CADH9_HUMAN
ID CADH9_HUMAN Reviewed; 789 AA.
AC Q9ULB4; Q3B7I5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Cadherin-9;
DE Flags: Precursor;
GN Name=CDH9;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS CYS-6 AND VAL-38.
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).
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 {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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; AB035302; BAA87416.1; -; mRNA.
DR EMBL; BC107594; AAI07595.1; -; mRNA.
DR EMBL; BC113745; AAI13746.1; -; mRNA.
DR CCDS; CCDS3893.1; -.
DR RefSeq; NP_057363.3; NM_016279.3.
DR AlphaFoldDB; Q9ULB4; -.
DR SMR; Q9ULB4; -.
DR BioGRID; 107442; 5.
DR IntAct; Q9ULB4; 2.
DR STRING; 9606.ENSP00000231021; -.
DR GlyGen; Q9ULB4; 4 sites.
DR iPTMnet; Q9ULB4; -.
DR PhosphoSitePlus; Q9ULB4; -.
DR BioMuta; CDH9; -.
DR DMDM; 119370307; -.
DR jPOST; Q9ULB4; -.
DR MassIVE; Q9ULB4; -.
DR MaxQB; Q9ULB4; -.
DR PaxDb; Q9ULB4; -.
DR PeptideAtlas; Q9ULB4; -.
DR PRIDE; Q9ULB4; -.
DR ProteomicsDB; 84970; -.
DR Antibodypedia; 2349; 181 antibodies from 29 providers.
DR DNASU; 1007; -.
DR Ensembl; ENST00000231021.9; ENSP00000231021.4; ENSG00000113100.10.
DR GeneID; 1007; -.
DR KEGG; hsa:1007; -.
DR MANE-Select; ENST00000231021.9; ENSP00000231021.4; NM_016279.4; NP_057363.3.
DR UCSC; uc003jgs.2; human.
DR CTD; 1007; -.
DR DisGeNET; 1007; -.
DR GeneCards; CDH9; -.
DR HGNC; HGNC:1768; CDH9.
DR HPA; ENSG00000113100; Tissue enhanced (brain, kidney).
DR MIM; 609974; gene.
DR neXtProt; NX_Q9ULB4; -.
DR OpenTargets; ENSG00000113100; -.
DR PharmGKB; PA26305; -.
DR VEuPathDB; HostDB:ENSG00000113100; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000160496; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; Q9ULB4; -.
DR OMA; CIPLFIW; -.
DR OrthoDB; 201053at2759; -.
DR PhylomeDB; Q9ULB4; -.
DR TreeFam; TF329887; -.
DR PathwayCommons; Q9ULB4; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR SignaLink; Q9ULB4; -.
DR SIGNOR; Q9ULB4; -.
DR BioGRID-ORCS; 1007; 7 hits in 1059 CRISPR screens.
DR GeneWiki; CDH9; -.
DR GenomeRNAi; 1007; -.
DR Pharos; Q9ULB4; Tbio.
DR PRO; PR:Q9ULB4; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9ULB4; protein.
DR Bgee; ENSG00000113100; Expressed in endothelial cell and 94 other tissues.
DR ExpressionAtlas; Q9ULB4; baseline and differential.
DR Genevisible; Q9ULB4; 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; 2.
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; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..53
FT /evidence="ECO:0000255"
FT /id="PRO_0000003779"
FT CHAIN 54..789
FT /note="Cadherin-9"
FT /id="PRO_0000003780"
FT TOPO_DOM 54..615
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 637..789
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 54..159
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 160..268
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 269..383
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 384..486
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 487..608
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97326"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 6
FT /note="Y -> C (in dbSNP:rs2288467)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029799"
FT VARIANT 38
FT /note="A -> V (in dbSNP:rs2288466)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029800"
FT CONFLICT 18
FT /note="T -> I (in Ref. 1; BAA87416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 789 AA; 88689 MW; C580DA16B769047C CRC64;
MRTYHYIPLF IWTYMFHTVD TILLQEKPNS YLSSKKIAGL TKDDGKMLRR TKRGWMWNQF
FLLEEYTGTD TQYVGKLHTD QDKGDGNLKY ILTGDGAGSL FVIDENTGDI HAAKKLDREE
KSLYILRAKA IDRKTGRQVE PESEFIIKIH DINDNEPKFT KDLYTASVPE MSGVGTSVIQ
VTATDADDAN YGNSAKVVYS ILQGQPYFSV DPESGIIKTA LPDMSRENRE QYQVVIQAKD
MGGQMGGLSG TTTVNITLTD VNNNPPRFPQ STYQFNSPES VPLGTHLGRI KANDPDVGEN
AEMEYSIAEG DGADMFDVIT DKDTQEGIIT VKQNLDFENQ MLYTLRVDAS NTHPDPRFLH
LGPFKDTAVV KISVEDIDEP PVFTKVSYLI EVDEDVKEGS IIGQVTAYDP DARNNLIKYS
VDRHTDMDRI FGIHSENGSI FTLKALDRES SPWHNITVTA TEINNPKQSS HIPVFIRILD
INDHAPEFAM YYETFVCENA KPGQLIQTVS VMDKDDPPRG HKFFFEPVPE FTLNPNFTIV
DNKDNTAGIM TRKDGYSRNK MSTYLLPILI FDNDYPIQSS TGTLTIRVCA CDNQGNMQSC
TAEALILSAG LSTGALVAIL LCVLILLILV VLFAALKRQR KKEPLIISKD DVRDNIVTYN
DEGGGEEDTQ AFDIGTLRNP EAREDSKLRR DVMPETIFQI RRTVPLWENI DVQDFIHRRL
KENDADPSAP PYDSLATYAY EGNDSIADSL SSLESLTADC NQDYDYLSDW GPRFKKLADM
YGGDDSDRD
