MASP2_RAT
ID MASP2_RAT Reviewed; 685 AA.
AC Q9JJS8; Q9JJP3; Q9QX83; Q9QX84; Q9QX85; Q9QX86; Q9QX87; Q9QX88; Q9QX89;
AC Q9QX90; Q9QX91; Q9QXD4; Q9WUZ0;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 155.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBUNIT STRUCTURE,
RP ACTIVATION BY PROTEOLYTIC CLEAVAGE, AND TISSUE SPECIFICITY.
RC STRAIN=Fischer 344;
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 [2]
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 and
RT rat.";
RL Mamm. Genome 15:887-900(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-685 (ISOFORM 1), PROTEIN SEQUENCE OF
RP N-TERMINUS, SUBUNIT STRUCTURE, GLYCOSYLATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND INTERACTION WITH MBL2.
RC TISSUE=Liver;
RX PubMed=10913141; DOI=10.1074/jbc.m004030200;
RA Wallis R., Dodd R.B.;
RT "Interaction of mannose-binding protein with associated serine proteases:
RT effects of naturally occurring mutations.";
RL J. Biol. Chem. 275:30962-30969(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 87-294 (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=10092804;
RA Stover C.M., Thiel S., Thelen M., Lynch N.J., Vorup-Jensen T.,
RA Jensenius J.C., Schwaeble W.J.;
RT "Two constituents of the initiation complex of the mannan-binding lectin
RT activation pathway of complement are encoded by a single structural gene.";
RL J. Immunol. 162:3481-3490(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 20-299, HYDROXYLATION AT ASN-158,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-103.
RX PubMed=12743029; DOI=10.1093/emboj/cdg236;
RA Feinberg H., Uitdehaag J.C.M., Davies J.M., Wallis R., Drickamer K.,
RA Weis W.I.;
RT "Crystal structure of the CUB1-EGF-CUB2 region of mannose-binding protein
RT associated serine protease-2.";
RL EMBO J. 22:2348-2359(2003).
CC -!- FUNCTION: Serum protease that plays an important role in the activation
CC of the complement system via mannose-binding lectin. After activation
CC by auto-catalytic cleavage it cleaves C2 and C4, leading to their
CC activation and to the formation of C3 convertase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage after Arg-223 in complement component C2 (-
CC Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in complement
CC component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile).; EC=3.4.21.104;
CC -!- SUBUNIT: Homodimer; disulfide-linked. Binds MBL2. Isoform 2 binds to
CC 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=Q9JJS8-1; Sequence=Displayed;
CC Name=2; Synonyms=MAp19;
CC IsoId=Q9JJS8-2; Sequence=VSP_014638, VSP_014639;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver. Secreted in plasma.
CC {ECO:0000269|PubMed:10586086}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10913141,
CC ECO:0000269|PubMed:12743029}.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC -!- MISCELLANEOUS: Dimerization and MBL2 binding requires calcium ions.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; Y19161; CAB65248.1; -; mRNA.
DR EMBL; Y18565; CAB65382.1; -; mRNA.
DR EMBL; Y18566; CAB65383.1; -; mRNA.
DR EMBL; Y18567; CAB65384.1; -; mRNA.
DR EMBL; Y18568; CAB65385.1; -; mRNA.
DR EMBL; Y18569; CAB65386.1; -; mRNA.
DR EMBL; Y18570; CAB65387.1; -; mRNA.
DR EMBL; Y18571; CAB65388.1; -; mRNA.
DR EMBL; Y18572; CAB65389.1; -; mRNA.
DR EMBL; Y18573; CAB65390.1; -; mRNA.
DR EMBL; Y18564; CAB70973.1; -; mRNA.
DR EMBL; AJ277747; CAB90832.1; -; mRNA.
DR EMBL; Y18285; CAB50738.1; -; mRNA.
DR RefSeq; NP_742040.1; NM_172043.1.
DR PDB; 1NT0; X-ray; 2.70 A; A/G=20-299.
DR PDB; 5CIS; X-ray; 2.58 A; A=21-298.
DR PDB; 5CKM; X-ray; 2.73 A; A=21-297.
DR PDB; 5CKN; X-ray; 2.60 A; A/D=20-297.
DR PDBsum; 1NT0; -.
DR PDBsum; 5CIS; -.
DR PDBsum; 5CKM; -.
DR PDBsum; 5CKN; -.
DR AlphaFoldDB; Q9JJS8; -.
DR SMR; Q9JJS8; -.
DR CORUM; Q9JJS8; -.
DR STRING; 10116.ENSRNOP00000016317; -.
DR MEROPS; S01.229; -.
DR GlyGen; Q9JJS8; 3 sites.
DR iPTMnet; Q9JJS8; -.
DR PaxDb; Q9JJS8; -.
DR PeptideAtlas; Q9JJS8; -.
DR PRIDE; Q9JJS8; -.
DR ABCD; Q9JJS8; 10 sequenced antibodies.
DR GeneID; 64459; -.
DR KEGG; rno:64459; -.
DR CTD; 10747; -.
DR RGD; 620214; Masp2.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q9JJS8; -.
DR OrthoDB; 156878at2759; -.
DR PhylomeDB; Q9JJS8; -.
DR BRENDA; 3.4.21.104; 5301.
DR Reactome; R-RNO-166662; Lectin pathway of complement activation.
DR Reactome; R-RNO-166663; Initial triggering of complement.
DR Reactome; R-RNO-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface.
DR SABIO-RK; Q9JJS8; -.
DR EvolutionaryTrace; Q9JJS8; -.
DR PRO; PR:Q9JJS8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1905370; C:serine-type endopeptidase complex; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0001855; F:complement component C4b binding; ISO:RGD.
DR GO; GO:0008233; F:peptidase activity; IDA:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; ISO:RGD.
DR GO; GO:0006956; P:complement activation; NAS:RGD.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0001867; P:complement activation, lectin pathway; ISO:RGD.
DR GO; GO:1903028; P:positive regulation of opsonization; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.60.120.290; -; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR037571; MASP2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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 3D-structure; Alternative splicing; Autocatalytic cleavage; Calcium;
KW Complement pathway; Direct protein sequencing; 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
FT /evidence="ECO:0000269|PubMed:10913141"
FT CHAIN 20..685
FT /note="Mannan-binding lectin serine protease 2"
FT /id="PRO_0000027604"
FT CHAIN 20..443
FT /note="Mannan-binding lectin serine protease 2 A chain"
FT /id="PRO_0000027605"
FT CHAIN 444..685
FT /note="Mannan-binding lectin serine protease 2 B chain"
FT /id="PRO_0000027606"
FT DOMAIN 20..137
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 138..181
FT /note="EGF-like; calcium-binding"
FT DOMAIN 184..296
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 298..363
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 364..431
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 444..683
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 482
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 531
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 632
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT SITE 443..444
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MOD_RES 158
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000269|PubMed:12743029"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12743029"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 72..90
FT /evidence="ECO:0000269|PubMed:12743029"
FT DISULFID 152..165
FT /evidence="ECO:0000269|PubMed:12743029"
FT DISULFID 167..180
FT /evidence="ECO:0000269|PubMed:12743029"
FT DISULFID 184..211
FT /evidence="ECO:0000269|PubMed:12743029"
FT DISULFID 241..259
FT /evidence="ECO:0000269|PubMed:12743029"
FT DISULFID 300..348
FT /evidence="ECO:0000250"
FT DISULFID 328..361
FT /evidence="ECO:0000250"
FT DISULFID 366..411
FT /evidence="ECO:0000250"
FT DISULFID 396..429
FT /evidence="ECO:0000250"
FT DISULFID 433..551
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
FT ProRule:PRU00302"
FT DISULFID 597..617
FT /evidence="ECO:0000250"
FT DISULFID 628..659
FT /evidence="ECO:0000250"
FT VAR_SEQ 182..185
FT /note="ALCS -> EQSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10586086"
FT /id="VSP_014638"
FT VAR_SEQ 186..685
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10586086"
FT /id="VSP_014639"
FT CONFLICT 33
FT /note="L -> P (in Ref. 1; CAB90832)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="G -> A (in Ref. 1; CAB65385/CAB65387/CAB65390)"
FT /evidence="ECO:0000305"
FT CONFLICT 506..507
FT /note="LI -> PH (in Ref. 1; CAB90832)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="R -> A (in Ref. 1; CAB90832)"
FT /evidence="ECO:0000305"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:5CIS"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 55..65
FT /evidence="ECO:0007829|PDB:5CIS"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1NT0"
FT STRAND 109..118
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:5CIS"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:5CKM"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:5CIS"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:5CKN"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:5CKN"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:5CIS"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:5CIS"
SQ SEQUENCE 685 AA; 75667 MW; 0086154934509C64 CRC64;
MRLLIVLGLL WSLVATLLGS KWPEPVFGRL VSLGFPEKYG NHQDRSWTLT APPGFRLRLY
FTHFNLELSY RCEYDFVKLT SGTKVLATLC GQESTDTERA PGNDTFYSLG PSLKVTFHSD
YSNEKPFTGF EAFYAAEDVD ECRTSLGDSV PCDHYCHNYL GGYYCSCRVG YILHQNKHTC
SALCSGQVFT GRSGFLSSPE YPQPYPKLSS CAYNIRLEEG FSITLDFVES FDVEMHPEAQ
CPYDSLKIQT DKREYGPFCG KTLPPRIETD SNKVTITFTT DESGNHTGWK IHYTSTAQPC
PDPTAPPNGH ISPVQATYVL KDSFSVFCKT GFELLQGSVP LKSFTAVCQK DGSWDRPIPE
CSIIDCGPPD DLPNGHVDYI TGPEVTTYKA VIQYSCEETF YTMSSNGKYV CEADGFWTSS
KGEKSLPVCK PVCGLSTHTS GGRIIGGQPA KPGDFPWQVL LLGETTAAGA LIHDDWVLTA
AHAVYGKTEA MSSLDIRMGI LKRLSLIYTQ AWPEAVFIHE GYTHGAGFDN DIALIKLKNK
VTINRNIMPI CLPRKEAASL MKTDFVGTVA GWGLTQKGFL ARNLMFVDIP IVDHQKCATA
YTKQPYPGAK VTVNMLCAGL DRGGKDSCRG DSGGALVFLD NETQRWFVGG IVSWGSINCG
GSEQYGVYTK VTNYIPWIEN IINNF
