CAD20_CHICK
ID CAD20_CHICK Reviewed; 798 AA.
AC Q8QGH3; Q7ZYV7; Q804X8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Cadherin-20;
DE AltName: Full=F-cadherin;
DE AltName: Full=MN-cadherin;
DE Flags: Precursor;
GN Name=CDH20;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryonic spinal cord;
RX PubMed=12007407; DOI=10.1016/s0092-8674(02)00695-5;
RA Price S.R., De Marco Garcia N.V., Ranscht B., Jessell T.M.;
RT "Regulation of motor neuron pool sorting by differential expression of type
RT II cadherins.";
RL Cell 109:205-216(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=White leghorn; TISSUE=Embryonic spinal cord;
RX PubMed=15992777; DOI=10.1016/j.bbrc.2005.06.080;
RA Shirabe K., Kimura Y., Matsuo N., Fukushima M., Yoshioka H., Tanaka H.;
RT "MN-cadherin and its novel variant are transiently expressed in chick
RT embryo spinal cord.";
RL Biochem. Biophys. Res. Commun. 334:108-116(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 60-156, FUNCTION, AND SUBUNIT.
RX PubMed=16564015; DOI=10.1016/j.cell.2005.12.046;
RA Patel S.D., Ciatto C., Chen C.P., Bahna F., Rajebhosale M., Arkus N.,
RA Schieren I., Jessell T.M., Honig B., Price S.R., Shapiro L.;
RT "Type II cadherin ectodomain structures: implications for classical
RT cadherin specificity.";
RL Cell 124:1255-1268(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. {ECO:0000269|PubMed:12007407,
CC ECO:0000269|PubMed:15992777, ECO:0000269|PubMed:16564015}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15992777};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:15992777}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=Q8QGH3-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q8QGH3-2; Sequence=VSP_034199, VSP_034200;
CC -!- TISSUE SPECIFICITY: Detected in embryonic spinal cord, in the brachial
CC and lumbar section of motor neurons (at protein level). Detected in
CC ventro-lateral portion of embryonic spinal cord, in the brachial and
CC lumbar section of embryonic motor neurons. Detected in embryonic
CC adductor motor neurons and embryonic dorsal root ganglion. Detected in
CC the caudal half of newly generated somites and in presomitic mesoderm.
CC {ECO:0000269|PubMed:12007407, ECO:0000269|PubMed:15992777}.
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; AF459439; AAL93123.1; -; mRNA.
DR EMBL; AF465257; AAO33355.1; -; mRNA.
DR EMBL; AF465258; AAO33356.1; -; mRNA.
DR RefSeq; NP_989465.1; NM_204134.1. [Q8QGH3-1]
DR RefSeq; XP_015137644.1; XM_015282158.1. [Q8QGH3-1]
DR RefSeq; XP_015137645.1; XM_015282159.1. [Q8QGH3-1]
DR RefSeq; XP_015137646.1; XM_015282160.1. [Q8QGH3-1]
DR RefSeq; XP_015137647.1; XM_015282161.1. [Q8QGH3-1]
DR PDB; 1ZVN; X-ray; 2.16 A; A/B=60-156.
DR PDBsum; 1ZVN; -.
DR AlphaFoldDB; Q8QGH3; -.
DR SMR; Q8QGH3; -.
DR STRING; 9031.ENSGALP00000021013; -.
DR PaxDb; Q8QGH3; -.
DR Ensembl; ENSGALT00000021043; ENSGALP00000021013; ENSGALG00000012906. [Q8QGH3-1]
DR Ensembl; ENSGALT00000048550; ENSGALP00000056375; ENSGALG00000012906. [Q8QGH3-1]
DR Ensembl; ENSGALT00000106436; ENSGALP00000071272; ENSGALG00000012906. [Q8QGH3-1]
DR GeneID; 373927; -.
DR KEGG; gga:373927; -.
DR CTD; 28316; -.
DR VEuPathDB; HostDB:geneid_373927; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000158167; -.
DR InParanoid; Q8QGH3; -.
DR OMA; HEQNTFY; -.
DR PhylomeDB; Q8QGH3; -.
DR TreeFam; TF329887; -.
DR EvolutionaryTrace; Q8QGH3; -.
DR PRO; PR:Q8QGH3; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000012906; Expressed in cerebellum and 4 other tissues.
DR ExpressionAtlas; Q8QGH3; baseline and differential.
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; Alternative splicing; 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..35
FT /evidence="ECO:0000255"
FT PROPEP 36..58
FT /evidence="ECO:0000255"
FT /id="PRO_0000340243"
FT CHAIN 59..798
FT /note="Cadherin-20"
FT /id="PRO_0000340244"
FT TOPO_DOM 59..618
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 640..798
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 60..164
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 165..273
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 274..392
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 389..493
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 493..615
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT MOTIF 88..90
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..255
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15992777"
FT /id="VSP_034199"
FT VAR_SEQ 256..276
FT /note="TTTVNITLSDVNDNPPRFPQK -> MQFLVPFHSLLFCFSLLLVPE (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15992777"
FT /id="VSP_034200"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:1ZVN"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1ZVN"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1ZVN"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1ZVN"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1ZVN"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:1ZVN"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:1ZVN"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1ZVN"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:1ZVN"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:1ZVN"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1ZVN"
FT STRAND 127..137
FT /evidence="ECO:0007829|PDB:1ZVN"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1ZVN"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1ZVN"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:1ZVN"
SQ SEQUENCE 798 AA; 89157 MW; 8224FB837937F106 CRC64;
MWTSGRMSNA KNLFGLGVSL YFWGLMDLTT TVLSGSARPL TEGPEDNLSD KLHQRMKRSW
VWNQFFVLEE YTGTDPLYVG KLHSDMDRGD GSIKYILSGE GAGIVFTIDD TTGDIHAIQR
LDREERSQYT LRAQALDRRT GRPMEPESEF IIKIQDINDN EPKFLDGPYV ASVPEMSPVG
TSVIQVTATD ADDPTYGNSA RVVYSILQGQ PYFSVDSRTG LIRTALMNMD REAKEYYEVI
VQAKDMGGQL GGLAGTTTVN ITLSDVNDNP PRFPQKHYQM SVLESAPVSS TVGRVVAKDL
DEGINAEMKY SLVDGDGLDV FDINTDPNYQ VGIITVRKPL SFESKKSYTL KVEGANPHLE
MRFLNLGPFR DTTTVHISVE DVDEPPVFEP SFYFVEVPED VEIGATIQII SAKDPDVTNN
SIRYSIDRSS DPGRFFYVDI TSGALMTARP LDREDVSWHN ITVLAMELNN PSQVGSVSVT
VKVLDVNDNA PEFARFYEAF VCENAKAGQL IQTVSAIDRD DPQEGQHFYY SLAPEAANNP
NFTLRDNQDN TAWILTRRSG FRQHEQNIFY LPILISDNGR PVLSSTGTLT VHVCSCDEGG
MVMSCNAEAY VLPVSLSRGA LIAILACIFV LLVLVLLILS MRRQRKQPYI IDEEENIHEN
IVRYDDEGGG EEDTEAFDIA AMWNPREAQL VVKNRQDMLP EIESLSRYVP QACIMDNNVH
NYVLAKLYEA DMDLWAPPFD SLQTYMFEGN GSVAESLSSL QSVTTDSDQS YDYLTDWGPR
FKKLAEMYGA TDSSGALW
