ID A0A093H3E7_STRCA Unreviewed; 277 AA.
AC A0A093H3E7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Collectin-10 {ECO:0000313|EMBL:KFV73900.1};
GN ORFNames=N308_09605 {ECO:0000313|EMBL:KFV73900.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV73900.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV73900.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV73900.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; KL205751; KFV73900.1; -; Genomic_DNA.
DR RefSeq; XP_009681223.1; XM_009682928.1.
DR AlphaFoldDB; A0A093H3E7; -.
DR STRING; 441894.ENSSCUP00000002291; -.
DR Ensembl; ENSSCUT00000003024; ENSSCUP00000002291; ENSSCUG00000001717.
DR GeneID; 104149337; -.
DR KEGG; scam:104149337; -.
DR CTD; 10584; -.
DR OrthoDB; 4835894at2759; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0042056; F:chemoattractant activity; IEA:Ensembl.
DR GO; GO:0005537; F:mannose binding; IEA:Ensembl.
DR GO; GO:0001867; P:complement activation, lectin pathway; IEA:Ensembl.
DR GO; GO:1904888; P:cranial skeletal system development; IEA:Ensembl.
DR GO; GO:1903028; P:positive regulation of opsonization; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:Ensembl.
DR CDD; cd03591; CLECT_collectin_like; 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; IPR018378; C-type_lectin_CS.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR033990; Collectin_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR PANTHER; PTHR22801:SF61; C-TYPE LECTIN DOMAIN FAMILY 4 MEMBER F ISOFORM X1-RELATED; 1.
DR PANTHER; PTHR22801; LITHOSTATHINE; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 155..271
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 39..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 277 AA; 30531 MW; 61D527DCB12A005D CRC64;
MSSKKEQQLR KYGTLVVLFI FQVQIFGFDV DNRPTTDVCS THTILPGPKG DEGEKGDRGE
VGRQGKVGPK GPKGNKGTVG DIGDQGMIGK IGPIGGKGDK GAKGFSGVPG KKGKAGTVCD
CGRYRRVVGQ LNVNVARLNT SIKFVKNVIA GIRETDEKFY YIVKEEKNYR EALMHCRDRG
GTLAMPKDEA TNDLIADYVS KSGLFRAFIG MNDIEKEGQF VYADNTSLQN YSNWKEGEPN
DPAGREDCVE MLSTGEWNDS ECQVTIYFVC EFLKRRK
//