Reviewed, UniProtKB/Swiss-Prot O00187 (MASP2_HUMAN)

Names and origin

Protein names

Recommended name:
    Mannan-binding lectin serine protease 2
    EC=3.4.21.104
Alternative name(s):
    Mannose-binding protein-associated serine protease 2
      Short name=MASP-2
    MBL-associated serine protease 2
Cleaved into the following 2 chains:
    1- Recommended name:
            Mannan-binding lectin serine protease 2 A chain
    2- Recommended name:
            Mannan-binding lectin serine protease 2 B chain

Gene names

Name:

MASP2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	686 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.11
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. Ref.12 Ref.13
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. Activated by cleavage after Arg-444. The uncleaved zymogen is inactive towards synthetic substrates, but has sufficient activity to effect autocatalytic cleavage.
Involvement in disease	Genetic variation in MASP2 is the cause of MASP2 deficiency [MIM:605102]. It is associated with susceptibility to infections and with the development of immunologic disease. Ref.15
Miscellaneous	Dimerization and MBL2 binding requires calcium ions.
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.

Ontologies

Keywords
Biological process	Complement pathway Immune response Innate immunity
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	EGF-like domain Repeat Signal Sushi
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Hydroxylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW complement activation, lectin pathway Ref.1 Inferred from direct assay. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from Experiment. Source: Reactome
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-dependent protein binding Inferred from physical interaction. Source: UniProtKB serine-type endopeptidase activity Ref.1 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O00187-1)

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: O00187-2)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 15

15

Potential

Chain

16 – 686

671

Mannan-binding lectin serine protease 2

PRO_0000027598

Chain

16 – 444

429

Mannan-binding lectin serine protease 2 A chain

PRO_0000027599

Chain

445 – 686

242

Mannan-binding lectin serine protease 2 B chain

PRO_0000027600

Regions

Domain

16 – 137

122

CUB 1

Domain

138 – 181

44

EGF-like; calcium-binding

Domain

184 – 296

113

CUB 2

Domain

298 – 363

66

Sushi 1

Domain

364 – 432

69

Sushi 2

Domain

445 – 684

240

Peptidase S1

Sites

Active site

483

1

Charge relay system

Active site

532

1

Charge relay system

Active site

633

1

Charge relay system

Metal binding

67

1

Calcium 1

Metal binding

75

1

Calcium 1

Metal binding

120

1

Calcium 1

Metal binding

122

1

Calcium 1; via carbonyl oxygen

Metal binding

123

1

Calcium 1

Metal binding

138

1

Calcium 2

Metal binding

139

1

Calcium 2; via carbonyl oxygen

Metal binding

141

1

Calcium 2

Metal binding

158

1

Calcium 2

Metal binding

159

1

Calcium 2; via carbonyl oxygen

Metal binding

162

1

Calcium 2; via carbonyl oxygen

Site

444 – 445

2

Cleavage By similarity

Amino acid modifications

Modified residue

158

1

(3R)-3-hydroxyasparagine Potential

Disulfide bond

72 ↔ 90

Ref.12 Ref.13

Disulfide bond

142 ↔ 156

Ref.12 Ref.13

Disulfide bond

152 ↔ 165

Ref.12 Ref.13

Disulfide bond

167 ↔ 180

Ref.12 Ref.13

Disulfide bond

184 ↔ 211

By similarity

Disulfide bond

241 ↔ 259

By similarity

Disulfide bond

300 ↔ 348

By similarity

Disulfide bond

328 ↔ 361

By similarity

Disulfide bond

366 ↔ 412

Ref.12 Ref.13

Disulfide bond

396 ↔ 430

Ref.12 Ref.13

Disulfide bond

434 ↔ 552

Interchain (between A and B chains) Ref.12 Ref.13

Disulfide bond

598 ↔ 618

Ref.12 Ref.13

Disulfide bond

629 ↔ 660

Ref.12 Ref.13

Natural variations

Alternative sequence

182 – 185

4

ALCS → EQSL in isoform 2.

VSP_005383

Alternative sequence

186 – 686

501

Missing in isoform 2.

VSP_005384

Natural variant

99

1

R → Q in Sub-Saharans but not in North Africans or Spaniards.

VAR_025344

Natural variant

118

1

R → C in North Africans but not in Sub-Saharans or Spaniards.

VAR_025345

Natural variant

120

1

D → G in North Africans but not in Sub-Saharans or Spaniards; strongly decreases affinity for MBL2 and FCN2.

VAR_025346

Natural variant

126

1

P → L in Spaniards and North Africans but not in Sub-Saharans.

VAR_025347

Natural variant

155

1

H → R: dbSNP rs2273343.

VAR_028784

Natural variant

371

1

Y → D: dbSNP rs12711521. Ref.1 Ref.2 Ref.3 Ref.8 Ref.10

VAR_028785

Natural variant

377

1

V → A: dbSNP rs2273346. Ref.10

VAR_028786

Natural variant

439

1

R → H: dbSNP rs12085877.

VAR_028787

Experimental info

Mutagenesis

74

1

Y → A: Strongly decreases affinity for MBL2. Decreases affinity for FCN2. Ref.12

Mutagenesis

121

1

Y → A: Strongly decreases affinity for MBL2, but not for FCN2. Ref.12

Mutagenesis

124

1

E → A: Decreases affinity for MBL2. Slight decrease in affinity for FCN2. Ref.12

Mutagenesis

444

1

R → Q: Abolishes autocatalytic cleavage.

Sequence conflict

41

1

N → S in BAF83512. Ref.7

Sequence conflict

225

1

L → P in BAF83512. Ref.7

Sequence conflict

298 – 299

2

HA → QP in BAF83512. Ref.7

Sequence conflict

298 – 299

2

HA → QP in CAI22102. Ref.8

Sequence conflict

361 – 362

2

Missing in CAB50733. Ref.3

Sequence conflict

361 – 362

2

Missing in CAB50735. Ref.3

Sequence conflict

372

1

L → LCS in CAB50733. Ref.3

Sequence conflict

372

1

L → LCS in CAB50735. Ref.3

Sequence conflict

399

1

T → A in BAF83512. Ref.7

Sequence conflict

442

1

G → E in AAG50274. Ref.6

Sequence conflict

447

1

G → E in AAG50274. Ref.6

Sequence conflict

461 – 462

2

Missing in CAB50733. Ref.3

Sequence conflict

461 – 462

2

Missing in CAB50735. Ref.3

Sequence conflict

473

1

L → LIL in CAB50733. Ref.3

Sequence conflict

473

1

L → LIL in CAB50735. Ref.3

Secondary structure

1

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686

Helix Strand Turn

Details...

Beta strand

27 – 31

5

Turn

33 – 36

4

Beta strand

44 – 50

7

Beta strand

55 – 65

11

Beta strand

74 – 89

16

Turn

93 – 96

4

Beta strand

98 – 100

3

Beta strand

109 – 118

10

Beta strand

129 – 138

10

Beta strand

151 – 159

9

Beta strand

162 – 166

5

Beta strand

171 – 173

3

Beta strand

309 – 313

5

Beta strand

323 – 328

6

Beta strand

332 – 336

5

Beta strand

345 – 348

4

Beta strand

350 – 356

7

Beta strand

360 – 362

3

Beta strand

375 – 382

8

Beta strand

391 – 396

6

Turn

398 – 400

3

Beta strand

401 – 405

5

Beta strand

408 – 412

5

Beta strand

418 – 420

3

Beta strand

429 – 432

4

Beta strand

459 – 462

4

Beta strand

464 – 473

10

Turn

474 – 476

3

Beta strand

477 – 480

4

Helix

482 – 489

8

Turn

490 – 492

3

Beta strand

496 – 500

5

Beta strand

509 – 519

11

Beta strand

534 – 540

7

Helix

556 – 561

6

Beta strand

567 – 574

8

Beta strand

586 – 593

8

Helix

595 – 601

7

Beta strand

616 – 619

4

Beta strand

636 – 641

6

Turn

642 – 645

4

Beta strand

646 – 655

10

Beta strand

667 – 671

5

Helix

672 – 675

4

Helix

676 – 685

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 31, 2006. Version 3. Checksum: E6DDD504AE6D8D08	FASTA	686	75,733
	10 20 30 40 50 60 MRLLTLLGLL CGSVATPLGP KWPEPVFGRL ASPGFPGEYA NDQERRWTLT APPGYRLRLY 70 80 90 100 110 120 FTHFDLELSH LCEYDFVKLS SGAKVLATLC GQESTDTERA PGKDTFYSLG SSLDITFRSD 130 140 150 160 170 180 YSNEKPFTGF EAFYAAEDID ECQVAPGEAP TCDHHCHNHL GGFYCSCRAG YVLHRNKRTC 190 200 210 220 230 240 SALCSGQVFT QRSGELSSPE YPRPYPKLSS CTYSISLEEG FSVILDFVES FDVETHPETL 250 260 270 280 290 300 CPYDFLKIQT DREEHGPFCG KTLPHRIETK SNTVTITFVT DESGDHTGWK IHYTSTAHAC 310 320 330 340 350 360 PYPMAPPNGH VSPVQAKYIL KDSFSIFCET GYELLQGHLP LKSFTAVCQK DGSWDRPMPA 370 380 390 400 410 420 CSIVDCGPPD YLPSGRVEYI TGPGVTTYKA VIQYSCEETF YTMKVNDGKY VCEADGFWTS 430 440 450 460 470 480 SKGEKSLPVC EPVCGLSART TGGRIYGGQK AKPGDFPWQV LILGGTTAAG ALLYDNWVLT 490 500 510 520 530 540 AAHAVYEQKH DASALDIRMG TLKRLSPHYT QAWSEAVFIH EGYTHDAGFD NDIALIKLNN 550 560 570 580 590 600 KVVINSNITP ICLPRKEAES FMRTDDIGTA SGWGLTQRGF LARNLMYVDI PIVDHQKCTA 610 620 630 640 650 660 AYEKPPYPRG SVTANMLCAG LESGGKDSCR GDSGGALVFL DSETERWFVG GIVSWGSMNC 670 680 GEAGQYGVYT KVINYIPWIE NIISDF
	Isoform 2 (MAp19) (Small MBL-associated protein) (sMAP). Checksum: 73B133D56FB229C2	FASTA	185	20,629
	10 20 30 40 50 60 MRLLTLLGLL CGSVATPLGP KWPEPVFGRL ASPGFPGEYA NDQERRWTLT APPGYRLRLY 70 80 90 100 110 120 FTHFDLELSH LCEYDFVKLS SGAKVLATLC GQESTDTERA PGKDTFYSLG SSLDITFRSD 130 140 150 160 170 180 YSNEKPFTGF EAFYAAEDID ECQVAPGEAP TCDHHCHNHL GGFYCSCRAG YVLHRNKRTC SEQSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A second serine protease associated with mannan-binding lectin that activates complement." Thiel S., Vorup-Jensen T., Stover C.M., Schwaeble W.J., Laursen S.B., Poulsen K., Willis A.C., Eggleton P., Hansen S., Holmskov U., Reid K.B.M., Jensenius J.C. Nature 386:506-510(1997) [PubMed: 9087411] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-371. 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: 10330290] [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: 10092804] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), ACTIVATION BY PROTEOLYTIC CLEAVAGE, MASS SPECTROMETRY, VARIANT ASP-371. 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), VARIANT ASP-371.
[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].
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-371. 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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-371.
[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: 8618346] [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: 11426320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-284 AND 364-686, VARIANTS ASP-371 AND 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: 10946292] [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: 15117939] [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: 15364579] [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: 16040602] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 287-686, AUTOCATALYTIC CLEAVAGE AT ARG-444, MUTAGENESIS OF ARG-444.
[15]	"Inherited deficiency of mannan-binding lectin-associated serine protease 2." Stengaard-Pedersen K., Thiel S., Gadjeva M., Moller-Kristensen M., Sorensen R., Jensen L.T., Sjoeholm A.G., Fugger L., Jensenius J.C. N. Engl. J. Med. 349:554-560(2003) [PubMed: 12904520] [Abstract] Cited for: VARIANT GLY-120, CHARACTERIZATION OF VARIANT GLY-120, INVOLVEMENT IN MASP2 DEFICIENCY.
[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: 16029433] [Abstract] Cited for: VARIANTS GLN-99; CYS-118; GLY-120 AND LEU-126.
+	Additional computationally mapped references.

Web resources

MASP2base

MASP2 mutation db

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00294713.
IPI00306378.

PIR

A59271.

RefSeq

NP_006601.2.
NP_631947.1.

UniGene

Hs.655645
Hs.709233

3D structure databases

PDBPDBe

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	[»]

SMR

O00187. Positions 24-297.

ModBase

Search...

Protein family/group databases

MEROPS

S01.229.

PTM databases

PhosphoSite

O00187.

Proteomic databases

PRIDE

O00187.

Genome annotation databases

Ensembl

ENSG00000009724. Homo sapiens. [Contig view]

GeneID

10747.

KEGG

hsa:10747.

Organism-specific databases

GeneCards

GC01M011020.

H-InvDB

HIX0028492.

HGNC

HGNC:6902. MASP2.

MIM

605102. gene+phenotype.

PharmGKB

PA30645.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

O00187.

Enzyme and pathway databases

BRENDA

3.4.21.104. 247.

Reactome

REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpress

O00187.

Bgee

O00187.

GermOnline

ENSG00000009724. Homo sapiens.

Family and domain databases

InterPro

IPR016060. Complement_control_module.
IPR000859. CUB.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_CS.
IPR001881. EGF_Ca_bd.
IPR018097. EGF_Ca_bd_CS.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP.
[Graphical view]

Gene3D

G3DSA:2.10.70.10. Complement_control_module. 1 hit.
G3DSA:2.60.120.290. CUB. 2 hits.

Pfam

PF00431. CUB. 2 hits.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00722. CHYMOTRYPSIN.

SMART

SM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]

PROSITE

PS00010. 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]

ProtoNet

Search...

Other Resources

NextBio

40811.

SOURCE

Search...

Entry information

Entry name

MASP2_HUMAN

Accession

Primary (citable) accession number: O00187
Secondary accession number(s): A8K458 , O75754, Q5TEQ5, Q5TER0, Q96QG4, Q9BZH0, Q9H498, Q9H499, Q9UBP3, Q9UC48, Q9ULC7, Q9UMV3, Q9Y270

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	October 31, 2006
Last modified:	June 16, 2009
This is version 112 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)