ID A0A2D0REU7_ICTPU Unreviewed; 660 AA.
AC A0A2D0REU7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Mannan-binding lectin serine protease 2 isoform X2 {ECO:0000313|RefSeq:XP_017329062.1};
GN Name=LOC108268542 {ECO:0000313|RefSeq:XP_017329062.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017329062.1};
RN [1] {ECO:0000313|RefSeq:XP_017329062.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017329062.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_017329062.1; XM_017473573.3.
DR AlphaFoldDB; A0A2D0REU7; -.
DR STRING; 7998.ENSIPUP00000000088; -.
DR Ensembl; ENSIPUT00000000114; ENSIPUP00000000088; ENSIPUG00000000090.
DR GeneID; 108268542; -.
DR OMA; DFADAPC; -.
DR OrthoDB; 5394076at2759; -.
DR Proteomes; UP000221080; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0032502; P:developmental process; IEA:UniProt.
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; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
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:SF29; WU:FD46C06 PROTEIN; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF14670; FXa_inhibition; 1.
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; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50923; SUSHI; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR001155-4};
KW Complement pathway {ECO:0000256|ARBA:ARBA00022875};
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};
KW Hydroxylation {ECO:0000256|PIRSR:PIRSR001155-3};
KW Immunity {ECO:0000256|ARBA:ARBA00022875};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022875};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001155-4};
KW Protease {ECO:0000256|ARBA:ARBA00022670,
KW ECO:0000313|RefSeq:XP_017329062.1}; 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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..660
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012112941"
FT DOMAIN 5..131
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 171..283
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 285..345
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 346..414
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 427..658
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 465
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT ACT_SITE 511
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT ACT_SITE 604
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
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 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT MOD_RES 149
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-3"
FT DISULFID 65..83
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 136..147
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 143..156
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 158..171
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 175..200
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 229..246
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 287..331
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 314..343
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 348..391
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2,
FT ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 376..412
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 416..531
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 576..589
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 600..634
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
SQ SEQUENCE 660 AA; 72292 MW; 01ADBC0FD3851A22 CRC64;
MLIFCVCVVL VSVCQCLPLS GWIQSPGFPY GYGSHVSETW RRCAPPGHIL SLTLLHLDLE
ESYECKDDAL QVSEGQNVLA QLCGKMTLKE LQSSVNPSLR SSSGGCLSLT FQSDYSNTER
HAGFKAFYTT QDVDECWEND VECSHFCHNY IGGYSCSCKP GYYLADDQHE CRASCTENHH
GAGVLTAPGS PGPYFENADC IFSLSADEGN QLELKFTGVF DVESRDGKCI DYLTIKTDTE
TFGPFCGKDK PAHILTAAQQ VRVLFHSDTE GTNRGFSLEY KPKVMECPGK VTPNSVVSPV
KDRYQVGESV TVRCLTGYVL PDATETFRST CQLNGNWSPR QNCELVNCGP PELPDLMVLT
EENPSTSYED KITVKCSSVY YNLVGNAHFT CDAAGVWVAE NGQNFSQNAP QCVAVCGVTK
TSVGGRILGG KKATLGQIPW QLLIKGPKRG GASLINDRWA ITAAHVVENQ GSLMVTGGMV
DGQDEAKVEM QAEKIIIHPN YPRQSTNYDN DIALVKLSSR VPLSENIIPV CLPKTKTNGP
ALEGKMGTVS GYGLKKNLKI SQYLQYAHVK EYEGFCFENN MKVTENMFCA GEEDSKVDSC
KGDSGGPLVI PMVGFGSSNT PYTIKGLVSW GPPCEVTNYK GYYTKVENYL DWIRETMANN
//
