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Protein

Mannose-binding protein C

Gene

Mbl2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  • calcium ion binding Source: RGD
  • galactose binding Source: RGD
  • mannose binding Source: RGD
  • phosphatidylinositol-4-phosphate binding Source: RGD
  • protease binding Source: RGD
  • protein self-association Source: RGD

GO - Biological processi

  • complement activation, classical pathway Source: UniProtKB-KW
  • complement activation, lectin pathway Source: UniProtKB-KW
  • positive regulation of complement activation Source: RGD
  • positive regulation of protein processing Source: RGD
  • protein homooligomerization Source: RGD
  • protein homotrimerization Source: RGD
  • protein oligomerization Source: RGD
Complete GO annotation...

Keywords - Biological processi

Complement activation lectin pathway, Complement pathway, Immunity, Innate immunity

Keywords - Ligandi

Calcium, Lectin, Mannose-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Mbl2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi67380. Mbl2.

Subcellular locationi

GO - Cellular componenti

  • collagen trimer Source: UniProtKB-KW
  • extracellular space Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 244226Mannose-binding protein C1 PublicationPRO_0000017411Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 – 29Interchain
Disulfide bondi34 – 34Interchain
Modified residuei43 – 4314-hydroxyprolineSequence analysis
Modified residuei58 – 5814-hydroxyprolineSequence analysis
Modified residuei69 – 6914-hydroxyprolineSequence analysis
Modified residuei78 – 7814-hydroxyprolineSequence analysis
Modified residuei81 – 8114-hydroxyprolineSequence analysis
Disulfide bondi151 ↔ 240
Disulfide bondi218 ↔ 232

Keywords - PTMi

Disulfide bond, Hydroxylation

Proteomic databases

PaxDbiP08661.
PRIDEiP08661.

Expressioni

Gene expression databases

GenevisibleiP08661. RN.

Interactioni

Subunit structurei

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).By similarity

GO - Molecular functioni

  • protease binding Source: RGD
  • protein self-association Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064876.

Structurei

Secondary structure

1
244
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi134 – 1374Combined sources
Helixi144 – 15310Combined sources
Helixi164 – 17310Combined sources
Beta strandi178 – 1836Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi190 – 1934Combined sources
Beta strandi218 – 2214Combined sources
Beta strandi227 – 2304Combined sources
Beta strandi236 – 2427Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP08661.
SMRiP08661. Positions 129-243.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08661.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 9659Collagen-likeAdd
BLAST
Domaini129 – 241113C-type lectinPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili108 – 12619By similarityAdd
BLAST

Domaini

The coiled-coil domain mediates trimerization.By similarity

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation
Contains 1 collagen-like domain.Curated

Keywords - Domaini

Coiled coil, Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00700000104102.
HOVERGENiHBG108270.
InParanoidiP08661.
KOiK03991.
OMAiQKTCHVV.
OrthoDBiEOG7VTDPW.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
[Graphical view]
PfamiPF01391. Collagen. 1 hit.
PF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08661-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLFTSFLLL CVLTAVYAET LTEGAQSSCP VIACSSPGLN GFPGKDGHDG
60 70 80 90 100
AKGEKGEPGQ GLRGLQGPPG KVGPAGPPGN PGSKGATGPK GDRGESVEFD
110 120 130 140 150
TTNIDLEIAA LRSELRAMRK WVLLSMSENV GKKYFMSSVR RMPLNRAKAL
160 170 180 190 200
CSELQGTVAT PRNAEENRAI QNVAKDVAFL GITDQRTENV FEDLTGNRVR
210 220 230 240
YTNWNEGEPN NVGSGENCVV LLTNGKWNDV PCSDSFLVVC EFSD
Length:244
Mass (Da):26,014
Last modified:February 1, 1991 - v2
Checksum:iF0706E2AA9331531
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 392GL → AW in AAA41554 (PubMed:3009480).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14103 mRNA. Translation: AAA41554.1.
X05023 mRNA. Translation: CAA28687.1.
PIRiA24791. LNRTMC.
RefSeqiNP_073195.2. NM_022704.2.
XP_003749135.1. XM_003749087.3.
XP_003749136.1. XM_003749088.3.
XP_006231311.1. XM_006231249.2.
XP_006231312.1. XM_006231250.2.
UniGeneiRn.9667.

Genome annotation databases

EnsembliENSRNOT00000072188; ENSRNOP00000064876; ENSRNOG00000050305.
GeneIDi100911854.
64668.
KEGGirno:100911854.
rno:64668.
UCSCiRGD:67380. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14103 mRNA. Translation: AAA41554.1.
X05023 mRNA. Translation: CAA28687.1.
PIRiA24791. LNRTMC.
RefSeqiNP_073195.2. NM_022704.2.
XP_003749135.1. XM_003749087.3.
XP_003749136.1. XM_003749088.3.
XP_006231311.1. XM_006231249.2.
XP_006231312.1. XM_006231250.2.
UniGeneiRn.9667.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP08661.
SMRiP08661. Positions 129-243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064876.

Proteomic databases

PaxDbiP08661.
PRIDEiP08661.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000072188; ENSRNOP00000064876; ENSRNOG00000050305.
GeneIDi100911854.
64668.
KEGGirno:100911854.
rno:64668.
UCSCiRGD:67380. rat.

Organism-specific databases

CTDi4153.
RGDi67380. Mbl2.

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00700000104102.
HOVERGENiHBG108270.
InParanoidiP08661.
KOiK03991.
OMAiQKTCHVV.
OrthoDBiEOG7VTDPW.

Miscellaneous databases

EvolutionaryTraceiP08661.
PROiP08661.

Gene expression databases

GenevisibleiP08661. RN.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
[Graphical view]
PfamiPF01391. Collagen. 1 hit.
PF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of rat liver mannan-binding protein gene."
    Wada M., Itoh N., Ohta M., Kawasaki T.
    J. Biochem. 111:66-73(1992) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 133-244.

Entry informationi

Entry nameiMBL2_RAT
AccessioniPrimary (citable) accession number: P08661
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: February 1, 1991
Last modified: June 8, 2016
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.