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P21180 (CO2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length760 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processComplement pathway
Immunity
Innate immunity
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Sushi
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcomplement 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_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 760742Complement C2
PRO_0000027613
Chain19 – 250232Complement C2b fragment
PRO_0000027614
Chain251 – 760510Complement C2a fragment
PRO_0000027615

Regions

Domain20 – 9071Sushi 1
Domain92 – 15160Sushi 2
Domain154 – 21259Sushi 3
Domain261 – 459199VWFA
Domain471 – 752282Peptidase S1

Sites

Active site5141Charge relay system By similarity
Active site5701Charge relay system By similarity
Active site6891Charge relay system By similarity

Amino acid modifications

Glycosylation271N-linked (GlcNAc...) Potential
Glycosylation321N-linked (GlcNAc...) Potential
Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation3401N-linked (GlcNAc...) Potential
Glycosylation4741N-linked (GlcNAc...) Potential
Glycosylation4781N-linked (GlcNAc...) Potential
Glycosylation6631N-linked (GlcNAc...) Potential
Disulfide bond22 ↔ 62 By similarity
Disulfide bond49 ↔ 89 By similarity
Disulfide bond94 ↔ 136 By similarity
Disulfide bond122 ↔ 149 By similarity
Disulfide bond156 ↔ 197 By similarity
Disulfide bond182 ↔ 210 By similarity
Disulfide bond499 ↔ 515 By similarity
Disulfide bond685 ↔ 715 By similarity

Natural variations

Alternative sequence606 – 6127Missing in isoform Short.
VSP_005385

Experimental info

Sequence conflict123 – 1242EQ → DE in AAA37380. Ref.1
Sequence conflict123 – 1242EQ → DE in AAA37381. Ref.1
Sequence conflict123 – 1242EQ → DE in AAA63294. Ref.1
Sequence conflict2991S → T in AAA37380. Ref.1
Sequence conflict2991S → T in AAA37381. Ref.1
Sequence conflict2991S → T in AAA63294. Ref.1
Sequence conflict3441T → A in AAA37380. Ref.1
Sequence conflict3441T → A in AAA37381. Ref.1
Sequence conflict3441T → A in AAA63294. Ref.1
Sequence conflict3591S → T in AAA37380. Ref.1
Sequence conflict3591S → T in AAA37381. Ref.1
Sequence conflict3591S → T in AAA63294. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 91C896A3EDC7D448

FASTA76084,741
        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 

« Hide

Isoform Short [UniParc].

Checksum: C997F5CBA3A12278
Show »

FASTA75384,013

References

« Hide '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. 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: 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. expand/collapse author list , 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 expand/collapse EMBL AC list , M60563, M60564, M60565, M60566, M60567, M60568, M60569, M60570, M60571, M60572, M60573, M60574, M60575, M60605, M60576, M60577, M60578 Genomic DNA. Translation: AAA37380.1.
M60579 expand/collapse EMBL AC list , 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.
PIRC2MS. A38876.
RefSeqNP_038512.2. NM_013484.2.
UniGeneMm.283217.

3D structure databases

ProteinModelPortalP21180.
SMRP21180. Positions 22-223, 251-760.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.194.

PTM databases

PhosphoSiteP21180.

Proteomic databases

PRIDEP21180.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025230; ENSMUSP00000025230; ENSMUSG00000024371. [P21180-1]
GeneID12263.
KEGGmmu:12263.
UCSCuc008cdz.2. mouse. [P21180-1]

Organism-specific databases

CTD717.
MGIMGI:88226. C2.

Phylogenomic databases

GeneTreeENSGT00530000063826.
HOGENOMHOG000038034.
HOVERGENHBG002567.
InParanoidO70350.
KOK01332.
OMARDMTEVI.
TreeFamTF330194.

Gene expression databases

ArrayExpressP21180.
BgeeP21180.
CleanExMM_C2.
GenevestigatorP21180.

Family and domain databases

Gene3D3.40.50.410. 1 hit.
InterProIPR011360. 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]
PfamPF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
PIRSFPIRSF001154. Compl_C2_B. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00032. CCP. 2 hits.
SM00020. Tryp_SPc. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF57535. SSF57535. 3 hits.
PROSITEPS50923. SUSHI. 3 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSC2. mouse.
NextBio280706.
PROP21180.
SOURCESearch...

Entry information

Entry nameCO2_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 126 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