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Protein

Complement C1s subcomponent

Gene

C1s

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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 regulationi

Inhibited by SERPING1.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi60CalciumBy similarity1
Metal bindingi68CalciumBy similarity1
Metal bindingi113CalciumBy similarity1
Metal bindingi131CalciumBy similarity1
Metal bindingi132Calcium; via carbonyl oxygenBy similarity1
Metal bindingi134CalciumBy similarity1
Metal bindingi149CalciumBy similarity1
Metal bindingi150Calcium; via carbonyl oxygenBy similarity1
Metal bindingi153Calcium; via carbonyl oxygenBy similarity1
Active sitei475Charge relay systemBy similarity1
Active sitei529Charge relay systemBy similarity1
Active sitei631Charge relay systemBy similarity1

GO - Molecular functioni

GO - Biological processi

  • complement activation, classical pathway Source: UniProtKB-KW
  • glial cell differentiation Source: RGD
  • innate immune response Source: UniProtKB-KW
  • response to cAMP Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Complement pathway, Immunity, Innate immunity

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

MEROPSiS01.193.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement C1s subcomponent (EC:3.4.21.42)
Alternative name(s):
C1 esterase
Complement component 1 subcomponent s
Cleaved into the following 2 chains:
Gene namesi
Name:C1s
Synonyms:r-gsp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619983. C1s.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 15By similarityAdd BLAST15
ChainiPRO_000004220216 – 688Complement C1s subcomponentAdd BLAST673
ChainiPRO_000004220316 – 437Complement C1s subcomponent heavy chainBy similarityAdd BLAST422
ChainiPRO_0000042204438 – 688Complement C1s subcomponent light chainBy similarityAdd BLAST251

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi65 ↔ 83By similarity
Disulfide bondi135 ↔ 147By similarity
Disulfide bondi143 ↔ 156By similarity
Modified residuei149(3R)-3-hydroxyasparagineBy similarity1
Disulfide bondi158 ↔ 171By similarity
Glycosylationi174N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi175 ↔ 202By similarity
Disulfide bondi234 ↔ 251By similarity
Disulfide bondi294 ↔ 341By similarity
Disulfide bondi321 ↔ 354By similarity
Disulfide bondi359 ↔ 403By similarity
Disulfide bondi386 ↔ 421By similarity
Glycosylationi406N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi425 ↔ 549Interchain (between heavy and light chains)PROSITE-ProRule annotation
Disulfide bondi595 ↔ 618By similarity
Disulfide bondi627 ↔ 659By similarity

Post-translational modificationi

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiQ6P6T1.
PeptideAtlasiQ6P6T1.
PRIDEiQ6P6T1.

PTM databases

iPTMnetiQ6P6T1.
PhosphoSitePlusiQ6P6T1.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016330.

Structurei

3D structure databases

ProteinModelPortaliQ6P6T1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 130CUB 1PROSITE-ProRule annotationAdd BLAST115
Domaini131 – 172EGF-like; calcium-bindingSequence analysisAdd BLAST42
Domaini175 – 290CUB 2PROSITE-ProRule annotationAdd BLAST116
Domaini292 – 356Sushi 1PROSITE-ProRule annotationAdd BLAST65
Domaini357 – 423Sushi 2PROSITE-ProRule annotationAdd BLAST67
Domaini438 – 680Peptidase S1PROSITE-ProRule annotationAdd BLAST243

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 CUB domains.PROSITE-ProRule annotation
Contains 1 EGF-like domain.Curated
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
Contains 2 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000237311.
HOVERGENiHBG000559.
InParanoidiQ6P6T1.
KOiK01331.
PhylomeDBiQ6P6T1.

Family and domain databases

CDDicd00033. CCP. 2 hits.
cd00041. CUB. 2 hits.
cd00190. Tryp_SPc. 1 hit.
Gene3Di2.60.120.290. 2 hits.
InterProiIPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024175. Pept_S1A_C1r/C1S/mannan-bd.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP_dom.
IPR001254. Trypsin_dom.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001155. C1r_C1s_MASP. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS01180. CUB. 2 hits.
PS01187. EGF_CA. 1 hit.
PS50923. SUSHI. 2 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6P6T1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWCFVFFSLL ASFSAEPTMY GEILSPNYPQ AYPNEVVKTW DIEVPEGFGI
60 70 80 90 100
HLYFTHLDME LSENCAYDSV QIISGGIEEE RLCGQRTSKS PNSPTVEEFQ
110 120 130 140 150
FPYNRLQVVF TSDFSNEERF TGFAAYYSAV DVNECTDFTD VPCSHFCNNF
160 170 180 190 200
IGGYFCSCPP EYFLHDDMRT CGVNCSGDVF TALIGEIASP NYPNPYPENS
210 220 230 240 250
RCEYQIRLQE GFRLVLTIRR EDFDVEPADS EGNCHDSLTF AAKNQQFGPY
260 270 280 290 300
CGNGFPGPLT IKTQSNTLDI VFQTDLTGQN KGWKLRYHGD PIPCPKEISA
310 320 330 340 350
NSIWEPEKAK YVFKDVVKIT CVDGFEVVEG NVGSTSFYST CQSNGQWSNS
360 370 380 390 400
RLECQPVDCG VPEPIENGKV EDPEDTVFGS VIHYTCEEPY YYMEQEEGGE
410 420 430 440 450
YHCAANGSWV NDQLGVELPK CIPVCGVPTE PFKVQQRIFG GYSTKIQSFP
460 470 480 490 500
WQVYFESPRG GGALIDEYWV LTAAHVVEGN SDPVMYVGST LLKIERLRNA
510 520 530 540 550
QRLITERVII HPSWKQEDDL NTRTNFDNDI ALVQLKDPVK MGPTVAPICL
560 570 580 590 600
PETSSDYNPS EGDLGLISGW GRTENRTNVI QLRGAKLPIT SLEKCQQVKV
610 620 630 640 650
ENPKARSNDY VFTDNMICAG EKGVDSCEGD SGGAFALPVP NVKDPKFYVA
660 670 680
GLVSWGKKCG TYGIYTKVKN YVDWILKTMQ ENSGPKKD
Length:688
Mass (Da):77,071
Last modified:September 27, 2005 - v2
Checksum:iB69C43027AE7A85F
GO

Sequence cautioni

The sequence AAH62042 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA25797 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti87T → S in BAA25797 (PubMed:9524231).Curated1
Sequence conflicti554S → F in BAA25797 (PubMed:9524231).Curated1
Sequence conflicti562G → V in BAA25797 (PubMed:9524231).Curated1
Sequence conflicti575N → I in BAA25797 (PubMed:9524231).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88250 mRNA. Translation: BAA25797.1. Different initiation.
BC062042 mRNA. Translation: AAH62042.1. Different initiation.
PIRiJC6554.
RefSeqiNP_620255.1. NM_138900.1.
UniGeneiRn.4037.

Genome annotation databases

GeneIDi192262.
KEGGirno:192262.
UCSCiRGD:619983. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88250 mRNA. Translation: BAA25797.1. Different initiation.
BC062042 mRNA. Translation: AAH62042.1. Different initiation.
PIRiJC6554.
RefSeqiNP_620255.1. NM_138900.1.
UniGeneiRn.4037.

3D structure databases

ProteinModelPortaliQ6P6T1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016330.

Protein family/group databases

MEROPSiS01.193.

PTM databases

iPTMnetiQ6P6T1.
PhosphoSitePlusiQ6P6T1.

Proteomic databases

PaxDbiQ6P6T1.
PeptideAtlasiQ6P6T1.
PRIDEiQ6P6T1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi192262.
KEGGirno:192262.
UCSCiRGD:619983. rat.

Organism-specific databases

CTDi716.
RGDi619983. C1s.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000237311.
HOVERGENiHBG000559.
InParanoidiQ6P6T1.
KOiK01331.
PhylomeDBiQ6P6T1.

Miscellaneous databases

PROiQ6P6T1.

Family and domain databases

CDDicd00033. CCP. 2 hits.
cd00041. CUB. 2 hits.
cd00190. Tryp_SPc. 1 hit.
Gene3Di2.60.120.290. 2 hits.
InterProiIPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024175. Pept_S1A_C1r/C1S/mannan-bd.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP_dom.
IPR001254. Trypsin_dom.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001155. C1r_C1s_MASP. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS01180. CUB. 2 hits.
PS01187. EGF_CA. 1 hit.
PS50923. SUSHI. 2 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiC1S_RAT
AccessioniPrimary (citable) accession number: Q6P6T1
Secondary accession number(s): O70542, Q8R099
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: September 27, 2005
Last modified: November 30, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.