ID   COL10_CHICK             Reviewed;         277 AA.
AC   Q2LK95;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Collectin-10;
DE   AltName: Full=Collectin-1;
DE            Short=CL-1;
DE            Short=cCL-1;
DE   Flags: Precursor;
GN   Name=COLEC10; Synonyms=CL1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=16289291; DOI=10.1016/j.molimm.2005.09.015;
RA   Hogenkamp A., van Eijk M., van Dijk A., van Asten A.J.A.M.,
RA   Veldhuizen E.J.A., Haagsman H.P.;
RT   "Characterization and expression sites of newly identified chicken
RT   collectins.";
RL   Mol. Immunol. 43:1604-1616(2006).
CC   -!- FUNCTION: Lectin that binds to various sugars: galactose > mannose =
CC       fucose > N-acetylglucosamine > N-acetylgalactosamine. Acts as a
CC       chemoattractant, probably involved in the regulation of cell migration.
CC       {ECO:0000250|UniProtKB:Q9Y6Z7}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9Y6Z7}. Golgi
CC       apparatus {ECO:0000250|UniProtKB:Q8CF98}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9Y6Z7}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in lung. Weakly
CC       expressed in larynx, syrinx and cranial air sac. Expressed throughout
CC       the lower gastrointestinal tract in increasing levels starting from a
CC       faint signal in duodenum and ending with relatively high signals in
CC       proctodeum, coprodeum and urodeum. In the upper part of the
CC       gastrointestinal tract, expressed in tongue, crop, and mucosa of the
CC       crop. {ECO:0000269|PubMed:16289291}.
CC   -!- SIMILARITY: Belongs to the COLEC10/COLEC11 family. {ECO:0000305}.
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DR   EMBL; DQ129668; AAZ29617.1; -; mRNA.
DR   RefSeq; NP_001034687.1; NM_001039598.1.
DR   AlphaFoldDB; Q2LK95; -.
DR   SMR; Q2LK95; -.
DR   STRING; 9031.ENSGALP00000043336; -.
DR   PaxDb; Q2LK95; -.
DR   Ensembl; ENSGALT00000069448; ENSGALP00000056221; ENSGALG00000033144.
DR   Ensembl; ENSGALT00000091970; ENSGALP00000069662; ENSGALG00000033144.
DR   GeneID; 420281; -.
DR   KEGG; gga:420281; -.
DR   CTD; 10584; -.
DR   VEuPathDB; HostDB:geneid_420281; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT00940000159374; -.
DR   HOGENOM; CLU_049894_3_2_1; -.
DR   InParanoid; Q2LK95; -.
DR   OMA; VCATHAI; -.
DR   OrthoDB; 1105722at2759; -.
DR   PhylomeDB; Q2LK95; -.
DR   Reactome; R-GGA-166662; Lectin pathway of complement activation.
DR   Reactome; R-GGA-166663; Initial triggering of complement.
DR   PRO; PR:Q2LK95; -.
DR   Proteomes; UP000000539; Chromosome 2.
DR   Bgee; ENSGALG00000033144; Expressed in liver and 11 other tissues.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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; Cytoplasm; Disulfide bond; Glycoprotein;
KW   Golgi apparatus; Lectin; Mannose-binding; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..277
FT                   /note="Collectin-10"
FT                   /id="PRO_5000140434"
FT   DOMAIN          56..115
FT                   /note="Collagen-like"
FT   DOMAIN          155..271
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   REGION          41..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"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        176..270
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        248..262
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   277 AA;  30436 MW;  B51F080A14003CA8 CRC64;
     MSRKKEQQLR KYGTLVVLFI FQVQIFGFDV DNRPTTDVCS THTILPGPKG DDGEKGDRGE
     VGKQGKVGPK GPKGNKGTVG DVGDQGMLGK IGPIGGKGDK GAKGISGVSG KKGKAGTVCD
     CGRYRRVVGQ LNINVARLNT SIKFVKNVIA GIRETDEKFY YIVKEEKNYR EALMHCRDRG
     GTLAMPKDEV TNALLADYIS SSGLFRAFIG LNDMEKEGQF VYADSSPLQN YSNWKDGEPH
     DSTGHEDCVE MLSTGEWNDS ECQVTIYFIC EFLKKRK