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Protein

Complement C1s-A subcomponent

Gene

C1sa

Organism
Mus musculus (Mouse)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi60 – 601CalciumBy similarity
Metal bindingi68 – 681CalciumBy similarity
Metal bindingi113 – 1131CalciumBy similarity
Metal bindingi131 – 1311CalciumBy similarity
Metal bindingi132 – 1321Calcium; via carbonyl oxygenBy similarity
Metal bindingi134 – 1341CalciumBy similarity
Metal bindingi149 – 1491CalciumBy similarity
Metal bindingi150 – 1501Calcium; via carbonyl oxygenBy similarity
Metal bindingi153 – 1531Calcium; via carbonyl oxygenBy similarity
Active sitei475 – 4751Charge relay systemBy similarity
Active sitei529 – 5291Charge relay systemBy similarity
Active sitei631 – 6311Charge relay systemBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. identical protein binding Source: MGI
  3. serine-type endopeptidase activity Source: MGI

GO - Biological processi

  1. complement activation, classical pathway Source: UniProtKB-KW
  2. innate immune response Source: UniProtKB-KW
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

MEROPSiS01.360.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement C1s-A subcomponent (EC:3.4.21.42)
Alternative name(s):
C1 esterase
Complement component 1 subcomponent s-A
Cleaved into the following 2 chains:
Gene namesi
Name:C1sa
Synonyms:C1s
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1355312. C1s.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: MGI
  2. extracellular vesicular exosome Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515By similarityAdd
BLAST
Chaini16 – 688673Complement C1s-A subcomponentPRO_0000042193Add
BLAST
Chaini16 – 437422Complement C1s-A subcomponent heavy chainBy similarityPRO_0000042194Add
BLAST
Chaini438 – 688251Complement C1s-A subcomponent light chainBy similarityPRO_0000042195Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi65 ↔ 83By similarity
Disulfide bondi135 ↔ 147By similarity
Disulfide bondi143 ↔ 156By similarity
Modified residuei149 – 1491(3R)-3-hydroxyasparagineBy similarity
Disulfide bondi158 ↔ 171By similarity
Glycosylationi174 – 1741N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi175 ↔ 202By similarity
Disulfide bondi234 ↔ 251By similarity
Disulfide bondi294 ↔ 341By similarity
Disulfide bondi321 ↔ 354By similarity
Disulfide bondi359 ↔ 403By similarity
Disulfide bondi386 ↔ 421By similarity
Disulfide bondi425 ↔ 549Interchain (between heavy and light chains)PROSITE-ProRule annotation
Disulfide bondi595 ↔ 618By similarity
Disulfide bondi627 ↔ 659By similarity
Glycosylationi641 – 6411N-linked (GlcNAc...)Sequence Analysis

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

MaxQBiQ8CG14.
PaxDbiQ8CG14.
PRIDEiQ8CG14.

PTM databases

PhosphoSiteiQ8CG14.

Expressioni

Tissue specificityi

Predominantly expressed in liver.1 Publication

Gene expression databases

CleanExiMM_C1S.
GenevestigatoriQ8CG14.

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

Structurei

3D structure databases

ProteinModelPortaliQ8CG14.
SMRiQ8CG14. Positions 17-683.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 130115CUB 1PROSITE-ProRule annotationAdd
BLAST
Domaini131 – 17242EGF-like; calcium-bindingSequence AnalysisAdd
BLAST
Domaini175 – 290116CUB 2PROSITE-ProRule annotationAdd
BLAST
Domaini292 – 35665Sushi 1PROSITE-ProRule annotationAdd
BLAST
Domaini357 – 42367Sushi 2PROSITE-ProRule annotationAdd
BLAST
Domaini438 – 680243Peptidase S1PROSITE-ProRule annotationAdd
BLAST

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

eggNOGiCOG5640.
HOVERGENiHBG000559.
InParanoidiQ8CG14.
KOiK01331.
PhylomeDBiQ8CG14.

Family and domain databases

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.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP_dom.
IPR009003. Trypsin-like_Pept_dom.
[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.

Q8CG14-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWCLVLFSLL ASFSAEPTMH GEILSPNYPQ AYPNDVVKSW DIEVPEGFGI
60 70 80 90 100
HLYFTHVDIE PSESCAYDSV QIISGGIEEG RLCGQKTSKS PNSPIIEEFQ
110 120 130 140 150
FPYNKLQVVF TSDFSNEERF TGFAAYYTAI DINECTDFTD VPCSHFCNNF
160 170 180 190 200
IGGYFCSCPP EYFLHDDMRN CGVNCSGDVF TALIGEISSP NYPNPYPENS
210 220 230 240 250
RCEYQIQLQE GFQVVVTMQR EDFDVEPADS EGNCPDSLTF ASKNQQFGPY
260 270 280 290 300
CGNGFPGPLT IRTQSNTLGI VFQTDLMGQK KGWKLRYHGD PISCAKKITA
310 320 330 340 350
NSTWEPDKAK YVFKDVVKIT CVDGFEVVEG HVSSTSYYST CQSDGQWSNS
360 370 380 390 400
GLKCQPVYCG IPDPIANGKV EEPENSVFGT VVHYTCEEPY YYMEHEEGGE
410 420 430 440 450
YRCAANGRWV NDQLGIELPR CIPACGVPTE PFQVHQRIFG GQPAKIENFP
460 470 480 490 500
WQVFFNHPRA SGALINEYWV LTAAHVLEKI SDPLMYVGTM SVRTTLLENA
510 520 530 540 550
QRLYSKRVFI HPSWKKEDDP NTRTNFDNDI ALVQLKDPVK MGPKVSPICL
560 570 580 590 600
PGTSSEYNVS PGDMGLISGW GSTEKKVFVI NLRGAKVPVT SLETCKQVKE
610 620 630 640 650
ENPTVRPEDY VFTDNMICAG EKGVDSCHGD SGGAFAFQVP NVTVPKFYVA
660 670 680
GLVSWGKRCG TYGVYTKVKN YVDWILKTMQ ENSGPRKD
Length:688
Mass (Da):76,858
Last modified:September 26, 2005 - v2
Checksum:iBAC166C861CB8A25
GO

Sequence cautioni

The sequence BAC39910.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761G → D in AAO15556 (PubMed:12513694).Curated
Sequence conflicti76 – 761G → D in BAC39910 (PubMed:16141072).Curated
Sequence conflicti86 – 861K → R in AAO15556 (PubMed:12513694).Curated
Sequence conflicti86 – 861K → R in BAC39910 (PubMed:16141072).Curated
Sequence conflicti305 – 3051E → Q in AAO15556 (PubMed:12513694).Curated
Sequence conflicti305 – 3051E → Q in BAC39910 (PubMed:16141072).Curated
Sequence conflicti378 – 3781F → L in BAC39910 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF459019 mRNA. Translation: AAO15558.1.
AF459017, AF459015, AF459016 Genomic DNA. Translation: AAO15556.1.
AK087522 mRNA. Translation: BAC39910.1. Different initiation.
BC022123 mRNA. Translation: AAH22123.1.
BC018319 mRNA. Translation: AAH18319.1.
RefSeqiNP_001091086.1. NM_001097617.1.
NP_659187.2. NM_144938.2.
UniGeneiMm.219527.

Genome annotation databases

GeneIDi50908.
KEGGimmu:50908.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF459019 mRNA. Translation: AAO15558.1.
AF459017, AF459015, AF459016 Genomic DNA. Translation: AAO15556.1.
AK087522 mRNA. Translation: BAC39910.1. Different initiation.
BC022123 mRNA. Translation: AAH22123.1.
BC018319 mRNA. Translation: AAH18319.1.
RefSeqiNP_001091086.1. NM_001097617.1.
NP_659187.2. NM_144938.2.
UniGeneiMm.219527.

3D structure databases

ProteinModelPortaliQ8CG14.
SMRiQ8CG14. Positions 17-683.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.360.

PTM databases

PhosphoSiteiQ8CG14.

Proteomic databases

MaxQBiQ8CG14.
PaxDbiQ8CG14.
PRIDEiQ8CG14.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi50908.
KEGGimmu:50908.

Organism-specific databases

CTDi50908.
MGIiMGI:1355312. C1s.

Phylogenomic databases

eggNOGiCOG5640.
HOVERGENiHBG000559.
InParanoidiQ8CG14.
KOiK01331.
PhylomeDBiQ8CG14.

Miscellaneous databases

NextBioi307885.
PROiQ8CG14.
SOURCEiSearch...

Gene expression databases

CleanExiMM_C1S.
GenevestigatoriQ8CG14.

Family and domain databases

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.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP_dom.
IPR009003. Trypsin-like_Pept_dom.
[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...

Publicationsi

« Hide 'large scale' publications
  1. "Complement C1r and C1s genes are duplicated in the mouse: differential expression generates alternative isomorphs in the liver and in the male reproductive system."
    Garnier G., Circolo A., Xu Y., Volanakis J.E.
    Biochem. J. 371:631-640(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
    Strain: 129/SvJ and BALB/c.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Eye.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.

Entry informationi

Entry nameiCS1A_MOUSE
AccessioniPrimary (citable) accession number: Q8CG14
Secondary accession number(s): Q8BJC4, Q8CH28, Q8VBY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2005
Last sequence update: September 26, 2005
Last modified: February 3, 2015
This is version 101 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.