COL10_XENTR
ID COL10_XENTR Reviewed; 275 AA.
AC Q5M8X6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Collectin-10;
DE Flags: Precursor;
GN Name=colec10;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lectin that binds to various sugars: galactose > mannose =
CC fucose > N-acetylglucosamine > N-acetylgalactosamine. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the COLEC10/COLEC11 family. {ECO:0000305}.
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DR EMBL; BC087791; AAH87791.1; -; mRNA.
DR RefSeq; NP_001011227.1; NM_001011227.1.
DR AlphaFoldDB; Q5M8X6; -.
DR SMR; Q5M8X6; -.
DR STRING; 8364.ENSXETP00000033873; -.
DR PaxDb; Q5M8X6; -.
DR DNASU; 496663; -.
DR GeneID; 496663; -.
DR KEGG; xtr:496663; -.
DR CTD; 10584; -.
DR Xenbase; XB-GENE-945586; colec10.
DR eggNOG; KOG4297; Eukaryota.
DR HOGENOM; CLU_049894_3_2_1; -.
DR InParanoid; Q5M8X6; -.
DR OrthoDB; 1105722at2759; -.
DR PhylomeDB; Q5M8X6; -.
DR Reactome; R-XTR-166662; Lectin pathway of complement activation.
DR Reactome; R-XTR-166663; Initial triggering of complement.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR ExpressionAtlas; Q5M8X6; baseline.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR CDD; cd03591; CLECT_collectin_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR033990; Collectin_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Collagen; Disulfide bond; Glycoprotein; Lectin; Mannose-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..275
FT /note="Collectin-10"
FT /id="PRO_0000314236"
FT DOMAIN 51..110
FT /note="Collagen-like"
FT DOMAIN 153..269
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 39..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 174..268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 246..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 275 AA; 29731 MW; 0C7A567F505FE3DC CRC64;
MKYGKLWPIG VSVLGVIALH VRVLSLEVEN SSAVDTCSTH TILPGPKGDD GEAGDTGVLG
KLGKDGPKGQ KGNKGIIGDS GDLGLIGKIG PIGSKGDKGH KGLPGLPGGK GKSGSYCDCG
RYRKVVGQLD VNVAHLKSSL KFVKNVIAGI RETDEKYYYI VREERNYRDA LTQCRIRGGT
LAMPKDQATN SLIADYISKM GLFRVFIGIN DIEKEKQFVY ADNSPLQTYS SWKAGEPNDG
SGYEDCVEML STGHWNDVDC SLTIYFVCEF LKKTK