Reviewed, UniProtKB/Swiss-Prot Q8CG14 (CS1A_MOUSE)

Names and origin

Protein names

Recommended name:
    Complement C1s-A subcomponent
    EC=3.4.21.42
Alternative name(s):
    C1 esterase
Cleaved into the following 2 chains:
    1- Recommended name:
            Complement C1s-A subcomponent heavy chain
    2- Recommended name:
            Complement C1s-A subcomponent light chain

Gene names

Name:	C1sa
Synonyms:	C1s

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	688 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	C1s B chain is a serine protease that combines with C1q and C1s 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.

Ontologies

Keywords
Biological process	Complement pathway Immune response Innate immunity
Domain	EGF-like domain Repeat Signal Sushi
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Hydroxylation
Gene Ontology (GO)
Biological process	complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 15	15	By similarity
	Chain	16 – 688	673	Complement C1s-A subcomponent		PRO_0000042193
	Chain	16 – 437	422	Complement C1s-A subcomponent heavy chain By similarity		PRO_0000042194
	Chain	438 – 688	251	Complement C1s-A subcomponent light chain By similarity		PRO_0000042195
Regions
	Domain	16 – 130	115	CUB 1
	Domain	131 – 172	42	EGF-like; calcium-binding Potential
	Domain	175 – 290	116	CUB 2
	Domain	292 – 356	65	Sushi 1
	Domain	357 – 423	67	Sushi 2
	Domain	438 – 680	243	Peptidase S1
Sites
	Active site	475	1	Charge relay system By similarity
	Active site	529	1	Charge relay system By similarity
	Active site	631	1	Charge relay system By similarity
	Metal binding	60	1	Calcium By similarity
	Metal binding	68	1	Calcium By similarity
	Metal binding	113	1	Calcium By similarity
	Metal binding	131	1	Calcium By similarity
	Metal binding	132	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	134	1	Calcium By similarity
	Metal binding	149	1	Calcium By similarity
	Metal binding	150	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	153	1	Calcium; via carbonyl oxygen By similarity
Amino acid modifications
	Modified residue	149	1	(3R)-3-hydroxyasparagine By similarity
	Glycosylation	174	1	N-linked (GlcNAc...) Potential
	Glycosylation	641	1	N-linked (GlcNAc...) Potential
	Disulfide bond	65 ↔ 83		By similarity
	Disulfide bond	135 ↔ 147		By similarity
	Disulfide bond	143 ↔ 156		By similarity
	Disulfide bond	158 ↔ 171		By similarity
	Disulfide bond	175 ↔ 202		By similarity
	Disulfide bond	234 ↔ 251		By similarity
	Disulfide bond	294 ↔ 341		By similarity
	Disulfide bond	321 ↔ 354		By similarity
	Disulfide bond	359 ↔ 403		By similarity
	Disulfide bond	386 ↔ 421		By similarity
	Disulfide bond	425 ↔ 549		Interchain (between heavy and light chains) By similarity
	Disulfide bond	595 ↔ 618		By similarity
	Disulfide bond	627 ↔ 659		By similarity
Experimental info
	Sequence conflict	76	1	G → D in AAO15556. Ref.1
	Sequence conflict	76	1	G → D in BAC39910. Ref.2
	Sequence conflict	86	1	K → R in AAO15556. Ref.1
	Sequence conflict	86	1	K → R in BAC39910. Ref.2
	Sequence conflict	305	1	E → Q in AAO15556. Ref.1
	Sequence conflict	305	1	E → Q in BAC39910. Ref.2
	Sequence conflict	378	1	F → L in BAC39910. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8CG14-1 [UniParc]. Last modified September 27, 2005. Version 2. Checksum: BAC166C861CB8A25	FASTA	688	76,858
	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

References

	« Hide 'large scale' referencesShow '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: 12513694] [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(2005) [PubMed: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00653675.
RefSeq	NP_001091086.1. NP_659187.2.
UniGene	Mm.219527
3D structure databases
HSSP	HSSP built from PDB template 1NZI based on UniProtKB Q9UCV4.
SMR	Q8CG14. Positions 18-174.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8CG14.
Protein family/group databases
MEROPS	S01.360.
PTM databases
PhosphoSite	Q8CG14.
Proteomic databases
PRIDE	Q8CG14.
Genome annotation databases
Ensembl	ENSMUST00000077416; ENSMUSP00000076632; ENSMUSG00000038521; Mus musculus. [Genome view]
GeneID	50908.
KEGG	mmu:50908.
UCSC	uc009drb.1. mouse.
Organism-specific databases
CTD	50908.
MGI	MGI:1355312. C1s.
Phylogenomic databases
HOGENOM	Q8CG14.
HOVERGEN	Q8CG14.
Enzyme and pathway databases
BRENDA	3.4.21.42. 244.
Gene expression databases
ArrayExpress	Q8CG14.
Bgee	Q8CG14.
CleanEx	MM_C1S.
Genevestigator	Q8CG14.
GermOnline	ENSMUSG00000038521. Mus musculus.
Family and domain databases
InterPro	IPR016060. Complement_control_module. IPR000859. CUB. IPR006209. EGF. IPR013032. EGF-like_reg_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR001881. EGF_Ca_bd. IPR018097. EGF_Ca_bd_CS. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. IPR000436. Sushi_SCR_CCP. [Graphical view]
Gene3D	G3DSA:2.10.70.10. Complement_control_module. 1 hit. G3DSA:2.60.120.290. CUB. 2 hits.
Pfam	PF00431. CUB. 2 hits. PF00008. EGF. 1 hit. PF00084. Sushi. 2 hits. PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00032. CCP. 2 hits. SM00042. CUB. 2 hits. SM00179. EGF_CA. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS00010. ASX_HYDROXYL. 1 hit. PS01180. CUB. 2 hits. PS00022. EGF_1. False negative. PS01186. EGF_2. False negative. PS50026. EGF_3. False negative. PS01187. EGF_CA. 1 hit. PS50923. SUSHI. 2 hits. PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. False negative. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	307885.
SOURCE	Search...

Entry information

Entry name

CS1A_MOUSE

Accession

Primary (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:	October 13, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)