ID A0A0D9R9Z9_CHLSB Unreviewed; 699 AA.
AC A0A0D9R9Z9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=MBL associated serine protease 1 {ECO:0000313|Ensembl:ENSCSAP00000005438.1};
GN Name=MASP1 {ECO:0000313|Ensembl:ENSCSAP00000005438.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000005438.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000005438.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000005438.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains.
CC {ECO:0000256|PIRSR:PIRSR001155-3}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR EMBL; AQIB01076657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008007689.1; XM_008009498.1.
DR AlphaFoldDB; A0A0D9R9Z9; -.
DR STRING; 60711.ENSCSAP00000005438; -.
DR Ensembl; ENSCSAT00000007254.1; ENSCSAP00000005438.1; ENSCSAG00000009191.1.
DR GeneID; 103241880; -.
DR KEGG; csab:103241880; -.
DR CTD; 5648; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00950000183084; -.
DR OMA; CDWLIRA; -.
DR OrthoDB; 5394076at2759; -.
DR BioGRID-ORCS; 103241880; 0 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 15.
DR Bgee; ENSCSAG00000009191; Expressed in liver and 1 other cell type or tissue.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0001867; P:complement activation, lectin pathway; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 2.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024175; Pept_S1A_C1r/C1S/mannan-bd.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24255; COMPLEMENT COMPONENT 1, S SUBCOMPONENT-RELATED; 1.
DR PANTHER; PTHR24255:SF13; MANNAN-BINDING LECTIN SERINE PROTEASE 1; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001155; C1r_C1s_MASP; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00032; CCP; 2.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50923; SUSHI; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR001155-4};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR001155-2};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278,
KW ECO:0000256|PIRSR:PIRSR001155-3}; Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001155-4};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..699
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002345066"
FT DOMAIN 11..138
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 185..297
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 299..364
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 365..434
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 449..696
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 490
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT ACT_SITE 552
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT ACT_SITE 646
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT MOD_RES 159
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-3"
FT DISULFID 73..91
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 143..157
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 153..166
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 168..181
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 185..212
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2,
FT ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 242..260
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 301..349
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 329..362
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 367..414
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 397..432
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 436..572
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 614..631
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 642..672
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
SQ SEQUENCE 699 AA; 79328 MW; 4E032F1E72852252 CRC64;
MRWLLLYHAL CFSLSKASAH TVELNDMFGQ IQSPGYPDSY PSDSEVTWNI TVPDGFRIKL
YFMHFNLESS YLCEYDYVKV ETEDQVLATF CGRETTDTEQ TPGQEVVLSP GSFMSITFRS
DFSNEERFTG FDAHYMAVDV DECKEREDEE LSCDHYCHNY IGGYYCSCRF GYILHTDNRT
CRVECSDNLF TQRTGVITSP DFPNPYPKSS ECLYTIELEE GFMVNLQFED IFDIEDHPEV
PCPYDYIKIK VGPKVLGPFC GEKAPEPIST KSHSVLILFH SDNSGENRGW RLSYRAAGNE
CPELQPPVHG KIEPSQAKYS FKDQVLVSCD TGYKVLKDNV EMDTFQIECL KDGTWSNKIP
TCKIVDCRAP GELEHGLVTF STRNNLTTYK SEIRYSCQEP YYKMLNNITG IYTCSAQGVW
MNKVLGRRLP TCLPVCGLPK FSRKLMARIF NGRPAQKGTT PWIAMLSHLN GQPFCGGSLL
GTSWIVTAAH CLHQSLDPED PSLRNSDLLS PSDFKIILGK HWRLQSDENE QHLGVKHITL
HPQYDPSTFE NDVALVELLE SPVLNAFVMP ICLPEGPQQE GAMVIVSGWG KQFLQRFPET
LMEIEIPIVD RGTCQKAYAP LKKKVTRDMI CAGEKEGGKD ACAGDSGGPM VTLNRERGQW
YLVGTVSWGD DCGKKDRYGV YSYIYHNKDW IQRVTRLRN
//
