CONG_BOVIN
ID CONG_BOVIN Reviewed; 371 AA.
AC P23805; O97748; Q58CU7; Q9TRF6;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Conglutinin;
DE Flags: Precursor;
GN Name=CGN1;
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 [MRNA].
RX PubMed=8460993; DOI=10.1006/bbrc.1993.1222;
RA Suzuki Y., Yin Y., Makino M., Kurimura T., Wakamiya N.;
RT "Cloning and sequencing of a cDNA coding for bovine conglutinin.";
RL Biochem. Biophys. Res. Commun. 191:335-342(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7684896; DOI=10.1042/bj2920157;
RA Lu J., Laursen S.B., Thiel S., Jensenius J.C., Reid B.M.;
RT "The cDNA cloning of conglutinin and identification of liver as a primary
RT site of synthesis of conglutinin in members of the Bovidae.";
RL Biochem. J. 292:157-162(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8163202; DOI=10.1016/0378-1119(94)90585-1;
RA Liou L.S., Sastry R., Hartshorn K.L., Lee Y.M., Okarma T.B., Tauber A.I.,
RA Sastry K.N.;
RT "Bovine conglutinin (BC) mRNA expressed in liver: cloning and
RT characterization of the BC cDNA reveals strong homology to surfactant
RT protein-D.";
RL Gene 141:277-281(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Semen;
RX PubMed=8207234;
RA Liou L.S., Sastry R., Hartshorn K.L., Lee Y.M., Okarma T.B., Tauber A.I.,
RA Sastry K.N.;
RT "Bovine conglutinin gene exon structure reveals its evolutionary
RT relationship to surfactant protein-D.";
RL J. Immunol. 153:173-180(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8297370; DOI=10.1006/bbrc.1994.1087;
RA Kawasaki N., Itoh N., Kawasaki T.;
RT "Gene organization and 5'-flanking region sequence of conglutinin: a C-type
RT mammalian lectin containing a collagen-like domain.";
RL Biochem. Biophys. Res. Commun. 198:597-604(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [7]
RP PROTEIN SEQUENCE OF 21-371, AND HYDROXYLATION AT LYS-63; PRO-78; LYS-87;
RP PRO-96; LYS-99; PRO-108; PRO-111; PRO-129; PRO-132; LYS-135; LYS-141;
RP PRO-147; PRO-153; LYS-159; LYS-162; PRO-171; PRO-195 AND LYS-198.
RX PubMed=1993651; DOI=10.1016/s0021-9258(18)49904-8;
RA Lee Y.-M., Leiby K.R., Allar J., Paris K., Lerch B., Okarma T.B.;
RT "Primary structure of bovine conglutinin, a member of the C-type animal
RT lectin family.";
RL J. Biol. Chem. 266:2715-2723(1991).
RN [8]
RP PRELIMINARY PROTEIN SEQUENCE OF 21-52.
RX PubMed=3566740; DOI=10.1016/0006-291x(87)91402-1;
RA Young N.M., Leon M.A.;
RT "The carbohydrate specificity of conglutinin and its homology to proteins
RT in the hepatic lectin family.";
RL Biochem. Biophys. Res. Commun. 143:645-651(1987).
RN [9]
RP PROTEIN SEQUENCE OF 21-80.
RX PubMed=8328957; DOI=10.1042/bj2930015;
RA Malhotra R., Laursen S.B., Willis A.C., Sim R.B.;
RT "Localization of the receptor-binding site in the collectin family of
RT proteins.";
RL Biochem. J. 293:15-19(1993).
CC -!- FUNCTION: Calcium-dependent lectin-like protein which binds to a yeast
CC cell wall extract and immune complexes through the complement component
CC (C3bi). It is capable of binding non-reducing terminal N-
CC acetylglucosamine, mannose, and fucose residues.
CC -!- SUBUNIT: Oligomeric complex of 4 set of homotrimers.
CC -!- PTM: The hydroxylysines may be O-glycosylated.
CC -!- SIMILARITY: Belongs to the SFTPD family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D14085; BAA03170.1; -; mRNA.
DR EMBL; X71774; CAA50665.1; -; mRNA.
DR EMBL; L18871; AAA20126.1; -; mRNA.
DR EMBL; U06860; AAB60624.1; -; Genomic_DNA.
DR EMBL; U06854; AAB60624.1; JOINED; Genomic_DNA.
DR EMBL; U06855; AAB60624.1; JOINED; Genomic_DNA.
DR EMBL; U06856; AAB60624.1; JOINED; Genomic_DNA.
DR EMBL; U06857; AAB60624.1; JOINED; Genomic_DNA.
DR EMBL; U06858; AAB60624.1; JOINED; Genomic_DNA.
DR EMBL; U06859; AAB60624.1; JOINED; Genomic_DNA.
DR EMBL; D25302; BAA04983.2; -; Genomic_DNA.
DR EMBL; BT021850; AAX46697.1; -; mRNA.
DR PIR; I45878; I45878.
DR PIR; JN0450; JN0450.
DR RefSeq; NP_783630.2; NM_175699.2.
DR PDB; 6RYG; X-ray; 0.97 A; A=244-371.
DR PDB; 6RYJ; X-ray; 1.25 A; A=244-371.
DR PDB; 6RYM; X-ray; 1.46 A; A=244-371.
DR PDB; 6RYN; X-ray; 1.00 A; A=244-371.
DR PDBsum; 6RYG; -.
DR PDBsum; 6RYJ; -.
DR PDBsum; 6RYM; -.
DR PDBsum; 6RYN; -.
DR AlphaFoldDB; P23805; -.
DR SMR; P23805; -.
DR STRING; 9913.ENSBTAP00000003773; -.
DR PaxDb; P23805; -.
DR PRIDE; P23805; -.
DR Ensembl; ENSBTAT00000003773; ENSBTAP00000003773; ENSBTAG00000047317.
DR GeneID; 281068; -.
DR KEGG; bta:281068; -.
DR CTD; 281068; -.
DR VEuPathDB; HostDB:ENSBTAG00000047317; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000155748; -.
DR HOGENOM; CLU_049894_3_0_1; -.
DR InParanoid; P23805; -.
DR OMA; EVESICY; -.
DR OrthoDB; 1341167at2759; -.
DR TreeFam; TF330481; -.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000047317; Expressed in liver and 27 other tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; 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 3D-structure; Calcium; Collagen; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydroxylation; Lectin; Mannose-binding; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1993651,
FT ECO:0000269|PubMed:8328957"
FT CHAIN 21..371
FT /note="Conglutinin"
FT /id="PRO_0000017370"
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 47..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 MOD_RES 63
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 78
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 87
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 96
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 99
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 108
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 111
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 129
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 132
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 135
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 141
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 147
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 153
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 159
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 162
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 171
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 195
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1993651"
FT MOD_RES 198
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:1993651"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 275..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 347..361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 173
FT /note="R -> H (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="K -> S (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="V -> A (in Ref. 2; CAA50665)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="E -> V (in Ref. 2; CAA50665)"
FT /evidence="ECO:0000305"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:6RYG"
FT STRAND 257..266
FT /evidence="ECO:0007829|PDB:6RYG"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:6RYG"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:6RYN"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:6RYG"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:6RYG"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:6RYG"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:6RYG"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:6RYG"
SQ SEQUENCE 371 AA; 37995 MW; 867BB41992544B1F CRC64;
MLLLPLSVLL LLTQPWRSLG AEMTTFSQKI LANACTLVMC SPLESGLPGH DGQDGRECPH
GEKGDPGSPG PAGRAGRPGW VGPIGPKGDN GFVGEPGPKG DTGPRGPPGM PGPAGREGPS
GKQGSMGPPG TPGPKGETGP KGGVGAPGIQ GFPGPSGLKG EKGAPGETGA PGRAGVTGPS
GAIGPQGPSG ARGPPGLKGD RGDPGETGAK GESGLAEVNA LKQRVTILDG HLRRFQNAFS
QYKKAVLFPD GQAVGEKIFK TAGAVKSYSD AEQLCREAKG QLASPRSSAE NEAVTQMVRA
QEKNAYLSMN DISTEGRFTY PTGEILVYSN WADGEPNNSD EGQPENCVEI FPDGKWNDVP
CSKQLLVICE F
