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Protein

Mannan-binding lectin serine protease 1

Gene

MASP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 IGFBP5.1 Publication

Enzyme regulationi

Inhibited by SERPING1 and A2M.2 Publications

Kineticsi

  1. KM=0.10 mM for Ac-Gly-Lys-OMe (at 30 degrees Celsius)2 Publications
  2. KM=310 µM for Bz-Arg-OEt (at 30 degrees Celsius)2 Publications
  3. KM=4.8 µM for C2 (at 37 degrees Celsius)2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi68 – 681Calcium 1
    Metal bindingi76 – 761Calcium 1
    Metal bindingi121 – 1211Calcium 1
    Metal bindingi123 – 1231Calcium 1; via carbonyl oxygen
    Metal bindingi139 – 1391Calcium 2
    Metal bindingi140 – 1401Calcium 2; via carbonyl oxygen
    Metal bindingi142 – 1421Calcium 2
    Metal bindingi159 – 1591Calcium 2
    Metal bindingi160 – 1601Calcium 2; via carbonyl oxygen
    Metal bindingi163 – 1631Calcium 2; via carbonyl oxygen
    Metal bindingi235 – 2351Calcium 3
    Metal bindingi245 – 2451Calcium 3
    Metal bindingi282 – 2821Calcium 3
    Metal bindingi284 – 2841Calcium 3; via carbonyl oxygen
    Sitei448 – 4492Cleavage; by autolysis
    Active sitei490 – 4901Charge relay systemBy similarity
    Active sitei552 – 5521Charge relay systemBy similarity
    Active sitei646 – 6461Charge relay systemBy similarity

    GO - Molecular functioni

    • calcium-dependent protein binding Source: UniProtKB
    • calcium ion binding Source: UniProtKB
    • peptidase activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    • serine-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    • complement activation Source: Reactome
    • complement activation, lectin pathway Source: UniProtKB
    • innate immune response Source: Reactome
    • negative regulation of complement activation Source: UniProtKB
    • receptor-mediated endocytosis Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Complement activation lectin pathway, Immunity, Innate immunity

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.4.21.B7. 2681.
    ReactomeiREACT_163699. Scavenging by Class A Receptors.
    REACT_163810. Ficolins bind to repetitive carbohydrate structures on the target cell surface.
    REACT_7964. Lectin pathway of complement activation.
    REACT_8024. Initial triggering of complement.
    SABIO-RKP48740.

    Protein family/group databases

    MEROPSiS01.198.

    Names & Taxonomyi

    Protein namesi
    Recommended 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
    Cleaved into the following 2 chains:
    Gene namesi
    Name:MASP1
    Synonyms:CRARF, CRARF1, PRSS5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:6901. MASP1.

    Subcellular locationi

    GO - Cellular componenti

    • extracellular region Source: Reactome
    • extracellular space Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    3MC syndrome 1 (3MC1)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA 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.

    See also OMIM:257920
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 2 (identifier: P48740-2)
    Natural varianti497 – 4971H → Y in 3MC1. 1 Publication
    Natural varianti630 – 6301C → R in 3MC1. 1 Publication
    Natural varianti666 – 6661G → E in 3MC1. 1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi68 – 681E → A or Q: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
    Mutagenesisi77 – 771Y → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
    Mutagenesisi99 – 991E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
    Mutagenesisi121 – 1211D → A or N: Loss of interaction with FNC2 and FCN3 and partial loss of interaction with MBL2. 1 Publication
    Mutagenesisi122 – 1221F → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
    Mutagenesisi123 – 1231S → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
    Mutagenesisi125 – 1251E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
    Mutagenesisi237 – 2371H → A: Loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
    Mutagenesisi239 – 2391E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
    Mutagenesisi244 – 2441Y → A: Loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
    Mutagenesisi262 – 2621E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
    Mutagenesisi274 – 2741S → A: Partial loss of interaction with FCN2 and FCN3. No effect on interaction with MBL2. 1 Publication
    Mutagenesisi283 – 2831N → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
    Mutagenesisi286 – 2861E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication
    Mutagenesisi646 – 6461S → A: No autoproteolytic processing. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi257920. phenotype.
    Orphaneti293843. Craniofacial-ulnar-renal syndrome.
    PharmGKBiPA30644.

    Polymorphism and mutation databases

    BioMutaiMASP1.
    DMDMi218512135.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 699680Mannan-binding lectin serine protease 1PRO_0000027592Add
    BLAST
    Chaini20 – 448429Mannan-binding lectin serine protease 1 heavy chainPRO_0000027593Add
    BLAST
    Chaini449 – 699251Mannan-binding lectin serine protease 1 light chainPRO_0000027594Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi49 – 491N-linked (GlcNAc...)1 Publication
    Disulfide bondi73 ↔ 911 Publication
    Disulfide bondi143 ↔ 1571 Publication
    Disulfide bondi153 ↔ 1661 Publication
    Modified residuei159 – 1591(3R)-3-hydroxyasparagineSequence Analysis
    Disulfide bondi168 ↔ 1811 Publication
    Glycosylationi178 – 1781N-linked (GlcNAc...) (complex)2 Publications
    Disulfide bondi185 ↔ 2121 Publication
    Disulfide bondi242 ↔ 2601 Publication
    Disulfide bondi301 ↔ 349By similarity
    Disulfide bondi329 ↔ 362By similarity
    Disulfide bondi367 ↔ 414By similarity
    Glycosylationi385 – 3851N-linked (GlcNAc...) (complex)1 Publication
    Disulfide bondi397 ↔ 432By similarity
    Glycosylationi407 – 4071N-linked (GlcNAc...)1 Publication
    Disulfide bondi436 ↔ 572Interchain (between heavy and light chains)PROSITE-ProRule annotation
    Disulfide bondi475 ↔ 491By similarity
    Disulfide bondi614 ↔ 631By similarity
    Disulfide bondi642 ↔ 672By similarity

    Post-translational modificationi

    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).By similarity
    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.1 Publication

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    PaxDbiP48740.
    PRIDEiP48740.

    PTM databases

    PhosphoSiteiP48740.

    Miscellaneous databases

    PMAP-CutDBQ96RS4.

    Expressioni

    Tissue specificityi

    Protein of the plasma which is primarily expressed by liver.4 Publications

    Gene expression databases

    BgeeiP48740.
    CleanExiHS_MASP1.
    ExpressionAtlasiP48740. baseline and differential.
    GenevisibleiP48740. HS.

    Organism-specific databases

    HPAiHPA001617.
    HPA009641.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with the oligomeric lectins MBL2, FCN2 and FCN3; triggers the lectin pathway of complement through activation of C3. Interacts with SERPING1.8 Publications

    Protein-protein interaction databases

    BioGridi111629. 17 interactions.
    IntActiP48740. 15 interactions.
    MINTiMINT-4657209.

    Structurei

    Secondary structure

    1
    699
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 325Combined sources
    Turni34 – 374Combined sources
    Beta strandi42 – 5110Combined sources
    Beta strandi56 – 6611Combined sources
    Helixi71 – 733Combined sources
    Beta strandi75 – 817Combined sources
    Beta strandi86 – 905Combined sources
    Beta strandi92 – 998Combined sources
    Beta strandi110 – 12011Combined sources
    Beta strandi130 – 13910Combined sources
    Turni142 – 1443Combined sources
    Beta strandi154 – 1607Combined sources
    Beta strandi163 – 1675Combined sources
    Beta strandi192 – 1998Combined sources
    Turni200 – 2034Combined sources
    Beta strandi211 – 2177Combined sources
    Beta strandi223 – 2286Combined sources
    Beta strandi238 – 2447Combined sources
    Beta strandi246 – 2516Combined sources
    Beta strandi254 – 2596Combined sources
    Beta strandi261 – 2633Combined sources
    Beta strandi273 – 2808Combined sources
    Beta strandi291 – 2977Combined sources
    Beta strandi310 – 3145Combined sources
    Beta strandi317 – 3204Combined sources
    Beta strandi324 – 3296Combined sources
    Beta strandi333 – 3375Combined sources
    Beta strandi340 – 34910Combined sources
    Beta strandi355 – 3573Combined sources
    Beta strandi361 – 3644Combined sources
    Beta strandi376 – 3827Combined sources
    Beta strandi392 – 3976Combined sources
    Turni399 – 4013Combined sources
    Beta strandi402 – 4043Combined sources
    Helixi405 – 4073Combined sources
    Beta strandi411 – 4144Combined sources
    Turni416 – 4183Combined sources
    Beta strandi420 – 4223Combined sources
    Turni423 – 4253Combined sources
    Beta strandi426 – 4283Combined sources
    Beta strandi432 – 4343Combined sources
    Beta strandi463 – 4686Combined sources
    Beta strandi473 – 4808Combined sources
    Turni481 – 4833Combined sources
    Beta strandi484 – 4874Combined sources
    Helixi489 – 4913Combined sources
    Beta strandi499 – 5013Combined sources
    Turni505 – 5073Combined sources
    Turni511 – 5133Combined sources
    Beta strandi514 – 5196Combined sources
    Beta strandi522 – 5254Combined sources
    Beta strandi531 – 54010Combined sources
    Turni546 – 5494Combined sources
    Beta strandi554 – 5607Combined sources
    Beta strandi565 – 5673Combined sources
    Beta strandi583 – 5919Combined sources
    Beta strandi594 – 5963Combined sources
    Beta strandi602 – 6098Combined sources
    Helixi611 – 6188Combined sources
    Helixi619 – 6213Combined sources
    Beta strandi629 – 6324Combined sources
    Beta strandi649 – 6546Combined sources
    Turni655 – 6584Combined sources
    Beta strandi659 – 6668Combined sources
    Helixi672 – 6754Combined sources
    Beta strandi677 – 6837Combined sources
    Helixi684 – 6874Combined sources
    Helixi688 – 6958Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliP48740.
    SMRiP48740. Positions 22-699.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP48740.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 138119CUB 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini139 – 18244EGF-like; calcium-bindingAdd
    BLAST
    Domaini185 – 297113CUB 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini299 – 36466Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini365 – 43470Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini449 – 696248Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni20 – 278259Interaction with FCN2Add
    BLAST
    Regioni20 – 184165HomodimerizationBy similarityAdd
    BLAST
    Regioni20 – 184165Interaction with MBL2Add
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 2 CUB domains.PROSITE-ProRule annotation
    Contains 1 EGF-like domain.Curated
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
    Contains 2 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Sushi

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00760000118890.
    HOVERGENiHBG000559.
    InParanoidiP48740.
    KOiK03992.
    OMAiVWEQMGS.
    OrthoDBiEOG7W6WK4.
    PhylomeDBiP48740.
    TreeFamiTF330373.

    Family and domain databases

    Gene3Di2.60.120.290. 2 hits.
    InterProiIPR000859. 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_dom.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00431. CUB. 2 hits.
    PF07645. EGF_CA. 1 hit.
    PF00084. Sushi. 2 hits.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001155. C1r_C1s_MASP. 1 hit.
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00032. CCP. 2 hits.
    SM00042. CUB. 2 hits.
    SM00179. EGF_CA. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49854. SSF49854. 2 hits.
    SSF50494. SSF50494. 1 hit.
    SSF57535. SSF57535. 2 hits.
    PROSITEiPS00010. 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]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P48740-1) [UniParc]FASTAAdd to basket

    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.

    « Hide

            10         20         30         40         50
    MRWLLLYYAL CFSLSKASAH TVELNNMFGQ IQSPGYPDSY PSDSEVTWNI
    60 70 80 90 100
    TVPDGFRIKL YFMHFNLESS YLCEYDYVKV ETEDQVLATF CGRETTDTEQ
    110 120 130 140 150
    TPGQEVVLSP GSFMSITFRS DFSNEERFTG FDAHYMAVDV DECKEREDEE
    160 170 180 190 200
    LSCDHYCHNY IGGYYCSCRF GYILHTDNRT CRVECSDNLF TQRTGVITSP
    210 220 230 240 250
    DFPNPYPKSS ECLYTIELEE GFMVNLQFED IFDIEDHPEV PCPYDYIKIK
    260 270 280 290 300
    VGPKVLGPFC GEKAPEPIST QSHSVLILFH SDNSGENRGW RLSYRAAGNE
    310 320 330 340 350
    CPELQPPVHG KIEPSQAKYF FKDQVLVSCD TGYKVLKDNV EMDTFQIECL
    360 370 380 390 400
    KDGTWSNKIP TCKIVDCRAP GELEHGLITF STRNNLTTYK SEIKYSCQEP
    410 420 430 440 450
    YYKMLNNNTG IYTCSAQGVW MNKVLGRSLP TCLPVCGLPK FSRKLMARIF
    460 470 480 490 500
    NGRPAQKGTT PWIAMLSHLN GQPFCGGSLL GSSWIVTAAH CLHQSLDPED
    510 520 530 540 550
    PTLRDSDLLS PSDFKIILGK HWRLRSDENE QHLGVKHTTL HPQYDPNTFE
    560 570 580 590 600
    NDVALVELLE SPVLNAFVMP ICLPEGPQQE GAMVIVSGWG KQFLQRFPET
    610 620 630 640 650
    LMEIEIPIVD HSTCQKAYAP LKKKVTRDMI CAGEKEGGKD ACAGDSGGPM
    660 670 680 690
    VTLNRERGQW YLVGTVSWGD DCGKKDRYGV YSYIHHNKDW IQRVTGVRN
    Length:699
    Mass (Da):79,247
    Last modified:December 16, 2008 - v3
    Checksum:i5B37C7FB9F51FD1D
    GO
    Isoform 2 (identifier: P48740-2) [UniParc]FASTAAdd to basket

    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-599.1 Publication
    Show »
    Length:728
    Mass (Da):81,860
    Checksum:i09B5297A6C14283A
    GO
    Isoform 3 (identifier: P48740-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         364-380: IVDCRAPGELEHGLITF → KNEIDLESELKSEQVTE
         381-699: Missing.

    Show »
    Length:380
    Mass (Da):43,640
    Checksum:iDDED114311A62714
    GO
    Isoform 4 (identifier: P48740-4) [UniParc]FASTAAdd to basket

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

    Show »
    Length:615
    Mass (Da):68,918
    Checksum:iEEE63886709340FA
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21R → K in BAF84375 (PubMed:14702039).Curated
    Sequence conflicti89 – 891T → A in CAH18409 (PubMed:17974005).Curated
    Sequence conflicti232 – 2321F → L in BAF84375 (PubMed:14702039).Curated
    Sequence conflicti235 – 2351E → Q in BAA05928 (PubMed:8018603).Curated
    Sequence conflicti235 – 2351E → Q in BAA34864 (PubMed:8921412).Curated
    Sequence conflicti285 – 2851G → A in BAA05928 (PubMed:8018603).Curated
    Sequence conflicti285 – 2851G → A in BAA34864 (PubMed:8921412).Curated
    Sequence conflicti285 – 2851G → A in BAA89206 (PubMed:10475605).Curated
    Sequence conflicti392 – 3921E → G in BAF83846 (PubMed:14702039).Curated
    Sequence conflicti499 – 4991E → G in BAA05928 (PubMed:8018603).Curated
    Sequence conflicti499 – 4991E → K in BAA04477 (PubMed:8240317).Curated
    Sequence conflicti499 – 4991E → K in BAA89206 (PubMed:10475605).Curated
    Sequence conflicti527 – 5271D → A in BAA34864 (PubMed:8921412).Curated
    Sequence conflicti543 – 5431Q → K in BAA04477 (PubMed:8240317).Curated
    Sequence conflicti552 – 5521D → V in BAA34864 (PubMed:8921412).Curated
    Sequence conflicti643 – 6431A → S in BAA04477 (PubMed:8240317).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti21 – 211T → I.
    Corresponds to variant rs1062049 [ dbSNP | Ensembl ].
    VAR_051831
    Natural varianti568 – 5681V → A.
    Corresponds to variant rs13322090 [ dbSNP | Ensembl ].
    VAR_051832
    Natural varianti679 – 6791G → R.
    Corresponds to variant rs3774266 [ dbSNP | Ensembl ].
    VAR_051833
    Isoform 2 (identifier: P48740-2)
    Natural varianti497 – 4971H → Y in 3MC1. 1 Publication
    Natural varianti630 – 6301C → R in 3MC1. 1 Publication
    Natural varianti666 – 6661G → E in 3MC1. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 113113Missing in isoform 4. 1 PublicationVSP_036809Add
    BLAST
    Alternative sequencei364 – 38017IVDCR…GLITF → KNEIDLESELKSEQVTE in isoform 3. 2 PublicationsVSP_036810Add
    BLAST
    Alternative sequencei381 – 699319Missing in isoform 3. 2 PublicationsVSP_036811Add
    BLAST
    Alternative sequencei435 – 4351V → ECGQPSRSLPSLVKRIIGGR NAEPGLFPWQALIVVEDTSR VPNDKWFGSGALLSASWILT AAHVLRSQRRDTTVIPVSKE HVTVYLGLHDVRDKSGAVNS SAARVVLHPDFNIQNYNHDI ALVQLQEPVPLGPHVMPVCL PRLEPEGPAPHMLGLVAGWG ISNPNVTVDEIISSGTRTLS DVLQYVKLPVVPHAECKTSY ESRSGNYSVTENMFCAGYYE GGKDTCLGDSGGAFVIFDDL SQRWVVQGLVSWGGPEECGS KQVYGVYTKVSNYVDWVWEQ MGLPQSVVEPQVER in isoform 2 and isoform 4. 3 PublicationsVSP_036812
    Alternative sequencei436 – 699264Missing in isoform 2 and isoform 4. 3 PublicationsVSP_036813Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS33907.1. [P48740-1]
    CCDS33908.1. [P48740-2]
    CCDS33909.1. [P48740-3]
    PIRiI54763.
    RefSeqiNP_001027019.1. NM_001031849.2. [P48740-3]
    NP_001870.3. NM_001879.5. [P48740-1]
    NP_624302.1. NM_139125.3. [P48740-2]
    UniGeneiHs.89983.

    Genome annotation databases

    EnsembliENST00000169293; ENSP00000169293; ENSG00000127241. [P48740-3]
    ENST00000296280; ENSP00000296280; ENSG00000127241. [P48740-2]
    ENST00000337774; ENSP00000336792; ENSG00000127241.
    ENST00000392472; ENSP00000376264; ENSG00000127241. [P48740-4]
    GeneIDi5648.
    KEGGihsa:5648.
    UCSCiuc003frh.2. human. [P48740-1]
    uc003fri.3. human. [P48740-2]
    uc003frk.2. human. [P48740-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS33907.1. [P48740-1]
    CCDS33908.1. [P48740-2]
    CCDS33909.1. [P48740-3]
    PIRiI54763.
    RefSeqiNP_001027019.1. NM_001031849.2. [P48740-3]
    NP_001870.3. NM_001879.5. [P48740-1]
    NP_624302.1. NM_139125.3. [P48740-2]
    UniGeneiHs.89983.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliP48740.
    SMRiP48740. Positions 22-699.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111629. 17 interactions.
    IntActiP48740. 15 interactions.
    MINTiMINT-4657209.

    Protein family/group databases

    MEROPSiS01.198.

    PTM databases

    PhosphoSiteiP48740.

    Polymorphism and mutation databases

    BioMutaiMASP1.
    DMDMi218512135.

    Proteomic databases

    PaxDbiP48740.
    PRIDEiP48740.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000169293; ENSP00000169293; ENSG00000127241. [P48740-3]
    ENST00000296280; ENSP00000296280; ENSG00000127241. [P48740-2]
    ENST00000337774; ENSP00000336792; ENSG00000127241.
    ENST00000392472; ENSP00000376264; ENSG00000127241. [P48740-4]
    GeneIDi5648.
    KEGGihsa:5648.
    UCSCiuc003frh.2. human. [P48740-1]
    uc003fri.3. human. [P48740-2]
    uc003frk.2. human. [P48740-3]

    Organism-specific databases

    CTDi5648.
    GeneCardsiGC03M186935.
    HGNCiHGNC:6901. MASP1.
    HPAiHPA001617.
    HPA009641.
    MIMi257920. phenotype.
    600521. gene.
    neXtProtiNX_P48740.
    Orphaneti293843. Craniofacial-ulnar-renal syndrome.
    PharmGKBiPA30644.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00760000118890.
    HOVERGENiHBG000559.
    InParanoidiP48740.
    KOiK03992.
    OMAiVWEQMGS.
    OrthoDBiEOG7W6WK4.
    PhylomeDBiP48740.
    TreeFamiTF330373.

    Enzyme and pathway databases

    BRENDAi3.4.21.B7. 2681.
    ReactomeiREACT_163699. Scavenging by Class A Receptors.
    REACT_163810. Ficolins bind to repetitive carbohydrate structures on the target cell surface.
    REACT_7964. Lectin pathway of complement activation.
    REACT_8024. Initial triggering of complement.
    SABIO-RKP48740.

    Miscellaneous databases

    ChiTaRSiMASP1. human.
    EvolutionaryTraceiP48740.
    GeneWikiiMASP1_(protein).
    GenomeRNAii5648.
    NextBioi21938.
    PMAP-CutDBQ96RS4.
    PROiP48740.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP48740.
    CleanExiHS_MASP1.
    ExpressionAtlasiP48740. baseline and differential.
    GenevisibleiP48740. HS.

    Family and domain databases

    Gene3Di2.60.120.290. 2 hits.
    InterProiIPR000859. 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_dom.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00431. CUB. 2 hits.
    PF07645. EGF_CA. 1 hit.
    PF00084. Sushi. 2 hits.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001155. C1r_C1s_MASP. 1 hit.
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00032. CCP. 2 hits.
    SM00042. CUB. 2 hits.
    SM00179. EGF_CA. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49854. SSF49854. 2 hits.
    SSF50494. SSF50494. 1 hit.
    SSF57535. SSF57535. 2 hits.
    PROSITEiPS00010. 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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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.
      , 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. 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.
      , 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. 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. 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. 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. Cited for: VARIANTS 3MC1 TYR-497; ARG-630 AND GLU-666 (ISOFORM 2).

    Entry informationi

    Entry nameiMASP1_HUMAN
    AccessioniPrimary (citable) accession number: P48740
    Secondary accession number(s): A8K542
    , A8K6M1, B4E2L7, O95570, Q68D21, Q8IUV8, Q96RS4, Q9UF09
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: December 16, 2008
    Last modified: July 22, 2015
    This is version 158 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.