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Q91WP0

- MASP2_MOUSE

UniProt

Q91WP0 - MASP2_MOUSE

Protein

Mannan-binding lectin serine protease 2

Gene

Masp2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      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 By similarity.By similarity

    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 2By similarity
    Metal bindingi141 – 1411Calcium 2By similarity
    Metal bindingi158 – 1581Calcium 2By similarity
    Metal bindingi162 – 1621Calcium 2; via carbonyl oxygenBy similarity
    Sitei443 – 4442CleavageBy similarity
    Active sitei483 – 4831Charge relay systemBy similarity
    Active sitei532 – 5321Charge relay systemBy similarity
    Active sitei632 – 6321Charge relay systemBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. serine-type endopeptidase activity Source: Ensembl

    GO - Biological processi

    1. complement activation, classical pathway Source: UniProtKB-KW
    2. complement activation, lectin pathway Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Complement pathway, Immunity, Innate immunity

    Keywords - Ligandi

    Calcium, Metal-binding

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1330832. Masp2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919By similarityAdd
    BLAST
    Chaini20 – 685666Mannan-binding lectin serine protease 2PRO_0000027601Add
    BLAST
    Chaini20 – 443424Mannan-binding lectin serine protease 2 A chainPRO_0000027602Add
    BLAST
    Chaini444 – 685242Mannan-binding lectin serine protease 2 B chainPRO_0000027603Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi72 ↔ 90By similarity
    Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi142 ↔ 156By similarity
    Disulfide bondi152 ↔ 165By similarity
    Modified residuei158 – 1581(3R)-3-hydroxyasparagineSequence Analysis
    Disulfide bondi167 ↔ 180By similarity
    Disulfide bondi184 ↔ 211By similarity
    Disulfide bondi241 ↔ 259By similarity
    Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi300 ↔ 348By similarity
    Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi328 ↔ 361By similarity
    Disulfide bondi366 ↔ 411By similarity
    Disulfide bondi396 ↔ 429By similarity
    Disulfide bondi433 ↔ 552Interchain (between A and B chains)PROSITE-ProRule annotation
    Glycosylationi545 – 5451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi598 ↔ 617By similarity
    Disulfide bondi628 ↔ 659By similarity
    Glycosylationi641 – 6411N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    MaxQBiQ91WP0.
    PaxDbiQ91WP0.
    PRIDEiQ91WP0.

    PTM databases

    PhosphoSiteiQ91WP0.

    Expressioni

    Tissue specificityi

    Plasma.

    Gene expression databases

    BgeeiQ91WP0.
    CleanExiMM_MASP2.
    GenevestigatoriQ91WP0.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000101327.

    Structurei

    3D structure databases

    ProteinModelPortaliQ91WP0.
    SMRiQ91WP0. Positions 24-685.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    eggNOGiCOG5640.
    GeneTreeiENSGT00560000076882.
    HOVERGENiHBG000559.
    InParanoidiB1ARY3.
    KOiK03993.
    OMAiWTLTAPP.
    OrthoDBiEOG7W6WK4.
    PhylomeDBiQ91WP0.
    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: Q91WP0-1) [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

    MRLLIFLGLL WSLVATLLGS KWPEPVFGRL VSPGFPEKYA DHQDRSWTLT    50
    APPGYRLRLY FTHFDLELSY RCEYDFVKLS SGTKVLATLC GQESTDTEQA 100
    PGNDTFYSLG PSLKVTFHSD YSNEKPFTGF EAFYAAEDVD ECRVSLGDSV 150
    PCDHYCHNYL GGYYCSCRAG YVLHQNKHTC SALCSGQVFT GRSGYLSSPE 200
    YPQPYPKLSS CTYSIRLEDG FSVILDFVES FDVETHPEAQ CPYDSLKIQT 250
    DKGEHGPFCG KTLPPRIETD SHKVTITFAT DESGNHTGWK IHYTSTARPC 300
    PDPTAPPNGS ISPVQAIYVL KDRFSVFCKT GFELLQGSVP LKSFTAVCQK 350
    DGSWDRPMPE CSIIDCGPPD DLPNGHVDYI TGPEVTTYKA VIQYSCEETF 400
    YTMSSNGKYV CEADGFWTSS KGEKLPPVCE PVCGLSTHTI GGRIVGGQPA 450
    KPGDFPWQVL LLGQTTAAAG ALIHDNWVLT AAHAVYEKRM AASSLNIRMG 500
    ILKRLSPHYT QAWPEEIFIH EGYTHGAGFD NDIALIKLKN KVTINGSIMP 550
    VCLPRKEAAS LMRTDFTGTV AGWGLTQKGL LARNLMFVDI PIADHQKCTA 600
    VYEKLYPGVR VSANMLCAGL ETGGKDSCRG DSGGALVFLD NETQRWFVGG 650
    IVSWGSINCG AADQYGVYTK VINYIPWIEN IISNF 685
    Length:685
    Mass (Da):75,517
    Last modified:December 1, 2001 - v1
    Checksum:iF56A6D522BC7099D
    GO
    Isoform 2 (identifier: Q91WP0-2) [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):20,974
    Checksum:i72E01900D30A18B9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 22MR → MSLPCPQ(PubMed:10586086)Curated
    Sequence conflicti172 – 1721V → I in BAA34674. (PubMed:9794427)Curated
    Sequence conflicti172 – 1721V → I in CAB65247. (PubMed:10586086)Curated
    Sequence conflicti192 – 1921R → K in CAB65250. (PubMed:10586086)Curated
    Sequence conflicti317 – 3171I → T in BAA34674. (PubMed:9794427)Curated
    Sequence conflicti325 – 3251S → Y in CAB65250. (PubMed:10586086)Curated
    Sequence conflicti384 – 3841E → Q in BAA34674. (PubMed:9794427)Curated
    Sequence conflicti600 – 6001A → T in BAA34674. (PubMed:9794427)Curated
    Sequence conflicti663 – 6631D → G in BAA34674. (PubMed:9794427)Curated
    Sequence conflicti678 – 6781I → N in BAA34674. (PubMed:9794427)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei182 – 1854ALCS → EQSL in isoform 2. 1 PublicationVSP_014636
    Alternative sequencei186 – 685500Missing in isoform 2. 1 PublicationVSP_014637Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS18941.1. [Q91WP0-1]
    CCDS18942.1. [Q91WP0-2]
    RefSeqiNP_001003893.1. NM_001003893.2. [Q91WP0-1]
    NP_034897.1. NM_010767.3. [Q91WP0-2]
    UniGeneiMm.378962.

    Genome annotation databases

    EnsembliENSMUST00000052060; ENSMUSP00000049729; ENSMUSG00000028979. [Q91WP0-1]
    ENSMUST00000105701; ENSMUSP00000101326; ENSMUSG00000028979. [Q91WP0-2]
    GeneIDi17175.
    KEGGimmu:17175.
    UCSCiuc008vux.1. mouse. [Q91WP0-2]
    uc008vuy.1. mouse. [Q91WP0-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS18941.1. [Q91WP0-1 ]
    CCDS18942.1. [Q91WP0-2 ]
    RefSeqi NP_001003893.1. NM_001003893.2. [Q91WP0-1 ]
    NP_034897.1. NM_010767.3. [Q91WP0-2 ]
    UniGenei Mm.378962.

    3D structure databases

    ProteinModelPortali Q91WP0.
    SMRi Q91WP0. Positions 24-685.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000101327.

    Protein family/group databases

    MEROPSi S01.229.

    PTM databases

    PhosphoSitei Q91WP0.

    Proteomic databases

    MaxQBi Q91WP0.
    PaxDbi Q91WP0.
    PRIDEi Q91WP0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000052060 ; ENSMUSP00000049729 ; ENSMUSG00000028979 . [Q91WP0-1 ]
    ENSMUST00000105701 ; ENSMUSP00000101326 ; ENSMUSG00000028979 . [Q91WP0-2 ]
    GeneIDi 17175.
    KEGGi mmu:17175.
    UCSCi uc008vux.1. mouse. [Q91WP0-2 ]
    uc008vuy.1. mouse. [Q91WP0-1 ]

    Organism-specific databases

    CTDi 10747.
    MGIi MGI:1330832. Masp2.

    Phylogenomic databases

    eggNOGi COG5640.
    GeneTreei ENSGT00560000076882.
    HOVERGENi HBG000559.
    InParanoidi B1ARY3.
    KOi K03993.
    OMAi WTLTAPP.
    OrthoDBi EOG7W6WK4.
    PhylomeDBi Q91WP0.
    TreeFami TF330373.

    Miscellaneous databases

    ChiTaRSi MASP2. mouse.
    NextBioi 291480.
    PROi Q91WP0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q91WP0.
    CleanExi MM_MASP2.
    Genevestigatori Q91WP0.

    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. "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.
      , 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. 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.
      Strain: C57BL/6.
      Tissue: Plasma.

    Entry informationi

    Entry nameiMASP2_MOUSE
    AccessioniPrimary (citable) accession number: Q91WP0
    Secondary accession number(s): B1ARY2
    , B1ARY3, Q9QXA4, Q9QXD2, Q9QXD5, Q9Z338
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Dimerization and MBL2 binding requires calcium ions.By similarity

    Keywords - Technical termi

    Complete proteome, 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

    External Data

    Dasty 3