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Complement C1s subcomponent (EC 3.4.21.42) (C1 esterase) (Complement component 1 subcomponent s) [Cleaved into: Complement C1s subcomponent heavy chain; Complement C1s subcomponent light chain]

 C1S_RAT                 Reviewed;         688 AA.
Q6P6T1; O70542; Q8R099;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
27-SEP-2005, sequence version 2.
22-NOV-2017, entry version 111.
RecName: Full=Complement C1s subcomponent;
EC=3.4.21.42;
AltName: Full=C1 esterase;
AltName: Full=Complement component 1 subcomponent s;
Contains:
RecName: Full=Complement C1s subcomponent heavy chain;
Contains:
RecName: Full=Complement C1s subcomponent light chain;
Flags: Precursor;
Name=C1s; Synonyms=r-gsp;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9524231; DOI=10.1016/S0378-1119(98)00015-8;
Sakai H., Nakashima S., Yoshimura S., Nishimura Y., Sakai N.,
Nozawa Y.;
"Molecular cloning of a cDNA encoding a serine protease homologous to
complement Cls precursor from rat C6 glial cells and its expression
during glial differentiation.";
Gene 209:87-94(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: C1s B chain is a serine protease that combines with C1q
and C1r to form C1, the first component of the classical pathway
of the complement system. C1r activates C1s so that it can, in
turn, activate C2 and C4 (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Cleavage of Arg-|-Ala bond in complement
component C4 to form C4a and C4b, and Lys(or Arg)-|-Lys bond in
complement component C2 to form C2a and C2b: the 'classical'
pathway C3 convertase.
-!- ENZYME REGULATION: Inhibited by SERPING1. {ECO:0000250}.
-!- SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q,
C1r and C1s in the molar ration of 1:2:2. Activated C1s is an
disulfide-linked heterodimer of a heavy chain and a light chain
(By similarity). {ECO:0000250}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
aspartate and asparagine is (R) stereospecific within EGF domains.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- SEQUENCE CAUTION:
Sequence=AAH62042.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAA25797.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; D88250; BAA25797.1; ALT_INIT; mRNA.
EMBL; BC062042; AAH62042.1; ALT_INIT; mRNA.
PIR; JC6554; JC6554.
RefSeq; NP_620255.1; NM_138900.1.
UniGene; Rn.4037; -.
ProteinModelPortal; Q6P6T1; -.
SMR; Q6P6T1; -.
STRING; 10116.ENSRNOP00000016330; -.
MEROPS; S01.193; -.
iPTMnet; Q6P6T1; -.
PhosphoSitePlus; Q6P6T1; -.
PaxDb; Q6P6T1; -.
PeptideAtlas; Q6P6T1; -.
PRIDE; Q6P6T1; -.
GeneID; 192262; -.
KEGG; rno:192262; -.
UCSC; RGD:619983; rat.
CTD; 716; -.
RGD; 619983; C1s.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
HOGENOM; HOG000237311; -.
HOVERGEN; HBG000559; -.
InParanoid; Q6P6T1; -.
KO; K01331; -.
PhylomeDB; Q6P6T1; -.
PRO; PR:Q6P6T1; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0072562; C:blood microparticle; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005576; C:extracellular region; IDA:RGD.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0004252; F:serine-type endopeptidase activity; ISO:RGD.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0001867; P:complement activation, lectin pathway; IBA:GO_Central.
GO; GO:0010001; P:glial cell differentiation; IEP:RGD.
GO; GO:0051591; P:response to cAMP; IEP:RGD.
CDD; cd00033; CCP; 2.
CDD; cd00041; CUB; 2.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.60.120.290; -; 2.
InterPro; IPR035708; Complement_C1s_subcomponent.
InterPro; IPR000859; CUB_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR035914; Sperma_CUB_dom_sf.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR24255:SF18; PTHR24255:SF18; 1.
Pfam; PF00431; CUB; 2.
Pfam; PF00084; Sushi; 2.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00032; CCP; 2.
SMART; SM00042; CUB; 2.
SMART; SM00179; EGF_CA; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF49854; SSF49854; 2.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57535; SSF57535; 2.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS01180; CUB; 2.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS50923; SUSHI; 2.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
2: Evidence at transcript level;
Calcium; Complement pathway; Complete proteome; Disulfide bond;
EGF-like domain; Glycoprotein; Hydrolase; Hydroxylation; Immunity;
Innate immunity; Metal-binding; Protease; Reference proteome; Repeat;
Serine protease; Signal; Sushi.
SIGNAL 1 15 {ECO:0000250}.
CHAIN 16 688 Complement C1s subcomponent.
/FTId=PRO_0000042202.
CHAIN 16 437 Complement C1s subcomponent heavy chain.
{ECO:0000250}.
/FTId=PRO_0000042203.
CHAIN 438 688 Complement C1s subcomponent light chain.
{ECO:0000250}.
/FTId=PRO_0000042204.
DOMAIN 16 130 CUB 1. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 131 172 EGF-like; calcium-binding. {ECO:0000255}.
DOMAIN 175 290 CUB 2. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 292 356 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 357 423 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 438 680 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 475 475 Charge relay system. {ECO:0000250}.
ACT_SITE 529 529 Charge relay system. {ECO:0000250}.
ACT_SITE 631 631 Charge relay system. {ECO:0000250}.
METAL 60 60 Calcium. {ECO:0000250}.
METAL 68 68 Calcium. {ECO:0000250}.
METAL 113 113 Calcium. {ECO:0000250}.
METAL 131 131 Calcium. {ECO:0000250}.
METAL 132 132 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 134 134 Calcium. {ECO:0000250}.
METAL 149 149 Calcium. {ECO:0000250}.
METAL 150 150 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 153 153 Calcium; via carbonyl oxygen.
{ECO:0000250}.
MOD_RES 149 149 (3R)-3-hydroxyasparagine. {ECO:0000250}.
CARBOHYD 174 174 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 65 83 {ECO:0000250}.
DISULFID 135 147 {ECO:0000250}.
DISULFID 143 156 {ECO:0000250}.
DISULFID 158 171 {ECO:0000250}.
DISULFID 175 202 {ECO:0000250}.
DISULFID 234 251 {ECO:0000250}.
DISULFID 294 341 {ECO:0000250}.
DISULFID 321 354 {ECO:0000250}.
DISULFID 359 403 {ECO:0000250}.
DISULFID 386 421 {ECO:0000250}.
DISULFID 425 549 Interchain (between heavy and light
chains). {ECO:0000255|PROSITE-
ProRule:PRU00059, ECO:0000255|PROSITE-
ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00302}.
DISULFID 595 618 {ECO:0000250}.
DISULFID 627 659 {ECO:0000250}.
CONFLICT 87 87 T -> S (in Ref. 1; BAA25797).
{ECO:0000305}.
CONFLICT 554 554 S -> F (in Ref. 1; BAA25797).
{ECO:0000305}.
CONFLICT 562 562 G -> V (in Ref. 1; BAA25797).
{ECO:0000305}.
CONFLICT 575 575 N -> I (in Ref. 1; BAA25797).
{ECO:0000305}.
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


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