Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P01027

- CO3_MOUSE

UniProt

P01027 - CO3_MOUSE

(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)

Protein

Complement C3

Gene

C3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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 apoptotic cell clearance Source: Ensembl
  9. positive regulation of glucose transport Source: UniProtKB
  10. positive regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
  11. positive regulation of lipid storage Source: UniProtKB
  12. positive regulation of phagocytosis Source: MGI
  13. positive regulation of protein phosphorylation Source: UniProtKB
  14. positive regulation of type IIa hypersensitivity Source: MGI
  15. positive regulation vascular endothelial growth factor production Source: Ensembl
  16. regulation of triglyceride biosynthetic process Source: UniProtKB
Complete GO annotation...

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.
REACT_235286. Peptide ligand-binding receptors.
REACT_250376. G alpha (i) signalling events.

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. blood microparticle Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

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

BgeeiP01027.
CleanExiMM_C3.
ExpressionAtlasiP01027. baseline and differential.
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.
GeneTreeiENSGT00760000118982.
HOGENOMiHOG000286028.
HOVERGENiHBG005110.
InParanoidiP01027.
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

        10         20         30         40         50
MGPASGSQLL VLLLLLASSP LALGIPMYSI ITPNVLRLES EETIVLEAHD
60 70 80 90 100
AQGDIPVTVT VQDFLKRQVL TSEKTVLTGA SGHLRSVSIK IPASKEFNSD
110 120 130 140 150
KEGHKYVTVV ANFGETVVEK AVMVSFQSGY LFIQTDKTIY TPGSTVLYRI
160 170 180 190 200
FTVDNNLLPV GKTVVILIET PDGIPVKRDI LSSNNQHGIL PLSWNIPELV
210 220 230 240 250
NMGQWKIRAF YEHAPKQIFS AEFEVKEYVL PSFEVRVEPT ETFYYIDDPN
260 270 280 290 300
GLEVSIIAKF LYGKNVDGTA FVIFGVQDGD KKISLAHSLT RVVIEDGVGD
310 320 330 340 350
AVLTRKVLME GVRPSNADAL VGKSLYVSVT VILHSGSDMV EAERSGIPIV
360 370 380 390 400
TSPYQIHFTK TPKFFKPAMP FDLMVFVTNP DGSPASKVLV VTQGSNAKAL
410 420 430 440 450
TQDDGVAKLS INTPNSRQPL TITVRTKKDT LPESRQATKT MEAHPYSTMH
460 470 480 490 500
NSNNYLHLSV SRMELKPGDN LNVNFHLRTD PGHEAKIRYY TYLVMNKGKL
510 520 530 540 550
LKAGRQVREP GQDLVVLSLP ITPEFIPSFR LVAYYTLIGA SGQREVVADS
560 570 580 590 600
VWVDVKDSCI GTLVVKGDPR DNHLAPGQQT TLRIEGNQGA RVGLVAVDKG
610 620 630 640 650
VFVLNKKNKL TQSKIWDVVE KADIGCTPGS GKNYAGVFMD AGLAFKTSQG
660 670 680 690 700
LQTEQRADLE CTKPAARRRR SVQLMERRMD KAGQYTDKGL RKCCEDGMRD
710 720 730 740 750
IPMRYSCQRR ARLITQGENC IKAFIDCCNH ITKLREQHRR DHVLGLARSE
760 770 780 790 800
LEEDIIPEED IISRSHFPQS WLWTIEELKE PEKNGISTKV MNIFLKDSIT
810 820 830 840 850
TWEILAVSLS DKKGICVADP YEIRVMQDFF IDLRLPYSVV RNEQVEIRAV
860 870 880 890 900
LFNYREQEEL KVRVELLHNP AFCSMATAKN RYFQTIKIPP KSSVAVPYVI
910 920 930 940 950
VPLKIGQQEV EVKAAVFNHF ISDGVKKTLK VVPEGMRINK TVAIHTLDPE
960 970 980 990 1000
KLGQGGVQKV DVPAADLSDQ VPDTDSETRI ILQGSPVVQM AEDAVDGERL
1010 1020 1030 1040 1050
KHLIVTPAGC GEQNMIGMTP TVIAVHYLDQ TEQWEKFGIE KRQEALELIK
1060 1070 1080 1090 1100
KGYTQQLAFK QPSSAYAAFN NRPPSTWLTA YVVKVFSLAA NLIAIDSHVL
1110 1120 1130 1140 1150
CGAVKWLILE KQKPDGVFQE DGPVIHQEMI GGFRNAKEAD VSLTAFVLIA
1160 1170 1180 1190 1200
LQEARDICEG QVNSLPGSIN KAGEYIEASY MNLQRPYTVA IAGYALALMN
1210 1220 1230 1240 1250
KLEEPYLGKF LNTAKDRNRW EEPDQQLYNV EATSYALLAL LLLKDFDSVP
1260 1270 1280 1290 1300
PVVRWLNEQR YYGGGYGSTQ ATFMVFQALA QYQTDVPDHK DLNMDVSFHL
1310 1320 1330 1340 1350
PSRSSATTFR LLWENGNLLR SEETKQNEAF SLTAKGKGRG TLSVVAVYHA
1360 1370 1380 1390 1400
KLKSKVTCKK FDLRVSIRPA PETAKKPEEA KNTMFLEICT KYLGDVDATM
1410 1420 1430 1440 1450
SILDISMMTG FAPDTKDLEL LASGVDRYIS KYEMNKAFSN KNTLIIYLEK
1460 1470 1480 1490 1500
ISHTEEDCLT FKVHQYFNVG LIQPGSVKVY SYYNLEESCT RFYHPEKDDG
1510 1520 1530 1540 1550
MLSKLCHSEM CRCAEENCFM QQSQEKINLN VRLDKACEPG VDYVYKTELT
1560 1570 1580 1590 1600
NIELLDDFDE YTMTIQQVIK SGSDEVQAGQ QRKFISHIKC RNALKLQKGK
1610 1620 1630 1640 1650
KYLMWGLSSD LWGEKPNTSY IIGKDTWVEH WPEAEECQDQ KYQKQCEELG
1660
AFTESMVVYG CPN
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 ENSGT00760000118982.
HOGENOMi HOG000286028.
HOVERGENi HBG005110.
InParanoidi P01027.
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.
REACT_235286. Peptide ligand-binding receptors.
REACT_250376. G alpha (i) signalling events.

Miscellaneous databases

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

Gene expression databases

Bgeei P01027.
CleanExi MM_C3.
ExpressionAtlasi P01027. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 152 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