ID A0A091L2P0_9GRUI Unreviewed; 682 AA.
AC A0A091L2P0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Collectin-12 {ECO:0000256|ARBA:ARBA00017460};
DE Flags: Fragment;
GN ORFNames=N324_07760 {ECO:0000313|EMBL:KFP45885.1};
OS Chlamydotis macqueenii (Macqueen's bustard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP45885.1, ECO:0000313|Proteomes:UP000053330};
RN [1] {ECO:0000313|EMBL:KFP45885.1, ECO:0000313|Proteomes:UP000053330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP45885.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK764315; KFP45885.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091L2P0; -.
DR Proteomes; UP000053330; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR CDD; cd03590; CLECT_DC-SIGN_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; IPR033989; CD209-like_CTLD.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR016187; CTDL_fold.
DR PANTHER; PTHR22803:SF146; COLLECTIN-12; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000053330}.
FT DOMAIN 554..671
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 379..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 237..271
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 419..433
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..484
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..532
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP45885.1"
FT NON_TER 682
FT /evidence="ECO:0000313|EMBL:KFP45885.1"
SQ SEQUENCE 682 AA; 74921 MW; F2E8A55D1955C195 CRC64;
VVEKMDNVTG GLETSHRRYT EKLTEVESDL KKLDDQAGQK AMNTNTELSS FRSDILALRQ
QLHDIAEKTT RNKDTLEKLQ ESGNVLDDRQ SQMRSALDSN SFMIISVNKT LQAYTGYINN
LQQDTSTIQT NLQNQVHSHN VVIMNLNNLN LTQIQQRNLI TVLQKSMEDT SLAILRIKND
FQNLQQVVLQ ARKDTDWLKE KVQNLQTLAA NNSALAKANN DTLEDMNNQL SSFSGQMENI
TTIAQANEQN LKDLQEQHKE YENRTSTKFN QLEERFQVFE TDIVNIISNI SYTAHHLRTL
TSNLNEVRTT CTDTLSKHSD ELIFMNSTLA NIRLDSASLR MQQDLMRSRL DVEVANLSVI
MEEMKLVDSK HGQLIKNFTI LQGPPGPRGP KGDRGPQGPL GPSGLKGQKG EKGEPGPPGP
AGEKGPPGPT GPPGEKGGKG SRGSPGSKGQ RGSPGKTGLP GPSGDPGPPG PQGKDGPPGP
QGPPGFQGLQ GTVGEPGVPG PRGLPGLPGV PGMPGPKGPP GPPGPPGPGM PMALQSEPTS
APEANGCSPH WKNYTEKCYY FSIEREIFEE AKLFCEEKAS RLVIINNKEE QQWIKRQIFG
KGSFWIGLTD SEKENEWRWL DGSLPVYTNW KTGQPDNWSH GHGPGEDCAG LIYAGLWNDF
YCEDVNNFIC EKDMDKGQIF GV
//
