C1S_RAT
ID C1S_RAT Reviewed; 688 AA.
AC Q6P6T1; O70542; Q8R099;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 126.
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; Synonyms=r-gsp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9524231; DOI=10.1016/s0378-1119(98)00015-8;
RA Sakai H., Nakashima S., Yoshimura S., Nishimura Y., Sakai N., Nozawa Y.;
RT "Molecular cloning of a cDNA encoding a serine protease homologous to
RT complement Cls precursor from rat C6 glial cells and its expression during
RT glial differentiation.";
RL Gene 209:87-94(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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=AAH62042.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA25797.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; D88250; BAA25797.1; ALT_INIT; mRNA.
DR EMBL; BC062042; AAH62042.1; ALT_INIT; mRNA.
DR PIR; JC6554; JC6554.
DR RefSeq; NP_620255.1; NM_138900.1.
DR AlphaFoldDB; Q6P6T1; -.
DR SMR; Q6P6T1; -.
DR STRING; 10116.ENSRNOP00000016330; -.
DR MEROPS; S01.193; -.
DR MEROPS; S01.210; -.
DR GlyGen; Q6P6T1; 2 sites.
DR iPTMnet; Q6P6T1; -.
DR PhosphoSitePlus; Q6P6T1; -.
DR PaxDb; Q6P6T1; -.
DR PeptideAtlas; Q6P6T1; -.
DR GeneID; 192262; -.
DR KEGG; rno:192262; -.
DR UCSC; RGD:619983; rat.
DR CTD; 716; -.
DR RGD; 619983; C1s.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q6P6T1; -.
DR OrthoDB; 156878at2759; -.
DR PhylomeDB; Q6P6T1; -.
DR Reactome; R-RNO-166663; Initial triggering of complement.
DR Reactome; R-RNO-173623; Classical antibody-mediated complement activation.
DR Reactome; R-RNO-977606; Regulation of Complement cascade.
DR PRO; PR:Q6P6T1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:RGD.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0010001; P:glial cell differentiation; IEP:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
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; 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:0000250"
FT CHAIN 16..688
FT /note="Complement C1s subcomponent"
FT /id="PRO_0000042202"
FT CHAIN 16..437
FT /note="Complement C1s subcomponent heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042203"
FT CHAIN 438..688
FT /note="Complement C1s subcomponent light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042204"
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..680
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 631
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 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 627..659
FT /evidence="ECO:0000250"
FT CONFLICT 87
FT /note="T -> S (in Ref. 1; BAA25797)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="S -> F (in Ref. 1; BAA25797)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="G -> V (in Ref. 1; BAA25797)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="N -> I (in Ref. 1; BAA25797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 688 AA; 77071 MW; B69C43027AE7A85F CRC64;
MWCFVFFSLL ASFSAEPTMY GEILSPNYPQ AYPNEVVKTW DIEVPEGFGI HLYFTHLDME
LSENCAYDSV QIISGGIEEE RLCGQRTSKS PNSPTVEEFQ FPYNRLQVVF TSDFSNEERF
TGFAAYYSAV DVNECTDFTD VPCSHFCNNF IGGYFCSCPP EYFLHDDMRT CGVNCSGDVF
TALIGEIASP NYPNPYPENS RCEYQIRLQE GFRLVLTIRR EDFDVEPADS EGNCHDSLTF
AAKNQQFGPY CGNGFPGPLT IKTQSNTLDI VFQTDLTGQN KGWKLRYHGD PIPCPKEISA
NSIWEPEKAK YVFKDVVKIT CVDGFEVVEG NVGSTSFYST CQSNGQWSNS RLECQPVDCG
VPEPIENGKV EDPEDTVFGS VIHYTCEEPY YYMEQEEGGE YHCAANGSWV NDQLGVELPK
CIPVCGVPTE PFKVQQRIFG GYSTKIQSFP WQVYFESPRG GGALIDEYWV LTAAHVVEGN
SDPVMYVGST LLKIERLRNA QRLITERVII HPSWKQEDDL NTRTNFDNDI ALVQLKDPVK
MGPTVAPICL PETSSDYNPS EGDLGLISGW GRTENRTNVI QLRGAKLPIT SLEKCQQVKV
ENPKARSNDY VFTDNMICAG EKGVDSCEGD SGGAFALPVP NVKDPKFYVA GLVSWGKKCG
TYGIYTKVKN YVDWILKTMQ ENSGPKKD
