CADH7_HUMAN
ID CADH7_HUMAN Reviewed; 785 AA.
AC Q9ULB5; Q9H157;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Cadherin-7;
DE Flags: Precursor;
GN Name=CDH7; Synonyms=CDH7L1;
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], AND VARIANT SER-576.
RX PubMed=10995570; DOI=10.1006/geno.2000.6305;
RA Kools P., Van Imschoot G., van Roy F.;
RT "Characterization of three novel human cadherin genes (CDH7, CDH19, and
RT CDH20) clustered on chromosome 18q22-q23 and with high homology to chicken
RT cadherin-7.";
RL Genomics 68:283-295(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-576.
RX PubMed=10861224; DOI=10.1042/0264-6021:3490159;
RA Shimoyama Y., Tsujimoto G., Kitajima M., Natori M.;
RT "Identification of three human type-II classic cadherins and frequent
RT heterophilic interactions between different subclasses of type-II classic
RT cadherins.";
RL Biochem. J. 349:159-167(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
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 -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain. {ECO:0000250}.
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DR EMBL; AJ007611; CAC13127.1; -; mRNA.
DR EMBL; AB035301; BAA87415.1; -; mRNA.
DR EMBL; AC023394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS11993.1; -.
DR RefSeq; NP_001304143.1; NM_001317214.1.
DR RefSeq; NP_004352.2; NM_004361.3.
DR RefSeq; NP_387450.1; NM_033646.2.
DR RefSeq; XP_016881012.1; XM_017025523.1.
DR AlphaFoldDB; Q9ULB5; -.
DR SMR; Q9ULB5; -.
DR BioGRID; 107440; 2.
DR IntAct; Q9ULB5; 1.
DR STRING; 9606.ENSP00000381058; -.
DR GlyGen; Q9ULB5; 2 sites.
DR iPTMnet; Q9ULB5; -.
DR PhosphoSitePlus; Q9ULB5; -.
DR BioMuta; CDH7; -.
DR DMDM; 296434420; -.
DR MassIVE; Q9ULB5; -.
DR PaxDb; Q9ULB5; -.
DR PeptideAtlas; Q9ULB5; -.
DR PRIDE; Q9ULB5; -.
DR ProteomicsDB; 84971; -.
DR Antibodypedia; 2257; 190 antibodies from 29 providers.
DR DNASU; 1005; -.
DR Ensembl; ENST00000323011.7; ENSP00000319166.3; ENSG00000081138.14.
DR Ensembl; ENST00000397968.4; ENSP00000381058.2; ENSG00000081138.14.
DR GeneID; 1005; -.
DR KEGG; hsa:1005; -.
DR MANE-Select; ENST00000397968.4; ENSP00000381058.2; NM_004361.5; NP_004352.2.
DR UCSC; uc002ljz.3; human.
DR CTD; 1005; -.
DR DisGeNET; 1005; -.
DR GeneCards; CDH7; -.
DR HGNC; HGNC:1766; CDH7.
DR HPA; ENSG00000081138; Tissue enriched (brain).
DR MIM; 605806; gene.
DR neXtProt; NX_Q9ULB5; -.
DR OpenTargets; ENSG00000081138; -.
DR PharmGKB; PA26303; -.
DR VEuPathDB; HostDB:ENSG00000081138; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000157031; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; Q9ULB5; -.
DR OMA; TGPECLY; -.
DR OrthoDB; 217088at2759; -.
DR PhylomeDB; Q9ULB5; -.
DR TreeFam; TF329887; -.
DR PathwayCommons; Q9ULB5; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR SignaLink; Q9ULB5; -.
DR SIGNOR; Q9ULB5; -.
DR BioGRID-ORCS; 1005; 9 hits in 1060 CRISPR screens.
DR ChiTaRS; CDH7; human.
DR GenomeRNAi; 1005; -.
DR Pharos; Q9ULB5; Tbio.
DR PRO; PR:Q9ULB5; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9ULB5; protein.
DR Bgee; ENSG00000081138; Expressed in sural nerve and 58 other tissues.
DR ExpressionAtlas; Q9ULB5; baseline and differential.
DR Genevisible; Q9ULB5; 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; TAS:Reactome.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
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:0098609; P:cell-cell adhesion; NAS:UniProtKB.
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 Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW Glycoprotein; Membrane; Metal-binding; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..47
FT /evidence="ECO:0000255"
FT /id="PRO_0000003769"
FT CHAIN 48..785
FT /note="Cadherin-7"
FT /id="PRO_0000003770"
FT TOPO_DOM 28..607
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 629..785
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 49..153
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 154..262
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 263..377
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 378..482
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 482..599
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 370
FT /note="D -> E (in dbSNP:rs2306675)"
FT /id="VAR_061057"
FT VARIANT 576
FT /note="N -> S (in dbSNP:rs2291343)"
FT /evidence="ECO:0000269|PubMed:10861224,
FT ECO:0000269|PubMed:10995570"
FT /id="VAR_060247"
FT CONFLICT 23
FT /note="G -> E (in Ref. 1; CAC13127)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="S -> P (in Ref. 1; CAC13127)"
FT /evidence="ECO:0000305"
FT CONFLICT 591..600
FT /note="AQTCNAEAYV -> TQTAMQRLC (in Ref. 1; CAC13127)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 785 AA; 87086 MW; 3C504CD1C620F4BC CRC64;
MKLGKVEFCH FLQLIALFLC FSGMSQAELS RSRSKPYFQS GRSRTKRSWV WNQFFVLEEY
MGSDPLYVGK LHSDVDKGDG SIKYILSGEG ASSIFIIDEN TGDIHATKRL DREEQAYYTL
RAQALDRLTN KPVEPESEFV IKIQDINDNE PKFLDGPYTA GVPEMSPVGT SVVQVTATDA
DDPTYGNSAR VVYSILQGQP YFSVEPKTGV IKTALPNMDR EAKDQYLLVI QAKDMVGQNG
GLSGTTSVTV TLTDVNDNPP RFPRRSYQYN VPESLPVASV VARIKAADAD IGANAEMEYK
IVDGDGLGIF KISVDKETQE GIITIQKELD FEAKTSYTLR IEAANKDADP RFLSLGPFSD
TTTVKIIVED VDEPPVFSSP LYPMEVSEAT QVGNIIGTVA AHDPDSSNSP VRYSIDRNTD
LERYFNIDAN SGVITTAKSL DRETNAIHNI TVLAMESQNP SQVGRGYVAI TILDINDNAP
EFAMDYETTV CENAQPGQVI QKISAVDKDE PSNGHQFYFS LTTDATNNHN FSLKDNKDNT
ASILTRRNGF RRQEQSVYYL PIFIVDSGSP SLSSTNTLTI RVCDCDADGV AQTCNAEAYV
LPAGLSTGAL IAILACVLTL LVLILLIVTM RRRKKEPLIF DEERDIRENI VRYDDEGGGE
EDTEAFDMAA LRNLNVIRDT KTRRDVTPEI QFLSRPAFKS IPDNVIFREF IWERLKEADV
DPGAPPYDSL QTYAFEGNGS VAESLSSLDS ISSNSDQNYD YLSDWGPRFK RLADMYGTGQ
ESLYS
