ID A0A3B0JP32_DROGU Unreviewed; 501 AA.
AC A0A3B0JP32;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=C-type lectin domain-containing protein {ECO:0000259|PROSITE:PS50041};
GN ORFNames=DGUA_6G003133 {ECO:0000313|EMBL:SPP75339.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP75339.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; OUUW01000001; SPP75339.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0JP32; -.
DR STRING; 7266.A0A3B0JP32; -.
DR OrthoDB; 3660997at2759; -.
DR Proteomes; UP000268350; Unassembled WGS sequence.
DR CDD; cd00037; CLECT; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..501
FT /note="C-type lectin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017263730"
FT DOMAIN 26..175
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 126..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..402
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 55094 MW; 1C3C9A5632ADB0C5 CRC64;
MAKIILFCVL SLLACAAGQR ITTIHLDGVQ YFISRMNPYS PELNYFLAYQ YCRSLGLQLA
SFETKEKAES MTTYLKNAGY GNYDFWTSGN RLGTGMFLWM STGLPFNATF DFFENSADAI
QAGLLDPVDH NSNTSPQRTA RDSSSGAEKG CVILKQPTLK WMPEDCSAVK DFICEQTRCY
YYNYGSIPVS SAQGRPITST TPRPPAALMH LHAATTTTPL PLLMSTTGGL YTAAKAKSSP
AIAHRLAEEA SSPSFHSFKL NQDRSLTDKD AIDVEVDDQD ADMDAEEHDE HDHEHEHEVE
SDGDVEGDDH DGDSDNFSEH ARELVGDGEG DDIKEHVFPL HDNELHHEMH SIEEVQQQLQ
HHDEDAAPAA AAAAEESVSA EHEPEAEGDS DPEAEAEAET DSEAESQAPG QASEALPSST
ESPAAAAIEE RIKQIAQDFQ KMASSQEMQT PSNEENLPKQ SLSLNDLIRT LRPNEQQIIP
QIDSDYSNAM RVLGKTLVPH N
//