10.1128/jvi.01457-07;
RA Zheng A., Yuan F., Li Y., Zhu F., Hou P., Li J., Song X., Ding M., Deng H.;
RT "Claudin-6 and claudin-9 function as additional coreceptors for hepatitis C
RT virus.";
RL J. Virol. 81:12465-12471(2007).
RN [4]
RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND INTERACTION WITH
RP CLDN1; CD81 AND OCLN.
RX PubMed=20375010; DOI=10.1074/jbc.m110.104836;
RA Harris H.J., Davis C., Mullins J.G., Hu K., Goodall M., Farquhar M.J.,
RA Mee C.J., McCaffrey K., Young S., Drummer H., Balfe P., McKeating J.A.;
RT "Claudin association with CD81 defines hepatitis C virus entry.";
RL J. Biol. Chem. 285:21092-21102(2010).
RN [5]
RP INVOLVEMENT IN DFNB116, AND SUBCELLULAR LOCATION.
RX PubMed=31175426; DOI=10.1007/s00439-019-02037-1;
RA Sineni C.J., Yildirim-Baylan M., Guo S., Camarena V., Wang G.,
RA Tokgoz-Yilmaz S., Duman D., Bademci G., Tekin M.;
RT "A truncating CLDN9 variant is associated with autosomal recessive
RT nonsyndromic hearing loss.";
RL Hum. Genet. 138:1071-1075(2019).
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:O95832}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C
CC virus (HCV) entry into hepatic cells. {ECO:0000269|PubMed:17804490,
CC ECO:0000269|PubMed:20375010}.
CC -!- SUBUNIT: Interacts with CLDN1, CD81 and OCLN (PubMed:20375010).
CC {ECO:0000269|PubMed:20375010}.
CC -!- INTERACTION:
CC O95484; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-18341636, EBI-10827839;
CC O95484; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-18341636, EBI-19125216;
CC O95484; Q16853: AOC3; NbExp=3; IntAct=EBI-18341636, EBI-3921628;
CC O95484; Q12983: BNIP3; NbExp=3; IntAct=EBI-18341636, EBI-749464;
CC O95484; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-18341636, EBI-12003442;
CC O95484; P49447: CYB561; NbExp=3; IntAct=EBI-18341636, EBI-8646596;
CC O95484; P54849: EMP1; NbExp=3; IntAct=EBI-18341636, EBI-4319440;
CC O95484; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-18341636, EBI-10976398;
CC O95484; Q92935: EXTL1; NbExp=3; IntAct=EBI-18341636, EBI-1760167;
CC O95484; Q14416: GRM2; NbExp=3; IntAct=EBI-18341636, EBI-10232876;
CC O95484; P24593: IGFBP5; NbExp=3; IntAct=EBI-18341636, EBI-720480;
CC O95484; Q9UBY5: LPAR3; NbExp=3; IntAct=EBI-18341636, EBI-12033434;
CC O95484; P21145: MAL; NbExp=3; IntAct=EBI-18341636, EBI-3932027;
CC O95484; Q13021: MALL; NbExp=3; IntAct=EBI-18341636, EBI-750078;
CC O95484; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-18341636, EBI-11721828;
CC O95484; Q96GM1: PLPPR2; NbExp=3; IntAct=EBI-18341636, EBI-12955265;
CC O95484; Q9NS64: RPRM; NbExp=3; IntAct=EBI-18341636, EBI-1052363;
CC O95484; Q9UNK0: STX8; NbExp=3; IntAct=EBI-18341636, EBI-727240;
CC O95484; Q6UX27-3: VSTM1; NbExp=3; IntAct=EBI-18341636, EBI-12190699;
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane
CC {ECO:0000269|PubMed:20375010, ECO:0000269|PubMed:31175426}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the liver, in peripheral blood
CC mononuclear cells and hepatocarcinoma cell lines.
CC {ECO:0000269|PubMed:17804490}.
CC -!- DISEASE: Deafness, autosomal recessive, 116 (DFNB116) [MIM:619093]: A
CC form of non-syndromic deafness characterized by slowly progressive,
CC moderate to profound sensorineural hearing loss. Sensorineural deafness
CC results from damage to the neural receptors of the inner ear, the nerve
CC pathways to the brain, or the area of the brain that receives sound
CC information. {ECO:0000269|PubMed:31175426}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
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/CLDN9ID51555ch16p13.html";
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DR EMBL; AJ130941; CAA10254.1; -; Genomic_DNA.
DR EMBL; BC051870; AAH51870.1; -; mRNA.
DR EMBL; BC065830; AAH65830.1; -; mRNA.
DR CCDS; CCDS10487.1; -.
DR RefSeq; NP_066192.1; NM_020982.3.
DR PDB; 6OV2; X-ray; 3.20 A; A=1-217.
DR PDB; 6OV3; X-ray; 3.25 A; A=1-217.
DR PDBsum; 6OV2; -.
DR PDBsum; 6OV3; -.
DR AlphaFoldDB; O95484; -.
DR SMR; O95484; -.
DR BioGRID; 114536; 17.
DR IntAct; O95484; 19.
DR STRING; 9606.ENSP00000398017; -.
DR iPTMnet; O95484; -.
DR PhosphoSitePlus; O95484; -.
DR BioMuta; CLDN9; -.
DR jPOST; O95484; -.
DR MassIVE; O95484; -.
DR MaxQB; O95484; -.
DR PaxDb; O95484; -.
DR PeptideAtlas; O95484; -.
DR PRIDE; O95484; -.
DR ProteomicsDB; 50911; -.
DR ABCD; O95484; 3 sequenced antibodies.
DR Antibodypedia; 10653; 93 antibodies from 28 providers.
DR DNASU; 9080; -.
DR Ensembl; ENST00000445369.3; ENSP00000398017.2; ENSG00000213937.4.
DR GeneID; 9080; -.
DR KEGG; hsa:9080; -.
DR MANE-Select; ENST00000445369.3; ENSP00000398017.2; NM_020982.4; NP_066192.1.
DR UCSC; uc010uwo.1; human.
DR CTD; 9080; -.
DR DisGeNET; 9080; -.
DR GeneCards; CLDN9; -.
DR HGNC; HGNC:2051; CLDN9.
DR HPA; ENSG00000213937; Tissue enhanced (brain, pituitary gland).
DR MalaCards; CLDN9; -.
DR MIM; 615799; gene.
DR MIM; 619093; phenotype.
DR neXtProt; NX_O95484; -.
DR OpenTargets; ENSG00000213937; -.
DR PharmGKB; PA26577; -.
DR VEuPathDB; HostDB:ENSG00000213937; -.
DR eggNOG; ENOG502QRZ8; Eukaryota.
DR GeneTree; ENSGT00940000162145; -.
DR HOGENOM; CLU_076370_1_2_1; -.
DR InParanoid; O95484; -.
DR OMA; YNPMVPD; -.
DR OrthoDB; 1231389at2759; -.
DR PhylomeDB; O95484; -.
DR TreeFam; TF331936; -.
DR PathwayCommons; O95484; -.
DR Reactome; R-HSA-420029; Tight junction interactions.
DR SignaLink; O95484; -.
DR BioGRID-ORCS; 9080; 28 hits in 1066 CRISPR screens.
DR GeneWiki; CLDN9; -.
DR GenomeRNAi; 9080; -.
DR Pharos; O95484; Tbio.
DR PRO; PR:O95484; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O95484; protein.
DR Bgee; ENSG00000213937; Expressed in right hemisphere of cerebellum and 92 other tissues.
DR Genevisible; O95484; HS.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
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:0001618; F:virus receptor activity; IMP:UniProtKB.
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 InterPro; IPR006187; Claudin.
DR InterPro; IPR003553; Claudin9.
DR InterPro; IPR017974; Claudin_CS.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR PANTHER; PTHR12002; PTHR12002; 1.
DR PANTHER; PTHR12002:SF42; PTHR12002:SF42; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01382; CLAUDIN9.
DR PROSITE; PS01346; CLAUDIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell membrane; Deafness;
KW Host cell receptor for virus entry; Host-virus interaction; Membrane;
KW Non-syndromic deafness; Receptor; Reference proteome; Tight junction;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..217
FT /note="Claudin-9"
FT /id="PRO_0000144755"
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..159
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 194..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 38
FT /note="N->S: Mildly decrease HCV infection susceptibility
FT in cell culture."
FT /evidence="ECO:0000269|PubMed:17804490"
FT MUTAGEN 43
FT /note="A->S: No effect on HCV infection susceptibility in
FT cell culture."
FT /evidence="ECO:0000269|PubMed:17804490"
FT MUTAGEN 45
FT /note="V->N: Abolishes HCV infection susceptibility in cell
FT culture."
FT /evidence="ECO:0000269|PubMed:17804490"
FT MUTAGEN 53
FT /note="S->N: No effect on HCV infection susceptibility in
FT cell culture."
FT /evidence="ECO:0000269|PubMed:17804490"
FT HELIX 6..25
FT /evidence="ECO:0007829|PDB:6OV2"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:6OV3"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:6OV2"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:6OV3"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:6OV2"
FT STRAND 50..60
FT /evidence="ECO:0007829|PDB:6OV2"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:6OV2"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6OV3"
FT HELIX 75..98
FT /evidence="ECO:0007829|PDB:6OV2"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:6OV3"
FT HELIX 111..144
FT /evidence="ECO:0007829|PDB:6OV2"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:6OV2"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:6OV3"
FT HELIX 162..182
FT /evidence="ECO:0007829|PDB:6OV2"
SQ SEQUENCE 217 AA; 22848 MW; 0E49C5B5CB3AAC9C CRC64;
MASTGLELLG MTLAVLGWLG TLVSCALPLW KVTAFIGNSI VVAQVVWEGL WMSCVVQSTG
QMQCKVYDSL LALPQDLQAA RALCVIALLL ALLGLLVAIT GAQCTTCVED EGAKARIVLT
AGVILLLAGI LVLIPVCWTA HAIIQDFYNP LVAEALKREL GASLYLGWAA AALLMLGGGL
LCCTCPPPQV ERPRGPRLGY SIPSRSGASG LDKRDYV
