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Protein

Mannose-binding protein A

Gene

Mbl1

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-dependent protein binding Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • mannose binding Source: RGD
  • phosphatidylinositol-4-phosphate binding Source: RGD
  • polysaccharide binding Source: RGD
  • protease binding Source: RGD
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

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 A
Short name:
MBP-A
Alternative name(s):
Mannan-binding protein
Gene namesi
Name:Mbl1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi3055. Mbl1.

Subcellular locationi

  • Secreted 1 Publication

  • Note: According to PubMed:10903744, long retention times in the endoplasmic reticulum and the Golgi apparatus that have been observed in former studies may reflect the abnormal physiology of the hepatoma cells used.

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401R → C: Prevents higher-order oligomer assembly. Slight reduction in secretion rate. 1 Publication
Mutagenesisi42 – 421G → E: Disrupts homotrimer formation. 5-fold reduction in secretion rate. Prevents K-44 hydroxylation and glycosylation. 10-fold decrease in complement activation. 1 Publication
Mutagenesisi44 – 441K → R: No effect on secretion rate, nor on homooligomer formation. 3-fold reduction in secretion rate; when associated eith R-47. Prevents higher-order oligomer assembly; when associated eith R-47. 10-fold decrease in complement activation; when associated eith R-47. 1 Publication
Mutagenesisi45 – 451G → D: Disrupts homotrimer formation. 5-fold reduction in secretion rate. Prevents K-47 hydroxylation and glycosylation. 1 Publication
Mutagenesisi47 – 471K → R: No effect on secretion rate, nor on homooligomer formation. 3-fold reduction in secretion rate; when associated eith R-44. Prevents higher-order oligomer assembly; when associated eith R-44. 10-fold decrease in complement activation; when associated eith R-44. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 PublicationAdd
BLAST
Chaini18 – 238221Mannose-binding protein APRO_0000017414Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 4314-hydroxyprolineSequence analysis
Modified residuei44 – 4415-hydroxylysine1 Publication
Glycosylationi44 – 441O-linked (Gal...)1 Publication
Modified residuei47 – 4715-hydroxylysine1 Publication
Glycosylationi47 – 471O-linked (Gal...)1 Publication
Modified residuei61 – 6114-hydroxyprolineSequence analysis
Modified residuei67 – 6714-hydroxyprolineSequence analysis
Modified residuei73 – 7314-hydroxyprolineSequence analysis
Modified residuei78 – 7814-hydroxyprolineSequence analysis
Modified residuei79 – 7915-hydroxylysineCurated
Modified residuei82 – 8215-hydroxylysineCurated
Disulfide bondi145 ↔ 234
Disulfide bondi212 ↔ 226

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP19999.
PRIDEiP19999.

Miscellaneous databases

PMAP-CutDBP19999.

Expressioni

Gene expression databases

GenevisibleiP19999. RN.

Interactioni

Subunit structurei

Oligomeric complex of 3 or more homotrimers. Oligomerization occurs in the endoplasmic reticulum (By similarity). Interacts with MASP1 and MASP2.By similarity1 Publication

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB
  • protease binding Source: RGD
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015723.

Structurei

Secondary structure

1
238
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi91 – 11929Combined sources
Beta strandi128 – 1369Combined sources
Helixi138 – 14710Combined sources
Beta strandi150 – 1523Combined sources
Helixi158 – 16811Combined sources
Beta strandi172 – 18110Combined sources
Beta strandi184 – 1874Combined sources
Beta strandi190 – 1923Combined sources
Beta strandi198 – 2025Combined sources
Beta strandi212 – 2154Combined sources
Helixi217 – 2193Combined sources
Beta strandi221 – 2244Combined sources
Beta strandi230 – 2367Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AFAX-ray2.001/2/390-238[»]
1AFBX-ray1.901/2/390-238[»]
1AFDX-ray2.001/2/390-238[»]
1BCHX-ray2.001/2/390-238[»]
1BCJX-ray2.101/2/390-238[»]
1BUUX-ray1.90A75-238[»]
1FIFX-ray1.95A/B/C90-238[»]
1FIHX-ray1.95A/B/C90-238[»]
1KMBX-ray2.101/2/390-238[»]
1KWTX-ray1.95A/B/C90-238[»]
1KWUX-ray1.95A/B/C90-238[»]
1KWVX-ray2.00A/B/C90-238[»]
1KWWX-ray1.90A/B/C90-238[»]
1KWXX-ray2.00A/B/C90-238[»]
1KWYX-ray2.00A/B/C90-238[»]
1KWZX-ray1.90A/B/C90-238[»]
1KX0X-ray2.00A/B/C90-238[»]
1KX1X-ray2.80A/B/C/D/E/F90-238[»]
1MSBX-ray2.30A/B124-238[»]
1RTMX-ray1.801/2/390-238[»]
1YTTX-ray1.80A/B124-238[»]
2KMBX-ray2.001/2/390-238[»]
2MSBX-ray1.70A/B124-238[»]
3KMBX-ray1.951/2/390-238[»]
4KMBX-ray2.001/2/390-238[»]
ProteinModelPortaliP19999.
SMRiP19999. Positions 90-238.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19999.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 8850Collagen-likeAdd
BLAST
Domaini143 – 23896C-type lectinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00700000104102.
HOGENOMiHOG000085660.
HOVERGENiHBG108270.
InParanoidiP19999.
KOiK03991.
OMAiIACEITE.
OrthoDBiEOG7VTDPW.
PhylomeDBiP19999.
TreeFamiTF330481.

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.

P19999-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLLPLLVLL CVVSVSSSGS QTCEETLKTC SVIACGRDGR DGPKGEKGEP
60 70 80 90 100
GQGLRGLQGP PGKLGPPGSV GAPGSQGPKG QKGDRGDSRA IEVKLANMEA
110 120 130 140 150
EINTLKSKLE LTNKLHAFSM GKKSGKKFFV TNHERMPFSK VKALCSELRG
160 170 180 190 200
TVAIPRNAEE NKAIQEVAKT SAFLGITDEV TEGQFMYVTG GRLTYSNWKK
210 220 230
DEPNDHGSGE DCVTIVDNGL WNDISCQASH TAVCEFPA
Length:238
Mass (Da):25,308
Last modified:February 1, 1991 - v1
Checksum:i1A927482B8A8CB3D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti156 – 1561R → K in AAA98781 (PubMed:3029088).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14105, M14104 Genomic DNA. Translation: AAA98781.1.
BC088159 mRNA. Translation: AAH88159.1.
PIRiB24791. LNRTMA.
RefSeqiNP_036731.2. NM_012599.2.
UniGeneiRn.10273.

Genome annotation databases

EnsembliENSRNOT00000015723; ENSRNOP00000015723; ENSRNOG00000011706.
GeneIDi24548.
KEGGirno:24548.
UCSCiRGD:3055. rat.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Mannose-binding protein A

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14105, M14104 Genomic DNA. Translation: AAA98781.1.
BC088159 mRNA. Translation: AAH88159.1.
PIRiB24791. LNRTMA.
RefSeqiNP_036731.2. NM_012599.2.
UniGeneiRn.10273.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AFAX-ray2.001/2/390-238[»]
1AFBX-ray1.901/2/390-238[»]
1AFDX-ray2.001/2/390-238[»]
1BCHX-ray2.001/2/390-238[»]
1BCJX-ray2.101/2/390-238[»]
1BUUX-ray1.90A75-238[»]
1FIFX-ray1.95A/B/C90-238[»]
1FIHX-ray1.95A/B/C90-238[»]
1KMBX-ray2.101/2/390-238[»]
1KWTX-ray1.95A/B/C90-238[»]
1KWUX-ray1.95A/B/C90-238[»]
1KWVX-ray2.00A/B/C90-238[»]
1KWWX-ray1.90A/B/C90-238[»]
1KWXX-ray2.00A/B/C90-238[»]
1KWYX-ray2.00A/B/C90-238[»]
1KWZX-ray1.90A/B/C90-238[»]
1KX0X-ray2.00A/B/C90-238[»]
1KX1X-ray2.80A/B/C/D/E/F90-238[»]
1MSBX-ray2.30A/B124-238[»]
1RTMX-ray1.801/2/390-238[»]
1YTTX-ray1.80A/B124-238[»]
2KMBX-ray2.001/2/390-238[»]
2MSBX-ray1.70A/B124-238[»]
3KMBX-ray1.951/2/390-238[»]
4KMBX-ray2.001/2/390-238[»]
ProteinModelPortaliP19999.
SMRiP19999. Positions 90-238.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015723.

Proteomic databases

PaxDbiP19999.
PRIDEiP19999.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000015723; ENSRNOP00000015723; ENSRNOG00000011706.
GeneIDi24548.
KEGGirno:24548.
UCSCiRGD:3055. rat.

Organism-specific databases

CTDi17194.
RGDi3055. Mbl1.

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00700000104102.
HOGENOMiHOG000085660.
HOVERGENiHBG108270.
InParanoidiP19999.
KOiK03991.
OMAiIACEITE.
OrthoDBiEOG7VTDPW.
PhylomeDBiP19999.
TreeFamiTF330481.

Miscellaneous databases

EvolutionaryTraceiP19999.
NextBioi603650.
PMAP-CutDBP19999.
PROiP19999.

Gene expression databases

GenevisibleiP19999. 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

« Hide 'large scale' publications
  1. "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 [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  2. "Exon structure of a mannose-binding protein gene reflects its evolutionary relationship to the asialoglycoprotein receptor and nonfibrillar collagens."
    Drickamer K., McCreary V.
    J. Biol. Chem. 262:2582-2589(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  4. "Serum lectin with known structure activates complement through the classical pathway."
    Ikeda K., Sannoh T., Kawasaki N., Kawasaki T., Yamashina I.
    J. Biol. Chem. 262:7451-7454(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 18-42.
  5. "Interaction of mannose-binding protein with associated serine proteases: effects of naturally occurring mutations."
    Wallis R., Dodd R.B.
    J. Biol. Chem. 275:30962-30969(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MASP1 AND MASP2.
    Tissue: Liver.
  6. "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, GLYCOSYLATION, OLIGOMERIZATION, MUTAGENESIS OF ARG-40; GLY-42; LYS-44; GLY-45 AND LYS-47, HYDROXYLATION AT LYS-44 AND LYS-47.
  7. "Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing."
    Weis W.I., Kahn R., Fourme R., Drickamer K., Hendrickson W.A.
    Science 254:1608-1615(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 124-238.
  8. "Structure of a C-type mannose-binding protein complexed with an oligosaccharide."
    Weis W.I., Drickamer K., Hendrickson W.A.
    Nature 360:127-134(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 124-238.
  9. "Trimeric structure of a C-type mannose-binding protein."
    Weis W.I., Drickamer K.
    Structure 2:1227-1240(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 84-238.
  10. "Ca2+-dependent structural changes in C-type mannose-binding proteins."
    Ng K.K.-S., Park-Snyder S., Weis W.I.
    Biochemistry 37:17965-17976(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 90-238.

Entry informationi

Entry nameiMBL1_RAT
AccessioniPrimary (citable) accession number: P19999
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 11, 2015
This is version 153 of the entry and version 1 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.