ID A0A1V4KG82_PATFA Unreviewed; 1346 AA.
AC A0A1V4KG82;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Desmoglein-2 {ECO:0000313|EMBL:OPJ83405.1};
GN Name=DSG2 {ECO:0000313|EMBL:OPJ83405.1};
GN ORFNames=AV530_006305 {ECO:0000313|EMBL:OPJ83405.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ83405.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ83405.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ83405.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ83405.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ83405.1}.
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DR EMBL; LSYS01003169; OPJ83405.1; -; Genomic_DNA.
DR STRING; 372326.A0A1V4KG82; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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 CDD; cd05469; Transthyretin_like; 1.
DR Gene3D; 2.60.40.60; Cadherins; 5.
DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR Gene3D; 2.60.40.180; Transthyretin/hydroxyisourate hydrolase domain; 2.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR023418; Thyroxine_BS.
DR InterPro; IPR000895; Transthyretin/HIU_hydrolase.
DR InterPro; IPR023416; Transthyretin/HIU_hydrolase_d.
DR InterPro; IPR036817; Transthyretin/HIU_hydrolase_sf.
DR PANTHER; PTHR24025; DESMOGLEIN FAMILY MEMBER; 1.
DR PANTHER; PTHR24025:SF1; DESMOGLEIN-2; 1.
DR Pfam; PF00028; Cadherin; 3.
DR Pfam; PF00576; Transthyretin; 2.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR00189; TRNSTHYRETIN.
DR SMART; SM00112; CA; 4.
DR SMART; SM00095; TR_THY; 2.
DR SUPFAM; SSF49313; Cadherin-like; 4.
DR SUPFAM; SSF49472; Transthyretin (synonym: prealbumin); 2.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 4.
DR PROSITE; PS00768; TRANSTHYRETIN_1; 2.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1346
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012392532"
FT DOMAIN 70..158
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 159..268
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 269..384
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 385..493
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 696..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1346 AA; 144759 MW; 9A79A9BD43654F5F CRC64;
MSRGPAAPVR LLALLICLNY GNGLYVKVYD QNGRSGTLSH PNSLVRQKRE WTVPPAFIRE
EEDNSYKNPI ARIHSDLEAS GIVVTYTISG QGVTEPPFGL FVIDGKTGDL NITGRVDREK
TPILLLRGHA LDRNGAKLEE PIDLPIKIVD INDNFPVFSH EVFVGSIEEL SETGTIVMRI
NATDADEPNN LNSKIAYRII SQSPSAAFSM NKDTGEVRVA TINLDREAYS SYSLVVEAKD
RGGESGGNAA TCSLEIKILD VNDNVPVVES RAFEVSIEEN RANVEMLRIK VFDKDEEFSD
NWLANFSFVS GNEGGFFHIV TDKKTNEGIL TLVKELDYEK MQSLNLGIVV TNKAEFHKSI
KYTHKAQTIP IRVSVINVRE GPLFPGGTKI IEASEKLEIG QIIGQYQAYD EDMGKAAVDI
KYLKGSDIAN WITINSQTGE IQLAQNLDYE SSYVVNGTYT FTMLGVTTVA PTKTITGTVV
VQVKDENDNC PVLVNPIQTV CSDAKSIDVT AHDLDGYPYS DPFSFTVIDE PEGTARKWII
VTRNGTSIQL IPQELKIGTT EVPILVKDFQ GLSCAKAQSL QLSVCKCADG GGCKDKVSGA
PLVSLGPGAI ALIVLAFLLL LLIPLLLLLC PCGSGAKGFA AIPDYSEEML RQWNSEGAAP
QEKPVLSLIP PTGLGSAGAA ASGAVTAAAA AAGMSTEETA TGGGSSASHV REQHVTGTKE
RWEEQRHLLS GAEYGAVAAG GAEGMTGIEG KTVLAGGGVT VGAVGAMNEE FLRDYFTDKA
VSFADEDETQ AANDCLLVYS QGESGSPHGS IGCCSFIDGD LDDHFLDDLG DKFKTLAEIC
IGRHTNMKDG SSRNESGFSL SDTKSRFLDQ QNASSSEQAF ASGRCFQPTG SGTGEETMSK
EVVTETTFAS RSGQHEVRPL PTAHAETNFT MTETSYSAGA PARSATVFLD PKFNENVVVT
ERVLAPASSL QGIVEIPDLP HGSNLVFTER MVKTEGTGSG VLLSQDLPDS QYVVVRERER
VLVPAAEQGS LSFPASAEGR SVVVTASGTQ SRAEQAAGAG WGSQEHILIT DSLRNQHESH
WRIPSTTSLY DLHGNAVQAG LVLFSEAAPL VTHGSVDSKC PLMVKVLDAV RGSPAANVAV
KVFKKAADGS WQDFATGKTT EYGEIHDLTT DEQFIEGIYR VEFDTSSYWK GLGLSPFHEY
ADVVFTANDS AGLAFFSEAA PPGSADSKHP LFIKILDSVR GSPASNVPVK LYKEAADGSW
ELLNSEQTND NGELHELTTK EQFATGIYKI ELDTASYWKI LGLNPFHHHA DVVFTANDVG
YRHYSIAVLL SPFSYSTTAV VSEPVE
//
