ID D5L7X4_PIG Unreviewed; 728 AA.
AC D5L7X4; F1SFI1; K7GPX6;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Complement component MASP3 {ECO:0000313|EMBL:ADF30843.1};
DE SubName: Full=Mannan-binding lectin serine protease 1 isoform 2 {ECO:0000313|EMBL:HDB10735.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:ADF30843.1};
RN [1] {ECO:0000313|EMBL:ADF30843.1}
RP NUCLEOTIDE SEQUENCE.
RA Wimmers K., Do V.A.K., Murani E., Ponsuksili S.;
RT "Molecular characterization of genes encoding the complement components.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDB10735.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
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; GU810083; ADF30843.1; -; mRNA.
DR EMBL; DQIR01155258; HDB10735.1; -; Transcribed_RNA.
DR RefSeq; NP_001171876.1; NM_001184947.1.
DR SMR; D5L7X4; -.
DR STRING; 9823.ENSSSCP00000062448; -.
DR MEROPS; S01.132; -.
DR PaxDb; 9823-ENSSSCP00000012577; -.
DR GeneID; 100152125; -.
DR KEGG; ssc:100152125; -.
DR CTD; 5648; -.
DR eggNOG; KOG3627; Eukaryota.
DR OMA; QHWVAQG; -.
DR OrthoDB; 5394076at2759; -.
DR TreeFam; TF330373; -.
DR Reactome; R-SSC-166662; Lectin pathway of complement activation.
DR Reactome; R-SSC-166663; Initial triggering of complement.
DR Reactome; R-SSC-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface.
DR Reactome; R-SSC-3000480; Scavenging by Class A Receptors.
DR Bgee; ENSSSCG00000011806; Expressed in liver and 33 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0001867; P:complement activation, lectin pathway; IBA:GO_Central.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
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; 2.
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; 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; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Calcium {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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:0000313|EMBL:HDB10735.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW 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..728
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015088599"
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 450..716
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 497
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT ACT_SITE 553
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT ACT_SITE 664
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..573
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 630..649
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 660..692
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
SQ SEQUENCE 728 AA; 81552 MW; CCCB065E7074BB97 CRC64;
MRWLLLSHAL CFSLLKASAH VVELNNMFGQ IQSPGYPDSY PSDSEVTWNI TVPEGFRIKL
YFMHFNLESS YLCEYDYVKV ETEDQVLATF CGKETTDTEQ TPGQEVVFSP GSFMSITFRS
DFSNEERYTG FDAHYMAVDV DECTEREDEE LSCDHYCHNY IGGYYCSCRF GYILHTDNRT
CRVECSDNLF TQRTGVITSP DYPSPYPKSS ECLYTIELEE GFMVSLQFED IFDIEDHPEV
SCPYDYIKIK AGPKLLGPFC GEKAPEPINT QSHSIQIQFR SDNSGENRGW RLLYRATGNE
CPKLQPPVHG KIEPLQAKYS FKDQVLISCD TGYKVLKDNV EMDVFQIECL KDGTWSNKIP
TCKIADCGTP AKLENGLVTF STRNNLTTYK SEIIYSCQQP YYKMLHSTTG VYTCSAQGVW
MNEVLGKSQP TCLPVCGQPS RSLPNLVKRI IGGRNAEPGL FPWQALIVVE DTSRVPNDKW
FGSGALLSES WILTAAHVLR SQRRDNTVTP VSKEHVTVYL GLHDVRDKSG AVNSSAARVV
LHPDFDIQNY NHDIALVQLQ EPVPLGPHVM PVCLPRPEPE GPAPHMLGLV AGWGISNPNV
TVDEIISSGT RTLSDVLQYV KLPVVPHAEC KTSYESRSGN YSVTENMFCA GYYEGGKDTC
LGDSGGAFVI LDDLSQRWVA QGLVSWGGPE ECGSKQVYGV YTKVSNYVDW VWEQMGSPPG
LGELQVER
//
