ID   CL43_BOVIN              Reviewed;         321 AA.
AC   P42916; Q1LZ84; Q8WMF4;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-JAN-2003, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Collectin-43;
DE            Short=CL-43;
DE   AltName: Full=43 kDa collectin;
DE   Flags: Precursor;
GN   Name=CL43;
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].
RC   TISSUE=Liver;
RX   PubMed=12527419; DOI=10.1016/s0167-4781(02)00531-6;
RA   Hansen S., Holm D., Moeller V., Vitved L., Bendixen C., Skjoedt K.,
RA   Holmskov U.;
RT   "Genomic and molecular characterization of CL-43 and its proximal
RT   promoter.";
RL   Biochim. Biophys. Acta 1625:1-10(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 21-321, AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=8163480; DOI=10.1016/s0021-9258(17)32646-7;
RA   Lim B.-L., Willis A.C., Reid K.B.M., Lu J., Laursen S.B., Jensenius J.C.,
RA   Holmskov U.;
RT   "Primary structure of bovine collectin-43 (CL-43). Comparison with
RT   conglutinin and lung surfactant protein-D.";
RL   J. Biol. Chem. 269:11820-11824(1994).
CC   -!- FUNCTION: Lectin that binds to various sugars: mannose = ManNAc >
CC       fucose > GlcNAc > glucose = maltose > galactose > lactose > GalNAc.
CC       Could play a role in immune defense.
CC   -!- SUBUNIT: Oligomeric complex of 4 set of homotrimers.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Liver specific.
CC   -!- PTM: Hydroxylated. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SFTPD family. {ECO:0000305}.
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DR   EMBL; AY071821; AAL61855.1; -; mRNA.
DR   EMBL; AY071822; AAL61856.1; -; Genomic_DNA.
DR   EMBL; BC116147; AAI16148.1; -; mRNA.
DR   EMBL; X75912; CAA53511.1; ALT_SEQ; mRNA.
DR   PIR; A53570; A53570.
DR   RefSeq; NP_001002237.1; NM_001002237.1.
DR   AlphaFoldDB; P42916; -.
DR   SMR; P42916; -.
DR   PaxDb; P42916; -.
DR   PRIDE; P42916; -.
DR   GeneID; 431784; -.
DR   KEGG; bta:431784; -.
DR   CTD; 431784; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   InParanoid; P42916; -.
DR   OrthoDB; 1341167at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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   1: Evidence at protein level;
KW   Calcium; Collagen; Direct protein sequencing; Disulfide bond;
KW   Hydroxylation; Lectin; Mannose-binding; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..20
FT   CHAIN           21..321
FT                   /note="Collectin-43"
FT                   /id="PRO_0000017371"
FT   DOMAIN          49..162
FT                   /note="Collagen-like"
FT   DOMAIN          222..321
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   REGION          43..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        224..319
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        297..311
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CONFLICT        37
FT                   /note="L -> V (in Ref. 2; AAI16148)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="A -> T (in Ref. 2; AAI16148)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        125
FT                   /note="T -> A (in Ref. 3; CAA53511)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        159
FT                   /note="R -> K (in Ref. 2; AAI16148)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        286
FT                   /note="N -> G (in Ref. 3; CAA53511)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   321 AA;  33616 MW;  12BF120BB48861A1 CRC64;
     MLPLPLSILL LLTQSQSFLG EEMDVYSEKT LTDPCTLVVC APPADSLRGH DGRDGKEGPQ
     GEKGDPGPPG MPGPAGREGP SGRQGSMGPP GTPGPKGEPG PEGGVGAPGM PGSPGPAGLK
     GERGTPGPGG AIGPQGPSGA MGPPGLKGDR GDPGEKGARG ETSVLEVDTL RQRMRNLEGE
     VQRLQNIVTQ YRKAVLFPDG QAVGEKIFKT AGAVKSYSDA EQLCREAKGQ LASPRSSAEN
     EAVTQLVRAK NKHAYLSMND ISKEGKFTYP TGGSLDYSNW APGEPNNRAK DEGPENCLEI
     YSDGNWNDIE CREERLVICE F