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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)DescriptionActionsGraphical viewLength
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
Active sitei482Charge relay systemBy similarity1
Active sitei531Charge relay systemBy similarity1
Active sitei632Charge relay systemBy similarity1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
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
Disulfide bondi72 ↔ 901 Publication
Glycosylationi103N-linked (GlcNAc...)1 Publication1
Disulfide bondi152 ↔ 1651 Publication
Modified residuei158(3R)-3-hydroxyasparagine1 Publication1
Disulfide bondi167 ↔ 1801 Publication
Disulfide bondi184 ↔ 2111 Publication
Disulfide bondi241 ↔ 2591 Publication
Glycosylationi285N-linked (GlcNAc...)Sequence 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...)Sequence analysis1

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
Sitei443 – 444CleavageBy similarity2

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

1685
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 31Combined sources5
Turni33 – 36Combined sources4
Beta strandi45 – 50Combined sources6
Beta strandi55 – 65Combined sources11
Helixi70 – 72Combined sources3
Beta strandi74 – 81Combined sources8
Beta strandi84 – 89Combined sources6
Beta strandi91 – 93Combined sources3
Beta strandi105 – 107Combined sources3
Beta strandi109 – 118Combined sources10
Beta strandi129 – 138Combined sources10
Beta strandi153 – 159Combined sources7
Beta strandi162 – 166Combined sources5
Beta strandi171 – 173Combined sources3
Beta strandi180 – 182Combined sources3
Beta strandi185 – 189Combined sources5
Beta strandi191 – 197Combined sources7
Turni199 – 202Combined sources4
Beta strandi210 – 216Combined sources7
Beta strandi222 – 227Combined sources6
Beta strandi245 – 249Combined sources5
Beta strandi254 – 258Combined sources5
Beta strandi260 – 262Combined sources3
Beta strandi270 – 279Combined sources10
Beta strandi290 – 296Combined sources7

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9JJS8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

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

CDDicd00033. CCP. 2 hits.
cd00041. CUB. 2 hits.
cd00190. 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)DescriptionActionsGraphical viewLength
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
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:
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NT0X-ray2.70A/G20-299[»]
ProteinModelPortaliQ9JJS8.
SMRiQ9JJS8.
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

CDDicd00033. CCP. 2 hits.
cd00041. CUB. 2 hits.
cd00190. 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: November 30, 2016
This is version 132 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.