Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mannan-binding lectin serine protease 2

Gene

Masp2

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

Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase.

Miscellaneous

Dimerization and MBL2 binding requires calcium ions.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Selective cleavage after Arg-223 in complement component C2 (-Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile). EC:3.4.21.104

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi67Calcium 1By similarity1
Metal bindingi75Calcium 1By similarity1
Metal bindingi120Calcium 1By similarity1
Metal bindingi122Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi123Calcium 1By similarity1
Metal bindingi138Calcium 21
Metal bindingi139Calcium 2; via carbonyl oxygen1
Metal bindingi159Calcium 21
Metal bindingi162Calcium 2; via carbonyl oxygenBy similarity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei482Charge relay systemBy similarity1
Active sitei531Charge relay systemBy similarity1
Active sitei632Charge relay systemBy similarity1

<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

  • calcium ion binding Source: InterPro
  • peptidase activity Source: RGD
  • serine-type endopeptidase activity Source: UniProtKB

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

Molecular functionHydrolase, Protease, Serine protease
Biological processComplement pathway, Immunity, Innate immunity
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.21.104 5301

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q9JJS8

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S01.229

<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_and_taxonomy_section">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:
Mannan-binding lectin serine protease 2 (EC:3.4.21.104)
Alternative name(s):
MBL-associated serine protease 2
Mannose-binding protein-associated serine protease 2
Short name:
MASP-2
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Masp2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
620214 Masp2

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<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 – 191 PublicationAdd BLAST19
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002760420 – 685Mannan-binding lectin serine protease 2Add BLAST666
ChainiPRO_000002760520 – 443Mannan-binding lectin serine protease 2 A chainAdd BLAST424
ChainiPRO_0000027606444 – 685Mannan-binding lectin serine protease 2 B chainAdd BLAST242

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi72 ↔ 901 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi103N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi152 ↔ 1651 Publication
<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 residuei158(3R)-3-hydroxyasparagine1 Publication1
Disulfide bondi167 ↔ 1801 Publication
Disulfide bondi184 ↔ 2111 Publication
Disulfide bondi241 ↔ 2591 Publication
Glycosylationi285N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi300 ↔ 348By similarity
Disulfide bondi328 ↔ 361By similarity
Disulfide bondi366 ↔ 411By similarity
Disulfide bondi396 ↔ 429By similarity
Disulfide bondi433 ↔ 551Interchain (between A and B chains)PROSITE-ProRule annotation
Disulfide bondi597 ↔ 617By similarity
Disulfide bondi628 ↔ 659By similarity
Glycosylationi641N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

N-glycosylated.2 Publications
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei443 – 444CleavageBy similarity2

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

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

More...
PaxDbi
Q9JJS8

PeptideAtlas

More...
PeptideAtlasi
Q9JJS8

PRoteomics IDEntifications database

More...
PRIDEi
Q9JJS8

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9JJS8

<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

Highly expressed in liver. Secreted in plasma.1 Publication

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; disulfide-linked. Binds MBL2. Isoform 2 binds to MASP1. Binds SERPING1 (By similarity).By similarity

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q9JJS8

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000016317

<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

1685
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q9JJS8

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

More...
SMRi
Q9JJS8

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9JJS8

<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_and_domains_section">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>Domaini20 – 137CUB 1PROSITE-ProRule annotationAdd BLAST118
Domaini138 – 181EGF-like; calcium-bindingAdd BLAST44
Domaini184 – 296CUB 2PROSITE-ProRule annotationAdd BLAST113
Domaini298 – 363Sushi 1PROSITE-ProRule annotationAdd BLAST66
Domaini364 – 431Sushi 2PROSITE-ProRule annotationAdd BLAST68
Domaini444 – 683Peptidase S1PROSITE-ProRule annotationAdd BLAST240

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Sushi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3627 Eukaryota
COG5640 LUCA

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG000559

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9JJS8

KEGG Orthology (KO)

More...
KOi
K03993

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9JJS8

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00033 CCP, 2 hits
cd00041 CUB, 2 hits
cd00190 Tryp_SPc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.290, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000859 CUB_dom
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR018097 EGF_Ca-bd_CS
IPR037571 MASP2
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR035914 Sperma_CUB_dom_sf
IPR035976 Sushi/SCR/CCP_sf
IPR000436 Sushi_SCR_CCP_dom
IPR001254 Trypsin_dom
IPR033116 TRYPSIN_SER

The PANTHER Classification System

More...
PANTHERi
PTHR24255:SF10 PTHR24255:SF10, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00431 CUB, 2 hits
PF07645 EGF_CA, 1 hit
PF00084 Sushi, 2 hits
PF00089 Trypsin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00722 CHYMOTRYPSIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00032 CCP, 2 hits
SM00042 CUB, 2 hits
SM00181 EGF, 1 hit
SM00179 EGF_CA, 1 hit
SM00020 Tryp_SPc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49854 SSF49854, 2 hits
SSF50494 SSF50494, 1 hit
SSF57535 SSF57535, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00010 ASX_HYDROXYL, 1 hit
PS01180 CUB, 2 hits
PS01186 EGF_2, 1 hit
PS01187 EGF_CA, 1 hit
PS50923 SUSHI, 2 hits
PS50240 TRYPSIN_DOM, 1 hit
PS00135 TRYPSIN_SER, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9JJS8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MRLLIVLGLL WSLVATLLGS KWPEPVFGRL VSLGFPEKYG NHQDRSWTLT
60 70 80 90 100
APPGFRLRLY FTHFNLELSY RCEYDFVKLT SGTKVLATLC GQESTDTERA
110 120 130 140 150
PGNDTFYSLG PSLKVTFHSD YSNEKPFTGF EAFYAAEDVD ECRTSLGDSV
160 170 180 190 200
PCDHYCHNYL GGYYCSCRVG YILHQNKHTC SALCSGQVFT GRSGFLSSPE
210 220 230 240 250
YPQPYPKLSS CAYNIRLEEG FSITLDFVES FDVEMHPEAQ CPYDSLKIQT
260 270 280 290 300
DKREYGPFCG KTLPPRIETD SNKVTITFTT DESGNHTGWK IHYTSTAQPC
310 320 330 340 350
PDPTAPPNGH ISPVQATYVL KDSFSVFCKT GFELLQGSVP LKSFTAVCQK
360 370 380 390 400
DGSWDRPIPE CSIIDCGPPD DLPNGHVDYI TGPEVTTYKA VIQYSCEETF
410 420 430 440 450
YTMSSNGKYV CEADGFWTSS KGEKSLPVCK PVCGLSTHTS GGRIIGGQPA
460 470 480 490 500
KPGDFPWQVL LLGETTAAGA LIHDDWVLTA AHAVYGKTEA MSSLDIRMGI
510 520 530 540 550
LKRLSLIYTQ AWPEAVFIHE GYTHGAGFDN DIALIKLKNK VTINRNIMPI
560 570 580 590 600
CLPRKEAASL MKTDFVGTVA GWGLTQKGFL ARNLMFVDIP IVDHQKCATA
610 620 630 640 650
YTKQPYPGAK VTVNMLCAGL DRGGKDSCRG DSGGALVFLD NETQRWFVGG
660 670 680
IVSWGSINCG GSEQYGVYTK VTNYIPWIEN IINNF
Length:685
Mass (Da):75,667
Last modified:July 19, 2005 - v2
<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:i0086154934509C64
GO
Isoform 2 (identifier: Q9JJS8-2) [UniParc]FASTAAdd to basket
Also known as: MAp19

The sequence of this isoform differs from the canonical sequence as follows:
     182-185: ALCS → EQSL
     186-685: Missing.

Show »
Length:185
Mass (Da):20,996
Checksum:i551DD17564C37468
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A2VCV7A2VCV7_RAT
Mannan-binding lectin serine peptid...
Masp2 rCG_31002
685Annotation score:

Annotation score:2 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>
A0A0G2K392A0A0G2K392_RAT
Mannan-binding lectin serine protea...
Masp2
184Annotation score:

Annotation score:1 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 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 conflicti33L → P in CAB90832 (PubMed:10586086).Curated1
Sequence conflicti34G → A in CAB65385 (PubMed:10586086).Curated1
Sequence conflicti34G → A in CAB65387 (PubMed:10586086).Curated1
Sequence conflicti34G → A in CAB65390 (PubMed:10586086).Curated1
Sequence conflicti506 – 507LI → PH in CAB90832 (PubMed:10586086).Curated2
Sequence conflicti622R → A in CAB90832 (PubMed:10586086).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_014638182 – 185ALCS → EQSL in isoform 2. 1 Publication4
Alternative sequenceiVSP_014639186 – 685Missing in isoform 2. 1 PublicationAdd BLAST500

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
Y19161 mRNA Translation: CAB65248.1
Y18565 mRNA Translation: CAB65382.1
Y18566 mRNA Translation: CAB65383.1
Y18567 mRNA Translation: CAB65384.1
Y18568 mRNA Translation: CAB65385.1
Y18569 mRNA Translation: CAB65386.1
Y18570 mRNA Translation: CAB65387.1
Y18571 mRNA Translation: CAB65388.1
Y18572 mRNA Translation: CAB65389.1
Y18573 mRNA Translation: CAB65390.1
Y18564 mRNA Translation: CAB70973.1
AJ277747 mRNA Translation: CAB90832.1
Y18285 mRNA Translation: CAB50738.1

NCBI Reference Sequences

More...
RefSeqi
NP_742040.1, NM_172043.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.45144

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
64459

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:64459

Keywords - Coding sequence diversityi

Alternative splicing

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y19161 mRNA Translation: CAB65248.1
Y18565 mRNA Translation: CAB65382.1
Y18566 mRNA Translation: CAB65383.1
Y18567 mRNA Translation: CAB65384.1
Y18568 mRNA Translation: CAB65385.1
Y18569 mRNA Translation: CAB65386.1
Y18570 mRNA Translation: CAB65387.1
Y18571 mRNA Translation: CAB65388.1
Y18572 mRNA Translation: CAB65389.1
Y18573 mRNA Translation: CAB65390.1
Y18564 mRNA Translation: CAB70973.1
AJ277747 mRNA Translation: CAB90832.1
Y18285 mRNA Translation: CAB50738.1
RefSeqiNP_742040.1, NM_172043.1
UniGeneiRn.45144

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
1NT0X-ray2.70A/G20-299[»]
5CISX-ray2.58A21-298[»]
5CKMX-ray2.73A21-297[»]
5CKNX-ray2.60A/D20-297[»]
ProteinModelPortaliQ9JJS8
SMRiQ9JJS8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

CORUMiQ9JJS8
STRINGi10116.ENSRNOP00000016317

Protein family/group databases

MEROPSiS01.229

PTM databases

iPTMnetiQ9JJS8

Proteomic databases

PaxDbiQ9JJS8
PeptideAtlasiQ9JJS8
PRIDEiQ9JJS8

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64459
KEGGirno:64459

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10747
RGDi620214 Masp2

Phylogenomic databases

eggNOGiKOG3627 Eukaryota
COG5640 LUCA
HOVERGENiHBG000559
InParanoidiQ9JJS8
KOiK03993
PhylomeDBiQ9JJS8

Enzyme and pathway databases

BRENDAi3.4.21.104 5301
SABIO-RKiQ9JJS8

Miscellaneous databases

EvolutionaryTraceiQ9JJS8

Protein Ontology

More...
PROi
PR:Q9JJS8

Family and domain databases

CDDicd00033 CCP, 2 hits
cd00041 CUB, 2 hits
cd00190 Tryp_SPc, 1 hit
Gene3Di2.60.120.290, 2 hits
InterProiView protein in InterPro
IPR000859 CUB_dom
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR018097 EGF_Ca-bd_CS
IPR037571 MASP2
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR035914 Sperma_CUB_dom_sf
IPR035976 Sushi/SCR/CCP_sf
IPR000436 Sushi_SCR_CCP_dom
IPR001254 Trypsin_dom
IPR033116 TRYPSIN_SER
PANTHERiPTHR24255:SF10 PTHR24255:SF10, 1 hit
PfamiView protein in Pfam
PF00431 CUB, 2 hits
PF07645 EGF_CA, 1 hit
PF00084 Sushi, 2 hits
PF00089 Trypsin, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
SMARTiView protein in SMART
SM00032 CCP, 2 hits
SM00042 CUB, 2 hits
SM00181 EGF, 1 hit
SM00179 EGF_CA, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF49854 SSF49854, 2 hits
SSF50494 SSF50494, 1 hit
SSF57535 SSF57535, 2 hits
PROSITEiView protein in PROSITE
PS00010 ASX_HYDROXYL, 1 hit
PS01180 CUB, 2 hits
PS01186 EGF_2, 1 hit
PS01187 EGF_CA, 1 hit
PS50923 SUSHI, 2 hits
PS50240 TRYPSIN_DOM, 1 hit
PS00135 TRYPSIN_SER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<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 nameiMASP2_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: Q9JJS8
Secondary accession number(s): Q9JJP3
, Q9QX83, Q9QX84, Q9QX85, Q9QX86, Q9QX87, Q9QX88, Q9QX89, Q9QX90, Q9QX91, Q9QXD4, Q9WUZ0
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: December 5, 2018
This is version 142 of the entry and version 2 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, 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
  3. Peptidase families
    Classification of peptidase families and list of entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again