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P01027

- CO3_MOUSE

UniProt

P01027 - CO3_MOUSE

Protein

Complement C3

Gene

C3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates.
    Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. In chronic inflammation, acts as a chemoattractant for neutrophils By similarity. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. The short isoform has B-cell stimulatory activity.By similarity
    C3-beta-c: Acts as a chemoattractant for neutrophils in chronic inflammation.By similarity
    Acylation stimulating protein: adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of C5AR2.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei747 – 7482Cleavage; by carboxypeptidasesBy similarity
    Sitei748 – 7492Cleavage; by C3 convertase
    Sitei954 – 9552Cleavage; by factor ISequence Analysis
    Sitei1303 – 13042Cleavage; by factor I
    Sitei1320 – 13212Cleavage; by factor I

    GO - Molecular functioni

    1. C5L2 anaphylatoxin chemotactic receptor binding Source: UniProtKB
    2. endopeptidase inhibitor activity Source: InterPro
    3. protein binding Source: MGI

    GO - Biological processi

    1. complement activation Source: MGI
    2. complement activation, alternative pathway Source: UniProtKB-KW
    3. complement activation, classical pathway Source: UniProtKB-KW
    4. fatty acid metabolic process Source: UniProtKB-KW
    5. inflammatory response Source: UniProtKB-KW
    6. positive regulation of activation of membrane attack complex Source: BHF-UCL
    7. positive regulation of angiogenesis Source: BHF-UCL
    8. positive regulation of glucose transport Source: UniProtKB
    9. positive regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
    10. positive regulation of lipid storage Source: UniProtKB
    11. positive regulation of phagocytosis Source: MGI
    12. positive regulation of protein phosphorylation Source: UniProtKB
    13. positive regulation of type IIa hypersensitivity Source: MGI
    14. positive regulation vascular endothelial growth factor production Source: Ensembl
    15. regulation of triglyceride biosynthetic process Source: UniProtKB

    Keywords - Biological processi

    Complement alternate pathway, Complement pathway, Fatty acid metabolism, Immunity, Inflammatory response, Innate immunity, Lipid metabolism

    Enzyme and pathway databases

    ReactomeiREACT_198562. Regulation of Complement cascade.
    REACT_202937. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_213087. Activation of C3 and C5.
    REACT_218037. Alternative complement activation.

    Protein family/group databases

    MEROPSiI39.950.

    Names & Taxonomyi

    Protein namesi
    Gene namesi
    Name:C3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:88227. C3.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: InterPro
    2. extracellular vesicular exosome Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Null mice displayed altered lipid metabolism and morphological changes in adipocyte distribution. There is reduced adipsin/CFD expression, increased number of smaller fat cells, decreased DGAT1 expression and activity, and less triglyceride storage capacity associated with delayed postprandial clearance. Mice on a high-fat diet exihibited no diet-induced up-regulation of adipsin/CFD expression nor adipocyte differentiation.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24242 PublicationsAdd
    BLAST
    Chaini25 – 16631639Complement C3PRO_0000005917Add
    BLAST
    Chaini25 – 666642Complement C3 beta chainPRO_0000005918Add
    BLAST
    Chaini569 – 66698C3-beta-cBy similarityPRO_0000430431Add
    BLAST
    Chaini671 – 1663993Complement C3 alpha chainPRO_0000005919Add
    BLAST
    Chaini671 – 74878C3a anaphylatoxinPRO_0000005920Add
    BLAST
    Chaini671 – 74777Acylation stimulating proteinPRO_0000419936Add
    BLAST
    Chaini749 – 1663915Complement C3b alpha' chainPRO_0000005921Add
    BLAST
    Chaini749 – 954206Complement C3c alpha' chain fragment 1PRO_0000005922Add
    BLAST
    Chaini955 – 1303349Complement C3dg fragmentPRO_0000005923Add
    BLAST
    Chaini955 – 100147Complement C3g fragmentPRO_0000005924Add
    BLAST
    Chaini1002 – 1303302Complement C3d fragmentPRO_0000005925Add
    BLAST
    Peptidei1304 – 132017Complement C3f fragmentPRO_0000005927Add
    BLAST
    Chaini1321 – 1663343Complement C3c alpha' chain fragment 2PRO_0000273949Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi559 ↔ 816Interchain (between beta and alpha chains)PROSITE-ProRule annotation
    Disulfide bondi626 ↔ 661By similarity
    Disulfide bondi693 ↔ 720By similarity
    Disulfide bondi694 ↔ 727By similarity
    Disulfide bondi707 ↔ 728By similarity
    Disulfide bondi873 ↔ 1513By similarity
    Glycosylationi939 – 9391N-linked (GlcNAc...)
    Cross-linki1010 ↔ 1013Isoglutamyl cysteine thioester (Cys-Gln)By similarity
    Disulfide bondi1101 ↔ 1158By similarity
    Disulfide bondi1358 ↔ 1489By similarity
    Disulfide bondi1389 ↔ 1458By similarity
    Disulfide bondi1506 ↔ 1511By similarity
    Disulfide bondi1518 ↔ 1590By similarity
    Disulfide bondi1537 ↔ 1661By similarity
    Glycosylationi1617 – 16171N-linked (GlcNAc...)
    Disulfide bondi1637 ↔ 1646By similarity

    Post-translational modificationi

    C3b is rapidly split in two positions by factor I and a cofactor to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha' chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other proteases produce other fragments such as C3d or C3g. C3a is further processed by carboxypeptidases to release the C-terminal arginine residue generating the acylation stimulating protein (ASP). Levels of ASP are increased in adipocytes in the postprandial period and by dietary chylomicrons.
    Phosphorylation sites are present in the extracellular medium.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Thioester bond

    Proteomic databases

    MaxQBiP01027.
    PaxDbiP01027.
    PRIDEiP01027.

    PTM databases

    PhosphoSiteiP01027.

    Miscellaneous databases

    PMAP-CutDBQ80XP1.

    Expressioni

    Gene expression databases

    ArrayExpressiP01027.
    BgeeiP01027.
    CleanExiMM_C3.
    GenevestigatoriP01027.

    Interactioni

    Subunit structurei

    C3 precursor is first processed by the removal of 4 Arg residues, forming two chains, beta and alpha, linked by a disulfide bond. C3 convertase activates C3 by cleaving the alpha chain, releasing C3a anaphylatoxin and generating C3b (beta chain + alpha' chain). C3dg interacts with CR2 (via the N-terminal Sushi domains 1 and 2). Interacts with VSIG4. Interacts (both C3a and ASP) with C5AR2; the interaction occurs with higher affinity for ASP, enhancing the phosphorylation and activation of C5AR2, recruitment of ARRB2 to the cell surface and endocytosis of GRP77 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi198418. 1 interaction.
    IntActiP01027. 5 interactions.
    MINTiMINT-1858136.

    Structurei

    3D structure databases

    ProteinModelPortaliP01027.
    SMRiP01027. Positions 26-663, 672-1663.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini693 – 72836Anaphylatoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini1518 – 1661144NTRPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1424 – 145633Properdin-bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 anaphylatoxin-like domain.PROSITE-ProRule annotation
    Contains 1 NTR domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG241555.
    GeneTreeiENSGT00560000077078.
    HOGENOMiHOG000286028.
    HOVERGENiHBG005110.
    InParanoidiQ80XP1.
    KOiK03990.
    OMAiPGMPFDL.
    OrthoDBiEOG77HDCX.
    TreeFamiTF313285.

    Family and domain databases

    Gene3Di1.20.91.20. 1 hit.
    1.50.10.20. 1 hit.
    2.60.40.690. 1 hit.
    InterProiIPR009048. A-macroglobulin_rcpt-bd.
    IPR011626. A2M_comp.
    IPR002890. A2M_N.
    IPR011625. A2M_N_2.
    IPR000020. Anaphylatoxin/fibulin.
    IPR018081. Anaphylatoxin_comp_syst.
    IPR001840. Anaphylatoxn_comp_syst_dom.
    IPR001599. Macroglobln_a2.
    IPR019742. MacrogloblnA2_CS.
    IPR019565. MacrogloblnA2_thiol-ester-bond.
    IPR001134. Netrin_domain.
    IPR018933. Netrin_module_non-TIMP.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    IPR008993. TIMP-like_OB-fold.
    [Graphical view]
    PfamiPF00207. A2M. 1 hit.
    PF07678. A2M_comp. 1 hit.
    PF01835. A2M_N. 1 hit.
    PF07703. A2M_N_2. 1 hit.
    PF07677. A2M_recep. 1 hit.
    PF01821. ANATO. 1 hit.
    PF01759. NTR. 1 hit.
    PF10569. Thiol-ester_cl. 1 hit.
    [Graphical view]
    PRINTSiPR00004. ANAPHYLATOXN.
    SMARTiSM00104. ANATO. 1 hit.
    SM00643. C345C. 1 hit.
    [Graphical view]
    SUPFAMiSSF47686. SSF47686. 1 hit.
    SSF48239. SSF48239. 1 hit.
    SSF49410. SSF49410. 1 hit.
    SSF50242. SSF50242. 1 hit.
    PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
    PS01177. ANAPHYLATOXIN_1. 1 hit.
    PS01178. ANAPHYLATOXIN_2. 1 hit.
    PS50189. NTR. 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 initiation. Align

    Isoform Long (identifier: P01027-1) [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

    MGPASGSQLL VLLLLLASSP LALGIPMYSI ITPNVLRLES EETIVLEAHD     50
    AQGDIPVTVT VQDFLKRQVL TSEKTVLTGA SGHLRSVSIK IPASKEFNSD 100
    KEGHKYVTVV ANFGETVVEK AVMVSFQSGY LFIQTDKTIY TPGSTVLYRI 150
    FTVDNNLLPV GKTVVILIET PDGIPVKRDI LSSNNQHGIL PLSWNIPELV 200
    NMGQWKIRAF YEHAPKQIFS AEFEVKEYVL PSFEVRVEPT ETFYYIDDPN 250
    GLEVSIIAKF LYGKNVDGTA FVIFGVQDGD KKISLAHSLT RVVIEDGVGD 300
    AVLTRKVLME GVRPSNADAL VGKSLYVSVT VILHSGSDMV EAERSGIPIV 350
    TSPYQIHFTK TPKFFKPAMP FDLMVFVTNP DGSPASKVLV VTQGSNAKAL 400
    TQDDGVAKLS INTPNSRQPL TITVRTKKDT LPESRQATKT MEAHPYSTMH 450
    NSNNYLHLSV SRMELKPGDN LNVNFHLRTD PGHEAKIRYY TYLVMNKGKL 500
    LKAGRQVREP GQDLVVLSLP ITPEFIPSFR LVAYYTLIGA SGQREVVADS 550
    VWVDVKDSCI GTLVVKGDPR DNHLAPGQQT TLRIEGNQGA RVGLVAVDKG 600
    VFVLNKKNKL TQSKIWDVVE KADIGCTPGS GKNYAGVFMD AGLAFKTSQG 650
    LQTEQRADLE CTKPAARRRR SVQLMERRMD KAGQYTDKGL RKCCEDGMRD 700
    IPMRYSCQRR ARLITQGENC IKAFIDCCNH ITKLREQHRR DHVLGLARSE 750
    LEEDIIPEED IISRSHFPQS WLWTIEELKE PEKNGISTKV MNIFLKDSIT 800
    TWEILAVSLS DKKGICVADP YEIRVMQDFF IDLRLPYSVV RNEQVEIRAV 850
    LFNYREQEEL KVRVELLHNP AFCSMATAKN RYFQTIKIPP KSSVAVPYVI 900
    VPLKIGQQEV EVKAAVFNHF ISDGVKKTLK VVPEGMRINK TVAIHTLDPE 950
    KLGQGGVQKV DVPAADLSDQ VPDTDSETRI ILQGSPVVQM AEDAVDGERL 1000
    KHLIVTPAGC GEQNMIGMTP TVIAVHYLDQ TEQWEKFGIE KRQEALELIK 1050
    KGYTQQLAFK QPSSAYAAFN NRPPSTWLTA YVVKVFSLAA NLIAIDSHVL 1100
    CGAVKWLILE KQKPDGVFQE DGPVIHQEMI GGFRNAKEAD VSLTAFVLIA 1150
    LQEARDICEG QVNSLPGSIN KAGEYIEASY MNLQRPYTVA IAGYALALMN 1200
    KLEEPYLGKF LNTAKDRNRW EEPDQQLYNV EATSYALLAL LLLKDFDSVP 1250
    PVVRWLNEQR YYGGGYGSTQ ATFMVFQALA QYQTDVPDHK DLNMDVSFHL 1300
    PSRSSATTFR LLWENGNLLR SEETKQNEAF SLTAKGKGRG TLSVVAVYHA 1350
    KLKSKVTCKK FDLRVSIRPA PETAKKPEEA KNTMFLEICT KYLGDVDATM 1400
    SILDISMMTG FAPDTKDLEL LASGVDRYIS KYEMNKAFSN KNTLIIYLEK 1450
    ISHTEEDCLT FKVHQYFNVG LIQPGSVKVY SYYNLEESCT RFYHPEKDDG 1500
    MLSKLCHSEM CRCAEENCFM QQSQEKINLN VRLDKACEPG VDYVYKTELT 1550
    NIELLDDFDE YTMTIQQVIK SGSDEVQAGQ QRKFISHIKC RNALKLQKGK 1600
    KYLMWGLSSD LWGEKPNTSY IIGKDTWVEH WPEAEECQDQ KYQKQCEELG 1650
    AFTESMVVYG CPN 1663
    Length:1,663
    Mass (Da):186,484
    Last modified:July 27, 2011 - v3
    Checksum:i7E5546CC7C314779
    GO
    Isoform Short (identifier: P01027-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1128: Missing.

    Show »
    Length:535
    Mass (Da):60,952
    Checksum:i6F6187342DC868CD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti137 – 1371K → Q in AAA37339. (PubMed:6356427)Curated
    Sequence conflicti858 – 8581E → Q in AAC42013. (PubMed:6208565)Curated
    Sequence conflicti1553 – 15531E → K in AAC42013. (PubMed:6208565)Curated
    Sequence conflicti1553 – 15531E → K in AAA37336. (PubMed:6094532)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11281128Missing in isoform Short. CuratedVSP_018708Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02782 mRNA. Translation: AAC42013.1.
    BC043338 mRNA. Translation: AAH43338.1.
    M35659 mRNA. Translation: AAA37339.1.
    M33032 mRNA. Translation: AAA37378.1.
    J00369, J00367 Genomic DNA. Translation: AAA37336.1.
    Z37998 Genomic DNA. Translation: CAA86099.2.
    CCDSiCCDS37670.1. [P01027-1]
    PIRiA92459. C3MS.
    I48284.
    RefSeqiNP_033908.2. NM_009778.2. [P01027-1]
    UniGeneiMm.19131.

    Genome annotation databases

    EnsembliENSMUST00000024988; ENSMUSP00000024988; ENSMUSG00000024164. [P01027-1]
    GeneIDi12266.
    KEGGimmu:12266.
    UCSCiuc008deg.1. mouse. [P01027-1]

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02782 mRNA. Translation: AAC42013.1 .
    BC043338 mRNA. Translation: AAH43338.1 .
    M35659 mRNA. Translation: AAA37339.1 .
    M33032 mRNA. Translation: AAA37378.1 .
    J00369 , J00367 Genomic DNA. Translation: AAA37336.1 .
    Z37998 Genomic DNA. Translation: CAA86099.2 .
    CCDSi CCDS37670.1. [P01027-1 ]
    PIRi A92459. C3MS.
    I48284.
    RefSeqi NP_033908.2. NM_009778.2. [P01027-1 ]
    UniGenei Mm.19131.

    3D structure databases

    ProteinModelPortali P01027.
    SMRi P01027. Positions 26-663, 672-1663.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198418. 1 interaction.
    IntActi P01027. 5 interactions.
    MINTi MINT-1858136.

    Protein family/group databases

    MEROPSi I39.950.

    PTM databases

    PhosphoSitei P01027.

    Proteomic databases

    MaxQBi P01027.
    PaxDbi P01027.
    PRIDEi P01027.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000024988 ; ENSMUSP00000024988 ; ENSMUSG00000024164 . [P01027-1 ]
    GeneIDi 12266.
    KEGGi mmu:12266.
    UCSCi uc008deg.1. mouse. [P01027-1 ]

    Organism-specific databases

    CTDi 718.
    MGIi MGI:88227. C3.

    Phylogenomic databases

    eggNOGi NOG241555.
    GeneTreei ENSGT00560000077078.
    HOGENOMi HOG000286028.
    HOVERGENi HBG005110.
    InParanoidi Q80XP1.
    KOi K03990.
    OMAi PGMPFDL.
    OrthoDBi EOG77HDCX.
    TreeFami TF313285.

    Enzyme and pathway databases

    Reactomei REACT_198562. Regulation of Complement cascade.
    REACT_202937. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_213087. Activation of C3 and C5.
    REACT_218037. Alternative complement activation.

    Miscellaneous databases

    ChiTaRSi C3. mouse.
    NextBioi 280714.
    PMAP-CutDB Q80XP1.
    PROi P01027.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01027.
    Bgeei P01027.
    CleanExi MM_C3.
    Genevestigatori P01027.

    Family and domain databases

    Gene3Di 1.20.91.20. 1 hit.
    1.50.10.20. 1 hit.
    2.60.40.690. 1 hit.
    InterProi IPR009048. A-macroglobulin_rcpt-bd.
    IPR011626. A2M_comp.
    IPR002890. A2M_N.
    IPR011625. A2M_N_2.
    IPR000020. Anaphylatoxin/fibulin.
    IPR018081. Anaphylatoxin_comp_syst.
    IPR001840. Anaphylatoxn_comp_syst_dom.
    IPR001599. Macroglobln_a2.
    IPR019742. MacrogloblnA2_CS.
    IPR019565. MacrogloblnA2_thiol-ester-bond.
    IPR001134. Netrin_domain.
    IPR018933. Netrin_module_non-TIMP.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    IPR008993. TIMP-like_OB-fold.
    [Graphical view ]
    Pfami PF00207. A2M. 1 hit.
    PF07678. A2M_comp. 1 hit.
    PF01835. A2M_N. 1 hit.
    PF07703. A2M_N_2. 1 hit.
    PF07677. A2M_recep. 1 hit.
    PF01821. ANATO. 1 hit.
    PF01759. NTR. 1 hit.
    PF10569. Thiol-ester_cl. 1 hit.
    [Graphical view ]
    PRINTSi PR00004. ANAPHYLATOXN.
    SMARTi SM00104. ANATO. 1 hit.
    SM00643. C345C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47686. SSF47686. 1 hit.
    SSF48239. SSF48239. 1 hit.
    SSF49410. SSF49410. 1 hit.
    SSF50242. SSF50242. 1 hit.
    PROSITEi PS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
    PS01177. ANAPHYLATOXIN_1. 1 hit.
    PS01178. ANAPHYLATOXIN_2. 1 hit.
    PS50189. NTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of complementary DNA and derived amino acid sequence of murine complement protein C3."
      Fey G.H., Lundwall A., Wetsel R.A., Tack B.F., de Bruijn M.H.L., Domdey H.
      Philos. Trans. R. Soc. Lond., B, Biol. Sci. 306:333-344(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    2. "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.
    3. "Structure of murine complement component C3. I. Nucleotide sequence of cloned complementary and genomic DNA coding for the beta chain."
      Lundwall A., Wetsel R.A., Domdey H., Tack B.F., Fey G.H.
      J. Biol. Chem. 259:13851-13856(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-724 (ISOFORM LONG).
    4. "Isolation and analysis of genomic DNA clones encoding the third component of mouse complement."
      Wiebauer K., Domdey H., Diggelmann H., Fey G.
      Proc. Natl. Acad. Sci. U.S.A. 79:7077-7081(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
    5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-1663 (ISOFORM LONG).
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-240 (ISOFORM LONG).
    7. "A paracrine migration-stimulating factor for metastatic tumor cells secreted by mouse hepatic sinusoidal endothelial cells: identification as complement component C3b."
      Hamada J., Cavanaugh P.G., Miki K., Nicolson G.L.
      Cancer Res. 53:4418-4423(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-41 AND 749-760.
    8. "The specific production of the third component of complement by osteoblastic cells treated with 1 alpha,25-dihydroxyvitamin D3."
      Sato T., Hong M.H., Jin C.H., Ishimi Y., Udagawa N., Shinki T., Abe E., Suda T.
      FEBS Lett. 285:21-24(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-31 AND 671-680.
    9. "Amino acid sequences of mouse complement C3 derived from nucleotide sequences of cloned cDNA."
      Fey G.H., Wiebauer K., Domdey H.
      Ann. N. Y. Acad. Sci. 421:307-312(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 658-761.
    10. "Structure of murine complement component C3. II. Nucleotide sequence of cloned complementary DNA coding for the alpha chain."
      Wetsel R.A., Lundwall A., Davidson F., Gibson T., Tack B.F., Fey G.H.
      J. Biol. Chem. 259:13857-13862(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 671-1663 (ISOFORM LONG).
    11. "Characterization of the mRNA and cloned cDNA specifying the third component of mouse complement."
      Domdey H., Wiebauer K., Kazmaier M., Mueller V., Odink K., Fey G.H.
      Proc. Natl. Acad. Sci. U.S.A. 79:7619-7623(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 671-748.
    12. "The structure of an alternate form of complement C3 that displays costimulatory growth factor activity for B lymphocytes."
      Cahen-Kramer Y., Martensson I.L., Melchers F.
      J. Exp. Med. 180:2079-2088(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE INITIATION (ISOFORM SHORT).
    13. "Acylation-stimulating protein (ASP) deficiency induces obesity resistance and increased energy expenditure in ob/ob mice."
      Xia Z., Sniderman A.D., Cianflone K.
      J. Biol. Chem. 277:45874-45879(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Acylation-stimulating protein deficiency and altered adipose tissue in alternative complement pathway knockout mice."
      Paglialunga S., Fisette A., Yan Y., Deshaies Y., Brouillette J.F., Pekna M., Cianflone K.
      Am. J. Physiol. 294:E521-E529(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.

    Entry informationi

    Entry nameiCO3_MOUSE
    AccessioniPrimary (citable) accession number: P01027
    Secondary accession number(s): Q61370, Q80XP1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 150 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3