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Protein

Mannan-binding lectin serine protease 1

Gene

Masp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5.1 Publication

Enzyme regulationi

Inhibited by SERPING1 and A2M.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi73 – 731Calcium 1By similarity
Metal bindingi81 – 811Calcium 1By similarity
Metal bindingi126 – 1261Calcium 1By similarity
Metal bindingi128 – 1281Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi144 – 1441Calcium 2By similarity
Metal bindingi145 – 1451Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi147 – 1471Calcium 2By similarity
Metal bindingi164 – 1641Calcium 2By similarity
Metal bindingi165 – 1651Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi168 – 1681Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi240 – 2401Calcium 3By similarity
Metal bindingi250 – 2501Calcium 3By similarity
Metal bindingi287 – 2871Calcium 3By similarity
Metal bindingi289 – 2891Calcium 3; via carbonyl oxygenBy similarity
Active sitei495 – 4951Charge relay systemBy similarity
Active sitei557 – 5571Charge relay systemBy similarity
Active sitei651 – 6511Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

  • complement activation, lectin pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Complement activation lectin pathway, Immunity, Innate immunity

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.21.B7. 3474.

Protein family/group databases

MEROPSiS01.198.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan-binding lectin serine protease 1 (EC:3.4.21.-)
Alternative name(s):
Complement factor MASP-3
Complement-activating component of Ra-reactive factor
Mannose-binding lectin-associated serine protease 1
Short name:
MASP-1
Mannose-binding protein-associated serine protease
Ra-reactive factor serine protease p100
Short name:
RaRF
Serine protease 5
Cleaved into the following 2 chains:
Gene namesi
Name:Masp1
Synonyms:Crarf, Masp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:88492. Masp1.

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Mice are smaller and more vulnerable indicating developmental and growth defects. Mice serum has low C4 and C3 cleavage activity together with low MASP2 activation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 704680Mannan-binding lectin serine protease 1PRO_0000027595Add
BLAST
Chaini25 – 453429Mannan-binding lectin serine protease 1 heavy chainPRO_0000027596Add
BLAST
Chaini454 – 704251Mannan-binding lectin serine protease 1 light chainPRO_0000027597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi54 – 541N-linked (GlcNAc...)Sequence analysis
Disulfide bondi78 ↔ 96By similarity
Disulfide bondi148 ↔ 162By similarity
Disulfide bondi158 ↔ 171By similarity
Modified residuei164 – 1641(3R)-3-hydroxyasparagineSequence analysis
Disulfide bondi173 ↔ 186By similarity
Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence analysis
Disulfide bondi190 ↔ 217By similarity
Disulfide bondi247 ↔ 265By similarity
Disulfide bondi306 ↔ 354By similarity
Disulfide bondi334 ↔ 367By similarity
Disulfide bondi372 ↔ 419By similarity
Glycosylationi390 – 3901N-linked (GlcNAc...)Sequence analysis
Disulfide bondi402 ↔ 437By similarity
Glycosylationi412 – 4121N-linked (GlcNAc...)Sequence analysis
Disulfide bondi441 ↔ 577Interchain (between heavy and light chains)PROSITE-ProRule annotation
Disulfide bondi480 ↔ 496By similarity
Disulfide bondi619 ↔ 636By similarity
Disulfide bondi647 ↔ 677By similarity

Post-translational modificationi

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity
N-glycosylated. Some N-linked glycan are of the complex-type (By similarity).By similarity
Autoproteolytic processing of the proenzyme produces the active enzyme composed on the heavy and the light chain held together by a disulfide bond. Isoform 1 but not isoform 2 is activated through autoproteolytic processing (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei453 – 4542Cleavage; by autolysisBy similarity

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiP98064.
PaxDbiP98064.
PeptideAtlasiP98064.
PRIDEiP98064.

PTM databases

iPTMnetiP98064.
PhosphoSiteiP98064.

Expressioni

Tissue specificityi

Protein of the plasma which is primarily expressed by liver.2 Publications

Gene expression databases

BgeeiENSMUSG00000022887.
CleanExiMM_MASP1.

Interactioni

Subunit structurei

Homodimer. Interacts with the oligomeric lectins MBL1, MBL2, FCN2 and FCN3; triggers the lectin pathway of complement through activation of C3. Interacts with SERPING1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000087327.

Structurei

3D structure databases

ProteinModelPortaliP98064.
SMRiP98064. Positions 27-704.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 143119CUB 1PROSITE-ProRule annotationAdd
BLAST
Domaini144 – 18744EGF-like; calcium-bindingBy similarityAdd
BLAST
Domaini190 – 302113CUB 2PROSITE-ProRule annotationAdd
BLAST
Domaini304 – 36966Sushi 1PROSITE-ProRule annotationAdd
BLAST
Domaini370 – 43970Sushi 2PROSITE-ProRule annotationAdd
BLAST
Domaini454 – 701248Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 305281Interaction with MBL1By similarityAdd
BLAST
Regioni25 – 283259Interaction with FCN2By similarityAdd
BLAST
Regioni25 – 189165HomodimerizationBy similarityAdd
BLAST
Regioni25 – 189165Interaction with MBL2By similarityAdd
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.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000237311.
HOVERGENiHBG000559.
InParanoidiP98064.
KOiK03992.
OMAiVWGPFCG.
OrthoDBiEOG091G02DS.
PhylomeDBiP98064.
TreeFamiTF330373.

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.
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.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
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.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 1 hit.
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.
PS00134. TRYPSIN_HIS. 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: P98064-1) [UniParc]FASTAAdd to basket
Also known as: MASP-1

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
MRFLSFWRLL LYHALCLALP EVSAHTVELN EMFGQIQSPG YPDSYPSDSE
60 70 80 90 100
VTWNITVPEG FRIKLYFMHF NLESSYLCEY DYVKVETEDQ VLATFCGRET
110 120 130 140 150
TDTEQTPGQE VVLSPGTFMS VTFRSDFSNE ERFTGFDAHY MAVDVDECKE
160 170 180 190 200
REDEELSCDH YCHNYIGGYY CSCRFGYILH TDNRTCRVEC SGNLFTQRTG
210 220 230 240 250
TITSPDYPNP YPKSSECSYT IDLEEGFMVS LQFEDIFDIE DHPEVPCPYD
260 270 280 290 300
YIKIKAGSKV WGPFCGEKSP EPISTQTHSV QILFRSDNSG ENRGWRLSYR
310 320 330 340 350
AAGNECPKLQ PPVYGKIEPS QAVYSFKDQV LVSCDTGYKV LKDNEVMDTF
360 370 380 390 400
QIECLKDGAW SNKIPTCKIV DCGAPAGLKH GLVTFSTRNN LTTYKSEIRY
410 420 430 440 450
SCQQPYYKML HNTTGVYTCS AHGTWTNEVL KRSLPTCLPV CGVPKFSRKQ
460 470 480 490 500
ISRIFNGRPA QKGTMPWIAM LSHLNGQPFC GGSLLGSNWV LTAAHCLHQS
510 520 530 540 550
LDPEEPTLHS SYLLSPSDFK IIMGKHWRRR SDEDEQHLHV KRTTLHPLYN
560 570 580 590 600
PSTFENDLGL VELSESPRLN DFVMPVCLPE QPSTEGTMVI VSGWGKQFLQ
610 620 630 640 650
RFPENLMEIE IPIVNSDTCQ EAYTPLKKKV TKDMICAGEK EGGKDACAGD
660 670 680 690 700
SGGPMVTKDA ERDQWYLVGV VSWGEDCGKK DRYGVYSYIY PNKDWIQRIT

GVRN
Length:704
Mass (Da):79,968
Last modified:April 14, 2009 - v2
Checksum:i4CF0B17916C10961
GO
Isoform 2 (identifier: P98064-2) [UniParc]FASTAAdd to basket
Also known as: MASP-3

The sequence of this isoform differs from the canonical sequence as follows:
     443-443: V → QPSRALPNLV...RAVRDLQVER
     444-704: Missing.

Note: Glycosylated on Asn-538 and Asn-604.By similarity
Show »
Length:733
Mass (Da):82,446
Checksum:i6B3B54D5D3F5822B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2571G → A in AAI31638 (PubMed:15489334).Curated
Sequence conflicti345 – 3451E → G in BAA03944 (PubMed:8133044).Curated
Sequence conflicti345 – 3451E → G in BAB69688 (PubMed:12847554).Curated
Sequence conflicti428 – 4281E → K in BAA03944 (PubMed:8133044).Curated
Sequence conflicti465 – 4651M → T in AAN39850 (PubMed:12847554).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei443 – 4431V → QPSRALPNLVKRIIGGRNAE LGLFPWQALIVVEDTSRVPN DKWFGSGALLSESWILTAAH VLRSQRRDNTVIPVSKEHVT VYLGLHDVRDKSGAVNSSAA RVILHPDFNIQNYNHDIALV QLQKPVPLGAHVMPICLPRP EPEGPAPHMLGLVAGWGISN PNVTVDEIILSGTRTLSDVL QYVKLPVVSHAECKASYESR SGNYSVTENMFCAGYYEGGK DTCLGDSGGAFVIFDEMSQH WVAQGLVSWGGPEECGSKQV YGVYTKVSNYVDWLWEEMNS PRAVRDLQVER in isoform 2. 2 PublicationsVSP_036814
Alternative sequencei444 – 704261Missing in isoform 2. 2 PublicationsVSP_036815Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16492 mRNA. Translation: BAA03944.1.
AB049755 mRNA. Translation: BAB69688.1.
AY135527, AY135525 Genomic DNA. Translation: AAN39850.1.
AK031598 mRNA. Translation: BAC27469.1.
CH466521 Genomic DNA. Translation: EDK97670.1.
CH466521 Genomic DNA. Translation: EDK97671.1.
BC131637 mRNA. Translation: AAI31638.1.
BC131638 mRNA. Translation: AAI31639.1.
CCDSiCCDS37303.1. [P98064-1]
PIRiPC1235.
RefSeqiNP_032581.2. NM_008555.2. [P98064-1]
XP_006521891.1. XM_006521828.2. [P98064-2]
UniGeneiMm.1213.

Genome annotation databases

EnsembliENSMUST00000089883; ENSMUSP00000087327; ENSMUSG00000022887. [P98064-1]
GeneIDi17174.
KEGGimmu:17174.
UCSCiuc007ytr.1. mouse. [P98064-1]
uc007yts.1. mouse. [P98064-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16492 mRNA. Translation: BAA03944.1.
AB049755 mRNA. Translation: BAB69688.1.
AY135527, AY135525 Genomic DNA. Translation: AAN39850.1.
AK031598 mRNA. Translation: BAC27469.1.
CH466521 Genomic DNA. Translation: EDK97670.1.
CH466521 Genomic DNA. Translation: EDK97671.1.
BC131637 mRNA. Translation: AAI31638.1.
BC131638 mRNA. Translation: AAI31639.1.
CCDSiCCDS37303.1. [P98064-1]
PIRiPC1235.
RefSeqiNP_032581.2. NM_008555.2. [P98064-1]
XP_006521891.1. XM_006521828.2. [P98064-2]
UniGeneiMm.1213.

3D structure databases

ProteinModelPortaliP98064.
SMRiP98064. Positions 27-704.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000087327.

Protein family/group databases

MEROPSiS01.198.

PTM databases

iPTMnetiP98064.
PhosphoSiteiP98064.

Proteomic databases

MaxQBiP98064.
PaxDbiP98064.
PeptideAtlasiP98064.
PRIDEiP98064.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000089883; ENSMUSP00000087327; ENSMUSG00000022887. [P98064-1]
GeneIDi17174.
KEGGimmu:17174.
UCSCiuc007ytr.1. mouse. [P98064-1]
uc007yts.1. mouse. [P98064-2]

Organism-specific databases

CTDi5648.
MGIiMGI:88492. Masp1.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000237311.
HOVERGENiHBG000559.
InParanoidiP98064.
KOiK03992.
OMAiVWGPFCG.
OrthoDBiEOG091G02DS.
PhylomeDBiP98064.
TreeFamiTF330373.

Enzyme and pathway databases

BRENDAi3.4.21.B7. 3474.

Miscellaneous databases

PROiP98064.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022887.
CleanExiMM_MASP1.

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.
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.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
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.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 1 hit.
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.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMASP1_MOUSE
AccessioniPrimary (citable) accession number: P98064
Secondary accession number(s): A2RRH8
, A2RRH9, Q8CD27, Q8CIR8, Q920S0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: April 14, 2009
Last modified: September 7, 2016
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.