位置:首页 > 蛋白库 > CAD20_HUMAN
CAD20_HUMAN
ID   CAD20_HUMAN             Reviewed;         801 AA.
AC   Q9HBT6; Q495S3;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Cadherin-20;
DE   Flags: Precursor;
GN   Name=CDH20; Synonyms=CDH7L3;
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=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 [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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   VARIANTS [LARGE SCALE ANALYSIS] ILE-228; THR-416 AND HIS-746.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
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   -!- TISSUE SPECIFICITY: Expressed in placenta, adult brain, and fetal
CC       brain.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF217289; AAG23739.1; -; mRNA.
DR   EMBL; CH471096; EAW63108.1; -; Genomic_DNA.
DR   EMBL; BC101047; AAI01048.1; -; mRNA.
DR   EMBL; BC101048; AAI01049.1; -; mRNA.
DR   EMBL; BC101049; AAI01050.1; -; mRNA.
DR   CCDS; CCDS11977.1; -.
DR   RefSeq; NP_114097.2; NM_031891.3.
DR   AlphaFoldDB; Q9HBT6; -.
DR   SMR; Q9HBT6; -.
DR   BioGRID; 118200; 2.
DR   IntAct; Q9HBT6; 1.
DR   STRING; 9606.ENSP00000262717; -.
DR   GlyGen; Q9HBT6; 4 sites.
DR   iPTMnet; Q9HBT6; -.
DR   PhosphoSitePlus; Q9HBT6; -.
DR   BioMuta; CDH20; -.
DR   DMDM; 190359622; -.
DR   EPD; Q9HBT6; -.
DR   MassIVE; Q9HBT6; -.
DR   PaxDb; Q9HBT6; -.
DR   PeptideAtlas; Q9HBT6; -.
DR   PRIDE; Q9HBT6; -.
DR   ProteomicsDB; 81590; -.
DR   Antibodypedia; 2286; 118 antibodies from 25 providers.
DR   DNASU; 28316; -.
DR   Ensembl; ENST00000262717.9; ENSP00000262717.3; ENSG00000101542.10.
DR   Ensembl; ENST00000536675.2; ENSP00000444767.1; ENSG00000101542.10.
DR   Ensembl; ENST00000538374.5; ENSP00000442226.1; ENSG00000101542.10.
DR   GeneID; 28316; -.
DR   KEGG; hsa:28316; -.
DR   MANE-Select; ENST00000262717.9; ENSP00000262717.3; NM_031891.4; NP_114097.2.
DR   UCSC; uc002lif.3; human.
DR   CTD; 28316; -.
DR   DisGeNET; 28316; -.
DR   GeneCards; CDH20; -.
DR   HGNC; HGNC:1760; CDH20.
DR   HPA; ENSG00000101542; Group enriched (brain, retina, tongue).
DR   MIM; 605807; gene.
DR   neXtProt; NX_Q9HBT6; -.
DR   OpenTargets; ENSG00000101542; -.
DR   PharmGKB; PA26294; -.
DR   VEuPathDB; HostDB:ENSG00000101542; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000158167; -.
DR   HOGENOM; CLU_005284_3_1_1; -.
DR   InParanoid; Q9HBT6; -.
DR   OMA; HEQNTFY; -.
DR   OrthoDB; 217088at2759; -.
DR   PhylomeDB; Q9HBT6; -.
DR   TreeFam; TF329887; -.
DR   PathwayCommons; Q9HBT6; -.
DR   SignaLink; Q9HBT6; -.
DR   SIGNOR; Q9HBT6; -.
DR   BioGRID-ORCS; 28316; 7 hits in 1062 CRISPR screens.
DR   ChiTaRS; CDH20; human.
DR   GenomeRNAi; 28316; -.
DR   Pharos; Q9HBT6; Tbio.
DR   PRO; PR:Q9HBT6; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; Q9HBT6; protein.
DR   Bgee; ENSG00000101542; Expressed in ventricular zone and 87 other tissues.
DR   Genevisible; Q9HBT6; 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: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_0000003819"
FT   CHAIN           60..801
FT                   /note="Cadherin-20"
FT                   /id="PRO_0000003820"
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"
FT   VARIANT         228
FT                   /note="M -> I (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036103"
FT   VARIANT         328
FT                   /note="P -> H (in dbSNP:rs1943330)"
FT                   /id="VAR_039119"
FT   VARIANT         371
FT                   /note="Q -> R (in dbSNP:rs35923922)"
FT                   /id="VAR_039120"
FT   VARIANT         391
FT                   /note="P -> L (in dbSNP:rs17068463)"
FT                   /id="VAR_039121"
FT   VARIANT         416
FT                   /note="P -> T (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036104"
FT   VARIANT         746
FT                   /note="Q -> H (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036105"
FT   CONFLICT        621
FT                   /note="A -> P (in Ref. 1; AAG23739)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        694
FT                   /note="A -> G (in Ref. 1; AAG23739)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        709
FT                   /note="S -> F (in Ref. 1; AAG23739)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        739
FT                   /note="A -> T (in Ref. 1; AAG23739)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        755
FT                   /note="S -> P (in Ref. 1; AAG23739)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   801 AA;  88993 MW;  6B8B226519F49C5E CRC64;
     MWTSGRMSNA KNWLGLGMSL YFWGLMDLTT TVLSDTPTPQ GELEALLSDK PQSHQRTKRS
     WVWNQFFVLE EYTGTDPLYV GKLHSDMDRG DGSIKYILSG EGAGIVFTID DTTGDIHAIQ
     RLDREERAQY TLRAQALDRR TGRPMEPESE FIIKIQDIND NEPKFLDGPY VATVPEMSPV
     GTSVIQVTAT DADDPTYGNS ARVVYSILQG QPYFSVDSKT GVIRTALMNM DREAKEYYEV
     IIQAKDMGGQ LGGLAGTTTV NITLSDVNDN PPRFPQKHYQ MSVLESAPIS STVGRVFAKD
     LDEGINAEMK YTIVDGDGAD AFDISTDPNF QVGIITVKKP LSFESKKSYT LKVEGANPHL
     EMRFLNLGPF QDTTTVHISV EDVDEPPVFE PGFYFVEVPE DVAIGTTIQI ISAKDPDVTN
     NSIRYSIDRS SDPGRFFYVD ITTGALMTAR PLDREEFSWH NITVLAMEMN NPSQVGSVPV
     TIKVLDVNDN APEFPRFYEA FVCENAKAGQ LIQTVSAVDQ DDPRNGQHFY YSLAPEAANN
     PNFTIRDNQD NTARILTRRS GFRQQEQSVF HLPILIADSG QPVLSSTGTL TIQVCSCDDD
     GHVMSCSPEA YMLPVSLSRG ALIAILACIF VLLVLVLLIL SMRRHRKQPY IIDDEENIHE
     NIVRYDDEGG GEEDTEAFDI AAMWNPREAQ AGAAPKTRQD MLPEIESLSR YVPQTCAVNS
     TVHSYVLAKL YEADMDLWAP PFDSLQTYMF EGDGSVAGSL SSLQSATSDS EQSFDFLTDW
     GPRFRKLAEL YGASEGPAPL W
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024