P21180 (CO2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Complement C2
EC=3.4.21.43

Alternative name(s):
C3/C5 convertase

Cleaved into the following 2 chains:

1. Complement C2b fragment
2. Complement C2a fragment

Gene names

Name:

C2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	760 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	Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments: C2b and C2a. C2a, a serine protease, then combines with complement factor 4b to generate the C3 or C5 convertase.
Catalytic activity	Selective cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to form C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to form C5a and C5b.
Subcellular location	Secreted.
Miscellaneous	C2 is a major histocompatibility complex class-III protein.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain. Contains 3 Sushi (CCP/SCR) domains. Contains 1 VWFA domain.

Ontologies

Keywords
Biological process	Complement pathway Immunity Innate immunity
Cellular component	Secreted
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal Sushi
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
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: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P21180-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: P21180-2)

The sequence of this isoform differs from the canonical sequence as follows:
     606-612: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18
	Chain	19 – 760	742	Complement C2		PRO_0000027613
	Chain	19 – 250	232	Complement C2b fragment		PRO_0000027614
	Chain	251 – 760	510	Complement C2a fragment		PRO_0000027615
Regions
	Domain	20 – 90	71	Sushi 1
	Domain	92 – 151	60	Sushi 2
	Domain	154 – 212	59	Sushi 3
	Domain	261 – 459	199	VWFA
	Domain	471 – 752	282	Peptidase S1
Sites
	Active site	514	1	Charge relay system By similarity
	Active site	570	1	Charge relay system By similarity
	Active site	689	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	27	1	N-linked (GlcNAc...) Potential
	Glycosylation	32	1	N-linked (GlcNAc...) Potential
	Glycosylation	117	1	N-linked (GlcNAc...) Potential
	Glycosylation	297	1	N-linked (GlcNAc...) Potential
	Glycosylation	340	1	N-linked (GlcNAc...) Potential
	Glycosylation	474	1	N-linked (GlcNAc...) Potential
	Glycosylation	478	1	N-linked (GlcNAc...) Potential
	Glycosylation	663	1	N-linked (GlcNAc...) Potential
	Disulfide bond	22 ↔ 62		By similarity
	Disulfide bond	49 ↔ 89		By similarity
	Disulfide bond	94 ↔ 136		By similarity
	Disulfide bond	122 ↔ 149		By similarity
	Disulfide bond	156 ↔ 197		By similarity
	Disulfide bond	182 ↔ 210		By similarity
	Disulfide bond	499 ↔ 515		By similarity
	Disulfide bond	685 ↔ 715		By similarity
Natural variations
	Alternative sequence	606 – 612	7	Missing in isoform Short.		VSP_005385
Experimental info
	Sequence conflict	123 – 124	2	EQ → DE in AAA37380. Ref.1
	Sequence conflict	123 – 124	2	EQ → DE in AAA37381. Ref.1
	Sequence conflict	123 – 124	2	EQ → DE in AAA63294. Ref.1
	Sequence conflict	299	1	S → T in AAA37380. Ref.1
	Sequence conflict	299	1	S → T in AAA37381. Ref.1
	Sequence conflict	299	1	S → T in AAA63294. Ref.1
	Sequence conflict	344	1	T → A in AAA37380. Ref.1
	Sequence conflict	344	1	T → A in AAA37381. Ref.1
	Sequence conflict	344	1	T → A in AAA63294. Ref.1
	Sequence conflict	359	1	S → T in AAA37380. Ref.1
	Sequence conflict	359	1	S → T in AAA37381. Ref.1
	Sequence conflict	359	1	S → T in AAA63294. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 91C896A3EDC7D448	FASTA	760	84,741
	10 20 30 40 50 60 MAPLLALFYL LQLGPGLAAL FCNQNVNITG GNFTLSHGWA PGSLLIYSCP LGRYPSPAWR 70 80 90 100 110 120 KCQSNGQWLT PRSSSHHTLR SSRMVKAVCK PVRCLAPSSF ENGIYFPRLV SYPVGSNVSF 130 140 150 160 170 180 ECEQDFTLRG SPVRYCRPNG LWDGETAVCD NGASHCPNPG ISVGTARTGL NFDLGDKVRY 190 200 210 220 230 240 RCSSSNMVLT GSAERECQSN GVWSGSEPIC RQPYSYDFPE DVASALDTSL TNLLGATNPT 250 260 270 280 290 300 QNLLTKSLGR KIIIQRSGHL NLYLLLDASQ SVTEKDFDIF KKSAELMVER IFSFEVNVSV 310 320 330 340 350 360 AIITFASQPK TIMSILSERS QDVTEVITSL DSASYKDHEN ATGTNTYEVL IRVYSMMQSQ 370 380 390 400 410 420 MDRLGMETSA WKEIRHTIIL LTDGKSNMGD SPKKAVTRIR ELLSIEQNRD DYLDIYAIGV 430 440 450 460 470 480 GKLDVDWKEL NELGSKKDGE RHAFILQDAK ALQQIFEHML DVSKLTDTIC GVGNMSANAS 490 500 510 520 530 540 DQERTPWQVT FKPKSKETCQ GSLISDQWVL TAAHCFHDIQ MEDHHLWRVN VGDPTSQHGK 550 560 570 580 590 600 EFLVEDVIIA PGFNVHAKRK QGISEFYADD IALLKLSRKV KMSTHARPIC LPCTVGANMA 610 620 630 640 650 660 LRRSPGSTCK DHETELLSQQ KVPAHFVALN GNRLNINLRT GPEWTRCIQA VSQNKNIFPS 670 680 690 700 710 720 LTNVSEVVTD QFLCSGMEEE DDNPCKGESG GAVFLGRRYR FFQVGLVSWG LFDPCHGSSN 730 740 750 760 KNLRKKPPRG VLPRDFHISL FRLQPWLRQH LDGVLDFLPL
	Isoform Short [UniParc]. Checksum: C997F5CBA3A12278	FASTA	753	84,013
	10 20 30 40 50 60 MAPLLALFYL LQLGPGLAAL FCNQNVNITG GNFTLSHGWA PGSLLIYSCP LGRYPSPAWR 70 80 90 100 110 120 KCQSNGQWLT PRSSSHHTLR SSRMVKAVCK PVRCLAPSSF ENGIYFPRLV SYPVGSNVSF 130 140 150 160 170 180 ECEQDFTLRG SPVRYCRPNG LWDGETAVCD NGASHCPNPG ISVGTARTGL NFDLGDKVRY 190 200 210 220 230 240 RCSSSNMVLT GSAERECQSN GVWSGSEPIC RQPYSYDFPE DVASALDTSL TNLLGATNPT 250 260 270 280 290 300 QNLLTKSLGR KIIIQRSGHL NLYLLLDASQ SVTEKDFDIF KKSAELMVER IFSFEVNVSV 310 320 330 340 350 360 AIITFASQPK TIMSILSERS QDVTEVITSL DSASYKDHEN ATGTNTYEVL IRVYSMMQSQ 370 380 390 400 410 420 MDRLGMETSA WKEIRHTIIL LTDGKSNMGD SPKKAVTRIR ELLSIEQNRD DYLDIYAIGV 430 440 450 460 470 480 GKLDVDWKEL NELGSKKDGE RHAFILQDAK ALQQIFEHML DVSKLTDTIC GVGNMSANAS 490 500 510 520 530 540 DQERTPWQVT FKPKSKETCQ GSLISDQWVL TAAHCFHDIQ MEDHHLWRVN VGDPTSQHGK 550 560 570 580 590 600 EFLVEDVIIA PGFNVHAKRK QGISEFYADD IALLKLSRKV KMSTHARPIC LPCTVGANMA 610 620 630 640 650 660 LRRSPETELL SQQKVPAHFV ALNGNRLNIN LRTGPEWTRC IQAVSQNKNI FPSLTNVSEV 670 680 690 700 710 720 VTDQFLCSGM EEEDDNPCKG ESGGAVFLGR RYRFFQVGLV SWGLFDPCHG SSNKNLRKKP 730 740 750 PRGVLPRDFH ISLFRLQPWL RQHLDGVLDF LPL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Murine complement C2 and factor B genomic and cDNA cloning reveals different mechanisms for multiple transcripts of C2 and B." Ishikawa N., Nonaka M., Wetsel R.A., Colten H.R. J. Biol. Chem. 265:19040-19046(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS LONG AND SHORT).
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Amnion.
[3]	"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse." Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L. Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 129.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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]. Tissue: Mammary tumor.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M57891 mRNA. Translation: AAA63294.1. M60579 , M60563, M60564, M60565, M60566, M60567, M60568, M60569, M60570, M60571, M60572, M60573, M60574, M60575, M60605, M60576, M60577, M60578 Genomic DNA. Translation: AAA37380.1. M60579 , M60563, M60564, M60565, M60566, M60567, M60568, M60569, M60570, M60571, M60572, M60573, M60574, M60575, M60605, M60576, M60577, M60578 Genomic DNA. Translation: AAA37381.1. AK146812 mRNA. Translation: BAE27452.1. AF109906 Genomic DNA. Translation: AAC84162.1. CT025759 Genomic DNA. Translation: CAX15332.1. CH466666 Genomic DNA. Translation: EDL26734.1. BC011086 mRNA. Translation: AAH11086.1.
IPI	IPI00120192. IPI00222163.
PIR	C2MS. A38876.
RefSeq	NP_038512.2. NM_013484.2.
UniGene	Mm.283217.
3D structure databases
ProteinModelPortal	P21180.
SMR	P21180. Positions 22-223, 251-760.
ModBase	Search...
Protein family/group databases
MEROPS	S01.194.
PTM databases
PhosphoSite	P21180.
Proteomic databases
PRIDE	P21180.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000025230; ENSMUSP00000025230; ENSMUSG00000024371.
GeneID	12263.
KEGG	mmu:12263.
Organism-specific databases
CTD	717.
MGI	MGI:88226. C2.
Phylogenomic databases
GeneTree	ENSGT00530000063826.
HOGENOM	HOG000038034.
HOVERGEN	HBG002567.
InParanoid	O70350.
KO	K01332.
OMA	RDMTEVI.
Gene expression databases
ArrayExpress	P21180.
Bgee	P21180.
CleanEx	MM_C2.
Genevestigator	P21180.
GermOnline	ENSMUSG00000024372. Mus musculus.
Family and domain databases
InterPro	IPR011360. Compl_C2_B. IPR001254. Peptidase_S1. IPR018114. Peptidase_S1_AS. IPR001314. Peptidase_S1A. IPR000436. Sushi_SCR_CCP. IPR009003. Trypsin-like_Pept_dom. IPR002035. VWF_A. [Graphical view]
Pfam	PF00084. Sushi. 2 hits. PF00089. Trypsin. 1 hit. PF00092. VWA. 1 hit. [Graphical view]
PIRSF	PIRSF001154. Compl_C2_B. 1 hit.
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00032. CCP. 2 hits. SM00020. Tryp_SPc. 1 hit. SM00327. VWA. 1 hit. [Graphical view]
SUPFAM	SSF57535. Complement_control_module. 2 hits. SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS50923. SUSHI. 3 hits. PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. PS50234. VWFA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	C2. mouse.
NextBio	280706.
SOURCE	Search...

Entry information

Entry name

CO2_MOUSE

Accession

Primary (citable) accession number: P21180
Secondary accession number(s): O70350

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program