CAD10_CHICK
ID CAD10_CHICK Reviewed; 789 AA.
AC P79995;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cadherin-10;
DE Flags: Precursor;
GN Name=CDH10;
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].
RC TISSUE=Brain, and Retina;
RX PubMed=9215642;
RX DOI=10.1002/(sici)1097-0177(199707)209:3<269::aid-aja3>3.0.co;2-g;
RA Fushimi D., Arndt K., Takeichi M., Redies C.;
RT "Cloning and expression analysis of cadherin-10 in the CNS of the chicken
RT embryo.";
RL Dev. Dyn. 209:269-285(1997).
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 -!- 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; AB000512; BAA19130.1; -; mRNA.
DR RefSeq; NP_999838.1; NM_214673.1.
DR RefSeq; XP_015137653.1; XM_015282167.1.
DR AlphaFoldDB; P79995; -.
DR SMR; P79995; -.
DR STRING; 9031.ENSGALP00000021052; -.
DR PaxDb; P79995; -.
DR GeneID; 408049; -.
DR KEGG; gga:408049; -.
DR CTD; 1008; -.
DR VEuPathDB; HostDB:geneid_408049; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; P79995; -.
DR OrthoDB; 201053at2759; -.
DR PhylomeDB; P79995; -.
DR PRO; PR:P79995; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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..22
FT /evidence="ECO:0000255"
FT PROPEP 23..54
FT /evidence="ECO:0000255"
FT /id="PRO_0000003783"
FT CHAIN 55..789
FT /note="Cadherin-10"
FT /id="PRO_0000003784"
FT TOPO_DOM 55..606
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 607..634
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..789
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 55..160
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 161..269
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 270..384
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 385..487
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 488..606
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 789 AA; 88392 MW; D24AF46AA090D4D5 CRC64;
MTIQQVLLLL LLWMWLLHPC RTEMLFRRTP DLRPKGFVGR TSGSDGKALH RQKRGWMWNQ
FFLLEEYTGS DYQYVGKLHS DQDKGDGSLK YILSGDGAGT LFIIDEKTGD IHATRRIDRE
EKAFYTLRAQ AINRRTLRPV EPESEFVIKI HDINDNEPTF PEEIYTASVP EMSVVGTSVV
QVTATDADDP SYGNSARIIY SILQGQPYFS VEPETGIIRT ALPNMNRENR EQYQVVIQAK
DMGGQMGGLS GTTTVNITLT DVNDNPPRFP QSTIHLRIPE SSPVGTPIGS IKATDADTGK
NAEVEYRIID GDGTDMFDIV TQRDTQEGII TVRKPLDYET RRLYTLKVEA ENTHVDPRFY
YLGPFKDTTI VKISVEDVDE PPVFSRSSYL FEVHEDIELG TIIGTVMARD PDSASSPIRF
SLDRHTDLDR IFNIHSGNGS IYTSKPLDRE ISQWHNLSVI AAEINNLKDT TRVPVYVRIL
DVNDNAPQFA VFYDTFVCEN ARAGQLIQTI SAVDKDDPLG GQKFFFSLAA VNPNFTVQDN
EDNTARILTR RNGFSRHEIS TYLLPVVISD NDYPIQSSTG TLTIRVCACD SRGNMQSCNA
EALLLPAGLS TGALIAILLC IIILLVIVVL FAALKRQRKK EPLILSKEDI RDNIVSYNDE
GGGEEDTQAF DIGTLRNPAA IEDKKLRRDI IPETLFVPRR TPSAPDNTDV RDFINQRLKE
HDSDPSAPPY DSLATYAYEG NDSIAESLSS LESGTTEGDQ NYDYLREWGP RFNKLAEMYG
GGESDKDAS
