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Q91WP0 (MASP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Mannan-binding lectin serine protease 2 A chain
  2. Mannan-binding lectin serine protease 2 B chain
Gene names
Name:Masp2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length685 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

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).

Subunit structure

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

Subcellular location

Secreted.

Tissue specificity

Plasma.

Post-translational modification

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

Miscellaneous

Dimerization and MBL2 binding requires calcium ions By similarity.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 2 CUB domains.

Contains 1 EGF-like domain.

Contains 1 peptidase S1 domain.

Contains 2 Sushi (CCP/SCR) domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q91WP0-1)

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.
Isoform 2 (identifier: Q91WP0-2)

Also known as: MAp19;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 685666Mannan-binding lectin serine protease 2
PRO_0000027601
Chain20 – 443424Mannan-binding lectin serine protease 2 A chain
PRO_0000027602
Chain444 – 685242Mannan-binding lectin serine protease 2 B chain
PRO_0000027603

Regions

Domain20 – 137118CUB 1
Domain138 – 18144EGF-like; calcium-binding
Domain184 – 296113CUB 2
Domain298 – 36366Sushi 1
Domain364 – 43168Sushi 2
Domain444 – 683240Peptidase S1

Sites

Active site4831Charge relay system By similarity
Active site5321Charge relay system By similarity
Active site6321Charge relay system By similarity
Metal binding671Calcium 1 By similarity
Metal binding751Calcium 1 By similarity
Metal binding1201Calcium 1 By similarity
Metal binding1221Calcium 1; via carbonyl oxygen By similarity
Metal binding1231Calcium 1 By similarity
Metal binding1381Calcium 2 By similarity
Metal binding1411Calcium 2 By similarity
Metal binding1581Calcium 2 By similarity
Metal binding1621Calcium 2; via carbonyl oxygen By similarity
Site443 – 4442Cleavage By similarity

Amino acid modifications

Modified residue1581(3R)-3-hydroxyasparagine Potential
Glycosylation1031N-linked (GlcNAc...) Potential
Glycosylation2851N-linked (GlcNAc...) Potential
Glycosylation3081N-linked (GlcNAc...) Potential
Glycosylation5451N-linked (GlcNAc...) Potential
Glycosylation6411N-linked (GlcNAc...) Ref.7
Disulfide bond72 ↔ 90 By similarity
Disulfide bond142 ↔ 156 By similarity
Disulfide bond152 ↔ 165 By similarity
Disulfide bond167 ↔ 180 By similarity
Disulfide bond184 ↔ 211 By similarity
Disulfide bond241 ↔ 259 By similarity
Disulfide bond300 ↔ 348 By similarity
Disulfide bond328 ↔ 361 By similarity
Disulfide bond366 ↔ 411 By similarity
Disulfide bond396 ↔ 429 By similarity
Disulfide bond433 ↔ 552Interchain (between A and B chains) By similarity
Disulfide bond598 ↔ 617 By similarity
Disulfide bond628 ↔ 659 By similarity

Natural variations

Alternative sequence182 – 1854ALCS → EQSL in isoform 2.
VSP_014636
Alternative sequence186 – 685500Missing in isoform 2.
VSP_014637

Experimental info

Sequence conflict1 – 22MR → MSLPCPQ Ref.2
Sequence conflict1721V → I in BAA34674. Ref.1
Sequence conflict1721V → I in CAB65247. Ref.2
Sequence conflict1921R → K in CAB65250. Ref.2
Sequence conflict3171I → T in BAA34674. Ref.1
Sequence conflict3251S → Y in CAB65250. Ref.2
Sequence conflict3841E → Q in BAA34674. Ref.1
Sequence conflict6001A → T in BAA34674. Ref.1
Sequence conflict6631D → G in BAA34674. Ref.1
Sequence conflict6781I → N in BAA34674. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: F56A6D522BC7099D

FASTA68575,517
        10         20         30         40         50         60 
MRLLIFLGLL WSLVATLLGS KWPEPVFGRL VSPGFPEKYA DHQDRSWTLT APPGYRLRLY 

        70         80         90        100        110        120 
FTHFDLELSY RCEYDFVKLS SGTKVLATLC GQESTDTEQA PGNDTFYSLG PSLKVTFHSD 

       130        140        150        160        170        180 
YSNEKPFTGF EAFYAAEDVD ECRVSLGDSV PCDHYCHNYL GGYYCSCRAG YVLHQNKHTC 

       190        200        210        220        230        240 
SALCSGQVFT GRSGYLSSPE YPQPYPKLSS CTYSIRLEDG FSVILDFVES FDVETHPEAQ 

       250        260        270        280        290        300 
CPYDSLKIQT DKGEHGPFCG KTLPPRIETD SHKVTITFAT DESGNHTGWK IHYTSTARPC 

       310        320        330        340        350        360 
PDPTAPPNGS ISPVQAIYVL KDRFSVFCKT GFELLQGSVP LKSFTAVCQK DGSWDRPMPE 

       370        380        390        400        410        420 
CSIIDCGPPD DLPNGHVDYI TGPEVTTYKA VIQYSCEETF YTMSSNGKYV CEADGFWTSS 

       430        440        450        460        470        480 
KGEKLPPVCE PVCGLSTHTI GGRIVGGQPA KPGDFPWQVL LLGQTTAAAG ALIHDNWVLT 

       490        500        510        520        530        540 
AAHAVYEKRM AASSLNIRMG ILKRLSPHYT QAWPEEIFIH EGYTHGAGFD NDIALIKLKN 

       550        560        570        580        590        600 
KVTINGSIMP VCLPRKEAAS LMRTDFTGTV AGWGLTQKGL LARNLMFVDI PIADHQKCTA 

       610        620        630        640        650        660 
VYEKLYPGVR VSANMLCAGL ETGGKDSCRG DSGGALVFLD NETQRWFVGG IVSWGSINCG 

       670        680 
AADQYGVYTK VINYIPWIEN IISNF

« Hide

Isoform 2 (MAp19) [UniParc].

Checksum: 72E01900D30A18B9
Show »

FASTA18520,974

References

« Hide 'large scale' references
[1]"Two lineages of mannose-binding lectin-associated serine protease (MASP) in vertebrates."
Endo Y., Takahashi M., Nakao M., Saiga H., Sekine H., Matsushita M., Nonaka M., Fujita T.
J. Immunol. 161:4924-4930(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: BALB/c.
Tissue: Liver.
[2]"The rat and mouse homologues of MASP-2 and MAp19, components of the mannan-binding lectin activation pathway of complement."
Stover C.M., Thiel S., Lynch N.J., Schwaeble W.J.
J. Immunol. 163:6848-6859(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1-362 (ISOFORM 1).
Strain: C57BL/6J X CBA/J.
[3]"Organization of the MASP2 locus and its expression profile in mouse and rat."
Stover C.M., Lynch N.J., Hanson S.J., Windbichler M., Gregory S.G., Schwaeble W.J.
Mamm. Genome 15:887-900(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Liver.
[5]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N.
Tissue: Liver.
[7]"Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-641, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Plasma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB009459 mRNA. Translation: BAA34674.1.
AJ250369 mRNA. Translation: CAB63701.1.
Y19160 mRNA. Translation: CAB65247.1.
Y19163 mRNA. Translation: CAB65250.1.
AK050052 mRNA. Translation: BAC34052.1.
AL606969 Genomic DNA. Translation: CAM21185.1.
AL606969 Genomic DNA. Translation: CAM21186.1.
BC013893 mRNA. Translation: AAH13893.1.
IPIIPI00467068.
IPI00480212.
RefSeqNP_001003893.1. NM_001003893.2.
NP_034897.1. NM_010767.3.
UniGeneMm.378962.

3D structure databases

ProteinModelPortalQ91WP0.
SMRQ91WP0. Positions 24-685.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000101327.

Protein family/group databases

MEROPSS01.229.

PTM databases

PhosphoSiteQ91WP0.

Proteomic databases

PaxDbQ91WP0.
PRIDEQ91WP0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000052060; ENSMUSP00000049729; ENSMUSG00000028979.
ENSMUST00000105701; ENSMUSP00000101326; ENSMUSG00000028979.
GeneID17175.
KEGGmmu:17175.
UCSCuc008vux.1. mouse.
uc008vuy.1. mouse.

Organism-specific databases

CTD10747.
MGIMGI:1330832. Masp2.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00560000076882.
HOVERGENHBG000559.
InParanoidB1ARY3.
KOK03993.
OMARLYFTHF.
OrthoDBEOG4ZKJKQ.

Gene expression databases

BgeeQ91WP0.
CleanExMM_MASP2.
GenevestigatorQ91WP0.
GermOnlineENSMUSG00000028979. Mus musculus.

Family and domain databases

Gene3D2.60.120.290. 2 hits.
InterProIPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024175. Pept_S1A_C1r/C1S/mannan-bd.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00431. CUB. 2 hits.
PF07645. EGF_CA. 1 hit.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001155. C1r_C1s_MASP. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF57535. Complement_control_module. 2 hits.
SSF49854. CUB. 2 hits.
SSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS00010. ASX_HYDROXYL. 1 hit.
PS01180. CUB. 2 hits.
PS00022. EGF_1. False negative.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. False negative.
PS01187. EGF_CA. 1 hit.
PS50923. SUSHI. 2 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. False negative.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMASP2. mouse.
NextBio291480.
SOURCESearch...

Entry information

Entry nameMASP2_MOUSE
AccessionPrimary (citable) accession number: Q91WP0
Secondary accession number(s): B1ARY2 expand/collapse secondary AC list , B1ARY3, Q9QXA4, Q9QXD2, Q9QXD5, Q9Z338
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: December 1, 2001
Last modified: May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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