ID A0A091JQF4_EGRGA Unreviewed; 888 AA.
AC A0A091JQF4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Cadherin-2 {ECO:0000313|EMBL:KFP23264.1};
DE Flags: Fragment;
GN ORFNames=Z169_04960 {ECO:0000313|EMBL:KFP23264.1};
OS Egretta garzetta (Little egret).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP23264.1, ECO:0000313|Proteomes:UP000053119};
RN [1] {ECO:0000313|EMBL:KFP23264.1, ECO:0000313|Proteomes:UP000053119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP23264.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC {ECO:0000256|RuleBase:RU004357}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000256|ARBA:ARBA00004536}. Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004135}. 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}. Cell surface
CC {ECO:0000256|ARBA:ARBA00004241}.
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DR EMBL; KK502398; KFP23264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091JQF4; -.
DR STRING; 188379.A0A091JQF4; -.
DR Proteomes; UP000053119; Unassembled WGS sequence.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; 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 PANTHER; PTHR24027:SF79; CADHERIN-2; 1.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
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; 2.
DR PROSITE; PS50268; CADHERIN_2; 5.
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 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:UP000053119};
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 706..728
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 141..248
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 249..363
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 364..478
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 479..587
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 586..692
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 757..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP23264.1"
FT NON_TER 888
FT /evidence="ECO:0000313|EMBL:KFP23264.1"
SQ SEQUENCE 888 AA; 97683 MW; A0423C5E4495B435 CRC64;
QAPIKATCED MSCKTGFPED VHSAVVSRSV HGGQPLLNVR FRSCDGNKKI HFGSSEPEDF
RVGEDGVVYA ERSFQLSAEP TEFVVSAQDK ETQEEWQMRV KLTPEPAFSG ASEKDQKKTE
DIIFPWQQYK HSSPLKRQKR DWVIPPINLP ENSRGPFPQE LVRIRSDRDK SLSLRYSVTG
PGADQPPTGI FIINPISGQL SVTKPLDREQ IASFHLRAHA VDVNGNQVEN PIDIVINVID
MNDNRPEFLH QVWNGTVPEG SKPGTYVMTV TAIDADDPNA QNGMLRYRIL SQAPSSPSPN
MFTINNETGD IITVAAGLDR EKVQQYTLII QATDMEGNPT YGLSNTATAV ITVTDVNDNP
PEFTAMTFYG EVPENRVDVI VANLTVTDKD QPHTPAWNAM YRMTGGDPTG RFTILTDPNS
NDGLVTVVKP IDFETNRMFV LTVAAENQVP LAKGIQHPPQ STATVSITVI DVNESPYFVP
NPKLVRQEEG LLAGSVLTTF TAQDPDRYMQ QTSLRYSKLS DPANWLKIDP VNGQITTTAV
LDRESIYVQN NMYNATFLAS DNGIPPMSGT GTLQIYLLDI NDNAPQVNPK EATTCETLQP
NAINITAVDP DIDPNAGPFA FELPDTPASI KRNWTIVRIS GDHAQLSLRI RFLEAGIYDV
PIVITDSGNP HASSTSVLKV KVCQCDINGD CTDVDRIVGA GLGTGAIIAI LLCIIILLIL
VLMFVVWMKR RDKERQAKQL LIDPEDDVRD NILKYDEEGG GEEDQDYDLS QLQQPDTVEP
DAIKPVGIRR LDERPLHAEP QYPVRSAAPH PGDIGDFINE GLKAADNDPT APPYDSLLVF
DYEGSGSTAG SLSSLNSSSS GGEQDYDYLN DWGPRFKKLA DMYGGGDD
//