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CAD20_MOUSE
ID   CAD20_MOUSE             Reviewed;         801 AA.
AC   Q9Z0M3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Cadherin-20;
DE   AltName: Full=Cadherin-7;
DE   Flags: Precursor;
GN   Name=Cdh20; Synonyms=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], AND TISSUE SPECIFICITY.
RC   STRAIN=SWR/J; TISSUE=Eye;
RX   PubMed=10433813; DOI=10.1006/mcne.1999.0764;
RA   Faulkner-Jones B.E., Godinho L.N., Reese B.E., Pasquini G.F., Ruefli A.,
RA   Tan S.S.;
RT   "Cloning and expression of mouse cadherin-7, a type-II cadherin isolated
RT   from the developing eye.";
RL   Mol. Cell. Neurosci. 14:1-16(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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, AND DEVELOPMENTAL STAGE.
RC   STRAIN=BALB/cJ;
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).
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   -!- TISSUE SPECIFICITY: Expressed in brain. Highest level of expression in
CC       the retina. In embryo it is synthesized by the forebrain, anterior
CC       neural ridge, developing visual system, primitive external granular
CC       layer of the cerebellum and a subset of neural crest cells likely to
CC       develop into melanoblasts. {ECO:0000269|PubMed:10433813,
CC       ECO:0000269|PubMed:15273735}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis.
CC       {ECO:0000269|PubMed:15273735}.
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; AF007116; AAD01278.1; -; mRNA.
DR   EMBL; AK034475; BAC28721.1; -; mRNA.
DR   EMBL; BC119606; AAI19607.1; -; mRNA.
DR   EMBL; BC119607; AAI19608.1; -; mRNA.
DR   CCDS; CCDS15203.1; -.
DR   RefSeq; NP_035930.1; NM_011800.4.
DR   AlphaFoldDB; Q9Z0M3; -.
DR   SMR; Q9Z0M3; -.
DR   STRING; 10090.ENSMUSP00000052078; -.
DR   GlyGen; Q9Z0M3; 4 sites.
DR   iPTMnet; Q9Z0M3; -.
DR   PhosphoSitePlus; Q9Z0M3; -.
DR   PaxDb; Q9Z0M3; -.
DR   PeptideAtlas; Q9Z0M3; -.
DR   PRIDE; Q9Z0M3; -.
DR   ProteomicsDB; 265495; -.
DR   Antibodypedia; 2286; 118 antibodies from 25 providers.
DR   DNASU; 23836; -.
DR   Ensembl; ENSMUST00000062528; ENSMUSP00000052078; ENSMUSG00000050840.
DR   GeneID; 23836; -.
DR   KEGG; mmu:23836; -.
DR   UCSC; uc007cgc.1; mouse.
DR   CTD; 28316; -.
DR   MGI; MGI:1346069; Cdh20.
DR   VEuPathDB; HostDB:ENSMUSG00000050840; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000158167; -.
DR   HOGENOM; CLU_005284_3_1_1; -.
DR   InParanoid; Q9Z0M3; -.
DR   OMA; HEQNTFY; -.
DR   OrthoDB; 217088at2759; -.
DR   PhylomeDB; Q9Z0M3; -.
DR   TreeFam; TF329887; -.
DR   BioGRID-ORCS; 23836; 0 hits in 73 CRISPR screens.
DR   ChiTaRS; Cdh20; mouse.
DR   PRO; PR:Q9Z0M3; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q9Z0M3; protein.
DR   Bgee; ENSMUSG00000050840; Expressed in ganglionic layer of retina and 84 other tissues.
DR   Genevisible; Q9Z0M3; 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   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..34
FT                   /evidence="ECO:0000255"
FT   PROPEP          35..59
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000320096"
FT   CHAIN           60..801
FT                   /note="Cadherin-20"
FT                   /id="PRO_0000320097"
FT   TOPO_DOM        60..619
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        620..640
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        641..801
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          61..165
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          166..274
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          275..389
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          390..494
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          494..610
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        542
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   801 AA;  88998 MW;  AECF5C47A2D6CFBC CRC64;
     MWTTGRMSNA KSWLGLGTSL YFWALMDLTA TVLSSTPMPE VELETLFSGR SQSHQRSKRS
     WVWNQFFVLE EYTGTDPLYV GKLHSDMDRG DGSIKYILSG EGAGIVFTID DTTGDIHAIQ
     RLDREERAQY TLRAQALDRR TGRPMEPESE FIIKIQDIND NEPKFLDGPY IATVPEMSPV
     GTSVIQVTAT DADDPTYGNS ARVVYSILQG QPYFSVDSKT GVIRTALMNM DREAKEYYEV
     IIQAKDMGGQ LGGLAGTTTV NITLSDVNDN PPRFPQKHYQ MSVLESAPIS STVGRVFAKD
     LDEGINAEMK YTIVDGDGAD AFDINTDQNF QVGIITVKKP LSFESKKSYT LKVEGSNPHL
     EMRFLNLGPF QDTTTVHISV EDVDEPPVFE PGFYFVEVPE DVTIGTTIQI ISAKDPDVTN
     NSIRYSIDRG SDPGRFFYVD ITTGALMTAR PLDREEFSWH NITVLAMEMN NPSQVGSVAV
     TIKVLDVNDN APEFPRFYEA FICENAKAGQ LIQTVSAVDQ DDPHNGQHFY YSLAPEAANN
     PNFTVRDNQD NTARILTRRS GFRQQEQSVF YLPILIADSG QPVLSSTGTL TIQVCSCNDD
     GHVMSCSPEA YLLPVSLSRG ALIAILACIF VLLVLVLLIL SMRRHRKQPY IIDDDENIHE
     NIVRYDDEGG GEEDTEAFDI AAMWNPREAQ AGAAPKTRQD MLPEIESLSR YVPQTCAVSS
     TVHSYVLAKL YEADMDLWAP PFDSLQTYMF EGDGSVAGSL SSLQSATSDS EQSFDFLTDW
     GPRFRKLAEL YGASEGPAPL W
 
 
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