ID   CL46_BOVIN              Reviewed;         371 AA.
AC   Q8MHZ9;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Collectin-46;
DE            Short=CL-46;
DE   AltName: Full=46 kDa collectin;
DE   Flags: Precursor;
GN   Name=CL46;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=12421952; DOI=10.4049/jimmunol.169.10.5726;
RA   Hansen S., Holm D., Moeller V., Vitved L., Bendixen C., Reid K.B.M.,
RA   Skjoedt K., Holmskov U.;
RT   "CL-46, a novel collectin highly expressed in bovine thymus and liver.";
RL   J. Immunol. 169:5726-5734(2002).
CC   -!- SUBUNIT: Oligomeric complex of 4 set of homotrimers. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Highly expressed in thymus and liver.
CC   -!- PTM: Hydroxylated. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SFTPD family. {ECO:0000305}.
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DR   EMBL; AF509589; AAM34742.1; -; Genomic_DNA.
DR   EMBL; AF509590; AAM34743.1; -; mRNA.
DR   RefSeq; NP_001001856.1; NM_001001856.1.
DR   AlphaFoldDB; Q8MHZ9; -.
DR   SMR; Q8MHZ9; -.
DR   STRING; 9913.ENSBTAP00000018649; -.
DR   PaxDb; Q8MHZ9; -.
DR   Ensembl; ENSBTAT00000018649; ENSBTAP00000018649; ENSBTAG00000006536.
DR   GeneID; 415114; -.
DR   KEGG; bta:415114; -.
DR   CTD; 415114; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006536; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT00940000155748; -.
DR   InParanoid; Q8MHZ9; -.
DR   OMA; CRPPEGG; -.
DR   OrthoDB; 1341167at2759; -.
DR   Proteomes; UP000009136; Chromosome 28.
DR   Bgee; ENSBTAG00000006536; Expressed in anterior segment of eyeball and 24 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:0005771; C:multivesicular body; IBA:GO_Central.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IBA:GO_Central.
DR   GO; GO:0043129; P:surfactant homeostasis; IBA:GO_Central.
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; IPR016187; CTDL_fold.
DR   InterPro; IPR015097; Surfac_D-trimer.
DR   Pfam; PF01391; Collagen; 2.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF09006; Surfac_D-trimer; 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; Hydroxylation; Lectin;
KW   Mannose-binding; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..371
FT                   /note="Collectin-46"
FT                   /id="PRO_0000017372"
FT   DOMAIN          46..216
FT                   /note="Collagen-like"
FT   DOMAIN          273..371
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   REGION          43..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           201..203
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        100..114
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        275..369
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        347..361
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   371 AA;  37445 MW;  108AC45A91420E83 CRC64;
     MLLLPLSVLL LLTQPWRSLG AEMKIYSQKT LANGCTLVVC RPPEGGLPGR DGQDGREGPQ
     GEKGDPGSPG PAGRAGRPGP AGPIGPKGDN GSAGEPGPKG DTGPPGPPGM PGPAGREGPS
     GKQGSMGPPG TPGPKGDTGP KGGMGAPGMQ GSPGPAGLKG ERGAPGELGA PGSAGVAGPA
     GAIGPQGPSG ARGPPGLKGD RGDPGERGAK GESGLADVNA LKQRVTILEG QLQRLQNAFS
     RYKKAVLFPD GQAVGKKIFK TAGAVKSYSD AQQLCREAKG QLASPRSAAE NEAVAQLVRA
     KNNDAFLSMN DISTEGKFTY PTGESLVYSN WASGEPNNNN AGQPENCVQI YREGKWNDVP
     CSEPLLVICE F