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Q8CG14 (CS1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Complement C1s-A subcomponent

EC=3.4.21.42
Alternative name(s):
C1 esterase
Complement component 1 subcomponent s-A
Gene names
Name:C1sa
Synonyms:C1s
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length688 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

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 By similarity.

Subunit structure

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.

Tissue specificity

Predominantly expressed in liver. Ref.1

Post-translational modification

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

Sequence similarities

Belongs to the peptidase S1 family.

Contains 2 CUB domains.

Contains 1 EGF-like domain.

Contains 1 peptidase S1 domain.

Contains 2 Sushi (CCP/SCR) domains.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 By similarity
Chain16 – 688673Complement C1s-A subcomponent
PRO_0000042193
Chain16 – 437422Complement C1s-A subcomponent heavy chain By similarity
PRO_0000042194
Chain438 – 688251Complement C1s-A subcomponent light chain By similarity
PRO_0000042195

Regions

Domain16 – 130115CUB 1
Domain131 – 17242EGF-like; calcium-binding Potential
Domain175 – 290116CUB 2
Domain292 – 35665Sushi 1
Domain357 – 42367Sushi 2
Domain438 – 680243Peptidase S1

Sites

Active site4751Charge relay system By similarity
Active site5291Charge relay system By similarity
Active site6311Charge relay system By similarity
Metal binding601Calcium By similarity
Metal binding681Calcium By similarity
Metal binding1131Calcium By similarity
Metal binding1311Calcium By similarity
Metal binding1321Calcium; via carbonyl oxygen By similarity
Metal binding1341Calcium By similarity
Metal binding1491Calcium By similarity
Metal binding1501Calcium; via carbonyl oxygen By similarity
Metal binding1531Calcium; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue1491(3R)-3-hydroxyasparagine By similarity
Glycosylation1741N-linked (GlcNAc...) Potential
Glycosylation6411N-linked (GlcNAc...) Potential
Disulfide bond65 ↔ 83 By similarity
Disulfide bond135 ↔ 147 By similarity
Disulfide bond143 ↔ 156 By similarity
Disulfide bond158 ↔ 171 By similarity
Disulfide bond175 ↔ 202 By similarity
Disulfide bond234 ↔ 251 By similarity
Disulfide bond294 ↔ 341 By similarity
Disulfide bond321 ↔ 354 By similarity
Disulfide bond359 ↔ 403 By similarity
Disulfide bond386 ↔ 421 By similarity
Disulfide bond425 ↔ 549Interchain (between heavy and light chains) By similarity
Disulfide bond595 ↔ 618 By similarity
Disulfide bond627 ↔ 659 By similarity

Experimental info

Sequence conflict761G → D in AAO15556. Ref.1
Sequence conflict761G → D in BAC39910. Ref.2
Sequence conflict861K → R in AAO15556. Ref.1
Sequence conflict861K → R in BAC39910. Ref.2
Sequence conflict3051E → Q in AAO15556. Ref.1
Sequence conflict3051E → Q in BAC39910. Ref.2
Sequence conflict3781F → L in BAC39910. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8CG14 [UniParc].

Last modified September 27, 2005. Version 2.
Checksum: BAC166C861CB8A25

FASTA68876,858
        10         20         30         40         50         60 
MWCLVLFSLL ASFSAEPTMH GEILSPNYPQ AYPNDVVKSW DIEVPEGFGI HLYFTHVDIE 

        70         80         90        100        110        120 
PSESCAYDSV QIISGGIEEG RLCGQKTSKS PNSPIIEEFQ FPYNKLQVVF TSDFSNEERF 

       130        140        150        160        170        180 
TGFAAYYTAI DINECTDFTD VPCSHFCNNF IGGYFCSCPP EYFLHDDMRN CGVNCSGDVF 

       190        200        210        220        230        240 
TALIGEISSP NYPNPYPENS RCEYQIQLQE GFQVVVTMQR EDFDVEPADS EGNCPDSLTF 

       250        260        270        280        290        300 
ASKNQQFGPY CGNGFPGPLT IRTQSNTLGI VFQTDLMGQK KGWKLRYHGD PISCAKKITA 

       310        320        330        340        350        360 
NSTWEPDKAK YVFKDVVKIT CVDGFEVVEG HVSSTSYYST CQSDGQWSNS GLKCQPVYCG 

       370        380        390        400        410        420 
IPDPIANGKV EEPENSVFGT VVHYTCEEPY YYMEHEEGGE YRCAANGRWV NDQLGIELPR 

       430        440        450        460        470        480 
CIPACGVPTE PFQVHQRIFG GQPAKIENFP WQVFFNHPRA SGALINEYWV LTAAHVLEKI 

       490        500        510        520        530        540 
SDPLMYVGTM SVRTTLLENA QRLYSKRVFI HPSWKKEDDP NTRTNFDNDI ALVQLKDPVK 

       550        560        570        580        590        600 
MGPKVSPICL PGTSSEYNVS PGDMGLISGW GSTEKKVFVI NLRGAKVPVT SLETCKQVKE 

       610        620        630        640        650        660 
ENPTVRPEDY VFTDNMICAG EKGVDSCHGD SGGAFAFQVP NVTVPKFYVA GLVSWGKRCG 

       670        680 
TYGVYTKVKN YVDWILKTMQ ENSGPRKD 

« Hide

References

« Hide 'large scale' references
[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(2003) [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. expand/collapse author list , 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(2005) [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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001091086.1. NM_001097617.1.
NP_659187.2. NM_144938.2.
UniGeneMm.219527.

3D structure databases

ProteinModelPortalQ8CG14.
SMRQ8CG14. Positions 17-683.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.360.

PTM databases

PhosphoSiteQ8CG14.

Proteomic databases

PaxDbQ8CG14.
PRIDEQ8CG14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID50908.
KEGGmmu:50908.

Organism-specific databases

CTD716.
MGIMGI:1355312. C1s.

Phylogenomic databases

eggNOGCOG5640.
HOVERGENHBG000559.
InParanoidQ8CG14.
KOK01331.

Gene expression databases

CleanExMM_C1S.
GenevestigatorQ8CG14.

Family and domain databases

Gene3D2.60.120.290. 2 hits.
InterProIPR000859. 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.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00431. CUB. 2 hits.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001155. C1r_C1s_MASP. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

NextBio307885.
PROQ8CG14.
SOURCESearch...

Entry information

Entry nameCS1A_MOUSE
AccessionPrimary (citable) accession number: Q8CG14
Secondary accession number(s): Q8BJC4, Q8CH28, Q8VBY4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: September 27, 2005
Last modified: March 19, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot