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P48740 (MASP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mannan-binding lectin serine protease 1

EC=3.4.21.-
Alternative name(s):
Complement factor MASP-3
Complement-activating component of Ra-reactive factor
Mannose-binding lectin-associated serine protease 1
Short name=MASP-1
Mannose-binding protein-associated serine protease
Ra-reactive factor serine protease p100
Short name=RaRF
Serine protease 5
Gene names
Name:MASP1
Synonyms:CRARF, CRARF1, PRSS5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length699 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5. Ref.5 Ref.24

Enzyme regulation

Inhibited by SERPING1 and A2M. Ref.17 Ref.20

Subunit structure

Homodimer. Interacts with the oligomeric lectins MBL2, FCN2 and FCN3; triggers the lectin pathway of complement through activation of C3. Interacts with SERPING1. Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.26

Subcellular location

Secreted Ref.5.

Tissue specificity

Protein of the plasma which is primarily expressed by liver. Ref.1 Ref.2 Ref.5 Ref.12

Post-translational modification

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains By similarity.

N-glycosylated. Some N-linked glycan are of the complex-type By similarity. Ref.11 Ref.25 Ref.26

Autoproteolytic processing of the proenzyme produces the active enzyme composed on the heavy and the light chain held together by a disulfide bond. Isoform 1 but not isoform 2 is activated through autoproteolytic processing.

Involvement in disease

3MC syndrome 1 (3MC1) [MIM:257920]: A disorder characterized by facial dysmorphism that includes hypertelorism, blepharophimosis, blepharoptosis and highly arched eyebrows, cleft lip and/or palate, craniosynostosis, learning disability and genital, limb and vesicorenal anomalies. The term 3MC syndrome includes Carnevale, Mingarelli, Malpuech, and Michels syndromes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.27

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.

Biophysicochemical properties

Kinetic parameters:

KM=0.10 mM for Ac-Gly-Lys-OMe (at 30 degrees Celsius) Ref.17 Ref.20

KM=310 µM for Bz-Arg-OEt (at 30 degrees Celsius)

KM=4.8 µM for C2 (at 37 degrees Celsius)

Sequence caution

The sequence AAH39724.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processComplement activation lectin 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
Glycoprotein
Hydroxylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcomplement activation

Traceable author statement. Source: Reactome

complement activation, lectin pathway

Inferred from mutant phenotype Ref.24. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

negative regulation of complement activation

Inferred from direct assay Ref.5. Source: UniProtKB

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay Ref.5. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from direct assay Ref.26. Source: UniProtKB

calcium-dependent protein binding

Inferred from physical interaction Ref.19Ref.26. Source: UniProtKB

peptidase activity

Inferred from direct assay Ref.16Ref.20. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.16Ref.18Ref.5. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.26. Source: UniProtKB

serine-type endopeptidase activity

Inferred from direct assay Ref.17. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P48740-1)

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: P48740-2)

Also known as: MASP-3;

The sequence of this isoform differs from the canonical sequence as follows:
     435-435: V → ECGQPSRSLP...QSVVEPQVER
     436-699: Missing.
Note: Glycosylated on Asn-533 and Asn-599.
Isoform 3 (identifier: P48740-3)

The sequence of this isoform differs from the canonical sequence as follows:
     364-380: IVDCRAPGELEHGLITF → KNEIDLESELKSEQVTE
     381-699: Missing.
Isoform 4 (identifier: P48740-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-113: Missing.
     435-435: V → ECGQPSRSLP...QSVVEPQVER
     436-699: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.11
Chain20 – 699680Mannan-binding lectin serine protease 1
PRO_0000027592
Chain20 – 448429Mannan-binding lectin serine protease 1 heavy chain
PRO_0000027593
Chain449 – 699251Mannan-binding lectin serine protease 1 light chain
PRO_0000027594

Regions

Domain20 – 138119CUB 1
Domain139 – 18244EGF-like; calcium-binding
Domain185 – 297113CUB 2
Domain299 – 36466Sushi 1
Domain365 – 43470Sushi 2
Domain449 – 696248Peptidase S1
Region20 – 278259Interaction with FCN2
Region20 – 184165Homodimerization By similarity
Region20 – 184165Interaction with MBL2

Sites

Active site4901Charge relay system By similarity
Active site5521Charge relay system By similarity
Active site6461Charge relay system By similarity
Metal binding681Calcium 1
Metal binding761Calcium 1
Metal binding1211Calcium 1
Metal binding1231Calcium 1; via carbonyl oxygen
Metal binding1391Calcium 2
Metal binding1401Calcium 2; via carbonyl oxygen
Metal binding1421Calcium 2
Metal binding1591Calcium 2
Metal binding1601Calcium 2; via carbonyl oxygen
Metal binding1631Calcium 2; via carbonyl oxygen
Metal binding2351Calcium 3
Metal binding2451Calcium 3
Metal binding2821Calcium 3
Metal binding2841Calcium 3; via carbonyl oxygen
Site448 – 4492Cleavage; by autolysis

Amino acid modifications

Modified residue1591(3R)-3-hydroxyasparagine Potential
Glycosylation491N-linked (GlcNAc...) Ref.22
Glycosylation1781N-linked (GlcNAc...) (complex) Ref.22 Ref.25 Ref.26
Glycosylation3851N-linked (GlcNAc...) (complex) Ref.22 Ref.25
Glycosylation4071N-linked (GlcNAc...) Ref.22
Disulfide bond73 ↔ 91 Ref.26
Disulfide bond143 ↔ 157 Ref.26
Disulfide bond153 ↔ 166 Ref.26
Disulfide bond168 ↔ 181 Ref.26
Disulfide bond185 ↔ 212 Ref.26
Disulfide bond242 ↔ 260 Ref.26
Disulfide bond301 ↔ 349 By similarity
Disulfide bond329 ↔ 362 By similarity
Disulfide bond367 ↔ 414 By similarity
Disulfide bond397 ↔ 432 By similarity
Disulfide bond436 ↔ 572Interchain (between heavy and light chains) Potential
Disulfide bond475 ↔ 491 By similarity
Disulfide bond614 ↔ 631 By similarity
Disulfide bond642 ↔ 672 By similarity

Natural variations

Alternative sequence1 – 113113Missing in isoform 4.
VSP_036809
Alternative sequence364 – 38017IVDCR…GLITF → KNEIDLESELKSEQVTE in isoform 3.
VSP_036810
Alternative sequence381 – 699319Missing in isoform 3.
VSP_036811
Alternative sequence4351V → ECGQPSRSLPSLVKRIIGGR NAEPGLFPWQALIVVEDTSR VPNDKWFGSGALLSASWILT AAHVLRSQRRDTTVIPVSKE HVTVYLGLHDVRDKSGAVNS SAARVVLHPDFNIQNYNHDI ALVQLQEPVPLGPHVMPVCL PRLEPEGPAPHMLGLVAGWG ISNPNVTVDEIISSGTRTLS DVLQYVKLPVVPHAECKTSY ESRSGNYSVTENMFCAGYYE GGKDTCLGDSGGAFVIFDDL SQRWVVQGLVSWGGPEECGS KQVYGVYTKVSNYVDWVWEQ MGLPQSVVEPQVER in isoform 2 and isoform 4.
VSP_036812
Alternative sequence436 – 699264Missing in isoform 2 and isoform 4.
VSP_036813
Natural variant211T → I.
Corresponds to variant rs1062049 [ dbSNP | Ensembl ].
VAR_051831
Natural variant5681V → A.
Corresponds to variant rs13322090 [ dbSNP | Ensembl ].
VAR_051832
Natural variant6791G → R.
Corresponds to variant rs3774266 [ dbSNP | Ensembl ].
VAR_051833
Isoform 2:
Natural variant4971H → Y in 3MC1.
Natural variant6301C → R in 3MC1.
Natural variant6661G → E in 3MC1.

Experimental info

Mutagenesis681E → A or Q: Partial loss of interaction with FCN2, FCN3 and MBL2. Ref.26
Mutagenesis771Y → A: Partial loss of interaction with FCN2, FCN3 and MBL2. Ref.26
Mutagenesis991E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. Ref.26
Mutagenesis1211D → A or N: Loss of interaction with FNC2 and FCN3 and partial loss of interaction with MBL2. Ref.26
Mutagenesis1221F → A: Partial loss of interaction with FCN2, FCN3 and MBL2. Ref.26
Mutagenesis1231S → A: Partial loss of interaction with FCN2, FCN3 and MBL2. Ref.26
Mutagenesis1251E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. Ref.26
Mutagenesis2371H → A: Loss of interaction with FCN2, FCN3 and MBL2. Ref.26
Mutagenesis2391E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. Ref.26
Mutagenesis2441Y → A: Loss of interaction with FCN2, FCN3 and MBL2. Ref.26
Mutagenesis2621E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. Ref.26
Mutagenesis2741S → A: Partial loss of interaction with FCN2 and FCN3. No effect on interaction with MBL2. Ref.26
Mutagenesis2831N → A: Partial loss of interaction with FCN2, FCN3 and MBL2. Ref.26
Mutagenesis2861E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. Ref.26
Mutagenesis6461S → A: No autoproteolytic processing. Ref.21
Sequence conflict21R → K in BAF84375. Ref.6
Sequence conflict891T → A in CAH18409. Ref.7
Sequence conflict2321F → L in BAF84375. Ref.6
Sequence conflict2351E → Q in BAA05928. Ref.2
Sequence conflict2351E → Q in BAA34864. Ref.3
Sequence conflict2851G → A in BAA05928. Ref.2
Sequence conflict2851G → A in BAA34864. Ref.3
Sequence conflict2851G → A in BAA89206. Ref.4
Sequence conflict3921E → G in BAF83846. Ref.6
Sequence conflict4991E → G in BAA05928. Ref.2
Sequence conflict4991E → K in BAA04477. Ref.1
Sequence conflict4991E → K in BAA89206. Ref.4
Sequence conflict5271D → A in BAA34864. Ref.3
Sequence conflict5431Q → K in BAA04477. Ref.1
Sequence conflict5521D → V in BAA34864. Ref.3
Sequence conflict6431A → S in BAA04477. Ref.1

Secondary structure

............................................................................................................................ 699
Helix Strand Turn

Details...

Sequences

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

Last modified December 16, 2008. Version 3.
Checksum: 5B37C7FB9F51FD1D

FASTA69979,247
        10         20         30         40         50         60 
MRWLLLYYAL CFSLSKASAH TVELNNMFGQ IQSPGYPDSY PSDSEVTWNI TVPDGFRIKL 

        70         80         90        100        110        120 
YFMHFNLESS YLCEYDYVKV ETEDQVLATF CGRETTDTEQ TPGQEVVLSP GSFMSITFRS 

       130        140        150        160        170        180 
DFSNEERFTG FDAHYMAVDV DECKEREDEE LSCDHYCHNY IGGYYCSCRF GYILHTDNRT 

       190        200        210        220        230        240 
CRVECSDNLF TQRTGVITSP DFPNPYPKSS ECLYTIELEE GFMVNLQFED IFDIEDHPEV 

       250        260        270        280        290        300 
PCPYDYIKIK VGPKVLGPFC GEKAPEPIST QSHSVLILFH SDNSGENRGW RLSYRAAGNE 

       310        320        330        340        350        360 
CPELQPPVHG KIEPSQAKYF FKDQVLVSCD TGYKVLKDNV EMDTFQIECL KDGTWSNKIP 

       370        380        390        400        410        420 
TCKIVDCRAP GELEHGLITF STRNNLTTYK SEIKYSCQEP YYKMLNNNTG IYTCSAQGVW 

       430        440        450        460        470        480 
MNKVLGRSLP TCLPVCGLPK FSRKLMARIF NGRPAQKGTT PWIAMLSHLN GQPFCGGSLL 

       490        500        510        520        530        540 
GSSWIVTAAH CLHQSLDPED PTLRDSDLLS PSDFKIILGK HWRLRSDENE QHLGVKHTTL 

       550        560        570        580        590        600 
HPQYDPNTFE NDVALVELLE SPVLNAFVMP ICLPEGPQQE GAMVIVSGWG KQFLQRFPET 

       610        620        630        640        650        660 
LMEIEIPIVD HSTCQKAYAP LKKKVTRDMI CAGEKEGGKD ACAGDSGGPM VTLNRERGQW 

       670        680        690 
YLVGTVSWGD DCGKKDRYGV YSYIHHNKDW IQRVTGVRN 

« Hide

Isoform 2 (MASP-3) [UniParc].

Checksum: 09B5297A6C14283A
Show »

FASTA72881,860
Isoform 3 [UniParc].

Checksum: DDED114311A62714
Show »

FASTA38043,640
Isoform 4 [UniParc].

Checksum: EEE63886709340FA
Show »

FASTA61568,918

References

« Hide 'large scale' references
[1]"A new member of the C1s family of complement proteins found in a bactericidal factor, Ra-reactive factor, in human serum."
Takada F., Takayama Y., Hatsuse H., Kawakami M.
Biochem. Biophys. Res. Commun. 196:1003-1009(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Liver.
[2]"Molecular characterization of a novel serine protease involved in activation of the complement system by mannose-binding protein."
Sato T., Endo Y., Matsushita M., Fujita T.
Int. Immunol. 6:665-669(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Fetal liver.
[3]"Exon structure of the gene encoding the human mannose-binding protein-associated serine protease light chain: comparison with complement C1r and C1s genes."
Endo Y., Sato T., Matsushita M., Fujita T.
Int. Immunol. 8:1355-1358(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[4]"Gene structure of the P100 serine-protease component of the human Ra-reactive factor."
Takayama Y., Takada F., Nowatari M., Kawakami M., Matsu-ura N.
Mol. Immunol. 36:505-514(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"MASP-3 and its association with distinct complexes of the mannan-binding lectin complement activation pathway."
Dahl M.R., Thiel S., Matsushita M., Fujita T., Willis A.C., Christensen T., Vorup-Jensen T., Jensenius J.C.
Immunity 15:127-135(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 450-474; 506-526; 539-555; 577-590; 613-621 AND 679-695 (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Liver.
[6]"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] (ISOFORMS 2 AND 4).
Tissue: Placenta, Teratocarcinoma and Trachea.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Fetal brain.
[8]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Fetal brain.
[11]"Interaction properties of human mannan-binding lectin (MBL)-associated serine proteases-1 and -2, MBL-associated protein 19, and MBL."
Thielens N.M., Cseh S., Thiel S., Vorup-Jensen T., Rossi V., Jensenius J.C., Arlaud G.J.
J. Immunol. 166:5068-5077(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-29 AND 449-458, SIGNAL SEQUENCE CLEAVAGE SITE, CLEAVAGE AT ARG-448, GLYCOSYLATION, HOMODIMERIZATION, INTERACTION WITH MBL2.
[12]"Human serum mannose-binding lectin (MBL)-associated serine protease-1 (MASP-1): determination of levels in body fluids and identification of two forms in serum."
Terai I., Kobayashi K., Matsushita M., Fujita T.
Clin. Exp. Immunol. 110:317-323(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[13]"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: INTERACTION WITH MBL2.
Tissue: Liver.
[14]"Complement-activating complex of ficolin and mannose-binding lectin-associated serine protease."
Matsushita M., Endo Y., Fujita T.
J. Immunol. 164:2281-2284(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCN2.
[15]"Interaction of C1q and mannan-binding lectin (MBL) with C1r, C1s, MBL-associated serine proteases 1 and 2, and the MBL-associated protein MAp19."
Thiel S., Petersen S.V., Vorup-Jensen T., Matsushita M., Fujita T., Stover C.M., Schwaeble W.J., Jensenius J.C.
J. Immunol. 165:878-887(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MBL2.
[16]"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: CATALYTIC ACTIVITY, INTERACTION WITH SERPING1.
[17]"Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2."
Rossi V., Cseh S., Bally I., Thielens N.M., Jensenius J.C., Arlaud G.J.
J. Biol. Chem. 276:40880-40887(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[18]"Activation of the lectin complement pathway by H-ficolin (Hakata antigen)."
Matsushita M., Kuraya M., Hamasaki N., Tsujimura M., Shiraki H., Fujita T.
J. Immunol. 168:3502-3506(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCN3.
[19]"Characterization of the interaction between L-ficolin/p35 and mannan-binding lectin-associated serine proteases-1 and -2."
Cseh S., Vera L., Matsushita M., Fujita T., Arlaud G.J., Thielens N.M.
J. Immunol. 169:5735-5743(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCN2.
[20]"Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and -2: a study on recombinant catalytic fragments."
Ambrus G., Gal P., Kojima M., Szilagyi K., Balczer J., Antal J., Graf L., Laich A., Moffatt B.E., Schwaeble W., Sim R.B., Zavodszky P.
J. Immunol. 170:1374-1382(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[21]"Characterization of recombinant mannan-binding lectin-associated serine protease (MASP)-3 suggests an activation mechanism different from that of MASP-1 and MASP-2."
Zundel S., Cseh S., Lacroix M., Dahl M.R., Matsushita M., Andrieu J.-P., Schwaeble W.J., Jensenius J.C., Fujita T., Arlaud G.J., Thielens N.M.
J. Immunol. 172:4342-4350(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION (ISOFORM 2), MUTAGENESIS OF SER-646, AUTOCATALYTIC CLEAVAGE.
[22]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-49; ASN-178; ASN-385; ASN-407 (ISOFORM 1), GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-533 AND ASN-599 (ISOFORM 2).
Tissue: Plasma.
[23]"Mannan-binding lectin-associated serine protease 3 cleaves synthetic peptides and insulin-like growth factor-binding protein 5."
Cortesio C.L., Jiang W.
Arch. Biochem. Biophys. 449:164-170(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY (ISOFORM 2).
[24]"Cooperation between MASP-1 and MASP-2 in the generation of C3 convertase through the MBL pathway."
Moeller-Kristensen M., Thiel S., Sjoeholm A., Matsushita M., Jensenius J.C.
Int. Immunol. 19:141-149(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (ISOFORMS 1 AND 2).
[25]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-178 AND ASN-385.
[26]"Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins."
Teillet F., Gaboriaud C., Lacroix M., Martin L., Arlaud G.J., Thielens N.M.
J. Biol. Chem. 283:25715-25724(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 20-295 IN COMPLEX WITH CALCIUM IONS, HOMODIMERIZATION, GLYCOSYLATION AT ASN-178, DISULFIDE BONDS, CALCIUM-BINDING SITES, INTERACTION WITH FCN2; FCN3 AND MBL2, MUTAGENESIS OF GLU-68; TYR-77; GLU-99; ASP-121; PHE-122; SER-123; GLU-125; HIS-237; GLU-239; TYR-244; GLU-262; SER-274; ASN-283 AND GLU-286.
[27]"Mutations in lectin complement pathway genes COLEC11 and MASP1 cause 3MC syndrome."
Rooryck C., Diaz-Font A., Osborn D.P., Chabchoub E., Hernandez-Hernandez V., Shamseldin H., Kenny J., Waters A., Jenkins D., Kaissi A.A., Leal G.F., Dallapiccola B., Carnevale F., Bitner-Glindzicz M., Lees M., Hennekam R., Stanier P., Burns A.J. expand/collapse author list , Peeters H., Alkuraya F.S., Beales P.L.
Nat. Genet. 43:197-203(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS 3MC1 TYR-497; ARG-630 AND GLU-666 (ISOFORM 2).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D17525 mRNA. Translation: BAA04477.1.
D28593 mRNA. Translation: BAA05928.1.
D61695 Genomic DNA. Translation: BAA34864.1.
AB007617 Genomic DNA. Translation: BAA89206.1.
AF284421 mRNA. Translation: AAK84071.1.
AK291157 mRNA. Translation: BAF83846.1.
AK291686 mRNA. Translation: BAF84375.1.
AK304334 mRNA. Translation: BAG65179.1.
CR749615 mRNA. Translation: CAH18409.1.
AC007920 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78153.1.
BC039724 mRNA. Translation: AAH39724.1. Different initiation.
BC106945 mRNA. Translation: AAI06946.1.
BC106946 mRNA. Translation: AAI06947.1.
CCDSCCDS33907.1. [P48740-1]
CCDS33908.1. [P48740-2]
CCDS33909.1. [P48740-3]
PIRI54763.
RefSeqNP_001027019.1. NM_001031849.2. [P48740-3]
NP_001870.3. NM_001879.5. [P48740-1]
NP_624302.1. NM_139125.3. [P48740-2]
UniGeneHs.89983.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DEMX-ray2.30A/B20-297[»]
3GOVX-ray2.55A298-448[»]
B449-699[»]
4AQBX-ray4.20A20-363[»]
4DJZX-ray3.20A/C298-448[»]
B/D449-699[»]
4IGDX-ray2.50A298-699[»]
4IW4X-ray3.20E/F625-696[»]
4KKDX-ray2.60A/B298-696[»]
ProteinModelPortalP48740.
SMRP48740. Positions 22-699.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111629. 20 interactions.
IntActP48740. 15 interactions.
MINTMINT-4657209.

Protein family/group databases

MEROPSS01.132.

PTM databases

PhosphoSiteP48740.

Polymorphism databases

DMDM218512135.

Proteomic databases

PaxDbP48740.
PRIDEP48740.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000169293; ENSP00000169293; ENSG00000127241. [P48740-3]
ENST00000296280; ENSP00000296280; ENSG00000127241. [P48740-2]
ENST00000337774; ENSP00000336792; ENSG00000127241. [P48740-1]
ENST00000392472; ENSP00000376264; ENSG00000127241. [P48740-4]
GeneID5648.
KEGGhsa:5648.
UCSCuc003frh.2. human. [P48740-1]
uc003fri.3. human. [P48740-2]
uc003frk.2. human. [P48740-3]

Organism-specific databases

CTD5648.
GeneCardsGC03M186935.
HGNCHGNC:6901. MASP1.
HPAHPA001617.
HPA009641.
MIM257920. phenotype.
600521. gene.
neXtProtNX_P48740.
Orphanet2998. Carnevale syndrome.
293843. Craniofacial-ulnar-renal syndrome.
2453. Malpuech syndrome.
2506. Michels syndrome.
PharmGKBPA30644.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOVERGENHBG000559.
KOK03992.
OMAPANICCL.
OrthoDBEOG7W6WK4.
PhylomeDBP48740.
TreeFamTF330373.

Enzyme and pathway databases

ReactomeREACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP48740.
BgeeP48740.
CleanExHS_MASP1.
GenevestigatorP48740.

Family and domain databases

Gene3D2.60.120.290. 2 hits.
InterProIPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
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.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMASP1. human.
EvolutionaryTraceP48740.
GeneWikiMASP1_(protein).
GenomeRNAi5648.
NextBio21938.
PMAP-CutDBQ96RS4.
PROP48740.
SOURCESearch...

Entry information

Entry nameMASP1_HUMAN
AccessionPrimary (citable) accession number: P48740
Secondary accession number(s): A8K542 expand/collapse secondary AC list , A8K6M1, B4E2L7, O95570, Q68D21, Q8IUV8, Q96RS4, Q9UF09
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 16, 2008
Last modified: July 9, 2014
This is version 148 of the entry and version 3 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 3

Human chromosome 3: entries, gene names and cross-references to MIM