CADH7_RAT
ID CADH7_RAT Reviewed; 785 AA.
AC Q5DWV2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Cadherin-7;
DE Flags: Precursor;
GN Name=Cdh7; Synonyms=Cad7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Takahashi M., Osumi N.;
RT "Expressions of rat cadherin-7 and 20 in the developing nervous system.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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; AB121031; BAD90595.1; -; mRNA.
DR RefSeq; NP_001012755.1; NM_001012737.1.
DR AlphaFoldDB; Q5DWV2; -.
DR SMR; Q5DWV2; -.
DR STRING; 10116.ENSRNOP00000049491; -.
DR GlyGen; Q5DWV2; 2 sites.
DR PaxDb; Q5DWV2; -.
DR PRIDE; Q5DWV2; -.
DR GeneID; 29162; -.
DR KEGG; rno:29162; -.
DR UCSC; RGD:1306856; rat.
DR CTD; 1005; -.
DR RGD; 1306856; Cdh7.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q5DWV2; -.
DR PhylomeDB; Q5DWV2; -.
DR Reactome; R-RNO-418990; Adherens junctions interactions.
DR PRO; PR:Q5DWV2; -.
DR Proteomes; UP000002494; Unplaced.
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: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: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_0000320092"
FT CHAIN 48..785
FT /note="Cadherin-7"
FT /id="PRO_0000320093"
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"
SQ SEQUENCE 785 AA; 87270 MW; AAA4A157449FD55F CRC64;
MKLGKVELCR FLQLIALFLC FSGMNQAELP RSRSKPYFQL GRSRTKRSWV WNQFFVLEEY
MGSDPLYVGK LHSDVDKGDG FIKYILSGEG ASSIFIIDEN TGDIHATKRL DREEQAYYTL
RAQALDRLTN KPVEPESEFV IKIQDINDNE PKFLDGPYTA GVPEMSPVGT SVVQVTATDA
DDPTYGNSAR VVYSILQGQP YFSVEPKTGV IKTALPNMDR EAKDQYLLVI QAKDMVGQNG
GLSGTTSVTV TLTDVNDNPP RFPRRSYQYN GPESLPVASV VARIKAADAD IGVNAEMEYK
IVDGDGLGIF KISPDKDTQE GIITIQKELD FEAKTSYTLR IEAANRDADP RFLSLGPFSD
TTTVKIIVED VDEPPVFSSP LYPMEVSEAT QVGHIIGTVA AHDPDSSNSP VRYSIDRNTD
LERYFNIDAN SGIITTAKSL DRETNPVHNI TVLAMESQNP SQVGRGYVAI TILDINDNAP
EFAMDYETTV CENAQPGQVI QKISAIDKDE PSNGHQFYFS LTTDMANNLN SSLKDNKDNT
ASILTRRNGF RRQEQSVYYL PIFIVDNGSP SLSSTNTLTI RVCDCDADGI AQTCNAEAYI
LPAGLSTGAL IAILACVLTL LVLILLIVTM KRRKKEPLIF DEERDIRENI VRYDDEGGGE
EDTEAFDMAA LRNLNVVRDT KTRRDVTPEI QFLSRPTFKN IPDNVIFREF IWERLKEADV
DPGAPPYDSL QTYAFEGNGS VAESLGSLDS NSSNSDQNYD YLSDWGPRFK RLAEMYGNGQ
ESLYS
