O00187 (MASP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Mannan-binding lectin serine protease 2 A chain
2. Mannan-binding lectin serine protease 2 B chain

Gene names

Name:

MASP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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. Dimerization and MBL2 binding requires calcium ions. 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. Ref.3 Ref.14
Involvement in disease	MASP2 deficiency (MASPD) [MIM:613791]: A disorder that results in autoimmune manifestations, recurrent severe infections, and chronic inflammatory disease. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.17
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 Immunity Innate immunity
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	EGF-like domain Repeat Signal Sushi
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine protease
PTM	Autocatalytic cleavage Disulfide bond Hydroxylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW complement activation, lectin pathway Inferred from direct assay PubMed 17182967Ref.1. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Traceable author statement. Source: Reactome
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activity Inferred from direct assay Ref.1. 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. Ref.16 Ref.17

VAR_025344

Natural variant

118

1

R → C. Ref.16 Ref.17

VAR_025345

Natural variant

120

1

D → G in MASPD; found in a patient suffering from frequent infections and chronic inflammatory disease; strongly decreases affinity for MBL2 and FCN2. Ref.12 Ref.15 Ref.16 Ref.17

VAR_025346

Natural variant

126

1

P → L in MASPD. Ref.16 Ref.17
Corresponds to variant rs56392418 [ dbSNP | Ensembl ].

VAR_025347

Natural variant

155

1

H → R.
Corresponds to variant rs2273343 [ dbSNP | Ensembl ].

VAR_028784

Natural variant

156

1

C → CHNH in MASPD.

VAR_065814

Natural variant

371

1

D → Y. Ref.5
Corresponds to variant rs12711521 [ dbSNP | Ensembl ].

VAR_028785

Natural variant

377

1

V → A Associated with reduced MASP2 levels in plasma. Ref.10 Ref.17
Corresponds to variant rs2273346 [ dbSNP | Ensembl ].

VAR_028786

Natural variant

439

1

R → H.
Corresponds to variant rs12085877 [ dbSNP | Ensembl ].

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. Ref.14

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

QP → HA in CAA71059. Ref.1

Sequence conflict

298 – 299

2

QP → HA in CAB50733. Ref.3

Sequence conflict

298 – 299

2

QP → HA in CAB50735. Ref.3

Sequence conflict

298 – 299

2

QP → HA in CAA67050. Ref.4

Sequence conflict

298 – 299

2

QP → HA in AAG50274. Ref.6

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 – 363

4

Beta strand

375 – 382

8

Beta strand

391 – 396

6

Turn

398 – 400

3

Beta strand

401 – 406

6

Beta strand

408 – 412

5

Beta strand

418 – 420

3

Beta strand

429 – 432

4

Beta strand

459 – 465

7

Beta strand

468 – 473

6

Turn

474 – 476

3

Beta strand

477 – 480

4

Helix

482 – 485

4

Helix

486 – 488

3

Turn

490 – 492

3

Beta strand

495 – 500

6

Beta strand

510 – 519

10

Beta strand

534 – 540

7

Helix

556 – 561

6

Beta strand

567 – 573

7

Beta strand

577 – 579

3

Beta strand

586 – 593

8

Helix

595 – 601

7

Beta strand

604 – 606

3

Beta strand

616 – 619

4

Beta strand

636 – 641

6

Turn

642 – 645

4

Beta strand

646 – 656

11

Beta strand

667 – 671

5

Helix

672 – 675

4

Helix

676 – 683

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 11, 2011. Version 4. Checksum: ED952085FA115E21	FASTA	686	75,702
	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 IHYTSTAQPC 310 320 330 340 350 360 PYPMAPPNGH VSPVQAKYIL KDSFSIFCET GYELLQGHLP LKSFTAVCQK DGSWDRPMPA 370 380 390 400 410 420 CSIVDCGPPD DLPSGRVEYI 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) [UniParc]. 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] [Europe PMC] [Abstract] 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, 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]	"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] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

MASP2base

MASP2 mutation db

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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. NM_006610.3.
NP_631947.1. NM_139208.2.

UniGene

Hs.655645.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O00187.

SMR

O00187. Positions 17-686.

ModBase

Search...

Protein family/group databases

MEROPS

S01.229.

PTM databases

PhosphoSite

O00187.

Proteomic databases

PaxDb

O00187.

PRIDE

O00187.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000400897; ENSP00000383690; ENSG00000009724.
ENST00000400898; ENSP00000383691; ENSG00000009724.

GeneID

10747.

KEGG

hsa:10747.

UCSC

uc001aru.3. human.
uc001arv.3. human.

Organism-specific databases

CTD

10747.

GeneCards

GC01M011086.

HGNC

HGNC:6902. MASP2.

HPA

HPA029313.
HPA029314.

MIM

605102. gene.
613791. phenotype.

neXtProt

NX_O00187.

PharmGKB

PA30645.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5640.

HOVERGEN

HBG000559.

InParanoid

O00187.

KO

K03993.

OMA

RLYFTHF.

OrthoDB

EOG4ZKJKQ.

PhylomeDB

O00187.

Enzyme and pathway databases

BRENDA

3.4.21.104. 2681.

Reactome

REACT_6900. Immune System.

Gene expression databases

Bgee

O00187.

Genevestigator

O00187.

GermOnline

ENSG00000009724. Homo sapiens.

Family and domain databases

Gene3D

2.60.120.290. 2 hits.

InterPro

IPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd.
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]

Pfam

PF00431. CUB. 2 hits.
PF07645. EGF_CA. 1 hit.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]

PIRSF

PIRSF001155. C1r_C1s_MASP. 1 hit.

PRINTS

PR00722. CHYMOTRYPSIN.

SMART

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

SUPFAM

SSF57535. Complement_control_module. 2 hits.
SSF49854. CUB. 2 hits.
SSF50494. Pept_Ser_Cys. 1 hit.

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

EvolutionaryTrace

O00187.

GenomeRNAi

10747.

NextBio

40811.

SOURCE

Search...

Entry information

Entry name

MASP2_HUMAN

Accession

Primary (citable) accession number: O00187
Secondary accession number(s): A8K458 , A8MWJ2, 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:	January 11, 2011
Last modified:	May 1, 2013
This is version 150 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.