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Protein

Mannose-binding protein C

Gene

Mbl2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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
  • protein self-association Source: RGD

GO - Biological processi

  • complement activation, classical pathway Source: UniProtKB-KW
  • complement activation, lectin pathway Source: GO_Central
  • positive regulation of complement activation Source: RGD
  • positive regulation of protein processing Source: RGD
  • protein complex oligomerization Source: RGD
  • protein homooligomerization Source: RGD
  • protein homotrimerization Source: RGD

Keywordsi

Biological processComplement activation lectin pathway, Complement pathway, Immunity, Innate immunity
LigandCalcium, Lectin, Mannose-binding

Enzyme and pathway databases

ReactomeiR-RNO-166662 Lectin pathway of complement activation
R-RNO-166663 Initial triggering of complement

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi67380 Mbl2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Add BLAST18
ChainiPRO_000001741119 – 244Mannose-binding protein C1 PublicationAdd BLAST226

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi29Interchain
Disulfide bondi34Interchain
Modified residuei434-hydroxyprolineSequence analysis1
Modified residuei584-hydroxyprolineSequence analysis1
Modified residuei694-hydroxyprolineSequence analysis1
Modified residuei784-hydroxyprolineSequence analysis1
Modified residuei814-hydroxyprolineSequence analysis1
Disulfide bondi151 ↔ 240
Disulfide bondi218 ↔ 232

Keywords - PTMi

Disulfide bond, Hydroxylation

Proteomic databases

PaxDbiP08661
PeptideAtlasiP08661
PRIDEiP08661

Expressioni

Gene expression databases

BgeeiENSRNOG00000050305
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

  • protein self-association Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064876

Structurei

Secondary structure

1244
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi134 – 137Combined sources4
Helixi144 – 153Combined sources10
Helixi164 – 173Combined sources10
Beta strandi178 – 183Combined sources6
Beta strandi185 – 187Combined sources3
Beta strandi190 – 193Combined sources4
Beta strandi218 – 221Combined sources4
Beta strandi227 – 230Combined sources4
Beta strandi236 – 242Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08661

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini38 – 96Collagen-likeAdd BLAST59
Domaini129 – 241C-type lectinPROSITE-ProRule annotationAdd BLAST113

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili108 – 126By similarityAdd BLAST19

Domaini

The coiled-coil domain mediates trimerization.By similarity

Keywords - Domaini

Coiled coil, Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG4297 Eukaryota
ENOG410XPJ1 LUCA
GeneTreeiENSGT00700000104102
HOVERGENiHBG108270
InParanoidiP08661
KOiK03991
OMAiYSETVTC
OrthoDBiEOG091G0R93

Family and domain databases

CDDicd03591 CLECT_collectin_like, 1 hit
Gene3Di3.10.100.10, 1 hit
InterProiView protein in InterPro
IPR001304 C-type_lectin-like
IPR016186 C-type_lectin-like/link_sf
IPR018378 C-type_lectin_CS
IPR008160 Collagen
IPR033990 Collectin_CTLD
IPR016187 CTDL_fold
IPR037570 Mannose-binding_protein
PANTHERiPTHR24020:SF0 PTHR24020:SF0, 1 hit
PfamiView protein in Pfam
PF01391 Collagen, 1 hit
PF00059 Lectin_C, 1 hit
SMARTiView protein in SMART
SM00034 CLECT, 1 hit
SUPFAMiSSF56436 SSF56436, 1 hit
PROSITEiView protein in PROSITE
PS00615 C_TYPE_LECTIN_1, 1 hit
PS50041 C_TYPE_LECTIN_2, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti38 – 39GL → AW in AAA41554 (PubMed:3009480).Curated2

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

Similar proteinsi

Entry informationi

Entry nameiMBL2_RAT
AccessioniPrimary (citable) accession number: P08661
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: February 1, 1991
Last modified: May 23, 2018
This is version 165 of the entry and version 2 of the sequence. See 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

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