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P08661 (MBL2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Mannose-binding protein C
Short name=MBP-C
Alternative name(s):
Mannan-binding protein
Ra-reactive factor polysaccharide-binding component p28A
Short name=RaRF p28A
Gene names
Name:Mbl2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

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.

Subcellular location

Secreted By similarity Ref.4.

Sequence similarities

Contains 1 C-type lectin domain.

Contains 1 collagen-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 244226Mannose-binding protein C Ref.3
PRO_0000017411

Regions

Domain38 – 9659Collagen-like
Domain129 – 241113C-type lectin

Amino acid modifications

Modified residue4314-hydroxyproline Potential
Modified residue5814-hydroxyproline Potential
Modified residue6914-hydroxyproline
Modified residue7814-hydroxyproline Potential
Modified residue8114-hydroxyproline Potential
Disulfide bond29Interchain
Disulfide bond34Interchain
Disulfide bond151 ↔ 240
Disulfide bond218 ↔ 232

Experimental info

Sequence conflict38 – 392GL → AW in AAA41554. Ref.2

Secondary structure

1 ................. 244
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08661 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: F0706E2AA9331531

FASTA24426,014
        10         20         30         40         50         60 
MSLFTSFLLL CVLTAVYAET LTEGAQSSCP VIACSSPGLN GFPGKDGHDG AKGEKGEPGQ 

        70         80         90        100        110        120 
GLRGLQGPPG KVGPAGPPGN PGSKGATGPK GDRGESVEFD TTNIDLEIAA LRSELRAMRK 

       130        140        150        160        170        180 
WVLLSMSENV GKKYFMSSVR RMPLNRAKAL CSELQGTVAT PRNAEENRAI QNVAKDVAFL 

       190        200        210        220        230        240 
GITDQRTENV FEDLTGNRVR YTNWNEGEPN NVGSGENCVV LLTNGKWNDV PCSDSFLVVC 


EFSD

« Hide

References

[1]"Characterization of rat liver mannan-binding protein gene."
Wada M., Itoh N., Ohta M., Kawasaki T.
J. Biochem. 111:66-73(1992) [PubMed: 1607365] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Mannose-binding proteins isolated from rat liver contain carbohydrate-recognition domains linked to collagenous tails. Complete primary structures and homology with pulmonary surfactant apoprotein."
Drickamer K., Dordal M.S., Reynolds L.
J. Biol. Chem. 261:6878-6887(1986) [PubMed: 3009480] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[3]"Primary structure of rat liver mannan-binding protein deduced from its cDNA sequence."
Oka S., Itoh N., Kawasaki T., Yamashina I.
J. Biochem. 101:135-144(1987) [PubMed: 3032924] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Liver.
[4]"Impaired secretion of rat mannose-binding protein resulting from mutations in the collagen-like domain."
Heise C.T., Nicholls J.R., Leamy C.E., Wallis R.
J. Immunol. 165:1403-1409(2000) [PubMed: 10903744] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[5]"Structural analysis of monosaccharide recognition by rat liver mannose-binding protein."
Ng K.K.-S., Drickamer K., Weis W.I.
J. Biol. Chem. 271:663-674(1996) [PubMed: 8557671] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 133-244.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M14103 mRNA. Translation: AAA41554.1.
X05023 mRNA. Translation: CAA28687.1.
IPIIPI00382128.
PIRLNRTMC. A24791.
RefSeqNP_073195.2. NM_022704.2.
UniGeneRn.9667.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BV4X-ray1.85A/B/C/D127-244[»]
1KZAX-ray1.741/2129-243[»]
1KZBX-ray1.801/2129-243[»]
1KZCX-ray1.851/2129-243[»]
1KZDX-ray1.901/2129-243[»]
1KZEX-ray1.801/2129-243[»]
1RDIX-ray1.801/2132-244[»]
1RDJX-ray1.801/2132-244[»]
1RDKX-ray1.801/2132-244[»]
1RDLX-ray1.701/2132-244[»]
1RDMX-ray1.901/2132-244[»]
1RDNX-ray1.801/2132-244[»]
1RDOX-ray1.701/2132-244[»]
ProteinModelPortalP08661.
SMRP08661. Positions 129-243.
ModBaseSearch...

Protein-protein interaction databases

STRINGP08661.

Proteomic databases

PRIDEP08661.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID64668.
KEGGrno:64668.
UCSCNM_022704. rat.

Organism-specific databases

CTD4153.
RGD67380. Mbl2.

Phylogenomic databases

eggNOGroNOG15949.
HOVERGENHBG108270.
InParanoidP08661.
OMASYSETVT.

Gene expression databases

ArrayExpressP08661.
GenevestigatorP08661.
GermOnlineENSRNOG00000011637. Rattus norvegicus.

Family and domain databases

InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
[Graphical view]
Gene3DG3DSA:3.10.100.10. C-type_lectin-like. 1 hit.
KOK03991.
PfamPF01391. Collagen. 1 hit.
PF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMSSF56436. C-type_lectin_fold. 1 hit.
PROSITEPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio613657.

Entry information

Entry nameMBL2_RAT
AccessionPrimary (citable) accession number: P08661
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: February 1, 1991
Last modified: November 16, 2011
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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