C1S_BOVIN
ID C1S_BOVIN Reviewed; 689 AA.
AC Q0VCX1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Complement C1s subcomponent;
DE EC=3.4.21.42;
DE AltName: Full=C1 esterase;
DE AltName: Full=Complement component 1 subcomponent s;
DE Contains:
DE RecName: Full=Complement C1s subcomponent heavy chain;
DE Contains:
DE RecName: Full=Complement C1s subcomponent light chain;
DE Flags: Precursor;
GN Name=C1S;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: C1s B chain is a serine protease that combines with C1q and
CC C1r to form C1, the first component of the classical pathway of the
CC complement system. C1r activates C1s so that it can, in turn, activate
CC C2 and C4 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of Arg-|-Ala bond in complement component C4 to form
CC C4a and C4b, and Lys(or Arg)-|-Lys bond in complement component C2 to
CC form C2a and C2b: the 'classical' pathway C3 convertase.;
CC EC=3.4.21.42;
CC -!- ACTIVITY REGULATION: Inhibited by SERPING1. {ECO:0000250}.
CC -!- SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q, C1r and
CC C1s in the molar ration of 1:2:2. Activated C1s is an disulfide-linked
CC heterodimer of a heavy chain and a light chain (By similarity).
CC {ECO:0000250}.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI19957.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC119956; AAI19957.1; ALT_INIT; mRNA.
DR RefSeq; NP_001070018.1; NM_001076550.1.
DR AlphaFoldDB; Q0VCX1; -.
DR SMR; Q0VCX1; -.
DR BioGRID; 612993; 1.
DR STRING; 9913.ENSBTAP00000006358; -.
DR MEROPS; S01.193; -.
DR PaxDb; Q0VCX1; -.
DR PeptideAtlas; Q0VCX1; -.
DR PRIDE; Q0VCX1; -.
DR GeneID; 767827; -.
DR KEGG; bta:767827; -.
DR CTD; 716; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q0VCX1; -.
DR OrthoDB; 156878at2759; -.
DR Proteomes; UP000009136; Unplaced.
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:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.60.120.290; -; 2.
DR InterPro; IPR035708; Complement_C1s_subcomponent.
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; 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; PTHR24255:SF18; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 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; SSF49854; SSF49854; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57535; SSF57535; 2.
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 2: Evidence at transcript level;
KW Calcium; Complement pathway; Disulfide bond; EGF-like domain; Glycoprotein;
KW Hydrolase; Hydroxylation; Immunity; Innate immunity; Metal-binding;
KW Protease; Reference proteome; Repeat; Serine protease; Signal; Sushi.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..689
FT /note="Complement C1s subcomponent"
FT /id="PRO_0000285867"
FT CHAIN 16..437
FT /note="Complement C1s subcomponent heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000285868"
FT CHAIN 438..689
FT /note="Complement C1s subcomponent light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000285869"
FT DOMAIN 16..130
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 131..172
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255"
FT DOMAIN 175..290
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 292..356
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 357..423
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 438..681
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 475
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 529
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 632
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 149
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 65..83
FT /evidence="ECO:0000250"
FT DISULFID 135..147
FT /evidence="ECO:0000250"
FT DISULFID 143..156
FT /evidence="ECO:0000250"
FT DISULFID 158..171
FT /evidence="ECO:0000250"
FT DISULFID 175..202
FT /evidence="ECO:0000250"
FT DISULFID 234..251
FT /evidence="ECO:0000250"
FT DISULFID 294..341
FT /evidence="ECO:0000250"
FT DISULFID 321..354
FT /evidence="ECO:0000250"
FT DISULFID 359..403
FT /evidence="ECO:0000250"
FT DISULFID 386..421
FT /evidence="ECO:0000250"
FT DISULFID 425..549
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
FT ProRule:PRU00302"
FT DISULFID 595..618
FT /evidence="ECO:0000250"
FT DISULFID 628..660
FT /evidence="ECO:0000250"
SQ SEQUENCE 689 AA; 76609 MW; B10A00EC4B15465C CRC64;
MWCIVLFSLV AWVYAEPTMY GEILSPNYPQ VYPNEVEKSW DIEVPAGYGI HLYFTHLDIE
LSENCSYDSV QIMSGGHEEG KLCGRRTNKN SNSPVVKEFH IPYSKLQVIF RSDFSNEERF
TGFAAYYVAE DIDECTAFAD APCSHFCNNF LGGYFCSCPP EYFLHEDKKN CGVNCSGNVF
TTMTGEVESP NYPSPYPESS RCDYQIQLEE GFRVVVTMRR EDFDVEPADS EGHCPDSLLF
VAGDQHFGPY CGNGFPGPLT IETQSSALNI IFQTDGSEQR KGWKFRYHGD PIPCPKEVTA
NSFWEPERAK YVFRDVVKIT CVDGFEVVQG SVGSPSFYST CQSNGKWSNS KLRCQPVDCG
APEPIQHGRV EDPESTLFGS ITRYSCEMPY YSMECEGSEV YHCSGNGSWV NKVLGIEPPK
CIAVCGTPSE PFRSTQRIFG GSIAKIENFP WQVFFSNPWA GGALIDEYWV LTAAHVVEGN
DIPVMYVGSS SVVTSQLSNA QMLTAERVFI HPGWEVLDPS ITRKNFDNDI ALVRLRDPVK
MGPKVAPICL PGTSSEYDPP ENVLGLISGW GRTNVKSHVI KLRGAKLPVA PLSKCREMKG
VNPGIDISSF VFTENMICAG NDKGVDSCDG DSGGAFAVQD PKENKPKFYV AGLVSWGPQC
GTYGIYTRVK NYVDWIRKTM QEYSAPSVD
