MASP1
entrez
5648
canonical
uniprot
P48740
canonical
ensembl
ENSG00000127241
resolver
ensembl
ENSG00000291559
resolver
ensp
ENSP00000169293
resolver
ensp
ENSP00000296280
resolver
ensp
ENSP00000336792
resolver
genesymbol
MASP1
resolver
genesymbol_syn
CRARF
resolver
genesymbol_syn
CRARF1
resolver
genesymbol_syn
PRSS5
resolver
hgnc
HGNC:6901
resolver
uniprot
A8K542
resolver
uniprot
A8K6M1
resolver
uniprot
B4E2L7
resolver
uniprot
O95570
resolver
uniprot
Q68D21
resolver
uniprot
Q8IUV8
resolver
uniprot
Q96RS4
resolver
uniprot
Q9UF09
resolver
uniprot_entry
MASP1_HUMAN
resolver
uniprot_sec
A8K542
resolver
uniprot_sec
A8K6M1
resolver
uniprot_sec
B4E2L7
resolver
uniprot_sec
O95570
resolver
uniprot_sec
Q68D21
resolver
uniprot_sec
Q8IUV8
resolver
uniprot_sec
Q96RS4
resolver
uniprot_sec
Q9UF09
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by SERPING1. {ECO:0000269|PubMed:10946292}.; ACTIVITY REGULATION: [Isoform MASP-1]: The protease activity is specifically inhibited by SGMI-1 small protein inhibitor. {ECO:0000269|PubMed:22511776, ECO:0000269|PubMed:22691502}.; ACTIVITY REGULATION: [Isoform MASP-3]: The protease activity is specifically inhibited by TFMI-3. {ECO:0000269|PubMed:27535802}.; ACTIVITY REGULATION: [Isoform MASP-1]: (Microbial infection) Serine protease activity is inhibited by E.Coli ecotin (eco). {ECO:0000269|PubMed:35483450}.; ACTIVITY REGULATION: [Isoform MASP-3]: (Microbial infection) Serine protease activity is inhibited by E.Coli ecotin (eco). {ECO:0000269|PubMed:35483450}.
uniprot
proteins
amino_acid_sequence
MRWLLLYYALCFSLSKASAHTVELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSITFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDIFDIEDHPEVPCPYDYIKIKVGPKVLGPFCGEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRAAGNECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDTFQIECLKDGTWSNKIPTCKIVDCRAPGELEHGLITFSTRNNLTTYKSEIKYSCQEPYYKMLNNNTGIYTCSAQGVWMNKVLGRSLPTCLPVCGLPKFSRKLMARIFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSLDPEDPTLRDSDLLSPSDFKIILGKHWRLRSDENEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQQEGAMVIVSGWGKQFLQRFPETLMEIEIPIVDHSTCQKAYAPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTLNRERGQWYLVGTVSWGDDCGKKDRYGVYSYIHHNKDWIQRVTGVRN
uniprot
proteins
disease_involvement
DISEASE: 3MC syndrome 1 (3MC1) [MIM:257920]: A form of 3MC syndrome, an autosomal recessive disorder characterized by facial dysmorphism, craniosynostosis, learning disability, and genital, limb and vesicorenal anomalies. Facial features include hypertelorism, blepharophimosis, blepharoptosis and highly arched eyebrows, cleft lip and/or palate. The term 3MC syndrome includes Carnevale, Mingarelli, Malpuech, and Michels syndromes. {ECO:0000269|PubMed:21035106, ECO:0000269|PubMed:21258343, ECO:0000269|PubMed:23792966, ECO:0000269|PubMed:26419238, ECO:0000269|PubMed:28301481}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.21.-
uniprot
proteins
function
FUNCTION: Precursor of a serum protease that activates the complement pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system. {ECO:0000269|PubMed:10946292, ECO:0000269|PubMed:11485744, ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:12538697, ECO:0000269|PubMed:22691502, ECO:0000269|PubMed:22966085, ECO:0000269|PubMed:23386610, ECO:0000269|PubMed:9087411}.; FUNCTION: [Isoform MASP-1]: Serine protease that activates the lectin pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:10946292, PubMed:11527969, PubMed:12538697, PubMed:22691502, PubMed:22966085, PubMed:9087411). The lectin complement system is activated following association of lectins, such as MBL2, FCN1, FCN2 or FCN3, to carbohydrates on the pathogen surface (PubMed:22854970, PubMed:22966085, PubMed:23386610, PubMed:9087411). Following autoproteolytic processing in response to lectin-binding to pathogen carbohydrates, catalyzes cleavage and activation of MASP2, the next component of the lectin complement pathway (PubMed:22691502, PubMed:22966085, PubMed:23386610). {ECO:0000269|PubMed:10946292, ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:12538697, ECO:0000269|PubMed:22691502, ECO:0000269|PubMed:22854970, ECO:0000269|PubMed:22966085, ECO:0000269|PubMed:23386610, ECO:0000269|PubMed:9087411}.; FUNCTION: [Isoform MASP-3]: Serine protease that activates the alternative pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:20038603, PubMed:23792966, PubMed:27535802). The alternative complement pathway acts as an amplification loop that enhances other complement pathways (PubMed:27535802). Isoform MASP-3 specifically catalyzes cleavage and activation of factor D (CFD), the protease that initiates the alternative complement pathway (PubMed:20038603, PubMed:27535802). {ECO:0000269|PubMed:20038603, ECO:0000269|PubMed:23792966, ECO:0000269|PubMed:27535802}.
uniprot
proteins
mass_dalton
79247
uniprot
proteins
mutagenesis
MUTAGEN 68; /note="E->A,Q: Partial loss of interaction with FCN2, FCN3 and MBL2."; /evidence="ECO:0000269|PubMed:18596036"; MUTAGEN 77; /note="Y->A: Partial loss of interaction with FCN2, FCN3 and MBL2."; /evidence="ECO:0000269|PubMed:18596036"; MUTAGEN 99; /note="E->A: Partial loss of interaction with FCN2, FCN3 and MBL2."; /evidence="ECO:0000269|PubMed:18596036"; MUTAGEN 121; /note="D->A,N: Loss of interaction with FNC2 and FCN3 and partial loss of interaction with MBL2."; /evidence="ECO:0000269|PubMed:18596036"; MUTAGEN 122; /note="F->A: Partial loss of interaction with FCN2, FCN3 and MBL2."; /evidence="ECO:0000269|PubMed:18596036"; MUTAGEN 123; /note="S->A: Partial loss of interaction with FCN2, FCN3 and MBL2."; /evidence="ECO:0000269|PubMed:18596036"; MUTAGEN 125; /note="E->A: Partial loss of interaction with FCN2, FCN3 and MBL2."; /evidence="ECO:0000269|PubMed:18596036"; MUTAGEN 237; /note="H->A: Loss of interaction with FCN2, FCN3 and MBL2."; /evidence="ECO:0000269|PubMed:18596036"; MUTAGEN 239; /note="E->A: Partial loss of interaction with FCN2, FCN3 and MBL2."; /evidence="ECO:0000269|PubMed:18596036"; MUTAGEN 244; /note="Y->A: Loss of interaction with FCN2, FCN3 and MBL2."; /evidence="ECO:0000269|PubMed:18596036"; MUTAGEN 262; /note="E->A: Partial loss of interaction with FCN2, FCN3 and MBL2."; /evidence="ECO:0000269|PubMed:18596036"; MUTAGEN 274; /note="S->A: Partial loss of interaction with FCN2 and FCN3. No effect on interaction with MBL2."; /evidence="ECO:0000269|PubMed:18596036"; MUTAGEN 283; /note="N->A: Partial loss of interaction with FCN2, FCN3 and MBL2."; /evidence="ECO:0000269|PubMed:18596036"; MUTAGEN 286; /note="E->A: Partial loss of interaction with FCN2, FCN3 and MBL2."; /evidence="ECO:0000269|PubMed:18596036"; MUTAGEN 448; /note="R->Q: Abolished autocatalytic cleavage."; /evidence="ECO:0000269|PubMed:23386610"; MUTAGEN 646; /note="S->A: Abolished serine protease activity. No autoproteolytic processing."; /evidence="ECO:0000269|PubMed:15034049, ECO:0000269|PubMed:23386610"; MUTAGEN P48740-2:448; /note="K->Q: Promotes cleavage and activation by C1R."; /evidence="ECO:0000269|PubMed:23792966
uniprot
proteins
post_translational_modification
PTM: [Isoform MASP-1]: Autoproteolytic processing of the proenzyme produces the active enzyme composed on the heavy and the light chain held together by a disulfide bond. {ECO:0000269|PubMed:11290788, ECO:0000269|PubMed:15034049, ECO:0000269|PubMed:23386610}.; PTM: [Isoform MASP-3]: In contrast to isoform MASP-1, not activated through autoproteolytic processing. {ECO:0000269|PubMed:11290788, ECO:0000269|PubMed:23386610}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
10475605
uniprot
proteins
pubmed
10679061
uniprot
proteins
pubmed
10878362
uniprot
proteins
pubmed
10946292
uniprot
proteins
pubmed
11290788
uniprot
proteins
pubmed
11485744
uniprot
proteins
pubmed
11527969
uniprot
proteins
pubmed
11907111
uniprot
proteins
pubmed
12421953
uniprot
proteins
pubmed
12538697
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15034049
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16554018
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17182967
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18596036
uniprot
proteins
pubmed
19139490
uniprot
proteins
pubmed
19564340
uniprot
proteins
pubmed
20038603
uniprot
proteins
pubmed
20956340
uniprot
proteins
pubmed
21035106
uniprot
proteins
pubmed
21258343
uniprot
proteins
pubmed
22511776
uniprot
proteins
pubmed
22691502
uniprot
proteins
pubmed
22854970
uniprot
proteins
pubmed
22966085
uniprot
proteins
pubmed
23386610
uniprot
proteins
pubmed
23792966
uniprot
proteins
pubmed
23861840
uniprot
proteins
pubmed
26419238
uniprot
proteins
pubmed
27535802
uniprot
proteins
pubmed
28301481
uniprot
proteins
pubmed
35483450
uniprot
proteins
pubmed
8018603
uniprot
proteins
pubmed
8240317
uniprot
proteins
pubmed
8921412
uniprot
proteins
pubmed
9087411
uniprot
proteins
pubmed
9367419
uniprot
proteins
sequence_length
699
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11485744}.; SUBCELLULAR LOCATION: [Isoform MASP-1]: Secreted {ECO:0000269|PubMed:11290788}. Cell surface {ECO:0000269|PubMed:22966085}. Note=Recruited to the surface of pathogens by the mannose-binding proteins, such as MBL2. {ECO:0000269|PubMed:22966085}.; SUBCELLULAR LOCATION: [Isoform MASP-3]: Secreted {ECO:0000269|PubMed:27535802}.
uniprot
proteins