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O00187 (MASP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:MASP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length686 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processComplement pathway
Immunity
Innate immunity
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainEGF-like domain
Repeat
Signal
Sushi
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMAutocatalytic cleavage
Disulfide bond
Hydroxylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcomplement activation

Traceable author statement. Source: Reactome

complement activation, classical pathway

Inferred from electronic annotation. Source: UniProtKB-KW

complement activation, lectin pathway

Inferred from direct assay PubMed 17182967Ref.1. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent protein binding

Inferred from physical interaction PubMed 12421953. Source: UniProtKB

complement component C4b binding

Inferred from direct assay PubMed 22949645. Source: BHF-UCL

peptidase activity

Inferred from direct assay Ref.11PubMed 12538697. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11PubMed 11907111. Source: UniProtKB

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Potential
Chain16 – 686671Mannan-binding lectin serine protease 2
PRO_0000027598
Chain16 – 444429Mannan-binding lectin serine protease 2 A chain
PRO_0000027599
Chain445 – 686242Mannan-binding lectin serine protease 2 B chain
PRO_0000027600

Regions

Domain16 – 137122CUB 1
Domain138 – 18144EGF-like; calcium-binding
Domain184 – 296113CUB 2
Domain298 – 36366Sushi 1
Domain364 – 43269Sushi 2
Domain445 – 684240Peptidase S1

Sites

Active site4831Charge relay system
Active site5321Charge relay system
Active site6331Charge relay system
Metal binding671Calcium 1
Metal binding751Calcium 1
Metal binding1201Calcium 1
Metal binding1221Calcium 1; via carbonyl oxygen
Metal binding1231Calcium 1
Metal binding1381Calcium 2
Metal binding1391Calcium 2; via carbonyl oxygen
Metal binding1411Calcium 2
Metal binding1581Calcium 2
Metal binding1591Calcium 2; via carbonyl oxygen
Metal binding1621Calcium 2; via carbonyl oxygen
Site444 – 4452Cleavage By similarity

Amino acid modifications

Modified residue1581(3R)-3-hydroxyasparagine Potential
Disulfide bond72 ↔ 90 Ref.12 Ref.13
Disulfide bond142 ↔ 156 Ref.12 Ref.13
Disulfide bond152 ↔ 165 Ref.12 Ref.13
Disulfide bond167 ↔ 180 Ref.12 Ref.13
Disulfide bond184 ↔ 211 By similarity
Disulfide bond241 ↔ 259 By similarity
Disulfide bond300 ↔ 348 By similarity
Disulfide bond328 ↔ 361 By similarity
Disulfide bond366 ↔ 412 Ref.12 Ref.13
Disulfide bond396 ↔ 430 Ref.12 Ref.13
Disulfide bond434 ↔ 552Interchain (between A and B chains) Ref.12 Ref.13
Disulfide bond598 ↔ 618 Ref.12 Ref.13
Disulfide bond629 ↔ 660 Ref.12 Ref.13

Natural variations

Alternative sequence182 – 1854ALCS → EQSL in isoform 2.
VSP_005383
Alternative sequence186 – 686501Missing in isoform 2.
VSP_005384
Natural variant991R → Q. Ref.16 Ref.17
Corresponds to variant rs61735600 [ dbSNP | Ensembl ].
VAR_025344
Natural variant1181R → C. Ref.16 Ref.17
Corresponds to variant rs147270785 [ dbSNP | Ensembl ].
VAR_025345
Natural variant1201D → 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
Corresponds to variant rs72550870 [ dbSNP | Ensembl ].
VAR_025346
Natural variant1261P → L in MASPD. Ref.16 Ref.17
Corresponds to variant rs56392418 [ dbSNP | Ensembl ].
VAR_025347
Natural variant1551H → R.
Corresponds to variant rs2273343 [ dbSNP | Ensembl ].
VAR_028784
Natural variant1561C → CHNH in MASPD.
VAR_065814
Natural variant3711D → Y. Ref.5
Corresponds to variant rs12711521 [ dbSNP | Ensembl ].
VAR_028785
Natural variant3771V → A Associated with reduced MASP2 levels in plasma. Ref.10 Ref.17
Corresponds to variant rs2273346 [ dbSNP | Ensembl ].
VAR_028786
Natural variant4391R → H.
Corresponds to variant rs12085877 [ dbSNP | Ensembl ].
VAR_028787

Experimental info

Mutagenesis741Y → A: Strongly decreases affinity for MBL2. Decreases affinity for FCN2. Ref.12
Mutagenesis1211Y → A: Strongly decreases affinity for MBL2, but not for FCN2. Ref.12
Mutagenesis1241E → A: Decreases affinity for MBL2. Slight decrease in affinity for FCN2. Ref.12
Mutagenesis4441R → Q: Abolishes autocatalytic cleavage. Ref.14
Sequence conflict411N → S in BAF83512. Ref.7
Sequence conflict2251L → P in BAF83512. Ref.7
Sequence conflict298 – 2992QP → HA in CAA71059. Ref.1
Sequence conflict298 – 2992QP → HA in CAB50733. Ref.3
Sequence conflict298 – 2992QP → HA in CAB50735. Ref.3
Sequence conflict298 – 2992QP → HA in CAA67050. Ref.4
Sequence conflict298 – 2992QP → HA in AAG50274. Ref.6
Sequence conflict361 – 3622Missing in CAB50733. Ref.3
Sequence conflict361 – 3622Missing in CAB50735. Ref.3
Sequence conflict3721L → LCS in CAB50733. Ref.3
Sequence conflict3721L → LCS in CAB50735. Ref.3
Sequence conflict3991T → A in BAF83512. Ref.7
Sequence conflict4421G → E in AAG50274. Ref.6
Sequence conflict4471G → E in AAG50274. Ref.6
Sequence conflict461 – 4622Missing in CAB50733. Ref.3
Sequence conflict461 – 4622Missing in CAB50735. Ref.3
Sequence conflict4731L → LIL in CAB50733. Ref.3
Sequence conflict4731L → LIL in CAB50735. Ref.3

Secondary structure

..................................................................................... 686
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 4.
Checksum: ED952085FA115E21

FASTA68675,702
        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 

« Hide

Isoform 2 (MAp19) (Small MBL-associated protein) (sMAP) [UniParc].

Checksum: 73B133D56FB229C2
Show »

FASTA18520,629

References

« Hide '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, IDENTIFICATION BY 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. expand/collapse author list , 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. expand/collapse author list , 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 expand/collapse EMBL AC list , 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.
CCDSCCDS123.1. [O00187-1]
CCDS124.1. [O00187-2]
PIRA59271.
RefSeqNP_006601.2. NM_006610.3. [O00187-1]
NP_631947.1. NM_139208.2. [O00187-2]
UniGeneHs.655645.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q3XX-ray2.23A/B363-686[»]
1SZBX-ray2.50A/B16-181[»]
1ZJKX-ray2.18A287-686[»]
3TVJX-ray1.28A363-444[»]
B445-686[»]
4FXGX-ray3.75G/I291-444[»]
H/J445-686[»]
ProteinModelPortalO00187.
SMRO00187. Positions 17-686.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115970. 5 interactions.
IntActO00187. 1 interaction.
MINTMINT-7970114.

Protein family/group databases

MEROPSS01.229.

PTM databases

PhosphoSiteO00187.

Proteomic databases

PaxDbO00187.
PRIDEO00187.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000400897; ENSP00000383690; ENSG00000009724. [O00187-1]
ENST00000400898; ENSP00000383691; ENSG00000009724. [O00187-2]
GeneID10747.
KEGGhsa:10747.
UCSCuc001aru.3. human. [O00187-1]
uc001arv.3. human. [O00187-2]

Organism-specific databases

CTD10747.
GeneCardsGC01M011086.
HGNCHGNC:6902. MASP2.
HPAHPA029313.
HPA029314.
MIM605102. gene.
613791. phenotype.
neXtProtNX_O00187.
Orphanet331187. Immunodeficiency due to MASP-2 deficiency.
PharmGKBPA30645.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOVERGENHBG000559.
InParanoidO00187.
KOK03993.
OMAWTLTAPP.
OrthoDBEOG7W6WK4.
PhylomeDBO00187.
TreeFamTF330373.

Enzyme and pathway databases

BRENDA3.4.21.104. 2681.
ReactomeREACT_6900. Immune System.

Gene expression databases

BgeeO00187.
GenevestigatorO00187.

Family and domain databases

Gene3D2.60.120.290. 2 hits.
InterProIPR000859. 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]
PfamPF00431. CUB. 2 hits.
PF07645. EGF_CA. 1 hit.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001155. C1r_C1s_MASP. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

EvolutionaryTraceO00187.
GenomeRNAi10747.
NextBio40811.
PROO00187.
SOURCESearch...

Entry information

Entry nameMASP2_HUMAN
AccessionPrimary (citable) accession number: O00187
Secondary accession number(s): A8K458 expand/collapse secondary AC list , 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: July 9, 2014
This is version 163 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM