MBL2_BOVIN
ID MBL2_BOVIN Reviewed; 249 AA.
AC O02659; A4IFQ1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Mannose-binding protein C;
DE Short=MBP-C;
DE AltName: Full=Mannan-binding protein;
DE Flags: Precursor;
GN Name=MBL;
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].
RC TISSUE=Liver;
RX PubMed=9074491; DOI=10.1016/s0378-1119(96)00664-6;
RA Kawai T., Suzuki Y., Eda S., Ohtani K., Kase T., Fujinaga Y., Sakamoto T.,
RA Kurimura T., Wakamiya N.;
RT "Cloning and characterization of a cDNA encoding bovine mannan-binding
RT protein.";
RL Gene 186:161-165(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcium-dependent lectin involved in innate immune defense.
CC Binds mannose, fucose and N-acetylglucosamine on different
CC microorganisms and activates the lectin complement pathway. Binds to
CC late apoptotic cells, as well as to apoptotic blebs and to necrotic
CC cells, but not to early apoptotic cells, facilitating their uptake by
CC macrophages (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex of 3 or more homotrimers. Interacts with
CC MASP1 and MASP2 (By similarity). Interacts with MEP1A and MEP1B and may
CC inhibit their catalytic activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DOMAIN: The coiled-coil domain mediates trimerization. {ECO:0000250}.
CC -!- PTM: Hydroxylation on proline residues within the sequence motif, GXPG,
CC is most likely to be 4-hydroxy as this fits the requirement for 4-
CC hydroxylation in vertebrates. {ECO:0000250}.
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DR EMBL; D73408; BAA18935.1; -; mRNA.
DR EMBL; BC134704; AAI34705.1; -; mRNA.
DR RefSeq; NP_776532.1; NM_174107.2.
DR RefSeq; XP_005225409.1; XM_005225352.3.
DR AlphaFoldDB; O02659; -.
DR SMR; O02659; -.
DR STRING; 9913.ENSBTAP00000009270; -.
DR PaxDb; O02659; -.
DR PeptideAtlas; O02659; -.
DR PRIDE; O02659; -.
DR Ensembl; ENSBTAT00000009270; ENSBTAP00000009270; ENSBTAG00000007049.
DR GeneID; 281297; -.
DR KEGG; bta:281297; -.
DR CTD; 4153; -.
DR VEuPathDB; HostDB:ENSBTAG00000007049; -.
DR VGNC; VGNC:31280; MBL2.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154368; -.
DR HOGENOM; CLU_049894_3_0_1; -.
DR InParanoid; O02659; -.
DR OMA; CAKFQAS; -.
DR OrthoDB; 1222552at2759; -.
DR TreeFam; TF330481; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000007049; Expressed in liver and 23 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:1905370; C:serine-type endopeptidase complex; IEA:Ensembl.
DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0001867; P:complement activation, lectin pathway; IEA:UniProtKB-KW.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR GO; GO:0048525; P:negative regulation of viral process; IEA:Ensembl.
DR GO; GO:1903028; P:positive regulation of opsonization; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:Ensembl.
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; IPR037570; Mannose-binding_protein_C.
DR PANTHER; PTHR24024:SF34; PTHR24024:SF34; 1.
DR Pfam; PF01391; Collagen; 1.
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; Coiled coil; Collagen; Complement activation lectin pathway;
KW Complement pathway; Disulfide bond; Hydroxylation; Immunity;
KW Innate immunity; Lectin; Mannose-binding; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..249
FT /note="Mannose-binding protein C"
FT /id="PRO_0000017397"
FT DOMAIN 43..101
FT /note="Collagen-like"
FT DOMAIN 135..246
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 43..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 113..131
FT /evidence="ECO:0000250"
FT MOD_RES 48
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 63
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 74
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 83
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 86
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT DISULFID 34
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 39
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 156..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 223..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 249 AA; 26471 MW; 29FC9F5927A66DD5 CRC64;
MSLFTSLPFL LLTAVTASCA DTETENCENI RKTCPVIACG PPGINGIPGK DGRDGAKGEK
GEPGQGLRGS QGPPGKMGPQ GTPGIPGIPG PIGQKGDPGE NMGDYIRLAT SERATLQSEL
NQIKNWLIFS LGKRVGKKAF FTNGKKMPFN EVKTLCAQFQ GRVATPMNAE ENRALKDLVT
EEAFLGITDQ ETEGKFVDLT GKGVTYQNWN DGEPNNASPG EHCVTLLSDG TWNDIACSAS
FLTVCEFSL
