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Database: UniProt
Entry: A0A091IAK3_CALAN
LinkDB: A0A091IAK3_CALAN
Original site: A0A091IAK3_CALAN 
ID   A0A091IAK3_CALAN        Unreviewed;       403 AA.
AC   A0A091IAK3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Protein eva-1 C {ECO:0000313|EMBL:KFP05654.1};
DE   Flags: Fragment;
GN   ORFNames=N300_11280 {ECO:0000313|EMBL:KFP05654.1};
OS   Calypte anna (Anna's hummingbird) (Archilochus anna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC   Trochilidae; Calypte.
OX   NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP05654.1, ECO:0000313|Proteomes:UP000054308};
RN   [1] {ECO:0000313|EMBL:KFP05654.1, ECO:0000313|Proteomes:UP000054308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP05654.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the EVA1 family.
CC       {ECO:0000256|ARBA:ARBA00006023}.
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DR   EMBL; KL218474; KFP05654.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091IAK3; -.
DR   STRING; 9244.A0A091IAK3; -.
DR   Proteomes; UP000054308; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   CDD; cd22828; Gal_Rha_Lectin_EVA1_EVA1C_rpt1; 1.
DR   CDD; cd22829; Gal_Rha_Lectin_EVA1_EVA1C_rpt2; 1.
DR   Gene3D; 2.60.120.740; -; 2.
DR   InterPro; IPR039500; EVA1_dom.
DR   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR043159; Lectin_gal-bd_sf.
DR   PANTHER; PTHR46780; PROTEIN EVA-1; 1.
DR   PANTHER; PTHR46780:SF5; PROTEIN EVA-1 HOMOLOG C-LIKE ISOFORM X1; 1.
DR   Pfam; PF14851; FAM176; 1.
DR   Pfam; PF02140; Gal_Lectin; 2.
DR   PROSITE; PS50228; SUEL_LECTIN; 2.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..403
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013107971"
FT   DOMAIN          34..127
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
FT   DOMAIN          136..228
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
FT   REGION          324..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..347
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP05654.1"
FT   NON_TER         403
FT                   /evidence="ECO:0000313|EMBL:KFP05654.1"
SQ   SEQUENCE   403 AA;  44622 MW;  8D3CA1DF72C3AD13 CRC64;
     AAALVLLCLA VGLEASPELS GYLRKVLRNH TTHTCDGEQL LIICPHKTTI SILSAFYGRR
     VPSPNLCPSP GSASQESTQC SSTTAHLKLQ DECQDQQWCQ FSVHSQVFGP DPCPGTHKYL
     IASYKCRPGN HRVKTVCENN KLKLQCRPKS VLAIYSANYG RFLRGKPECD ALNTGAPHIE
     CLAPDALRRV SKKCHRKTNC TVAADQATFG DPCLPGMKKQ LRVSYTCVPK QLLEEVGPET
     SDPFLLSDYM HGGWYKGPRF SKLREDRMIF TSSLEVFAHL WGIPEKVGLY FLCGVSGGLM
     LLLCIISPKT TFLQEVGEGL KDPELSRTKL RDDQDEDLPD DSSSDSSFRR LTRTYRATDS
     IFGPELTAAM EGAVEHQGHG GEEIWMPKES SPYAIHKIKS ATK
//
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