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-Experimental evidence at protein leveli

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.

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi67 – 671Calcium 1By similarity
Metal bindingi75 – 751Calcium 1By similarity
Metal bindingi120 – 1201Calcium 1By similarity
Metal bindingi122 – 1221Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi123 – 1231Calcium 1By similarity
Metal bindingi138 – 1381Calcium 2
Metal bindingi139 – 1391Calcium 2; via carbonyl oxygen
Metal bindingi159 – 1591Calcium 2
Metal bindingi162 – 1621Calcium 2; via carbonyl oxygenBy similarity
Active sitei482 – 4821Charge relay systemBy similarity
Active sitei531 – 5311Charge relay systemBy similarity
Active sitei632 – 6321Charge relay systemBy similarity

GO - Molecular functioni

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

GO - Biological processi

  • complement activation Source: RGD
  • complement activation, classical pathway Source: UniProtKB-KW
  • innate immune response Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Complement pathway, Immunity, Innate immunity

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.21.104. 5301.

Protein family/group databases

MEROPSiS01.229.

Names & Taxonomyi

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:
Gene namesi
Name:Masp2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620214. Masp2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 685666Mannan-binding lectin serine protease 2PRO_0000027604Add
BLAST
Chaini20 – 443424Mannan-binding lectin serine protease 2 A chainPRO_0000027605Add
BLAST
Chaini444 – 685242Mannan-binding lectin serine protease 2 B chainPRO_0000027606Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi72 ↔ 901 Publication
Glycosylationi103 – 1031N-linked (GlcNAc...)1 Publication
Disulfide bondi152 ↔ 1651 Publication
Modified residuei158 – 1581(3R)-3-hydroxyasparagine1 Publication
Disulfide bondi167 ↔ 1801 Publication
Disulfide bondi184 ↔ 2111 Publication
Disulfide bondi241 ↔ 2591 Publication
Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi641 – 6411N-linked (GlcNAc...)Sequence analysis

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei443 – 4442CleavageBy similarity

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiQ9JJS8.
PeptideAtlasiQ9JJS8.
PRIDEiQ9JJS8.

Expressioni

Tissue specificityi

Highly expressed in liver. Secreted in plasma.1 Publication

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016317.

Structurei

Secondary structure

1
685
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 315Combined sources
Turni33 – 364Combined sources
Beta strandi45 – 506Combined sources
Beta strandi55 – 6511Combined sources
Helixi70 – 723Combined sources
Beta strandi74 – 818Combined sources
Beta strandi84 – 896Combined sources
Beta strandi91 – 933Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi109 – 11810Combined sources
Beta strandi129 – 13810Combined sources
Beta strandi153 – 1597Combined sources
Beta strandi162 – 1665Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi185 – 1895Combined sources
Beta strandi191 – 1977Combined sources
Turni199 – 2024Combined sources
Beta strandi210 – 2167Combined sources
Beta strandi222 – 2276Combined sources
Beta strandi245 – 2495Combined sources
Beta strandi254 – 2585Combined sources
Beta strandi260 – 2623Combined sources
Beta strandi270 – 27910Combined sources
Beta strandi290 – 2967Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NT0X-ray2.70A/G20-299[»]
ProteinModelPortaliQ9JJS8.
SMRiQ9JJS8. Positions 24-685.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JJS8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 137118CUB 1PROSITE-ProRule annotationAdd
BLAST
Domaini138 – 18144EGF-like; calcium-bindingAdd
BLAST
Domaini184 – 296113CUB 2PROSITE-ProRule annotationAdd
BLAST
Domaini298 – 36366Sushi 1PROSITE-ProRule annotationAdd
BLAST
Domaini364 – 43168Sushi 2PROSITE-ProRule annotationAdd
BLAST
Domaini444 – 683240Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 CUB domains.PROSITE-ProRule annotation
Contains 1 EGF-like domain.Curated
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
Contains 2 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOVERGENiHBG000559.
InParanoidiQ9JJS8.
KOiK03993.
PhylomeDBiQ9JJS8.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di2.60.120.290. 2 hits.
InterProiIPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR018097. EGF_Ca-bd_CS.
IPR024175. Pept_S1A_C1r/C1S/mannan-bd.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP_dom.
IPR001254. Trypsin_dom.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
PF07645. EGF_CA. 1 hit.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001155. C1r_C1s_MASP. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEiPS00010. 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.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331L → P in CAB90832 (PubMed:10586086).Curated
Sequence conflicti34 – 341G → A in CAB65385 (PubMed:10586086).Curated
Sequence conflicti34 – 341G → A in CAB65387 (PubMed:10586086).Curated
Sequence conflicti34 – 341G → A in CAB65390 (PubMed:10586086).Curated
Sequence conflicti506 – 5072LI → PH in CAB90832 (PubMed:10586086).Curated
Sequence conflicti622 – 6221R → A in CAB90832 (PubMed:10586086).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei182 – 1854ALCS → EQSL in isoform 2. 1 PublicationVSP_014638
Alternative sequencei186 – 685500Missing in isoform 2. 1 PublicationVSP_014639Add
BLAST

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.

Genome annotation databases

GeneIDi64459.
KEGGirno:64459.

Keywords - Coding sequence diversityi

Alternative splicing

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:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NT0X-ray2.70A/G20-299[»]
ProteinModelPortaliQ9JJS8.
SMRiQ9JJS8. Positions 24-685.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016317.

Protein family/group databases

MEROPSiS01.229.

Proteomic databases

PaxDbiQ9JJS8.
PeptideAtlasiQ9JJS8.
PRIDEiQ9JJS8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64459.
KEGGirno:64459.

Organism-specific databases

CTDi10747.
RGDi620214. Masp2.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOVERGENiHBG000559.
InParanoidiQ9JJS8.
KOiK03993.
PhylomeDBiQ9JJS8.

Enzyme and pathway databases

BRENDAi3.4.21.104. 5301.

Miscellaneous databases

EvolutionaryTraceiQ9JJS8.
PROiQ9JJS8.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di2.60.120.290. 2 hits.
InterProiIPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR018097. EGF_Ca-bd_CS.
IPR024175. Pept_S1A_C1r/C1S/mannan-bd.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP_dom.
IPR001254. Trypsin_dom.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
PF07645. EGF_CA. 1 hit.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001155. C1r_C1s_MASP. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEiPS00010. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMASP2_RAT
AccessioniPrimary (citable) accession number: Q9JJS8
Secondary accession number(s): Q9JJP3
, Q9QX83, Q9QX84, Q9QX85, Q9QX86, Q9QX87, Q9QX88, Q9QX89, Q9QX90, Q9QX91, Q9QXD4, Q9WUZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: September 7, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Dimerization and MBL2 binding requires calcium ions.

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. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.