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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)DescriptionActionsGraphical viewLength
Mutagenesisi40R → C: Prevents higher-order oligomer assembly. Slight reduction in secretion rate. 1 Publication1
Mutagenesisi42G → E: Disrupts homotrimer formation. 5-fold reduction in secretion rate. Prevents K-44 hydroxylation and glycosylation. 10-fold decrease in complement activation. 1 Publication1
Mutagenesisi44K → 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 Publication1
Mutagenesisi45G → D: Disrupts homotrimer formation. 5-fold reduction in secretion rate. Prevents K-47 hydroxylation and glycosylation. 1 Publication1
Mutagenesisi47K → 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 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 171 PublicationAdd BLAST17
ChainiPRO_000001741418 – 238Mannose-binding protein AAdd BLAST221

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei434-hydroxyprolineSequence analysis1
Modified residuei445-hydroxylysine1 Publication1
Glycosylationi44O-linked (Gal...)1 Publication1
Modified residuei475-hydroxylysine1 Publication1
Glycosylationi47O-linked (Gal...)1 Publication1
Modified residuei614-hydroxyprolineSequence analysis1
Modified residuei674-hydroxyprolineSequence analysis1
Modified residuei734-hydroxyprolineSequence analysis1
Modified residuei784-hydroxyprolineSequence analysis1
Modified residuei795-hydroxylysineCurated1
Modified residuei825-hydroxylysineCurated1
Disulfide bondi145 ↔ 234
Disulfide bondi212 ↔ 226

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP19999.
PRIDEiP19999.

Miscellaneous databases

PMAP-CutDBP19999.

Expressioni

Gene expression databases

BgeeiENSRNOG00000011706.
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

1238
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi91 – 119Combined sources29
Beta strandi128 – 136Combined sources9
Helixi138 – 147Combined sources10
Beta strandi150 – 152Combined sources3
Helixi158 – 168Combined sources11
Beta strandi172 – 181Combined sources10
Beta strandi184 – 187Combined sources4
Beta strandi190 – 192Combined sources3
Beta strandi198 – 202Combined sources5
Beta strandi212 – 215Combined sources4
Helixi217 – 219Combined sources3
Beta strandi221 – 224Combined sources4
Beta strandi230 – 236Combined sources7

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP19999.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 88Collagen-likeAdd BLAST50
Domaini143 – 238C-type lectinPROSITE-ProRule annotationAdd BLAST96

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.
OrthoDBiEOG091G0R93.
PhylomeDBiP19999.
TreeFamiTF330481.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR008160. Collagen.
IPR016187. CTDL_fold.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti156R → K in AAA98781 (PubMed:3029088).Curated1

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
PDB 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.
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.
OrthoDBiEOG091G0R93.
PhylomeDBiP19999.
TreeFamiTF330481.

Miscellaneous databases

EvolutionaryTraceiP19999.
PMAP-CutDBP19999.
PROiP19999.

Gene expression databases

BgeeiENSRNOG00000011706.
GenevisibleiP19999. RN.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR008160. Collagen.
IPR016187. CTDL_fold.
[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...

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 30, 2016
This is version 158 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.