CDHR3_HUMAN
ID CDHR3_HUMAN Reviewed; 885 AA.
AC Q6ZTQ4; Q8TCI7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Cadherin-related family member 3;
DE AltName: Full=Cadherin-like protein 28;
DE Flags: Precursor;
GN Name=CDHR3; Synonyms=CDH28;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Ileal mucosa, and Trachea;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT TYR-529, SUBCELLULAR
RP LOCATION, AND INVOLVEMENT IN SUSCEPTIBILITY TO ASTHMA.
RX PubMed=24241537; DOI=10.1038/ng.2830;
RA Bonnelykke K., Sleiman P., Nielsen K., Kreiner-Moller E., Mercader J.M.,
RA Belgrave D., den Dekker H.T., Husby A., Sevelsted A., Faura-Tellez G.,
RA Mortensen L.J., Paternoster L., Flaaten R., Molgaard A., Smart D.E.,
RA Thomsen P.F., Rasmussen M.A., Bonas-Guarch S., Holst C., Nohr E.A.,
RA Yadav R., March M.E., Blicher T., Lackie P.M., Jaddoe V.W., Simpson A.,
RA Holloway J.W., Duijts L., Custovic A., Davies D.E., Torrents D., Gupta R.,
RA Hollegaard M.V., Hougaard D.M., Hakonarson H., Bisgaard H.;
RT "A genome-wide association study identifies CDHR3 as a susceptibility locus
RT for early childhood asthma with severe exacerbations.";
RL Nat. Genet. 46:51-55(2014).
RN [5]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=25848009; DOI=10.1073/pnas.1421178112;
RA Bochkov Y.A., Watters K., Ashraf S., Griggs T.F., Devries M.K.,
RA Jackson D.J., Palmenberg A.C., Gern J.E.;
RT "Cadherin-related family member 3, a childhood asthma susceptibility gene
RT product, mediates rhinovirus C binding and replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:5485-5490(2015).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC preferentially interact with themselves in a homophilic manner in
CC connecting cells; cadherins may thus contribute to the sorting of
CC heterogeneous cell types.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for rhinovirus C.
CC {ECO:0000269|PubMed:25848009}.
CC -!- SUBUNIT: (Microbial infection) Interacts with rhinovirus C capsid
CC proteins. {ECO:0000269|PubMed:25848009}.
CC -!- INTERACTION:
CC Q6ZTQ4; P42331-2: ARHGAP25; NbExp=3; IntAct=EBI-12143631, EBI-21499901;
CC Q6ZTQ4; P50990: CCT8; NbExp=3; IntAct=EBI-12143631, EBI-356507;
CC Q6ZTQ4; Q13286: CLN3; NbExp=3; IntAct=EBI-12143631, EBI-3248760;
CC Q6ZTQ4; Q8TB03: CXorf38; NbExp=3; IntAct=EBI-12143631, EBI-12024320;
CC Q6ZTQ4; Q969S2: NEIL2; NbExp=3; IntAct=EBI-12143631, EBI-10281234;
CC Q6ZTQ4; Q9HBI0: PARVG; NbExp=3; IntAct=EBI-12143631, EBI-3921217;
CC Q6ZTQ4; P49458: SRP9; NbExp=3; IntAct=EBI-12143631, EBI-350743;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24241537};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZTQ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZTQ4-2; Sequence=VSP_028352, VSP_028353, VSP_028354;
CC -!- TISSUE SPECIFICITY: Expressed in bronchial epithelium from adults and
CC in fetal lung tissue. {ECO:0000269|PubMed:24241537}.
CC -!- DISEASE: Note=Asthma susceptibility may be associated with variants
CC affecting the gene represented in this entry in early childhood asthma
CC with severe exacerbations occurring between 2 and 6 years of age.
CC {ECO:0000269|PubMed:24241537}.
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DR EMBL; AK074414; BAB85073.1; -; mRNA.
DR EMBL; AK126338; BAC86529.1; -; mRNA.
DR EMBL; CH236947; EAL24403.1; -; Genomic_DNA.
DR EMBL; BC111696; AAI11697.1; -; mRNA.
DR EMBL; BC111738; AAI11739.1; -; mRNA.
DR CCDS; CCDS47684.1; -. [Q6ZTQ4-1]
DR RefSeq; NP_001288090.1; NM_001301161.1.
DR RefSeq; NP_689963.2; NM_152750.4. [Q6ZTQ4-1]
DR PDB; 6PPO; EM; 3.20 A; U=20-130.
DR PDB; 6PSF; EM; 3.50 A; U=20-237.
DR PDB; 7KNV; NMR; -; A=21-130.
DR PDBsum; 6PPO; -.
DR PDBsum; 6PSF; -.
DR PDBsum; 7KNV; -.
DR AlphaFoldDB; Q6ZTQ4; -.
DR SMR; Q6ZTQ4; -.
DR BioGRID; 128795; 45.
DR IntAct; Q6ZTQ4; 7.
DR STRING; 9606.ENSP00000325954; -.
DR GlyGen; Q6ZTQ4; 3 sites.
DR iPTMnet; Q6ZTQ4; -.
DR PhosphoSitePlus; Q6ZTQ4; -.
DR BioMuta; CDHR3; -.
DR DMDM; 74758833; -.
DR EPD; Q6ZTQ4; -.
DR jPOST; Q6ZTQ4; -.
DR MassIVE; Q6ZTQ4; -.
DR PaxDb; Q6ZTQ4; -.
DR PeptideAtlas; Q6ZTQ4; -.
DR PRIDE; Q6ZTQ4; -.
DR ProteomicsDB; 68286; -. [Q6ZTQ4-1]
DR ProteomicsDB; 68287; -. [Q6ZTQ4-2]
DR Antibodypedia; 2413; 65 antibodies from 16 providers.
DR DNASU; 222256; -.
DR Ensembl; ENST00000317716.14; ENSP00000325954.9; ENSG00000128536.16. [Q6ZTQ4-1]
DR GeneID; 222256; -.
DR KEGG; hsa:222256; -.
DR MANE-Select; ENST00000317716.14; ENSP00000325954.9; NM_152750.5; NP_689963.2.
DR UCSC; uc003vdl.5; human. [Q6ZTQ4-1]
DR CTD; 222256; -.
DR DisGeNET; 222256; -.
DR GeneCards; CDHR3; -.
DR HGNC; HGNC:26308; CDHR3.
DR HPA; ENSG00000128536; Group enriched (choroid plexus, fallopian tube).
DR MIM; 615610; gene.
DR neXtProt; NX_Q6ZTQ4; -.
DR OpenTargets; ENSG00000128536; -.
DR PharmGKB; PA165617747; -.
DR VEuPathDB; HostDB:ENSG00000128536; -.
DR eggNOG; KOG3594; Eukaryota.
DR eggNOG; KOG4289; Eukaryota.
DR GeneTree; ENSGT00940000161245; -.
DR InParanoid; Q6ZTQ4; -.
DR OMA; AGHKSFH; -.
DR OrthoDB; 592155at2759; -.
DR PhylomeDB; Q6ZTQ4; -.
DR TreeFam; TF336601; -.
DR PathwayCommons; Q6ZTQ4; -.
DR SignaLink; Q6ZTQ4; -.
DR BioGRID-ORCS; 222256; 10 hits in 1064 CRISPR screens.
DR ChiTaRS; CDHR3; human.
DR GenomeRNAi; 222256; -.
DR Pharos; Q6ZTQ4; Tbio.
DR PRO; PR:Q6ZTQ4; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q6ZTQ4; protein.
DR Bgee; ENSG00000128536; Expressed in right uterine tube and 112 other tissues.
DR ExpressionAtlas; Q6ZTQ4; baseline and differential.
DR Genevisible; Q6ZTQ4; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR Pfam; PF00028; Cadherin; 3.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Asthma; Calcium; Cell adhesion;
KW Cell membrane; Glycoprotein; Host cell receptor for virus entry;
KW Host-virus interaction; Membrane; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..885
FT /note="Cadherin-related family member 3"
FT /id="PRO_0000305903"
FT TOPO_DOM 20..713
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 735..885
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..132
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 136..236
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 237..344
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 346..466
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 462..566
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 567..695
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 808..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..283
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028352"
FT VAR_SEQ 477..560
FT /note="RTRVGQVRATDKDLPQSSLLYSISTGGASLQYPNVFWINPKTGELQLVTKVD
FT CETTPIYILRIQATNNEDTSSVTVTVNILEEN -> QGHLSGPEEKRLLSICMVRAVCH
FT HFGLHIASGSPRVPGRPIGQSRPQTLPLQDWEEQGTSDKERRNEDCRERRRGGNYPDEH
FT YL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028353"
FT VAR_SEQ 561..885
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028354"
FT VARIANT 55
FT /note="V -> M (in dbSNP:rs35008315)"
FT /id="VAR_035228"
FT VARIANT 61
FT /note="Q -> H (in dbSNP:rs34426483)"
FT /id="VAR_035229"
FT VARIANT 529
FT /note="C -> Y (increases cell surface expression;
FT dbSNP:rs6967330)"
FT /evidence="ECO:0000269|PubMed:24241537"
FT /id="VAR_035230"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6PPO"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:6PPO"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:6PPO"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:6PPO"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:6PPO"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6PPO"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:6PPO"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6PPO"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:6PPO"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:6PPO"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6PPO"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:6PPO"
SQ SEQUENCE 885 AA; 97977 MW; CDF0EEAFA904E9BE CRC64;
MQEAIILLAL LGAMSGGEAL HLILLPATGN VAENSPPGTS VHKFSVKLSA SLSPVIPGFP
QIVNSNPLTE AFRVNWLSGT YFEVVTTGME QLDFETGPNI FDLQIYVKDE VGVTDLQVLT
VQVTDVNEPP QFQGNLAEGL HLYIVERANP GFIYQVEAFD PEDTSRNIPL SYFLISPPKS
FRMSANGTLF STTELDFEAG HRSFHLIVEV RDSGGLKAST ELQVNIVNLN DEVPRFTSPT
RVYTVLEELS PGTIVANITA EDPDDEGFPS HLLYSITTVS KYFMINQLTG TIQVAQRIDR
DAGELRQNPT ISLEVLVKDR PYGGQENRIQ ITFIVEDVND NPATCQKFTF SIMVPERTAK
GTLLLDLNKF CFDDDSEAPN NRFNFTMPSG VGSGSRFLQD PAGSGKIVLI GDLDYENPSN
LAAGNKYTVI IQVQDVAPPY YKNNVYVYIL TSPENEFPLI FDRPSYVFDV SERRPARTRV
GQVRATDKDL PQSSLLYSIS TGGASLQYPN VFWINPKTGE LQLVTKVDCE TTPIYILRIQ
ATNNEDTSSV TVTVNILEEN DEKPICTPNS YFLALPVDLK VGTNIQNFKL TCTDLDSSPR
SFRYSIGPGN VNNHFTFSPN AGSNVTRLLL TSRFDYAGGF DKIWDYKLLV YVTDDNLMSD
RKKAEALVET GTVTLSIKVI PHPTTIITTT PRPRVTYQVL RKNVYSPSAW YVPFVITLGS
ILLLGLLVYL VVLLAKAIHR HCPCKTGKNK EPLTKKGETK TAERDVVVET IQMNTIFDGE
AIDPVTGETY EFNSKTGARK WKDPLTQMPK WKESSHQGAA PRRVTAGEGM GSLRSANWEE
DELSGKAWAE DAGLGSRNEG GKLGNPKNRN PAFMNRAYPK PHPGK
