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Mannose-binding protein C (MBP-C) (Mannan-binding protein) (Ra-reactive factor polysaccharide-binding component p28A) (RaRF p28A)

 MBL2_RAT                Reviewed;         244 AA.
P08661;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 2.
20-JUN-2018, entry version 166.
RecName: Full=Mannose-binding protein C;
Short=MBP-C;
AltName: Full=Mannan-binding protein;
AltName: Full=Ra-reactive factor polysaccharide-binding component p28A;
Short=RaRF p28A;
Flags: Precursor;
Name=Mbl2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=1607365;
Wada M., Itoh N., Ohta M., Kawasaki T.;
"Characterization of rat liver mannan-binding protein gene.";
J. Biochem. 111:66-73(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=3009480;
Drickamer K., Dordal M.S., Reynolds L.;
"Mannose-binding proteins isolated from rat liver contain
carbohydrate-recognition domains linked to collagenous tails. Complete
primary structures and homology with pulmonary surfactant
apoprotein.";
J. Biol. Chem. 261:6878-6887(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Liver;
PubMed=3032924;
Oka S., Itoh N., Kawasaki T., Yamashina I.;
"Primary structure of rat liver mannan-binding protein deduced from
its cDNA sequence.";
J. Biochem. 101:135-144(1987).
[4]
SUBCELLULAR LOCATION.
PubMed=10903744; DOI=10.4049/jimmunol.165.3.1403;
Heise C.T., Nicholls J.R., Leamy C.E., Wallis R.;
"Impaired secretion of rat mannose-binding protein resulting from
mutations in the collagen-like domain.";
J. Immunol. 165:1403-1409(2000).
[5]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 133-244.
PubMed=8557671; DOI=10.1074/jbc.271.2.663;
Ng K.K.-S., Drickamer K., Weis W.I.;
"Structural analysis of monosaccharide recognition by rat liver
mannose-binding protein.";
J. Biol. Chem. 271:663-674(1996).
-!- FUNCTION: Calcium-dependent lectin involved in innate immune
defense. Binds mannose, fucose and N-acetylglucosamine on
different microorganisms and activates the lectin complement
pathway. Binds to late apoptotic cells, as well as to apoptotic
blebs and to necrotic cells, but not to early apoptotic cells,
facilitating their uptake by macrophages (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Oligomeric complex of 3 or more homotrimers. Interacts
with MASP1 and MASP2 (By similarity). Interacts with MEP1A and
MEP1B and may inhibit their catalytic activity (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- DOMAIN: The coiled-coil domain mediates trimerization.
{ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; M14103; AAA41554.1; -; mRNA.
EMBL; X05023; CAA28687.1; -; mRNA.
PIR; A24791; LNRTMC.
RefSeq; NP_073195.2; NM_022704.2.
RefSeq; XP_003749135.1; XM_003749087.3.
RefSeq; XP_003749136.1; XM_003749088.3.
RefSeq; XP_006231311.1; XM_006231249.2.
RefSeq; XP_006231312.1; XM_006231250.2.
UniGene; Rn.9667; -.
PDB; 1BV4; X-ray; 1.85 A; A/B/C/D=127-244.
PDB; 1KZA; X-ray; 1.74 A; 1/2=129-243.
PDB; 1KZB; X-ray; 1.80 A; 1/2=129-243.
PDB; 1KZC; X-ray; 1.85 A; 1/2=129-243.
PDB; 1KZD; X-ray; 1.90 A; 1/2=129-243.
PDB; 1KZE; X-ray; 1.80 A; 1/2=129-243.
PDB; 1RDI; X-ray; 1.80 A; 1/2=132-244.
PDB; 1RDJ; X-ray; 1.80 A; 1/2=132-244.
PDB; 1RDK; X-ray; 1.80 A; 1/2=132-244.
PDB; 1RDL; X-ray; 1.70 A; 1/2=132-244.
PDB; 1RDM; X-ray; 1.90 A; 1/2=132-244.
PDB; 1RDN; X-ray; 1.80 A; 1/2=132-244.
PDB; 1RDO; X-ray; 1.70 A; 1/2=132-244.
PDBsum; 1BV4; -.
PDBsum; 1KZA; -.
PDBsum; 1KZB; -.
PDBsum; 1KZC; -.
PDBsum; 1KZD; -.
PDBsum; 1KZE; -.
PDBsum; 1RDI; -.
PDBsum; 1RDJ; -.
PDBsum; 1RDK; -.
PDBsum; 1RDL; -.
PDBsum; 1RDM; -.
PDBsum; 1RDN; -.
PDBsum; 1RDO; -.
ProteinModelPortal; P08661; -.
SMR; P08661; -.
STRING; 10116.ENSRNOP00000064876; -.
PaxDb; P08661; -.
PeptideAtlas; P08661; -.
PRIDE; P08661; -.
Ensembl; ENSRNOT00000072188; ENSRNOP00000064876; ENSRNOG00000050305.
GeneID; 100911854; -.
GeneID; 64668; -.
KEGG; rno:100911854; -.
KEGG; rno:64668; -.
UCSC; RGD:67380; rat.
CTD; 4153; -.
RGD; 67380; Mbl2.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00700000104102; -.
HOVERGEN; HBG108270; -.
InParanoid; P08661; -.
KO; K03991; -.
OMA; YSETVTC; -.
OrthoDB; EOG091G0R93; -.
Reactome; R-RNO-166662; Lectin pathway of complement activation.
Reactome; R-RNO-166663; Initial triggering of complement.
EvolutionaryTrace; P08661; -.
PRO; PR:P08661; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000050305; -.
Genevisible; P08661; RN.
GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; IDA:RGD.
GO; GO:0005534; F:galactose binding; IDA:RGD.
GO; GO:0005537; F:mannose binding; IDA:RGD.
GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:RGD.
GO; GO:0002020; F:protease binding; IPI:RGD.
GO; GO:0043621; F:protein self-association; IDA:RGD.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0001867; P:complement activation, lectin pathway; IBA:GO_Central.
GO; GO:0045917; P:positive regulation of complement activation; IDA:RGD.
GO; GO:0010954; P:positive regulation of protein processing; IDA:RGD.
GO; GO:0051259; P:protein complex oligomerization; IMP:RGD.
GO; GO:0051260; P:protein homooligomerization; IDA:RGD.
GO; GO:0070207; P:protein homotrimerization; IDA:RGD.
CDD; cd03591; CLECT_collectin_like; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR008160; Collagen.
InterPro; IPR033990; Collectin_CTLD.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR037570; Mannose-binding_protein.
PANTHER; PTHR24020:SF0; PTHR24020:SF0; 1.
Pfam; PF01391; Collagen; 1.
Pfam; PF00059; Lectin_C; 1.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
1: Evidence at protein level;
3D-structure; Calcium; Coiled coil; Collagen;
Complement activation lectin pathway; Complement pathway;
Complete proteome; Direct protein sequencing; Disulfide bond;
Hydroxylation; Immunity; Innate immunity; Lectin; Mannose-binding;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 18
CHAIN 19 244 Mannose-binding protein C.
{ECO:0000269|PubMed:3032924}.
/FTId=PRO_0000017411.
DOMAIN 38 96 Collagen-like.
DOMAIN 129 241 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
COILED 108 126 {ECO:0000250}.
MOD_RES 43 43 4-hydroxyproline. {ECO:0000255}.
MOD_RES 58 58 4-hydroxyproline. {ECO:0000255}.
MOD_RES 69 69 4-hydroxyproline. {ECO:0000255}.
MOD_RES 78 78 4-hydroxyproline. {ECO:0000255}.
MOD_RES 81 81 4-hydroxyproline. {ECO:0000255}.
DISULFID 29 29 Interchain.
DISULFID 34 34 Interchain.
DISULFID 151 240
DISULFID 218 232
CONFLICT 38 39 GL -> AW (in Ref. 2; AAA41554).
{ECO:0000305}.
STRAND 134 137 {ECO:0000244|PDB:1RDL}.
HELIX 144 153 {ECO:0000244|PDB:1RDL}.
HELIX 164 173 {ECO:0000244|PDB:1RDL}.
STRAND 178 183 {ECO:0000244|PDB:1RDL}.
STRAND 185 187 {ECO:0000244|PDB:1RDL}.
STRAND 190 193 {ECO:0000244|PDB:1BV4}.
STRAND 218 221 {ECO:0000244|PDB:1RDL}.
STRAND 227 230 {ECO:0000244|PDB:1RDL}.
STRAND 236 242 {ECO:0000244|PDB:1RDL}.
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


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