GenomeNet

Database: UniProt
Entry: Q91WP0
LinkDB: Q91WP0
Original site: Q91WP0 
ID   MASP2_MOUSE             Reviewed;         685 AA.
AC   Q91WP0; B1ARY2; B1ARY3; Q9QXA4; Q9QXD2; Q9QXD5; Q9Z338;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   10-APR-2019, entry version 147.
DE   RecName: Full=Mannan-binding lectin serine protease 2;
DE            EC=3.4.21.104;
DE   AltName: Full=MBL-associated serine protease 2;
DE   AltName: Full=Mannose-binding protein-associated serine protease 2;
DE            Short=MASP-2;
DE   Contains:
DE     RecName: Full=Mannan-binding lectin serine protease 2 A chain;
DE   Contains:
DE     RecName: Full=Mannan-binding lectin serine protease 2 B chain;
DE   Flags: Precursor;
GN   Name=Masp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/cJ; TISSUE=Liver;
RX   PubMed=9794427;
RA   Endo Y., Takahashi M., Nakao M., Saiga H., Sekine H., Matsushita M.,
RA   Nonaka M., Fujita T.;
RT   "Two lineages of mannose-binding lectin-associated serine protease
RT   (MASP) in vertebrates.";
RL   J. Immunol. 161:4924-4930(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [MRNA]
RP   OF 1-362 (ISOFORM 1).
RC   STRAIN=C57BL/6J X CBA/J;
RX   PubMed=10586086;
RA   Stover C.M., Thiel S., Lynch N.J., Schwaeble W.J.;
RT   "The rat and mouse homologues of MASP-2 and MAp19, components of the
RT   mannan-binding lectin activation pathway of complement.";
RL   J. Immunol. 163:6848-6859(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15672593; DOI=10.1007/s00335-004-3006-8;
RA   Stover C.M., Lynch N.J., Hanson S.J., Windbichler M., Gregory S.G.,
RA   Schwaeble W.J.;
RT   "Organization of the MASP2 locus and its expression profile in mouse
RT   and rat.";
RL   Mamm. Genome 15:887-900(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-641.
RC   STRAIN=C57BL/6J; TISSUE=Plasma;
RX   PubMed=16944957; DOI=10.1021/pr060186m;
RA   Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
RA   Gevaert K.;
RT   "Proteome-wide characterization of N-glycosylation events by diagonal
RT   chromatography.";
RL   J. Proteome Res. 5:2438-2447(2006).
CC   -!- FUNCTION: Serum protease that plays an important role in the
CC       activation of the complement system via mannose-binding lectin.
CC       After activation by auto-catalytic cleavage it cleaves C2 and C4,
CC       leading to their activation and to the formation of C3 convertase
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage after Arg-223 in complement component
CC         C2 (-Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in
CC         complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile).;
CC         EC=3.4.21.104;
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Binds MBL2. Isoform 2 binds
CC       to MASP1. Binds SERPING1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91WP0-1; Sequence=Displayed;
CC       Name=2; Synonyms=MAp19;
CC         IsoId=Q91WP0-2; Sequence=VSP_014636, VSP_014637;
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Dimerization and MBL2 binding requires calcium
CC       ions. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; AB009459; BAA34674.1; -; mRNA.
DR   EMBL; AJ250369; CAB63701.1; -; mRNA.
DR   EMBL; Y19160; CAB65247.1; -; mRNA.
DR   EMBL; Y19163; CAB65250.1; -; mRNA.
DR   EMBL; AK050052; BAC34052.1; -; mRNA.
DR   EMBL; AL606969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC013893; AAH13893.1; -; mRNA.
DR   CCDS; CCDS18941.1; -. [Q91WP0-1]
DR   CCDS; CCDS18942.1; -. [Q91WP0-2]
DR   RefSeq; NP_001003893.1; NM_001003893.2. [Q91WP0-1]
DR   RefSeq; NP_034897.1; NM_010767.3. [Q91WP0-2]
DR   UniGene; Mm.378962; -.
DR   ProteinModelPortal; Q91WP0; -.
DR   SMR; Q91WP0; -.
DR   STRING; 10090.ENSMUSP00000049729; -.
DR   MEROPS; S01.229; -.
DR   iPTMnet; Q91WP0; -.
DR   PhosphoSitePlus; Q91WP0; -.
DR   PaxDb; Q91WP0; -.
DR   PeptideAtlas; Q91WP0; -.
DR   PRIDE; Q91WP0; -.
DR   Ensembl; ENSMUST00000052060; ENSMUSP00000049729; ENSMUSG00000028979. [Q91WP0-1]
DR   Ensembl; ENSMUST00000105701; ENSMUSP00000101326; ENSMUSG00000028979. [Q91WP0-2]
DR   GeneID; 17175; -.
DR   KEGG; mmu:17175; -.
DR   UCSC; uc008vux.1; mouse. [Q91WP0-2]
DR   UCSC; uc008vuy.1; mouse. [Q91WP0-1]
DR   CTD; 10747; -.
DR   MGI; MGI:1330832; Masp2.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00950000183084; -.
DR   HOVERGEN; HBG000559; -.
DR   InParanoid; Q91WP0; -.
DR   KO; K03993; -.
DR   OMA; MFVDIPI; -.
DR   OrthoDB; 156878at2759; -.
DR   PhylomeDB; Q91WP0; -.
DR   TreeFam; TF330373; -.
DR   BRENDA; 3.4.21.104; 3474.
DR   Reactome; R-MMU-166662; Lectin pathway of complement activation.
DR   Reactome; R-MMU-166663; Initial triggering of complement.
DR   ChiTaRS; Masp2; mouse.
DR   PRO; PR:Q91WP0; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   Bgee; ENSMUSG00000028979; Expressed in 80 organ(s), highest expression level in left lobe of liver.
DR   Genevisible; Q91WP0; MM.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR   GO; GO:0001855; F:complement component C4b binding; ISO:MGI.
DR   GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0001867; P:complement activation, lectin pathway; IDA:MGI.
DR   CDD; cd00033; CCP; 2.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.60.120.290; -; 2.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR037571; MASP2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24255:SF10; PTHR24255:SF10; 1.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF00084; Sushi; 2.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00032; CCP; 2.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF49854; SSF49854; 2.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57535; SSF57535; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50923; SUSHI; 2.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Autocatalytic cleavage; Calcium;
KW   Complement pathway; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Hydrolase; Hydroxylation; Immunity;
KW   Innate immunity; Metal-binding; Protease; Reference proteome; Repeat;
KW   Secreted; Serine protease; Signal; Sushi.
FT   SIGNAL        1     19       {ECO:0000250}.
FT   CHAIN        20    685       Mannan-binding lectin serine protease 2.
FT                                /FTId=PRO_0000027601.
FT   CHAIN        20    443       Mannan-binding lectin serine protease 2 A
FT                                chain.
FT                                /FTId=PRO_0000027602.
FT   CHAIN       444    685       Mannan-binding lectin serine protease 2 B
FT                                chain.
FT                                /FTId=PRO_0000027603.
FT   DOMAIN       20    137       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      138    181       EGF-like; calcium-binding.
FT   DOMAIN      184    296       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      298    363       Sushi 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      364    431       Sushi 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      444    683       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    483    483       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    532    532       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    632    632       Charge relay system. {ECO:0000250}.
FT   METAL        67     67       Calcium 1. {ECO:0000250}.
FT   METAL        75     75       Calcium 1. {ECO:0000250}.
FT   METAL       120    120       Calcium 1. {ECO:0000250}.
FT   METAL       122    122       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       123    123       Calcium 1. {ECO:0000250}.
FT   METAL       138    138       Calcium 2. {ECO:0000250}.
FT   METAL       141    141       Calcium 2. {ECO:0000250}.
FT   METAL       158    158       Calcium 2. {ECO:0000250}.
FT   METAL       162    162       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   SITE        443    444       Cleavage. {ECO:0000250}.
FT   MOD_RES     158    158       (3R)-3-hydroxyasparagine. {ECO:0000255}.
FT   CARBOHYD    103    103       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    285    285       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    308    308       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    545    545       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    641    641       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16944957}.
FT   DISULFID     72     90       {ECO:0000250}.
FT   DISULFID    142    156       {ECO:0000250}.
FT   DISULFID    152    165       {ECO:0000250}.
FT   DISULFID    167    180       {ECO:0000250}.
FT   DISULFID    184    211       {ECO:0000250}.
FT   DISULFID    241    259       {ECO:0000250}.
FT   DISULFID    300    348       {ECO:0000250}.
FT   DISULFID    328    361       {ECO:0000250}.
FT   DISULFID    366    411       {ECO:0000250}.
FT   DISULFID    396    429       {ECO:0000250}.
FT   DISULFID    433    552       Interchain (between A and B chains).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00059,
FT                                ECO:0000255|PROSITE-ProRule:PRU00274,
FT                                ECO:0000255|PROSITE-ProRule:PRU00302}.
FT   DISULFID    598    617       {ECO:0000250}.
FT   DISULFID    628    659       {ECO:0000250}.
FT   VAR_SEQ     182    185       ALCS -> EQSL (in isoform 2).
FT                                {ECO:0000303|PubMed:10586086}.
FT                                /FTId=VSP_014636.
FT   VAR_SEQ     186    685       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:10586086}.
FT                                /FTId=VSP_014637.
FT   CONFLICT      1      2       MR -> MSLPCPQ (in Ref. 2). {ECO:0000305}.
FT   CONFLICT    172    172       V -> I (in Ref. 1; BAA34674 and 2;
FT                                CAB65247). {ECO:0000305}.
FT   CONFLICT    192    192       R -> K (in Ref. 2; CAB65250).
FT                                {ECO:0000305}.
FT   CONFLICT    317    317       I -> T (in Ref. 1; BAA34674).
FT                                {ECO:0000305}.
FT   CONFLICT    325    325       S -> Y (in Ref. 2; CAB65250).
FT                                {ECO:0000305}.
FT   CONFLICT    384    384       E -> Q (in Ref. 1; BAA34674).
FT                                {ECO:0000305}.
FT   CONFLICT    600    600       A -> T (in Ref. 1; BAA34674).
FT                                {ECO:0000305}.
FT   CONFLICT    663    663       D -> G (in Ref. 1; BAA34674).
FT                                {ECO:0000305}.
FT   CONFLICT    678    678       I -> N (in Ref. 1; BAA34674).
FT                                {ECO:0000305}.
SQ   SEQUENCE   685 AA;  75517 MW;  F56A6D522BC7099D CRC64;
     MRLLIFLGLL WSLVATLLGS KWPEPVFGRL VSPGFPEKYA DHQDRSWTLT APPGYRLRLY
     FTHFDLELSY RCEYDFVKLS SGTKVLATLC GQESTDTEQA PGNDTFYSLG PSLKVTFHSD
     YSNEKPFTGF EAFYAAEDVD ECRVSLGDSV PCDHYCHNYL GGYYCSCRAG YVLHQNKHTC
     SALCSGQVFT GRSGYLSSPE YPQPYPKLSS CTYSIRLEDG FSVILDFVES FDVETHPEAQ
     CPYDSLKIQT DKGEHGPFCG KTLPPRIETD SHKVTITFAT DESGNHTGWK IHYTSTARPC
     PDPTAPPNGS ISPVQAIYVL KDRFSVFCKT GFELLQGSVP LKSFTAVCQK DGSWDRPMPE
     CSIIDCGPPD DLPNGHVDYI TGPEVTTYKA VIQYSCEETF YTMSSNGKYV CEADGFWTSS
     KGEKLPPVCE PVCGLSTHTI GGRIVGGQPA KPGDFPWQVL LLGQTTAAAG ALIHDNWVLT
     AAHAVYEKRM AASSLNIRMG ILKRLSPHYT QAWPEEIFIH EGYTHGAGFD NDIALIKLKN
     KVTINGSIMP VCLPRKEAAS LMRTDFTGTV AGWGLTQKGL LARNLMFVDI PIADHQKCTA
     VYEKLYPGVR VSANMLCAGL ETGGKDSCRG DSGGALVFLD NETQRWFVGG IVSWGSINCG
     AADQYGVYTK VINYIPWIEN IISNF
//
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