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O00187

- MASP2_HUMAN

UniProt

O00187 - MASP2_HUMAN

Protein

Mannan-binding lectin serine protease 2

Gene

MASP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 4 (11 Jan 2011)
      Previous versions | rss
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    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.1 Publication

    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 1
    Metal bindingi75 – 751Calcium 1
    Metal bindingi120 – 1201Calcium 1
    Metal bindingi122 – 1221Calcium 1; via carbonyl oxygen
    Metal bindingi123 – 1231Calcium 1
    Metal bindingi138 – 1381Calcium 2
    Metal bindingi139 – 1391Calcium 2; via carbonyl oxygen
    Metal bindingi141 – 1411Calcium 2
    Metal bindingi158 – 1581Calcium 2
    Metal bindingi159 – 1591Calcium 2; via carbonyl oxygen
    Metal bindingi162 – 1621Calcium 2; via carbonyl oxygen
    Sitei444 – 4452CleavageBy similarity
    Active sitei483 – 4831Charge relay system
    Active sitei532 – 5321Charge relay system
    Active sitei633 – 6331Charge relay system

    GO - Molecular functioni

    1. calcium-dependent protein binding Source: UniProtKB
    2. calcium ion binding Source: InterPro
    3. complement component C4b binding Source: BHF-UCL
    4. peptidase activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. serine-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    1. complement activation Source: Reactome
    2. complement activation, classical pathway Source: UniProtKB-KW
    3. complement activation, lectin pathway Source: UniProtKB
    4. innate immune response Source: Reactome

    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. 2681.
    ReactomeiREACT_163810. Ficolins bind to repetitive carbohydrate structures on the target cell surface.
    REACT_7964. Lectin pathway of complement activation.
    REACT_8024. Initial triggering of complement.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6902. MASP2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    MASP2 deficiency (MASPD) [MIM:613791]: A disorder that results in autoimmune manifestations, recurrent severe infections, and chronic inflammatory disease.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti120 – 1201D → G in MASPD; found in a patient suffering from frequent infections and chronic inflammatory disease; strongly decreases affinity for MBL2 and FCN2. 3 Publications
    Corresponds to variant rs72550870 [ dbSNP | Ensembl ].
    VAR_025346
    Natural varianti126 – 1261P → L in MASPD. 2 Publications
    Corresponds to variant rs56392418 [ dbSNP | Ensembl ].
    VAR_025347
    Natural varianti156 – 1561C → CHNH in MASPD.
    VAR_065814

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi74 – 741Y → A: Strongly decreases affinity for MBL2. Decreases affinity for FCN2. 1 Publication
    Mutagenesisi121 – 1211Y → A: Strongly decreases affinity for MBL2, but not for FCN2. 1 Publication
    Mutagenesisi124 – 1241E → A: Decreases affinity for MBL2. Slight decrease in affinity for FCN2. 1 Publication
    Mutagenesisi444 – 4441R → Q: Abolishes autocatalytic cleavage. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi613791. phenotype.
    Orphaneti331187. Immunodeficiency due to MASP-2 deficiency.
    PharmGKBiPA30645.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515Sequence AnalysisAdd
    BLAST
    Chaini16 – 686671Mannan-binding lectin serine protease 2PRO_0000027598Add
    BLAST
    Chaini16 – 444429Mannan-binding lectin serine protease 2 A chainPRO_0000027599Add
    BLAST
    Chaini445 – 686242Mannan-binding lectin serine protease 2 B chainPRO_0000027600Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi72 ↔ 90
    Disulfide bondi142 ↔ 156
    Disulfide bondi152 ↔ 165
    Modified residuei158 – 1581(3R)-3-hydroxyasparagineSequence Analysis
    Disulfide bondi167 ↔ 180
    Disulfide bondi184 ↔ 211By similarity
    Disulfide bondi241 ↔ 259By similarity
    Disulfide bondi300 ↔ 348By similarity
    Disulfide bondi328 ↔ 361By similarity
    Disulfide bondi366 ↔ 412
    Disulfide bondi396 ↔ 430
    Disulfide bondi434 ↔ 552Interchain (between A and B chains)
    Disulfide bondi598 ↔ 618
    Disulfide bondi629 ↔ 660

    Post-translational modificationi

    The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity
    Activated by cleavage after Arg-444. The uncleaved zymogen is inactive towards synthetic substrates, but has sufficient activity to effect autocatalytic cleavage.

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Hydroxylation

    Proteomic databases

    PaxDbiO00187.
    PRIDEiO00187.

    PTM databases

    PhosphoSiteiO00187.

    Expressioni

    Tissue specificityi

    Plasma.

    Gene expression databases

    BgeeiO00187.
    GenevestigatoriO00187.

    Organism-specific databases

    HPAiHPA029313.
    HPA029314.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Binds MBL2. Isoform 2 binds to MASP1. Binds SERPING1. Dimerization and MBL2 binding requires calcium ions.3 Publications

    Protein-protein interaction databases

    BioGridi115970. 5 interactions.
    IntActiO00187. 1 interaction.
    MINTiMINT-7970114.

    Structurei

    Secondary structure

    1
    686
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 315
    Turni33 – 364
    Beta strandi44 – 507
    Beta strandi55 – 6511
    Beta strandi74 – 8916
    Turni93 – 964
    Beta strandi98 – 1003
    Beta strandi109 – 11810
    Beta strandi129 – 13810
    Beta strandi151 – 1599
    Beta strandi162 – 1665
    Beta strandi171 – 1733
    Beta strandi309 – 3135
    Beta strandi323 – 3286
    Beta strandi332 – 3365
    Beta strandi345 – 3484
    Beta strandi350 – 3567
    Beta strandi360 – 3634
    Beta strandi375 – 3828
    Beta strandi391 – 3966
    Turni398 – 4003
    Beta strandi401 – 4033
    Beta strandi409 – 4124
    Beta strandi416 – 4205
    Beta strandi430 – 4323
    Beta strandi459 – 47315
    Turni474 – 4763
    Beta strandi477 – 4804
    Helixi482 – 4854
    Turni487 – 4904
    Beta strandi496 – 5005
    Beta strandi510 – 51910
    Beta strandi534 – 5407
    Helixi558 – 5614
    Beta strandi567 – 5737
    Beta strandi577 – 5793
    Beta strandi586 – 5927
    Helixi595 – 6039
    Beta strandi604 – 6063
    Beta strandi616 – 6205
    Beta strandi636 – 6416
    Turni642 – 6454
    Beta strandi646 – 65914
    Beta strandi667 – 6715
    Helixi672 – 6754
    Helixi676 – 68510

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Q3XX-ray2.23A/B363-686[»]
    1SZBX-ray2.50A/B16-181[»]
    1ZJKX-ray2.18A287-686[»]
    3TVJX-ray1.28A363-444[»]
    B445-686[»]
    4FXGX-ray3.75G/I291-444[»]
    H/J445-686[»]
    ProteinModelPortaliO00187.
    SMRiO00187. Positions 17-686.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00187.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 137122CUB 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini138 – 18144EGF-like; calcium-bindingAdd
    BLAST
    Domaini184 – 296113CUB 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini298 – 36366Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini364 – 43269Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini445 – 684240Peptidase 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

    eggNOGiCOG5640.
    HOVERGENiHBG000559.
    InParanoidiO00187.
    KOiK03993.
    OMAiWTLTAPP.
    OrthoDBiEOG7W6WK4.
    PhylomeDBiO00187.
    TreeFamiTF330373.

    Family and domain databases

    Gene3Di2.60.120.290. 2 hits.
    InterProiIPR000859. CUB_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    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]
    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.
    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. Align

    Isoform 1 (identifier: O00187-1) [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

    MRLLTLLGLL CGSVATPLGP KWPEPVFGRL ASPGFPGEYA NDQERRWTLT    50
    APPGYRLRLY FTHFDLELSH LCEYDFVKLS SGAKVLATLC GQESTDTERA 100
    PGKDTFYSLG SSLDITFRSD YSNEKPFTGF EAFYAAEDID ECQVAPGEAP 150
    TCDHHCHNHL GGFYCSCRAG YVLHRNKRTC SALCSGQVFT QRSGELSSPE 200
    YPRPYPKLSS CTYSISLEEG FSVILDFVES FDVETHPETL CPYDFLKIQT 250
    DREEHGPFCG KTLPHRIETK SNTVTITFVT DESGDHTGWK IHYTSTAQPC 300
    PYPMAPPNGH VSPVQAKYIL KDSFSIFCET GYELLQGHLP LKSFTAVCQK 350
    DGSWDRPMPA CSIVDCGPPD DLPSGRVEYI TGPGVTTYKA VIQYSCEETF 400
    YTMKVNDGKY VCEADGFWTS SKGEKSLPVC EPVCGLSART TGGRIYGGQK 450
    AKPGDFPWQV LILGGTTAAG ALLYDNWVLT AAHAVYEQKH DASALDIRMG 500
    TLKRLSPHYT QAWSEAVFIH EGYTHDAGFD NDIALIKLNN KVVINSNITP 550
    ICLPRKEAES FMRTDDIGTA SGWGLTQRGF LARNLMYVDI PIVDHQKCTA 600
    AYEKPPYPRG SVTANMLCAG LESGGKDSCR GDSGGALVFL DSETERWFVG 650
    GIVSWGSMNC GEAGQYGVYT KVINYIPWIE NIISDF 686
    Length:686
    Mass (Da):75,702
    Last modified:January 11, 2011 - v4
    Checksum:iED952085FA115E21
    GO
    Isoform 2 (identifier: O00187-2) [UniParc]FASTAAdd to Basket

    Also known as: MAp19, Small MBL-associated protein, sMAP

    The sequence of this isoform differs from the canonical sequence as follows:
         182-185: ALCS → EQSL
         186-686: Missing.

    Show »
    Length:185
    Mass (Da):20,629
    Checksum:i73B133D56FB229C2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti41 – 411N → S in BAF83512. (PubMed:14702039)Curated
    Sequence conflicti225 – 2251L → P in BAF83512. (PubMed:14702039)Curated
    Sequence conflicti298 – 2992QP → HA in CAA71059. (PubMed:9087411)Curated
    Sequence conflicti298 – 2992QP → HA in CAB50733. (PubMed:10092804)Curated
    Sequence conflicti298 – 2992QP → HA in CAB50735. (PubMed:10092804)Curated
    Sequence conflicti298 – 2992QP → HA in CAA67050. 1 PublicationCurated
    Sequence conflicti298 – 2992QP → HA in AAG50274. 1 PublicationCurated
    Sequence conflicti361 – 3622Missing in CAB50733. (PubMed:10092804)Curated
    Sequence conflicti361 – 3622Missing in CAB50735. (PubMed:10092804)Curated
    Sequence conflicti372 – 3721L → LCS in CAB50733. (PubMed:10092804)Curated
    Sequence conflicti372 – 3721L → LCS in CAB50735. (PubMed:10092804)Curated
    Sequence conflicti399 – 3991T → A in BAF83512. (PubMed:14702039)Curated
    Sequence conflicti442 – 4421G → E in AAG50274. 1 PublicationCurated
    Sequence conflicti447 – 4471G → E in AAG50274. 1 PublicationCurated
    Sequence conflicti461 – 4622Missing in CAB50733. (PubMed:10092804)Curated
    Sequence conflicti461 – 4622Missing in CAB50735. (PubMed:10092804)Curated
    Sequence conflicti473 – 4731L → LIL in CAB50733. (PubMed:10092804)Curated
    Sequence conflicti473 – 4731L → LIL in CAB50735. (PubMed:10092804)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti99 – 991R → Q.2 Publications
    Corresponds to variant rs61735600 [ dbSNP | Ensembl ].
    VAR_025344
    Natural varianti118 – 1181R → C.2 Publications
    Corresponds to variant rs147270785 [ dbSNP | Ensembl ].
    VAR_025345
    Natural varianti120 – 1201D → G in MASPD; found in a patient suffering from frequent infections and chronic inflammatory disease; strongly decreases affinity for MBL2 and FCN2. 3 Publications
    Corresponds to variant rs72550870 [ dbSNP | Ensembl ].
    VAR_025346
    Natural varianti126 – 1261P → L in MASPD. 2 Publications
    Corresponds to variant rs56392418 [ dbSNP | Ensembl ].
    VAR_025347
    Natural varianti155 – 1551H → R.
    Corresponds to variant rs2273343 [ dbSNP | Ensembl ].
    VAR_028784
    Natural varianti156 – 1561C → CHNH in MASPD.
    VAR_065814
    Natural varianti371 – 3711D → Y.1 Publication
    Corresponds to variant rs12711521 [ dbSNP | Ensembl ].
    VAR_028785
    Natural varianti377 – 3771V → A Associated with reduced MASP2 levels in plasma. 2 Publications
    Corresponds to variant rs2273346 [ dbSNP | Ensembl ].
    VAR_028786
    Natural varianti439 – 4391R → H.
    Corresponds to variant rs12085877 [ dbSNP | Ensembl ].
    VAR_028787

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei182 – 1854ALCS → EQSL in isoform 2. 2 PublicationsVSP_005383
    Alternative sequencei186 – 686501Missing in isoform 2. 2 PublicationsVSP_005384Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09926 mRNA. Translation: CAA71059.1.
    AB008047 mRNA. Translation: BAA78616.1.
    Y18281 mRNA. Translation: CAB50728.1.
    Y18282 mRNA. Translation: CAB50729.1.
    Y18283 mRNA. Translation: CAB50730.1.
    Y18284 mRNA. Translation: CAB50731.1.
    Y18286 Genomic DNA. Translation: CAB50732.1.
    Y18286 Genomic DNA. Translation: CAB50733.1.
    Y18287 Genomic DNA. Translation: CAB50734.1.
    Y18287 Genomic DNA. Translation: CAB50735.1.
    X98400 mRNA. Translation: CAA67050.1.
    AB033742 Genomic DNA. Translation: BAA85658.1.
    AB033742 Genomic DNA. Translation: BAA85659.1.
    AF321558 Genomic DNA. Translation: AAG50275.1.
    AF321562
    , AF321558, AF321559, AF321560, AF321561 Genomic DNA. Translation: AAG50274.1.
    AK290823 mRNA. Translation: BAF83512.1.
    AL109811 Genomic DNA. Translation: CAI22102.1.
    AL109811 Genomic DNA. Translation: CAI22103.1.
    AJ297949 Genomic DNA. Translation: CAC17138.1.
    AJ297949 Genomic DNA. Translation: CAC17139.1.
    AJ300188 Genomic DNA. Translation: CAC15568.1.
    CCDSiCCDS123.1. [O00187-1]
    CCDS124.1. [O00187-2]
    PIRiA59271.
    RefSeqiNP_006601.2. NM_006610.3. [O00187-1]
    NP_631947.1. NM_139208.2. [O00187-2]
    UniGeneiHs.655645.

    Genome annotation databases

    EnsembliENST00000400897; ENSP00000383690; ENSG00000009724. [O00187-1]
    ENST00000400898; ENSP00000383691; ENSG00000009724. [O00187-2]
    GeneIDi10747.
    KEGGihsa:10747.
    UCSCiuc001aru.3. human. [O00187-1]
    uc001arv.3. human. [O00187-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    MASP2base

    MASP2 mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09926 mRNA. Translation: CAA71059.1 .
    AB008047 mRNA. Translation: BAA78616.1 .
    Y18281 mRNA. Translation: CAB50728.1 .
    Y18282 mRNA. Translation: CAB50729.1 .
    Y18283 mRNA. Translation: CAB50730.1 .
    Y18284 mRNA. Translation: CAB50731.1 .
    Y18286 Genomic DNA. Translation: CAB50732.1 .
    Y18286 Genomic DNA. Translation: CAB50733.1 .
    Y18287 Genomic DNA. Translation: CAB50734.1 .
    Y18287 Genomic DNA. Translation: CAB50735.1 .
    X98400 mRNA. Translation: CAA67050.1 .
    AB033742 Genomic DNA. Translation: BAA85658.1 .
    AB033742 Genomic DNA. Translation: BAA85659.1 .
    AF321558 Genomic DNA. Translation: AAG50275.1 .
    AF321562
    , AF321558 , AF321559 , AF321560 , AF321561 Genomic DNA. Translation: AAG50274.1 .
    AK290823 mRNA. Translation: BAF83512.1 .
    AL109811 Genomic DNA. Translation: CAI22102.1 .
    AL109811 Genomic DNA. Translation: CAI22103.1 .
    AJ297949 Genomic DNA. Translation: CAC17138.1 .
    AJ297949 Genomic DNA. Translation: CAC17139.1 .
    AJ300188 Genomic DNA. Translation: CAC15568.1 .
    CCDSi CCDS123.1. [O00187-1 ]
    CCDS124.1. [O00187-2 ]
    PIRi A59271.
    RefSeqi NP_006601.2. NM_006610.3. [O00187-1 ]
    NP_631947.1. NM_139208.2. [O00187-2 ]
    UniGenei Hs.655645.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Q3X X-ray 2.23 A/B 363-686 [» ]
    1SZB X-ray 2.50 A/B 16-181 [» ]
    1ZJK X-ray 2.18 A 287-686 [» ]
    3TVJ X-ray 1.28 A 363-444 [» ]
    B 445-686 [» ]
    4FXG X-ray 3.75 G/I 291-444 [» ]
    H/J 445-686 [» ]
    ProteinModelPortali O00187.
    SMRi O00187. Positions 17-686.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115970. 5 interactions.
    IntActi O00187. 1 interaction.
    MINTi MINT-7970114.

    Protein family/group databases

    MEROPSi S01.229.

    PTM databases

    PhosphoSitei O00187.

    Proteomic databases

    PaxDbi O00187.
    PRIDEi O00187.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000400897 ; ENSP00000383690 ; ENSG00000009724 . [O00187-1 ]
    ENST00000400898 ; ENSP00000383691 ; ENSG00000009724 . [O00187-2 ]
    GeneIDi 10747.
    KEGGi hsa:10747.
    UCSCi uc001aru.3. human. [O00187-1 ]
    uc001arv.3. human. [O00187-2 ]

    Organism-specific databases

    CTDi 10747.
    GeneCardsi GC01M011086.
    HGNCi HGNC:6902. MASP2.
    HPAi HPA029313.
    HPA029314.
    MIMi 605102. gene.
    613791. phenotype.
    neXtProti NX_O00187.
    Orphaneti 331187. Immunodeficiency due to MASP-2 deficiency.
    PharmGKBi PA30645.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOVERGENi HBG000559.
    InParanoidi O00187.
    KOi K03993.
    OMAi WTLTAPP.
    OrthoDBi EOG7W6WK4.
    PhylomeDBi O00187.
    TreeFami TF330373.

    Enzyme and pathway databases

    BRENDAi 3.4.21.104. 2681.
    Reactomei REACT_163810. Ficolins bind to repetitive carbohydrate structures on the target cell surface.
    REACT_7964. Lectin pathway of complement activation.
    REACT_8024. Initial triggering of complement.

    Miscellaneous databases

    EvolutionaryTracei O00187.
    GenomeRNAii 10747.
    NextBioi 40811.
    PROi O00187.
    SOURCEi Search...

    Gene expression databases

    Bgeei O00187.
    Genevestigatori O00187.

    Family and domain databases

    Gene3Di 2.60.120.290. 2 hits.
    InterProi IPR000859. CUB_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    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 ]
    Pfami PF00431. CUB. 2 hits.
    PF07645. EGF_CA. 1 hit.
    PF00084. Sushi. 2 hits.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001155. C1r_C1s_MASP. 1 hit.
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00032. CCP. 2 hits.
    SM00042. CUB. 2 hits.
    SM00179. EGF_CA. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49854. SSF49854. 2 hits.
    SSF50494. SSF50494. 1 hit.
    SSF57535. SSF57535. 2 hits.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "A truncated form of mannose-binding lectin-associated serine protease (MASP)-2 expressed by alternative polyadenylation is a component of the lectin complement pathway."
      Takahashi M., Endo Y., Fujita T., Matsushita M.
      Int. Immunol. 11:859-863(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
    3. "Two constituents of the initiation complex of the mannan-binding lectin activation pathway of complement are encoded by a single structural gene."
      Stover C.M., Thiel S., Thelen M., Lynch N.J., Vorup-Jensen T., Jensenius J.C., Schwaeble W.J.
      J. Immunol. 162:3481-3490(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), ACTIVATION BY PROTEOLYTIC CLEAVAGE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Liver.
    4. "Identification and characterization of a novel protein of the human complement system, mannan-binding lectin-associated serine protease-2 (MASP-2)."
      Thiel S., Vorup-Jensen T., Stover C.M., Schwaeble W., Laursen S.B., Poulsen K., Willis A.C., Eggleton P., Hansen S., Holmskov U., Reid K.B.M., Jensenius J.C.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "Partial genomic structure of human MBL-associated serine protease (MASP)-2 (from exon 1 to exon 5)."
      Takahashi M., Fujita T.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-371.
    6. "Structure of human MASP-2 gene."
      Park D., Kim B., Baek K., Yoon J.
      Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver.
    8. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "Towards a comprehensive database of proteins from the urine of patients with bladder cancer."
      Rasmussen H.H., Orntoft T.F., Wolf H., Celis J.E.
      J. Urol. 155:2113-2119(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 30-45.
      Tissue: Urine.
    10. "The human gene for mannan-binding lectin-associated serine protease-2 (MASP-2), the effector component of the lectin route of complement activation, is part of a tightly linked gene cluster on chromosome 1p36.2-3."
      Stover C., Endo Y., Takahashi M., Lynch N., Constantinescu C., Vorup-Jensen T., Thiel S., Friedl H., Hankeln T., Hall R., Gregory S., Fujita T., Schwaeble W.
      Genes Immun. 2:119-127(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-284 AND 364-686, VARIANT ALA-377.
    11. "Proteolytic activities of two types of mannose-binding lectin-associated serine protease."
      Matsushita M., Thiel S., Jensenius J.C., Terai I., Fujita T.
      J. Immunol. 165:2637-2642(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SERPING1.
    12. "The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan-binding lectin and L-ficolin."
      Gregory L.A., Thielens N.M., Matsushita M., Sorensen R., Arlaud G.J., Fontecilla-Camps J.-C., Gaboriaud C.
      J. Biol. Chem. 279:29391-29397(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 16-181 (ISOFORM 2), CHARACTERIZATION OF VARIANT GLY-120, CALCIUM-BINDING SITES, DIMERIZATION, MUTAGENESIS OF TYR-74; TYR-121 AND GLU-124, INTERACTION WITH MBL2 AND FCN2, DISULFIDE BONDS.
    13. "The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions."
      Harmat V., Gal P., Kardos J., Szilagyi K., Ambrus G., Vegh B., Naray-Szabo G., Zavodszky P.
      J. Mol. Biol. 342:1533-1546(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 363-686, DISULFIDE BONDS.
    14. "A true autoactivating enzyme. Structural insight into mannose-binding lectin-associated serine protease-2 activations."
      Gal P., Harmat V., Kocsis A., Bian T., Barna L., Ambrus G., Vegh B., Balczer J., Sim R.B., Naray-Szabo G., Zavodszky P.
      J. Biol. Chem. 280:33435-33444(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 287-686, AUTOCATALYTIC CLEAVAGE AT ARG-444, MUTAGENESIS OF ARG-444.
    15. Cited for: VARIANT MASPD GLY-120, CHARACTERIZATION OF VARIANT MASPD GLY-120.
    16. "Novel MASP2 variants detected among North African and Sub-Saharan individuals."
      Lozano F., Suarez B., Munoz A., Jensenius J.C., Mensa J., Vives J., Horcajada J.P.
      Tissue Antigens 66:131-135(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GLN-99; CYS-118; GLY-120 AND LEU-126.
    17. "Deficiency of mannan-binding lectin associated serine protease-2 due to missense polymorphisms."
      Thiel S., Steffensen R., Christensen I.J., Ip W.K., Lau Y.L., Reason I.J., Eiberg H., Gadjeva M., Ruseva M., Jensenius J.C.
      Genes Immun. 8:154-163(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MASPD GLY-120; LEU-126 AND HIS-ASN-HIS-156 INS, VARIANTS GLN-99; CYS-118 AND ALA-377.

    Entry informationi

    Entry nameiMASP2_HUMAN
    AccessioniPrimary (citable) accession number: O00187
    Secondary accession number(s): A8K458
    , A8MWJ2, O75754, Q5TEQ5, Q5TER0, Q96QG4, Q9BZH0, Q9H498, Q9H499, Q9UBP3, Q9UC48, Q9ULC7, Q9UMV3, Q9Y270
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 165 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3