P01027 (CO3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Complement C3

Alternative name(s):
HSE-MSF

Cleaved into the following 11 chains:

1. Complement C3 beta chain
2. Complement C3 alpha chain
3. C3a anaphylatoxin
4. Acylation stimulating protein
   Short name=ASP
   Alternative name(s):
   C3adesArg
5. Complement C3b alpha' chain
6. Complement C3c alpha' chain fragment 1
7. Complement C3dg fragment
8. Complement C3g fragment
9. Complement C3d fragment
10. Complement C3f fragment
11. Complement C3c alpha' chain fragment 2

Gene names

Name:

C3

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	1663 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.13 Ref.15 Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. 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. Ref.13 Ref.15 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 GPR77. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of GPR77. Ref.13 Ref.15
Subunit structure	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 GPR77; the interaction occurs with higher affinity for ASP, enhancing the phosphorylation and activation of GPR77, recruitment of ARRB2 to the cell surface and endocytosis of GRP77 By similarity.
Subcellular location	Secreted.
Post-translational modification	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.
Disruption phenotype	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. Ref.15
Sequence similarities	Contains 1 anaphylatoxin-like domain. Contains 1 NTR domain.

Ontologies

Keywords
Biological process	Complement alternate pathway Complement pathway Fatty acid metabolism Immunity Inflammatory response Innate immunity Lipid metabolism
Cellular component	Secreted
Coding sequence diversity	Alternative initiation
Domain	Signal
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein Thioester bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	complement activation Inferred from direct assay PubMed 18947875. Source: MGI complement activation, alternative pathway Inferred from electronic annotation. Source: UniProtKB-KW complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of endopeptidase activity Inferred from electronic annotation. Source: GOC positive regulation of G-protein coupled receptor protein signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of activation of membrane attack complex Inferred from mutant phenotype PubMed 15611275. Source: BHF-UCL positive regulation of angiogenesis Inferred from mutant phenotype PubMed 15611275PubMed 16452172. Source: BHF-UCL positive regulation of glucose transport Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of lipid storage Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of phagocytosis Inferred from mutant phenotype PubMed 11901193. Source: MGI positive regulation of protein phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of type IIa hypersensitivity Inferred from mutant phenotype PubMed 11901193. Source: MGI positive regulation vascular endothelial growth factor production Inferred from electronic annotation. Source: Compara regulation of triglyceride biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	extracellular space Inferred from electronic annotation. Source: InterPro
Molecular_function	C5L2 anaphylatoxin chemotactic receptor binding Inferred from sequence or structural similarity. Source: UniProtKB endopeptidase inhibitor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

Isoform Long (identifier: P01027-1)

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: P01027-2)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Ref.7 Ref.8
	Chain	25 – 1663	1639	Complement C3		PRO_0000005917
	Chain	25 – 666	642	Complement C3 beta chain		PRO_0000005918
	Chain	671 – 1663	993	Complement C3 alpha chain		PRO_0000005919
	Chain	671 – 748	78	C3a anaphylatoxin		PRO_0000005920
	Chain	671 – 747	77	Acylation stimulating protein		PRO_0000419936
	Chain	749 – 1663	915	Complement C3b alpha' chain		PRO_0000005921
	Chain	749 – 954	206	Complement C3c alpha' chain fragment 1		PRO_0000005922
	Chain	955 – 1303	349	Complement C3dg fragment		PRO_0000005923
	Chain	955 – 1001	47	Complement C3g fragment		PRO_0000005924
	Chain	1002 – 1303	302	Complement C3d fragment		PRO_0000005925
	Peptide	1304 – 1320	17	Complement C3f fragment		PRO_0000005927
	Chain	1321 – 1663	343	Complement C3c alpha' chain fragment 2		PRO_0000273949
Regions
	Domain	693 – 728	36	Anaphylatoxin-like
	Domain	1518 – 1661	144	NTR
	Region	1424 – 1456	33	Properdin-binding By similarity
Sites
	Site	747 – 748	2	Cleavage; by carboxypeptidases By similarity
	Site	748 – 749	2	Cleavage; by C3 convertase
	Site	954 – 955	2	Cleavage; by factor I Potential
	Site	1303 – 1304	2	Cleavage; by factor I
	Site	1320 – 1321	2	Cleavage; by factor I
Amino acid modifications
	Modified residue	489	1	Phosphotyrosine Ref.14
	Glycosylation	939	1	N-linked (GlcNAc...)
	Glycosylation	1617	1	N-linked (GlcNAc...)
	Disulfide bond	559 ↔ 816		Interchain (between beta and alpha chains) By similarity
	Disulfide bond	626 ↔ 661		By similarity
	Disulfide bond	693 ↔ 720		By similarity
	Disulfide bond	694 ↔ 727		By similarity
	Disulfide bond	707 ↔ 728		By similarity
	Disulfide bond	873 ↔ 1513		By similarity
	Disulfide bond	1101 ↔ 1158		By similarity
	Disulfide bond	1358 ↔ 1489		By similarity
	Disulfide bond	1389 ↔ 1458		By similarity
	Disulfide bond	1506 ↔ 1511		By similarity
	Disulfide bond	1518 ↔ 1590		By similarity
	Disulfide bond	1537 ↔ 1661		By similarity
	Disulfide bond	1637 ↔ 1646		By similarity
	Cross-link	1010 ↔ 1013		Isoglutamyl cysteine thioester (Cys-Gln) By similarity
Natural variations
	Alternative sequence	1 – 1128	1128	Missing in isoform Short.		VSP_018708
Experimental info
	Sequence conflict	137	1	K → Q in AAA37339. Ref.6
	Sequence conflict	858	1	E → Q in AAC42013. Ref.1
	Sequence conflict	1553	1	E → K in AAC42013. Ref.1
	Sequence conflict	1553	1	E → K in AAA37336. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 7E5546CC7C314779	FASTA	1,663	186,484
	10 20 30 40 50 60 MGPASGSQLL VLLLLLASSP LALGIPMYSI ITPNVLRLES EETIVLEAHD AQGDIPVTVT 70 80 90 100 110 120 VQDFLKRQVL TSEKTVLTGA SGHLRSVSIK IPASKEFNSD KEGHKYVTVV ANFGETVVEK 130 140 150 160 170 180 AVMVSFQSGY LFIQTDKTIY TPGSTVLYRI FTVDNNLLPV GKTVVILIET PDGIPVKRDI 190 200 210 220 230 240 LSSNNQHGIL PLSWNIPELV NMGQWKIRAF YEHAPKQIFS AEFEVKEYVL PSFEVRVEPT 250 260 270 280 290 300 ETFYYIDDPN GLEVSIIAKF LYGKNVDGTA FVIFGVQDGD KKISLAHSLT RVVIEDGVGD 310 320 330 340 350 360 AVLTRKVLME GVRPSNADAL VGKSLYVSVT VILHSGSDMV EAERSGIPIV TSPYQIHFTK 370 380 390 400 410 420 TPKFFKPAMP FDLMVFVTNP DGSPASKVLV VTQGSNAKAL TQDDGVAKLS INTPNSRQPL 430 440 450 460 470 480 TITVRTKKDT LPESRQATKT MEAHPYSTMH NSNNYLHLSV SRMELKPGDN LNVNFHLRTD 490 500 510 520 530 540 PGHEAKIRYY TYLVMNKGKL LKAGRQVREP GQDLVVLSLP ITPEFIPSFR LVAYYTLIGA 550 560 570 580 590 600 SGQREVVADS VWVDVKDSCI GTLVVKGDPR DNHLAPGQQT TLRIEGNQGA RVGLVAVDKG 610 620 630 640 650 660 VFVLNKKNKL TQSKIWDVVE KADIGCTPGS GKNYAGVFMD AGLAFKTSQG LQTEQRADLE 670 680 690 700 710 720 CTKPAARRRR SVQLMERRMD KAGQYTDKGL RKCCEDGMRD IPMRYSCQRR ARLITQGENC 730 740 750 760 770 780 IKAFIDCCNH ITKLREQHRR DHVLGLARSE LEEDIIPEED IISRSHFPQS WLWTIEELKE 790 800 810 820 830 840 PEKNGISTKV MNIFLKDSIT TWEILAVSLS DKKGICVADP YEIRVMQDFF IDLRLPYSVV 850 860 870 880 890 900 RNEQVEIRAV LFNYREQEEL KVRVELLHNP AFCSMATAKN RYFQTIKIPP KSSVAVPYVI 910 920 930 940 950 960 VPLKIGQQEV EVKAAVFNHF ISDGVKKTLK VVPEGMRINK TVAIHTLDPE KLGQGGVQKV 970 980 990 1000 1010 1020 DVPAADLSDQ VPDTDSETRI ILQGSPVVQM AEDAVDGERL KHLIVTPAGC GEQNMIGMTP 1030 1040 1050 1060 1070 1080 TVIAVHYLDQ TEQWEKFGIE KRQEALELIK KGYTQQLAFK QPSSAYAAFN NRPPSTWLTA 1090 1100 1110 1120 1130 1140 YVVKVFSLAA NLIAIDSHVL CGAVKWLILE KQKPDGVFQE DGPVIHQEMI GGFRNAKEAD 1150 1160 1170 1180 1190 1200 VSLTAFVLIA LQEARDICEG QVNSLPGSIN KAGEYIEASY MNLQRPYTVA IAGYALALMN 1210 1220 1230 1240 1250 1260 KLEEPYLGKF LNTAKDRNRW EEPDQQLYNV EATSYALLAL LLLKDFDSVP PVVRWLNEQR 1270 1280 1290 1300 1310 1320 YYGGGYGSTQ ATFMVFQALA QYQTDVPDHK DLNMDVSFHL PSRSSATTFR LLWENGNLLR 1330 1340 1350 1360 1370 1380 SEETKQNEAF SLTAKGKGRG TLSVVAVYHA KLKSKVTCKK FDLRVSIRPA PETAKKPEEA 1390 1400 1410 1420 1430 1440 KNTMFLEICT KYLGDVDATM SILDISMMTG FAPDTKDLEL LASGVDRYIS KYEMNKAFSN 1450 1460 1470 1480 1490 1500 KNTLIIYLEK ISHTEEDCLT FKVHQYFNVG LIQPGSVKVY SYYNLEESCT RFYHPEKDDG 1510 1520 1530 1540 1550 1560 MLSKLCHSEM CRCAEENCFM QQSQEKINLN VRLDKACEPG VDYVYKTELT NIELLDDFDE 1570 1580 1590 1600 1610 1620 YTMTIQQVIK SGSDEVQAGQ QRKFISHIKC RNALKLQKGK KYLMWGLSSD LWGEKPNTSY 1630 1640 1650 1660 IIGKDTWVEH WPEAEECQDQ KYQKQCEELG AFTESMVVYG CPN
	Isoform Short [UniParc]. Checksum: 6F6187342DC868CD	FASTA	535	60,952
	10 20 30 40 50 60 MIGGFRNAKE ADVSLTAFVL IALQEARDIC EGQVNSLPGS INKAGEYIEA SYMNLQRPYT 70 80 90 100 110 120 VAIAGYALAL MNKLEEPYLG KFLNTAKDRN RWEEPDQQLY NVEATSYALL ALLLLKDFDS 130 140 150 160 170 180 VPPVVRWLNE QRYYGGGYGS TQATFMVFQA LAQYQTDVPD HKDLNMDVSF HLPSRSSATT 190 200 210 220 230 240 FRLLWENGNL LRSEETKQNE AFSLTAKGKG RGTLSVVAVY HAKLKSKVTC KKFDLRVSIR 250 260 270 280 290 300 PAPETAKKPE EAKNTMFLEI CTKYLGDVDA TMSILDISMM TGFAPDTKDL ELLASGVDRY 310 320 330 340 350 360 ISKYEMNKAF SNKNTLIIYL EKISHTEEDC LTFKVHQYFN VGLIQPGSVK VYSYYNLEES 370 380 390 400 410 420 CTRFYHPEKD DGMLSKLCHS EMCRCAEENC FMQQSQEKIN LNVRLDKACE PGVDYVYKTE 430 440 450 460 470 480 LTNIELLDDF DEYTMTIQQV IKSGSDEVQA GQQRKFISHI KCRNALKLQK GKKYLMWGLS 490 500 510 520 530 SDLWGEKPNT SYIIGKDTWV EHWPEAEECQ DQKYQKQCEE LGAFTESMVV YGCPN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Common evolutionary origin of alpha 2-macroglobulin and complement components C3 and C4." Sottrup-Jensen L., Stepanik T.M., Kristensen T., Lonblad P.B., Jones C.M., Wierzbicki D.M., Magnusson S., Domdey H., Wetsel R.A., Lundwall A., Tack B.F., Fey G.H. Proc. Natl. Acad. Sci. U.S.A. 82:9-13(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-1663 (ISOFORM LONG).
[6]	"Structure and expression of the C3 gene." Fey G., Domdey H., Wiebauer K., Whitehead A.S., Odink K. Springer Semin. Immunopathol. 6:119-147(1983) [PubMed] [Europe PMC] [Abstract] 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]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-489, MASS SPECTROMETRY. Tissue: Liver.
[15]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00323624. IPI00759878.
PIR	C3MS. A92459. I48284.
RefSeq	NP_033908.2. NM_009778.2.
UniGene	Mm.19131.
3D structure databases
ProteinModelPortal	P01027.
SMR	P01027. Positions 26-663, 672-1663.
ModBase	Search...
Protein-protein interaction databases
IntAct	P01027. 1 interaction.
Protein family/group databases
MEROPS	I39.950.
PTM databases
PhosphoSite	P01027.
Proteomic databases
PaxDb	P01027.
PRIDE	P01027.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000024988; ENSMUSP00000024988; ENSMUSG00000024164.
GeneID	12266.
KEGG	mmu:12266.
Organism-specific databases
CTD	718.
MGI	MGI:88227. C3.
Phylogenomic databases
eggNOG	NOG241555.
GeneTree	ENSGT00560000077078.
HOGENOM	HOG000286028.
HOVERGEN	HBG005110.
InParanoid	Q80XP1.
KO	K03990.
OMA	AYYTLIG.
OrthoDB	EOG41G337.
Gene expression databases
ArrayExpress	P01027.
Bgee	P01027.
CleanEx	MM_C3.
Genevestigator	P01027.
GermOnline	ENSMUSG00000024164. Mus musculus.
Family and domain databases
Gene3D	1.20.91.20. 1 hit. 2.60.40.690. 1 hit.
InterPro	IPR009048. A-macroglobulin_rcpt-bd. IPR011626. A2M_comp. IPR002890. A2M_N. IPR011625. A2M_N_2. IPR000020. Anaphylatoxin/fibulin. IPR018081. Anaphylatoxin_. IPR001840. Anaphylatoxn. 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]
Pfam	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]
PRINTS	PR00004. ANAPHYLATOXN.
SMART	SM00104. ANATO. 1 hit. SM00643. C345C. 1 hit. [Graphical view]
SUPFAM	SSF49410. AM_receptor_bind. 1 hit. SSF47686. Anaphylatoxin. 1 hit. SSF48239. Terp_cyc_toroid. 1 hit. SSF50242. TIMP_like. 1 hit.
PROSITE	PS00477. ALPHA_2_MACROGLOBULIN. 1 hit. PS01177. ANAPHYLATOXIN_1. 1 hit. PS01178. ANAPHYLATOXIN_2. 1 hit. PS50189. NTR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	C3. mouse.
NextBio	280714.
PMAP-CutDB	Q80XP1.
SOURCE	Search...

Entry information

Entry name

CO3_MOUSE

Accession

Primary (citable) accession number: P01027
Secondary accession number(s): Q61370, Q80XP1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 27, 2011
Last modified:	April 3, 2013
This is version 135 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program