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Entry version 178 (26 Feb 2020)
Sequence version 1 (01 Feb 1991)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Calcium-dependent lectin (PubMed:1436090, PubMed:9033386, PubMed:11850428). Plays a role in the innate immune response by binding mannose, fucose and N-acetylglucosamine moieties on different microorganisms and mediating activation of the lectin complement pathway (PubMed:3584121). 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 similarity4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi178Calcium 1Combined sources4 Publications1
Metal bindingi182Calcium 1Combined sources4 Publications1
Metal bindingi202Calcium 2Combined sources4 Publications1
Metal bindingi204Calcium 2Combined sources4 Publications1
Metal bindingi205Calcium 1Combined sources4 Publications1
Metal bindingi210Calcium 1; via carbonyl oxygenCombined sources4 Publications1
Metal bindingi210Calcium 2Combined sources4 Publications1
Metal bindingi211Calcium 1Combined sources4 Publications1
Metal bindingi222Calcium 2Combined sources4 Publications1
Metal bindingi223Calcium 2Combined sources4 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-166662 Lectin pathway of complement activation
R-RNO-166663 Initial triggering of complement

Protein family/group databases

UniLectin database of carbohydrate-binding proteins

More...
UniLectini
P19999

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Mannose-binding protein A
Short name:
MBP-A1 Publication
Alternative name(s):
Mannan-binding protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Mbl1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 16

Organism-specific databases

Rat genome database

More...
RGDi
3055 Mbl1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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
Mutagenesisi228 – 230ASH → KKK: Changes carbohydrate binding specificity, leading to interaction with Lewis blood group antigens. 1 Publication3

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 171 PublicationAdd BLAST17
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001741418 – 238Mannose-binding protein AAdd BLAST221

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei434-hydroxyprolineSequence analysis1
Modified residuei445-hydroxylysine2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi44O-linked (Gal...) hydroxylysine2 Publications1
Modified residuei475-hydroxylysine2 Publications1
Glycosylationi47O-linked (Gal...) hydroxylysine2 Publications1
Modified residuei504-hydroxyproline1 Publication1
Modified residuei614-hydroxyprolineSequence analysis1
Modified residuei674-hydroxyprolineSequence analysis1
Modified residuei734-hydroxyprolineSequence analysis1
Modified residuei784-hydroxyprolineSequence analysis1
Modified residuei795-hydroxylysine1 Publication1
Glycosylationi79O-linked (Gal...) hydroxylysine1 Publication1
Modified residuei825-hydroxylysine1 Publication1
Glycosylationi82O-linked (Gal...) hydroxylysine1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi145 ↔ 234Combined sources4 Publications
Disulfide bondi212 ↔ 226Combined sources4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Hydroxylated on lysine and proline residues within the collagen-like domain.2 Publications
O-glycosylated. O-linked glycans on hydroxylysine residues consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P19999

PRoteomics IDEntifications database

More...
PRIDEi
P19999

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in blood serum (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000011706 Expressed in liver and 3 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P19999 RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotrimer (PubMed:7704532, PubMed:9033386, PubMed:11850428, PubMed:25419660). Forms higher oligomeric complexes formed by the association of two, three or more homotrimers (PubMed:10903744, PubMed:25419660). Oligomerization occurs in the endoplasmic reticulum (By similarity).

Interacts with MASP1 and MASP2 (PubMed:10913141).

By similarity6 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000015723

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1238
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P19999

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P19999

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini39 – 88Collagen-likeAdd BLAST50
Domaini143 – 238C-type lectinPROSITE-ProRule annotationAdd BLAST96

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni202 – 210Calcium-dependent carbohydrate binding3 Publications9

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The helical collagen-like domains from three protein chains assemble into a coiled coil and mediate trimerization.3 Publications

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4297 Eukaryota
ENOG410XPJ1 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154368

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_049894_3_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P19999

KEGG Orthology (KO)

More...
KOi
K03991

Identification of Orthologs from Complete Genome Data

More...
OMAi
TCSVVAC

Database of Orthologous Groups

More...
OrthoDBi
1222552at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P19999

TreeFam database of animal gene trees

More...
TreeFami
TF330481

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03591 CLECT_collectin_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.100.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View 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
IPR042129 Mannose-binding_protein_A

The PANTHER Classification System

More...
PANTHERi
PTHR24024:SF35 PTHR24024:SF35, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01391 Collagen, 1 hit
PF00059 Lectin_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00034 CLECT, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56436 SSF56436, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00615 C_TYPE_LECTIN_1, 1 hit
PS50041 C_TYPE_LECTIN_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i1A927482B8A8CB3D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti156R → K in AAA98781 (PubMed:3029088).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M14105, M14104 Genomic DNA Translation: AAA98781.1
BC088159 mRNA Translation: AAH88159.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B24791 LNRTMA

NCBI Reference Sequences

More...
RefSeqi
NP_036731.2, NM_012599.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000015723; ENSRNOP00000015723; ENSRNOG00000011706

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24548

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:24548

UCSC genome browser

More...
UCSCi
RGD:3055 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
SMRiP19999
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015723

Protein family/group databases

UniLectiniP19999

Proteomic databases

PaxDbiP19999
PRIDEiP19999

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
17194
RGDi3055 Mbl1

Phylogenomic databases

eggNOGiKOG4297 Eukaryota
ENOG410XPJ1 LUCA
GeneTreeiENSGT00940000154368
HOGENOMiCLU_049894_3_0_1
InParanoidiP19999
KOiK03991
OMAiTCSVVAC
OrthoDBi1222552at2759
PhylomeDBiP19999
TreeFamiTF330481

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP19999

Protein Ontology

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PROi
PR:P19999

Gene expression databases

BgeeiENSRNOG00000011706 Expressed in liver and 3 other tissues
GenevisibleiP19999 RN

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
IPR042129 Mannose-binding_protein_A
PANTHERiPTHR24024:SF35 PTHR24024:SF35, 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMBL1_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P19999
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: February 26, 2020
This is version 178 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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