Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P21180

- CO2_MOUSE

UniProt

P21180 - CO2_MOUSE

Protein

Complement C2

Gene

C2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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 C4b to generate the C3 or C5 convertase.

    Catalytic activityi

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi269 – 2691Divalent metal cationBy similarity
    Metal bindingi271 – 2711Divalent metal cationBy similarity
    Metal bindingi344 – 3441Divalent metal cationBy similarity
    Active sitei514 – 5141Charge relay systemBy similarity
    Active sitei570 – 5701Charge relay systemBy similarity
    Active sitei689 – 6891Charge relay systemBy similarity

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Complement pathway, Immunity, Innate immunity

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_198562. Regulation of Complement cascade.
    REACT_202834. Initial triggering of complement.
    REACT_213087. Activation of C3 and C5.

    Protein family/group databases

    MEROPSiS01.194.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Complement C2 (EC:3.4.21.43)
    Alternative name(s):
    C3/C5 convertase
    Cleaved into the following 2 chains:
    Gene namesi
    Name:C2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:88226. C2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Add
    BLAST
    Chaini19 – 760742Complement C2PRO_0000027613Add
    BLAST
    Chaini19 – 250232Complement C2b fragmentPRO_0000027614Add
    BLAST
    Chaini251 – 760510Complement C2a fragmentPRO_0000027615Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi22 ↔ 62By similarity
    Glycosylationi27 – 271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi32 – 321N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi49 ↔ 89By similarity
    Disulfide bondi94 ↔ 136By similarity
    Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi122 ↔ 149By similarity
    Disulfide bondi156 ↔ 197By similarity
    Disulfide bondi182 ↔ 210By similarity
    Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi474 – 4741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi478 – 4781N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi499 ↔ 515By similarity
    Glycosylationi663 – 6631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi685 ↔ 715By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP21180.
    PRIDEiP21180.

    PTM databases

    PhosphoSiteiP21180.

    Expressioni

    Gene expression databases

    ArrayExpressiP21180.
    BgeeiP21180.
    CleanExiMM_C2.
    GenevestigatoriP21180.

    Structurei

    3D structure databases

    ProteinModelPortaliP21180.
    SMRiP21180. Positions 22-223, 251-760.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 9071Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini92 – 15160Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini154 – 21259Sushi 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini261 – 459199VWFAPROSITE-ProRule annotationAdd
    BLAST
    Domaini471 – 752282Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi267 – 2715MIDAS-like motifBy similarity

    Domaini

    The MIDAS-like motif in the VWFA domain binds divalent metal cations.By similarity

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
    Contains 3 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation
    Contains 1 VWFA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Sushi

    Phylogenomic databases

    GeneTreeiENSGT00530000063826.
    HOGENOMiHOG000038034.
    HOVERGENiHBG002567.
    InParanoidiO70350.
    KOiK01332.
    OMAiRDMTEVI.
    TreeFamiTF330194.

    Family and domain databases

    Gene3Di3.40.50.410. 1 hit.
    InterProiIPR011360. 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]
    PfamiPF00084. Sushi. 2 hits.
    PF00089. Trypsin. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001154. Compl_C2_B. 1 hit.
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00032. CCP. 2 hits.
    SM00020. Tryp_SPc. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF53300. SSF53300. 1 hit.
    SSF57535. SSF57535. 3 hits.
    PROSITEiPS50923. SUSHI. 3 hits.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    PS50234. VWFA. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P21180-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAPLLALFYL LQLGPGLAAL FCNQNVNITG GNFTLSHGWA PGSLLIYSCP    50
    LGRYPSPAWR KCQSNGQWLT PRSSSHHTLR SSRMVKAVCK PVRCLAPSSF 100
    ENGIYFPRLV SYPVGSNVSF ECEQDFTLRG SPVRYCRPNG LWDGETAVCD 150
    NGASHCPNPG ISVGTARTGL NFDLGDKVRY RCSSSNMVLT GSAERECQSN 200
    GVWSGSEPIC RQPYSYDFPE DVASALDTSL TNLLGATNPT QNLLTKSLGR 250
    KIIIQRSGHL NLYLLLDASQ SVTEKDFDIF KKSAELMVER IFSFEVNVSV 300
    AIITFASQPK TIMSILSERS QDVTEVITSL DSASYKDHEN ATGTNTYEVL 350
    IRVYSMMQSQ MDRLGMETSA WKEIRHTIIL LTDGKSNMGD SPKKAVTRIR 400
    ELLSIEQNRD DYLDIYAIGV GKLDVDWKEL NELGSKKDGE RHAFILQDAK 450
    ALQQIFEHML DVSKLTDTIC GVGNMSANAS DQERTPWQVT FKPKSKETCQ 500
    GSLISDQWVL TAAHCFHDIQ MEDHHLWRVN VGDPTSQHGK EFLVEDVIIA 550
    PGFNVHAKRK QGISEFYADD IALLKLSRKV KMSTHARPIC LPCTVGANMA 600
    LRRSPGSTCK DHETELLSQQ KVPAHFVALN GNRLNINLRT GPEWTRCIQA 650
    VSQNKNIFPS LTNVSEVVTD QFLCSGMEEE DDNPCKGESG GAVFLGRRYR 700
    FFQVGLVSWG LFDPCHGSSN KNLRKKPPRG VLPRDFHISL FRLQPWLRQH 750
    LDGVLDFLPL 760
    Length:760
    Mass (Da):84,741
    Last modified:July 27, 2011 - v2
    Checksum:i91C896A3EDC7D448
    GO
    Isoform Short (identifier: P21180-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:753
    Mass (Da):84,013
    Checksum:iC997F5CBA3A12278
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti123 – 1242EQ → DE in AAA37380. (PubMed:2229060)Curated
    Sequence conflicti123 – 1242EQ → DE in AAA37381. (PubMed:2229060)Curated
    Sequence conflicti123 – 1242EQ → DE in AAA63294. (PubMed:2229060)Curated
    Sequence conflicti299 – 2991S → T in AAA37380. (PubMed:2229060)Curated
    Sequence conflicti299 – 2991S → T in AAA37381. (PubMed:2229060)Curated
    Sequence conflicti299 – 2991S → T in AAA63294. (PubMed:2229060)Curated
    Sequence conflicti344 – 3441T → A in AAA37380. (PubMed:2229060)Curated
    Sequence conflicti344 – 3441T → A in AAA37381. (PubMed:2229060)Curated
    Sequence conflicti344 – 3441T → A in AAA63294. (PubMed:2229060)Curated
    Sequence conflicti359 – 3591S → T in AAA37380. (PubMed:2229060)Curated
    Sequence conflicti359 – 3591S → T in AAA37381. (PubMed:2229060)Curated
    Sequence conflicti359 – 3591S → T in AAA63294. (PubMed:2229060)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei606 – 6127Missing in isoform Short. 1 PublicationVSP_005385

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS28664.1. [P21180-1]
    PIRiA38876. C2MS.
    RefSeqiNP_038512.2. NM_013484.2. [P21180-1]
    UniGeneiMm.283217.

    Genome annotation databases

    EnsembliENSMUST00000025230; ENSMUSP00000025230; ENSMUSG00000024371. [P21180-1]
    GeneIDi12263.
    KEGGimmu:12263.
    UCSCiuc008cdz.2. mouse. [P21180-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS28664.1. [P21180-1 ]
    PIRi A38876. C2MS.
    RefSeqi NP_038512.2. NM_013484.2. [P21180-1 ]
    UniGenei Mm.283217.

    3D structure databases

    ProteinModelPortali P21180.
    SMRi P21180. Positions 22-223, 251-760.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S01.194.

    PTM databases

    PhosphoSitei P21180.

    Proteomic databases

    MaxQBi P21180.
    PRIDEi P21180.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025230 ; ENSMUSP00000025230 ; ENSMUSG00000024371 . [P21180-1 ]
    GeneIDi 12263.
    KEGGi mmu:12263.
    UCSCi uc008cdz.2. mouse. [P21180-1 ]

    Organism-specific databases

    CTDi 717.
    MGIi MGI:88226. C2.

    Phylogenomic databases

    GeneTreei ENSGT00530000063826.
    HOGENOMi HOG000038034.
    HOVERGENi HBG002567.
    InParanoidi O70350.
    KOi K01332.
    OMAi RDMTEVI.
    TreeFami TF330194.

    Enzyme and pathway databases

    Reactomei REACT_198562. Regulation of Complement cascade.
    REACT_202834. Initial triggering of complement.
    REACT_213087. Activation of C3 and C5.

    Miscellaneous databases

    ChiTaRSi C2. mouse.
    NextBioi 280706.
    PROi P21180.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21180.
    Bgeei P21180.
    CleanExi MM_C2.
    Genevestigatori P21180.

    Family and domain databases

    Gene3Di 3.40.50.410. 1 hit.
    InterProi 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 ]
    Pfami PF00084. Sushi. 2 hits.
    PF00089. Trypsin. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001154. Compl_C2_B. 1 hit.
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00032. CCP. 2 hits.
    SM00020. Tryp_SPc. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF53300. SSF53300. 1 hit.
    SSF57535. SSF57535. 3 hits.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiCO2_MOUSE
    AccessioniPrimary (citable) accession number: P21180
    Secondary accession number(s): O70350
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 130 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    C2 is a major histocompatibility complex class-III protein.

    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