MBL2_RAT
ID MBL2_RAT Reviewed; 244 AA.
AC P08661;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Mannose-binding protein C;
DE Short=MBP-C;
DE AltName: Full=Mannan-binding protein;
DE AltName: Full=Ra-reactive factor polysaccharide-binding component p28A;
DE Short=RaRF p28A;
DE Flags: Precursor;
GN Name=Mbl2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1607365; DOI=10.1093/oxfordjournals.jbchem.a123720;
RA Wada M., Itoh N., Ohta M., Kawasaki T.;
RT "Characterization of rat liver mannan-binding protein gene.";
RL J. Biochem. 111:66-73(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=3009480; DOI=10.1016/s0021-9258(19)62698-0;
RA Drickamer K., Dordal M.S., Reynolds L.;
RT "Mannose-binding proteins isolated from rat liver contain carbohydrate-
RT recognition domains linked to collagenous tails. Complete primary
RT structures and homology with pulmonary surfactant apoprotein.";
RL J. Biol. Chem. 261:6878-6887(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=3032924; DOI=10.1093/oxfordjournals.jbchem.a121884;
RA Oka S., Itoh N., Kawasaki T., Yamashina I.;
RT "Primary structure of rat liver mannan-binding protein deduced from its
RT cDNA sequence.";
RL J. Biochem. 101:135-144(1987).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=10903744; DOI=10.4049/jimmunol.165.3.1403;
RA Heise C.T., Nicholls J.R., Leamy C.E., Wallis R.;
RT "Impaired secretion of rat mannose-binding protein resulting from mutations
RT in the collagen-like domain.";
RL J. Immunol. 165:1403-1409(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 133-244.
RX PubMed=8557671; DOI=10.1074/jbc.271.2.663;
RA Ng K.K.-S., Drickamer K., Weis W.I.;
RT "Structural analysis of monosaccharide recognition by rat liver mannose-
RT binding protein.";
RL J. Biol. Chem. 271:663-674(1996).
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}.
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DR EMBL; M14103; AAA41554.1; -; mRNA.
DR EMBL; X05023; CAA28687.1; -; mRNA.
DR PIR; A24791; LNRTMC.
DR RefSeq; NP_073195.2; NM_022704.2.
DR RefSeq; XP_003749135.1; XM_003749087.3.
DR RefSeq; XP_003749136.1; XM_003749088.3.
DR RefSeq; XP_006231311.1; XM_006231249.2.
DR RefSeq; XP_006231312.1; XM_006231250.2.
DR PDB; 1BV4; X-ray; 1.85 A; A/B/C/D=127-244.
DR PDB; 1KZA; X-ray; 1.74 A; 1/2=129-243.
DR PDB; 1KZB; X-ray; 1.80 A; 1/2=129-243.
DR PDB; 1KZC; X-ray; 1.85 A; 1/2=129-243.
DR PDB; 1KZD; X-ray; 1.90 A; 1/2=129-243.
DR PDB; 1KZE; X-ray; 1.80 A; 1/2=129-243.
DR PDB; 1RDI; X-ray; 1.80 A; 1/2=132-244.
DR PDB; 1RDJ; X-ray; 1.80 A; 1/2=132-244.
DR PDB; 1RDK; X-ray; 1.80 A; 1/2=132-244.
DR PDB; 1RDL; X-ray; 1.70 A; 1/2=132-244.
DR PDB; 1RDM; X-ray; 1.90 A; 1/2=132-244.
DR PDB; 1RDN; X-ray; 1.80 A; 1/2=132-244.
DR PDB; 1RDO; X-ray; 1.70 A; 1/2=132-244.
DR PDBsum; 1BV4; -.
DR PDBsum; 1KZA; -.
DR PDBsum; 1KZB; -.
DR PDBsum; 1KZC; -.
DR PDBsum; 1KZD; -.
DR PDBsum; 1KZE; -.
DR PDBsum; 1RDI; -.
DR PDBsum; 1RDJ; -.
DR PDBsum; 1RDK; -.
DR PDBsum; 1RDL; -.
DR PDBsum; 1RDM; -.
DR PDBsum; 1RDN; -.
DR PDBsum; 1RDO; -.
DR AlphaFoldDB; P08661; -.
DR SMR; P08661; -.
DR CORUM; P08661; -.
DR STRING; 10116.ENSRNOP00000064876; -.
DR UniLectin; P08661; -.
DR PaxDb; P08661; -.
DR PeptideAtlas; P08661; -.
DR GeneID; 64668; -.
DR KEGG; rno:64668; -.
DR UCSC; RGD:67380; rat.
DR CTD; 4153; -.
DR RGD; 67380; Mbl2.
DR eggNOG; KOG4297; Eukaryota.
DR HOGENOM; CLU_049894_3_0_1; -.
DR InParanoid; P08661; -.
DR OMA; CAKFQAS; -.
DR OrthoDB; 1222552at2759; -.
DR EvolutionaryTrace; P08661; -.
DR PRO; PR:P08661; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000050305; Expressed in liver and 2 other tissues.
DR Genevisible; P08661; RN.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IMP:RGD.
DR GO; GO:1905370; C:serine-type endopeptidase complex; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0005534; F:galactose binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0005537; F:mannose binding; IDA:RGD.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:RGD.
DR GO; GO:0002020; F:protease binding; IPI:RGD.
DR GO; GO:0043621; F:protein self-association; IDA:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; ISO:RGD.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0001867; P:complement activation, lectin pathway; ISO:RGD.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; ISO:RGD.
DR GO; GO:0051873; P:killing by host of symbiont cells; ISO:RGD.
DR GO; GO:0048525; P:negative regulation of viral process; ISO:RGD.
DR GO; GO:0045917; P:positive regulation of complement activation; IDA:RGD.
DR GO; GO:1903028; P:positive regulation of opsonization; ISO:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:RGD.
DR GO; GO:0010954; P:positive regulation of protein processing; IDA:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
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 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 1: Evidence at protein level;
KW 3D-structure; Calcium; Coiled coil; Collagen;
KW Complement activation lectin pathway; Complement pathway;
KW Direct protein sequencing; Disulfide bond; Hydroxylation; Immunity;
KW Innate immunity; Lectin; Mannose-binding; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..18
FT CHAIN 19..244
FT /note="Mannose-binding protein C"
FT /evidence="ECO:0000269|PubMed:3032924"
FT /id="PRO_0000017411"
FT DOMAIN 38..96
FT /note="Collagen-like"
FT DOMAIN 129..241
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 43..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 108..126
FT /evidence="ECO:0000250"
FT MOD_RES 43
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 58
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 69
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 78
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 81
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT DISULFID 29
FT /note="Interchain"
FT DISULFID 34
FT /note="Interchain"
FT DISULFID 151..240
FT DISULFID 218..232
FT CONFLICT 38..39
FT /note="GL -> AW (in Ref. 2; AAA41554)"
FT /evidence="ECO:0000305"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:1RDL"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:1RDL"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:1RDL"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:1RDL"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1RDL"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:1BV4"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:1RDL"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1RDL"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:1RDL"
SQ SEQUENCE 244 AA; 26014 MW; F0706E2AA9331531 CRC64;
MSLFTSFLLL CVLTAVYAET LTEGAQSSCP VIACSSPGLN GFPGKDGHDG AKGEKGEPGQ
GLRGLQGPPG KVGPAGPPGN PGSKGATGPK GDRGESVEFD TTNIDLEIAA LRSELRAMRK
WVLLSMSENV GKKYFMSSVR RMPLNRAKAL CSELQGTVAT PRNAEENRAI QNVAKDVAFL
GITDQRTENV FEDLTGNRVR YTNWNEGEPN NVGSGENCVV LLTNGKWNDV PCSDSFLVVC
EFSD
