CADH7_MOUSE
ID CADH7_MOUSE Reviewed; 785 AA.
AC Q8BM92; Q3UVE2; Q67G09;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cadherin-7;
DE Flags: Precursor;
GN Name=Cdh7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=15273735; DOI=10.1038/sj.onc.1207675;
RA Moore R., Champeval D., Denat L., Tan S.S., Faure F., Julien-Grille S.,
RA Larue L.;
RT "Involvement of cadherins 7 and 20 in mouse embryogenesis and melanocyte
RT transformation.";
RL Oncogene 23:6726-6735(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Diencephalon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(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 (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; AY267034; AAP94032.1; -; mRNA.
DR EMBL; AK034096; BAC28586.1; -; mRNA.
DR EMBL; AK137369; BAE23328.1; -; mRNA.
DR CCDS; CCDS15221.1; -.
DR RefSeq; NP_001303672.1; NM_001316743.1.
DR RefSeq; NP_766441.1; NM_172853.3.
DR RefSeq; XP_006529663.1; XM_006529600.3.
DR RefSeq; XP_006529664.1; XM_006529601.3.
DR RefSeq; XP_006529671.1; XM_006529608.3.
DR RefSeq; XP_006529672.1; XM_006529609.3.
DR RefSeq; XP_006529673.1; XM_006529610.3.
DR RefSeq; XP_006529674.1; XM_006529611.3.
DR RefSeq; XP_011246308.1; XM_011248006.2.
DR RefSeq; XP_017176182.1; XM_017320693.1.
DR RefSeq; XP_017176187.1; XM_017320698.1.
DR RefSeq; XP_017176188.1; XM_017320699.1.
DR RefSeq; XP_017176190.1; XM_017320701.1.
DR RefSeq; XP_017176192.1; XM_017320703.1.
DR PDB; 6CGS; X-ray; 1.72 A; A/B=48-254.
DR PDBsum; 6CGS; -.
DR AlphaFoldDB; Q8BM92; -.
DR SMR; Q8BM92; -.
DR STRING; 10090.ENSMUSP00000108321; -.
DR GlyGen; Q8BM92; 2 sites.
DR iPTMnet; Q8BM92; -.
DR PhosphoSitePlus; Q8BM92; -.
DR PaxDb; Q8BM92; -.
DR PRIDE; Q8BM92; -.
DR ProteomicsDB; 273580; -.
DR Antibodypedia; 2257; 190 antibodies from 29 providers.
DR DNASU; 241201; -.
DR Ensembl; ENSMUST00000027542; ENSMUSP00000027542; ENSMUSG00000026312.
DR Ensembl; ENSMUST00000112701; ENSMUSP00000108321; ENSMUSG00000026312.
DR Ensembl; ENSMUST00000172005; ENSMUSP00000129715; ENSMUSG00000026312.
DR GeneID; 241201; -.
DR KEGG; mmu:241201; -.
DR UCSC; uc007chw.1; mouse.
DR CTD; 1005; -.
DR MGI; MGI:2442792; Cdh7.
DR VEuPathDB; HostDB:ENSMUSG00000026312; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000157031; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; Q8BM92; -.
DR OMA; TGPECLY; -.
DR OrthoDB; 217088at2759; -.
DR PhylomeDB; Q8BM92; -.
DR TreeFam; TF329887; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR BioGRID-ORCS; 241201; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cdh7; mouse.
DR PRO; PR:Q8BM92; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BM92; protein.
DR Bgee; ENSMUSG00000026312; Expressed in lumbar subsegment of spinal cord and 82 other tissues.
DR ExpressionAtlas; Q8BM92; baseline and differential.
DR Genevisible; Q8BM92; MM.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..47
FT /evidence="ECO:0000255"
FT /id="PRO_0000320090"
FT CHAIN 48..785
FT /note="Cadherin-7"
FT /id="PRO_0000320091"
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 CONFLICT 307
FT /note="L -> V (in Ref. 1; AAP94032)"
FT /evidence="ECO:0000305"
FT CONFLICT 580
FT /note="I -> V (in Ref. 2; BAE23328)"
FT /evidence="ECO:0000305"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:6CGS"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6CGS"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:6CGS"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 116..126
FT /evidence="ECO:0007829|PDB:6CGS"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 157..165
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:6CGS"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6CGS"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6CGS"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 225..234
FT /evidence="ECO:0007829|PDB:6CGS"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:6CGS"
FT STRAND 243..253
FT /evidence="ECO:0007829|PDB:6CGS"
SQ SEQUENCE 785 AA; 87202 MW; 112A1F409BF85CED CRC64;
MKLGKVELCH FLQLIALFLC FSGMSQAELP 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 IGVNAEMEYK
IVDGDGLGIF KISADKDTQE GIITIQKELD FEAKTSYTLR IEAANRDADP RFLSLGPFSD
TTTVKIIVED VDEPPVFSSP LYPMEVSEAT QVGHIIGTVA AHDPDSSNSP VRYSIDRNTD
LERYFNIDAN SGVITTAKSL DRETNAVHNI TVLAMESQNP SQVGRGYVAI TILDINDNAP
EFAMDYETTV CENAQPGQVI QKISAVDKDE PSNGHQFYFS LTTDMTNNHN FSLKDNKDNT
ASILTRRNGF RRQEQSVYYL PIFIVDSGSP SLSSTNTLTI RVCDCDADGI AQTCNAEAYV
LPAGLSTGAL IAILACVLTL LVLILLIVTM RRRKKEPLIF DEERDIRENI VRYDDEGGGE
EDTEAFDMAA LRNLNAIRDS KTRRDVTPEI QFLSRPTFKN IPDNVIFREF IWERLKEADV
DPGAPPYDSL QTYAFEGNGS VAESLSSLDS ISSNSDQNYD YLSDWGPRFK RLAEMYGNGQ
ESLYS
