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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)DescriptionActionsGraphical viewLength
    Metal bindingi68Calcium 11
    Metal bindingi76Calcium 11
    Metal bindingi121Calcium 11
    Metal bindingi123Calcium 1; via carbonyl oxygen1
    Metal bindingi139Calcium 21
    Metal bindingi140Calcium 2; via carbonyl oxygen1
    Metal bindingi142Calcium 21
    Metal bindingi159Calcium 21
    Metal bindingi160Calcium 2; via carbonyl oxygen1
    Metal bindingi163Calcium 2; via carbonyl oxygen1
    Metal bindingi235Calcium 31
    Metal bindingi245Calcium 31
    Metal bindingi282Calcium 31
    Metal bindingi284Calcium 3; via carbonyl oxygen1
    Active sitei490Charge relay systemBy similarity1
    Active sitei552Charge relay systemBy similarity1
    Active sitei646Charge relay systemBy similarity1

    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
    • 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

    BioCyciZFISH:ENSG00000127241-MONOMER.
    BRENDAi3.4.21.B7. 2681.
    ReactomeiR-HSA-166662. Lectin pathway of complement activation.
    R-HSA-166663. Initial triggering of complement.
    R-HSA-2855086. Ficolins bind to repetitive carbohydrate structures on the target cell surface.
    R-HSA-3000480. Scavenging by Class A Receptors.
    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
    Proteomesi
    • UP000005640 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)2 Publications
    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)DescriptionActionsGraphical viewLength
    Isoform 2 (identifier: P48740-2)
    Natural varianti484G → E in 3MC1) (PubMed:26419238. 3 Publications1
    Natural varianti497H → Y in 3MC1) (PubMed:21258343. 3 Publications1
    Natural varianti553D → N in 3MC1) (PubMed:26419238. 3 Publications1
    Natural varianti630C → R in 3MC1) (PubMed:21258343. 3 Publications1
    Natural varianti663D → Y in 3MC1) (PubMed:26419238. 3 Publications1
    Natural varianti666G → E in 3MC1) (PubMed:21258343. 3 Publications1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi68E → A or Q: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication1
    Mutagenesisi77Y → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication1
    Mutagenesisi99E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication1
    Mutagenesisi121D → A or N: Loss of interaction with FNC2 and FCN3 and partial loss of interaction with MBL2. 1 Publication1
    Mutagenesisi122F → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication1
    Mutagenesisi123S → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication1
    Mutagenesisi125E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication1
    Mutagenesisi237H → A: Loss of interaction with FCN2, FCN3 and MBL2. 1 Publication1
    Mutagenesisi239E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication1
    Mutagenesisi244Y → A: Loss of interaction with FCN2, FCN3 and MBL2. 1 Publication1
    Mutagenesisi262E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication1
    Mutagenesisi274S → A: Partial loss of interaction with FCN2 and FCN3. No effect on interaction with MBL2. 1 Publication1
    Mutagenesisi283N → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication1
    Mutagenesisi286E → A: Partial loss of interaction with FCN2, FCN3 and MBL2. 1 Publication1
    Mutagenesisi646S → A: No autoproteolytic processing. 1 Publication1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNETi5648.
    MalaCardsiMASP1.
    MIMi257920. phenotype.
    OpenTargetsiENSG00000127241.
    Orphaneti293843. Craniofacial-ulnar-renal syndrome.
    PharmGKBiPA30644.

    Polymorphism and mutation databases

    BioMutaiMASP1.
    DMDMi218512135.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 191 PublicationAdd BLAST19
    ChainiPRO_000002759220 – 699Mannan-binding lectin serine protease 1Add BLAST680
    ChainiPRO_000002759320 – 448Mannan-binding lectin serine protease 1 heavy chainAdd BLAST429
    ChainiPRO_0000027594449 – 699Mannan-binding lectin serine protease 1 light chainAdd BLAST251

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi49N-linked (GlcNAc...)2 Publications1
    Disulfide bondi73 ↔ 911 Publication
    Disulfide bondi143 ↔ 1571 Publication
    Disulfide bondi153 ↔ 1661 Publication
    Modified residuei159(3R)-3-hydroxyasparagineSequence analysis1
    Disulfide bondi168 ↔ 1811 Publication
    Glycosylationi178N-linked (GlcNAc...) (complex)3 Publications1
    Disulfide bondi185 ↔ 2121 Publication
    Disulfide bondi242 ↔ 2601 Publication
    Disulfide bondi301 ↔ 349By similarity
    Disulfide bondi329 ↔ 362By similarity
    Disulfide bondi367 ↔ 414By similarity
    Glycosylationi385N-linked (GlcNAc...) (complex)2 Publications1
    Disulfide bondi397 ↔ 432By similarity
    Glycosylationi407N-linked (GlcNAc...)2 Publications1
    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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei448 – 449Cleavage; by autolysis2

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    PeptideAtlasiP48740.
    PRIDEiP48740.
    TopDownProteomicsiP48740-3. [P48740-3]

    PTM databases

    iPTMnetiP48740.
    PhosphoSitePlusiP48740.

    Miscellaneous databases

    PMAP-CutDBQ96RS4.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiENSG00000127241.
    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

    GO - Molecular functioni

    • calcium-dependent protein binding Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    BioGridi111629. 21 interactors.
    DIPiDIP-61382N.
    IntActiP48740. 16 interactors.
    MINTiMINT-4657209.

    Structurei

    Secondary structure

    1699
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi28 – 32Combined sources5
    Turni34 – 37Combined sources4
    Beta strandi42 – 51Combined sources10
    Beta strandi56 – 66Combined sources11
    Helixi71 – 73Combined sources3
    Beta strandi75 – 81Combined sources7
    Beta strandi86 – 90Combined sources5
    Beta strandi92 – 99Combined sources8
    Beta strandi110 – 120Combined sources11
    Beta strandi130 – 139Combined sources10
    Turni142 – 144Combined sources3
    Beta strandi154 – 160Combined sources7
    Beta strandi163 – 167Combined sources5
    Beta strandi192 – 199Combined sources8
    Turni200 – 203Combined sources4
    Beta strandi211 – 217Combined sources7
    Beta strandi223 – 228Combined sources6
    Beta strandi238 – 244Combined sources7
    Beta strandi246 – 251Combined sources6
    Beta strandi254 – 259Combined sources6
    Beta strandi261 – 263Combined sources3
    Beta strandi273 – 280Combined sources8
    Beta strandi291 – 297Combined sources7
    Beta strandi310 – 314Combined sources5
    Beta strandi317 – 320Combined sources4
    Beta strandi324 – 329Combined sources6
    Beta strandi333 – 337Combined sources5
    Beta strandi340 – 349Combined sources10
    Beta strandi355 – 357Combined sources3
    Beta strandi361 – 364Combined sources4
    Beta strandi376 – 382Combined sources7
    Beta strandi392 – 397Combined sources6
    Turni399 – 401Combined sources3
    Beta strandi402 – 404Combined sources3
    Helixi405 – 407Combined sources3
    Beta strandi411 – 414Combined sources4
    Turni416 – 418Combined sources3
    Beta strandi420 – 422Combined sources3
    Turni423 – 425Combined sources3
    Beta strandi426 – 428Combined sources3
    Beta strandi432 – 434Combined sources3
    Beta strandi463 – 468Combined sources6
    Beta strandi473 – 480Combined sources8
    Turni481 – 483Combined sources3
    Beta strandi484 – 487Combined sources4
    Helixi489 – 491Combined sources3
    Beta strandi499 – 501Combined sources3
    Turni505 – 507Combined sources3
    Turni511 – 513Combined sources3
    Beta strandi514 – 519Combined sources6
    Beta strandi522 – 525Combined sources4
    Beta strandi531 – 540Combined sources10
    Turni546 – 549Combined sources4
    Beta strandi554 – 560Combined sources7
    Beta strandi565 – 567Combined sources3
    Beta strandi583 – 591Combined sources9
    Beta strandi594 – 596Combined sources3
    Beta strandi602 – 609Combined sources8
    Helixi611 – 618Combined sources8
    Helixi619 – 621Combined sources3
    Beta strandi629 – 632Combined sources4
    Beta strandi649 – 654Combined sources6
    Turni655 – 658Combined sources4
    Beta strandi659 – 666Combined sources8
    Helixi672 – 675Combined sources4
    Beta strandi677 – 683Combined sources7
    Helixi684 – 687Combined sources4
    Helixi688 – 695Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP48740.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini20 – 138CUB 1PROSITE-ProRule annotationAdd BLAST119
    Domaini139 – 182EGF-like; calcium-bindingAdd BLAST44
    Domaini185 – 297CUB 2PROSITE-ProRule annotationAdd BLAST113
    Domaini299 – 364Sushi 1PROSITE-ProRule annotationAdd BLAST66
    Domaini365 – 434Sushi 2PROSITE-ProRule annotationAdd BLAST70
    Domaini449 – 696Peptidase S1PROSITE-ProRule annotationAdd BLAST248

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni20 – 278Interaction with FCN2Add BLAST259
    Regioni20 – 184HomodimerizationBy similarityAdd BLAST165
    Regioni20 – 184Interaction with MBL2Add BLAST165

    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

    GeneTreeiENSGT00760000118890.
    HOVERGENiHBG000559.
    InParanoidiP48740.
    KOiK03992.
    OMAiDLSQRWV.
    OrthoDBiEOG091G02DS.
    PhylomeDBiP48740.
    TreeFamiTF330373.

    Family and domain databases

    CDDicd00033. CCP. 2 hits.
    cd00041. CUB. 2 hits.
    cd00190. Tryp_SPc. 1 hit.
    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.
    IPR009003. Peptidase_S1_PA.
    IPR001314. Peptidase_S1A.
    IPR000436. Sushi_SCR_CCP_dom.
    IPR001254. Trypsin_dom.
    IPR018114. TRYPSIN_HIS.
    IPR033116. TRYPSIN_SER.
    [Graphical view]
    PfamiPF00431. CUB. 2 hits.
    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 (PubMed:16335952).3 Publications
    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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti2R → K in BAF84375 (PubMed:14702039).Curated1
    Sequence conflicti89T → A in CAH18409 (PubMed:17974005).Curated1
    Sequence conflicti232F → L in BAF84375 (PubMed:14702039).Curated1
    Sequence conflicti235E → Q in BAA05928 (PubMed:8018603).Curated1
    Sequence conflicti235E → Q in BAA34864 (PubMed:8921412).Curated1
    Sequence conflicti285G → A in BAA05928 (PubMed:8018603).Curated1
    Sequence conflicti285G → A in BAA34864 (PubMed:8921412).Curated1
    Sequence conflicti285G → A in BAA89206 (PubMed:10475605).Curated1
    Sequence conflicti392E → G in BAF83846 (PubMed:14702039).Curated1
    Sequence conflicti499E → G in BAA05928 (PubMed:8018603).Curated1
    Sequence conflicti499E → K in BAA04477 (PubMed:8240317).Curated1
    Sequence conflicti499E → K in BAA89206 (PubMed:10475605).Curated1
    Sequence conflicti527D → A in BAA34864 (PubMed:8921412).Curated1
    Sequence conflicti543Q → K in BAA04477 (PubMed:8240317).Curated1
    Sequence conflicti552D → V in BAA34864 (PubMed:8921412).Curated1
    Sequence conflicti643A → S in BAA04477 (PubMed:8240317).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_05183121T → I.Corresponds to variant rs1062049dbSNPEnsembl.1
    Natural variantiVAR_051832568V → A.Corresponds to variant rs13322090dbSNPEnsembl.1
    Natural variantiVAR_051833679G → R.Corresponds to variant rs3774266dbSNPEnsembl.1
    Isoform 2 (identifier: P48740-2)
    Natural varianti484G → E in 3MC1) (PubMed:26419238. 3 Publications1
    Natural varianti497H → Y in 3MC1) (PubMed:21258343. 3 Publications1
    Natural varianti553D → N in 3MC1) (PubMed:26419238. 3 Publications1
    Natural varianti630C → R in 3MC1) (PubMed:21258343. 3 Publications1
    Natural varianti663D → Y in 3MC1) (PubMed:26419238. 3 Publications1
    Natural varianti666G → E in 3MC1) (PubMed:21258343. 3 Publications1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0368091 – 113Missing in isoform 4. 1 PublicationAdd BLAST113
    Alternative sequenceiVSP_036810364 – 380IVDCR…GLITF → KNEIDLESELKSEQVTE in isoform 3. 2 PublicationsAdd BLAST17
    Alternative sequenceiVSP_036811381 – 699Missing in isoform 3. 2 PublicationsAdd BLAST319
    Alternative sequenceiVSP_036812435V → ECGQPSRSLPSLVKRIIGGR NAEPGLFPWQALIVVEDTSR VPNDKWFGSGALLSASWILT AAHVLRSQRRDTTVIPVSKE HVTVYLGLHDVRDKSGAVNS SAARVVLHPDFNIQNYNHDI ALVQLQEPVPLGPHVMPVCL PRLEPEGPAPHMLGLVAGWG ISNPNVTVDEIISSGTRTLS DVLQYVKLPVVPHAECKTSY ESRSGNYSVTENMFCAGYYE GGKDTCLGDSGGAFVIFDDL SQRWVVQGLVSWGGPEECGS KQVYGVYTKVSNYVDWVWEQ MGLPQSVVEPQVER in isoform 2 and isoform 4. 3 Publications1
    Alternative sequenceiVSP_036813436 – 699Missing in isoform 2 and isoform 4. 3 PublicationsAdd BLAST264

    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]
    XP_016862361.1. XM_017006872.1. [P48740-4]
    UniGeneiHs.89983.

    Genome annotation databases

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

    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]
    XP_016862361.1. XM_017006872.1. [P48740-4]
    UniGeneiHs.89983.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111629. 21 interactors.
    DIPiDIP-61382N.
    IntActiP48740. 16 interactors.
    MINTiMINT-4657209.

    Protein family/group databases

    MEROPSiS01.198.

    PTM databases

    iPTMnetiP48740.
    PhosphoSitePlusiP48740.

    Polymorphism and mutation databases

    BioMutaiMASP1.
    DMDMi218512135.

    Proteomic databases

    PeptideAtlasiP48740.
    PRIDEiP48740.
    TopDownProteomicsiP48740-3. [P48740-3]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi5648.
    DisGeNETi5648.
    GeneCardsiMASP1.
    HGNCiHGNC:6901. MASP1.
    HPAiHPA001617.
    HPA009641.
    MalaCardsiMASP1.
    MIMi257920. phenotype.
    600521. gene.
    neXtProtiNX_P48740.
    OpenTargetsiENSG00000127241.
    Orphaneti293843. Craniofacial-ulnar-renal syndrome.
    PharmGKBiPA30644.
    GenAtlasiSearch...

    Phylogenomic databases

    GeneTreeiENSGT00760000118890.
    HOVERGENiHBG000559.
    InParanoidiP48740.
    KOiK03992.
    OMAiDLSQRWV.
    OrthoDBiEOG091G02DS.
    PhylomeDBiP48740.
    TreeFamiTF330373.

    Enzyme and pathway databases

    BioCyciZFISH:ENSG00000127241-MONOMER.
    BRENDAi3.4.21.B7. 2681.
    ReactomeiR-HSA-166662. Lectin pathway of complement activation.
    R-HSA-166663. Initial triggering of complement.
    R-HSA-2855086. Ficolins bind to repetitive carbohydrate structures on the target cell surface.
    R-HSA-3000480. Scavenging by Class A Receptors.
    SABIO-RKP48740.

    Miscellaneous databases

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

    Gene expression databases

    BgeeiENSG00000127241.
    CleanExiHS_MASP1.
    ExpressionAtlasiP48740. baseline and differential.
    GenevisibleiP48740. HS.

    Family and domain databases

    CDDicd00033. CCP. 2 hits.
    cd00041. CUB. 2 hits.
    cd00190. Tryp_SPc. 1 hit.
    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.
    IPR009003. Peptidase_S1_PA.
    IPR001314. Peptidase_S1A.
    IPR000436. Sushi_SCR_CCP_dom.
    IPR001254. Trypsin_dom.
    IPR018114. TRYPSIN_HIS.
    IPR033116. TRYPSIN_SER.
    [Graphical view]
    PfamiPF00431. CUB. 2 hits.
    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...

    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: November 30, 2016
    This is version 170 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

    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 one 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.