ID A0A091G6H9_9AVES Unreviewed; 866 AA.
AC A0A091G6H9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Desmocollin-1 {ECO:0000313|EMBL:KFO76749.1};
DE Flags: Fragment;
GN ORFNames=N303_02928 {ECO:0000313|EMBL:KFO76749.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO76749.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO76749.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO76749.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of intercellular desmosome junctions. Involved in
CC the interaction of plaque proteins and intermediate filaments mediating
CC cell-cell adhesion. {ECO:0000256|RuleBase:RU004358}.
CC -!- SUBCELLULAR LOCATION: Cell junction, desmosome
CC {ECO:0000256|ARBA:ARBA00004568}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU003318}.
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DR EMBL; KL447754; KFO76749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091G6H9; -.
DR STRING; 55661.A0A091G6H9; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 4.
DR Gene3D; 2.60.40.60; Cadherins; 6.
DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR000233; Cadherin_Y-type_LIR.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR009122; Desmosomal_cadherin.
DR PANTHER; PTHR24027:SF80; CADHERIN-13; 1.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR01818; DESMOCADHERN.
DR PRINTS; PR01820; DESMOCOLLIN.
DR SMART; SM00112; CA; 5.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; Cadherin-like; 6.
DR PROSITE; PS00232; CADHERIN_1; 1.
DR PROSITE; PS50268; CADHERIN_2; 4.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU003318};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 666..689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 123..220
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 221..332
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 333..449
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 457..555
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO76749.1"
FT NON_TER 866
FT /evidence="ECO:0000313|EMBL:KFO76749.1"
SQ SEQUENCE 866 AA; 96601 MW; 4FAF5205E1A8FC6D CRC64;
VLSLCCEACK QVIFHVPSEL EAETLVGRVD LKECLPSAEF ISSSDGHFNV LEDGSVYTTS
AVSFAEKKTF TILLKDIKEH VQKKIHVSLV EEEKKTQKTR HARDTVLKRT KRRWGPIPSV
MIENSLGPFP LQIQQVQSDT AQNYTIYYSA SGPGIDQDPK GLFYIERETG NIFATRAVDR
EQYPSFQIIC FATTPDGYSP EVPLVHTIRI EDDNDNAPYF TQEVFQFSVP ENSKPGVFVG
KVIAEDRDEP YTLHTTLKYS IVSQIPESVR SFSIHPYLGD ISVLSPQLDR EMSPSYTLLV
EVRDMDGQPY GLCTTGTVVI RLEDTNDNAP SFKQKHYETQ VEENRVNVEI LRLTVLDLDE
PGSPGSAAVY EIIKGNDDRS FEITTDKNTN EGILCVVKGL DYESAKQRIL VIAVNNDAPY
MLAPHSQQVS QSTSSVTVNV LDMDEGPVFK PCHLLLEVKE CEDIGTSIGR YLAEDPETGN
SEGICYRIPP GQCNWISIDE KSGEVRTVKV LDRDIGEMRR GQCNITVLAI DRNGKTGTGT
IQVVIRPGNK NYPRITTTDY IMCRDRKPIC LTAQDDDESP YSTPFVYRIT DRSLASSWKI
TQHNDNSVYL SPKGDIPFGT YTIPVSVTDN GGKVGEQYVT VNFCDCVTPT ECDIRNRQFA
GSNVTLGLWA ILAMILGSLL LLLILITICG CCGSGVMHRQ VTDDCANHNL IISNTEAPGE
EVMDHNIIPL QNTNDQGGYG IKTGDHQTFE MVKGRGHTLE SVKGGGHQSL GSVKEGGQTM
MDTCRYSYSE WHNFTHPRLG EKVHLCRQDE EQKHSEDYLL SYNYEGRGSL AGSVGCCSDQ
HEEEALDFLD QLEPKFRTLA ETCIKR
//
