ID A0A1S3AJI6_ERIEU Unreviewed; 692 AA.
AC A0A1S3AJI6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Complement C1s subcomponent {ECO:0000313|RefSeq:XP_007535915.1};
GN Name=C1S {ECO:0000313|RefSeq:XP_007535915.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007535915.1};
RN [1] {ECO:0000313|RefSeq:XP_007535915.1}
RP IDENTIFICATION.
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_007535915.1; XM_007535853.2.
DR AlphaFoldDB; A0A1S3AJI6; -.
DR STRING; 9365.ENSEEUP00000004912; -.
DR GeneID; 103125084; -.
DR CTD; 716; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; A0A1S3AJI6; -.
DR OrthoDB; 5394076at2759; -.
DR Proteomes; UP000079721; Unplaced.
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:0006956; P:complement activation; IEA:InterPro.
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; 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:SF18; COMPLEMENT C1S SUBCOMPONENT; 1.
DR PANTHER; PTHR24255; COMPLEMENT COMPONENT 1, S SUBCOMPONENT-RELATED; 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; 2.
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; 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 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|PIRSR:PIRSR001155-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001155-4};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..692
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010175178"
FT DOMAIN 17..136
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 181..296
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 298..362
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 363..429
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 444..684
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 482
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT ACT_SITE 535
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT ACT_SITE 635
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 119
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 137
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 155
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 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT MOD_RES 155
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-3"
FT DISULFID 71..89
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 141..153
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 149..162
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 164..177
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 181..208
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2,
FT ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 240..257
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2,
FT ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 300..347
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 327..360
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 365..409
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 392..427
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 431..555
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 601..622
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 631..663
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
SQ SEQUENCE 692 AA; 76856 MW; FECB487D4BAD067B CRC64;
MDRRPEMWSL VLFSLLAGAH AEPTLHGEIL SPNYPQAYPN EVEQSWDLEV PEGYGIRLYF
THLDIELSED CAYDSVRIIS GDFEEGKLCG QRTSKNPNSP IVEEFQVPSN KLRVTFTSDF
SNEERFTGFA AYYVAVDIDE CTDFVDVPCS HFCNNFLGGY FCSCPPEYFL HDDMKTCGVN
CSGEVFTELI GEITSPNYPS PYPENSRCEY QILLEKGFQV VVTMRREDFD VEPADSEGNC
PDSLVFVAGD RKFGPYCGNG FPGPLKIETK SNTLDVIFQT DHAGEQKGWK LRYYGDPIPC
PKETGAHSVW EPDKAKYVFK DVVKITCMEG FEVVQGNVGS TSFYSTCQNN GQWSNSKLKC
QPVDCSLPES IPHGSFEEPA NTLFGSVIRY TCEEPYYSMQ TEGGGDYRCT GNGSWVNELL
GTELPLCVPV CGVPSEPFVG TQRIFGGSRT KIQSFPWQVY FPPPSRAGGA LIDEYWVLTA
AHVVENNPYP VMYAGTTSVV TSHLANAQLL TAEQVFIHPG WDMDSKDSRK NFDNDIALVR
LKEPVKMGPM VSPICLPSNS VEFEPLEGEL GLISGWGRTE KRQSVNQLMG AKLPIVPLKK
CQEVEGDGVN IKTYVFTDNM ICAGEKGTDS CGGDSGGAFA VQHPHEENPK FYVAGLVSWG
AKCGTYGIYT RVKNYVDWIV QTMQENSTPS ED
//
