Complement C3 precursor - Rattus norvegicus (Rat)

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P01026 (CO3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 138. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Complement C3

Cleaved into the following 12 chains:

Complement C3 beta chain
Complement C3 alpha chain
Alternative name(s):
ENCF-1
Neutrophil chemotactic factor-1
Neutrophil chemotactic factor-2
Alternative name(s):
ENCF-2
C3a anaphylatoxin
Acylation stimulating protein
Short name=ASP
Alternative name(s):
C3adesArg
Complement C3b alpha' chain
Complement C3c alpha' chain fragment 1
Complement C3dg fragment
Complement C3g fragment
Complement C3d fragment
Complement C3f fragment
Complement C3c alpha' chain fragment 2

Gene names

Name:

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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.2 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. Acts as a chemoattractant for neutophils. Ref.2 Neutrophil chemotactic factor-2 acts as a chemoattractant for neurophils. Ref.2 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 By similarity. Ref.2
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 By similarity. Phosphorylation sites are present in the extracellular medium By similarity.
Sequence similarities	Contains 1 anaphylatoxin-like domain. Contains 1 NTR domain.

Ontologies

Keywords
Biological process	Chemotaxis Complement alternate pathway Complement pathway Fatty acid metabolism Immunity Inflammatory response Innate immunity Lipid metabolism
Cellular component	Secreted
Domain	Signal
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein Thioester bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Inferred from mutant phenotype PubMed 15956288. Source: RGD chemotaxis Inferred from electronic annotation. Source: UniProtKB-KW complement activation, alternative pathway Inferred from electronic annotation. Source: UniProtKB-KW complement activation, classical pathway Traceable author statement PubMed 16996480. Source: RGD 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 ERK1 and ERK2 cascade Inferred from direct assay PubMed 18178156. Source: RGD positive regulation of G-protein coupled receptor protein signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of developmental growth Inferred from direct assay PubMed 20712003. Source: RGD 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 protein phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of triglyceride biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB response to estradiol stimulus Inferred from expression pattern PubMed 12370124. Source: RGD response to glucocorticoid stimulus Inferred from expression pattern PubMed 11566438. Source: RGD response to magnesium ion Inferred from expression pattern PubMed 12759143. Source: RGD response to progesterone stimulus Inferred from expression pattern PubMed 11566438. Source: RGD tolerance induction Inferred from expression pattern PubMed 16555329. Source: RGD
Cellular_component	extracellular space Inferred from direct assay PubMed 20712003. Source: RGD
Molecular_function	C5L2 anaphylatoxin chemotactic receptor binding Inferred from sequence or structural similarity. Source: UniProtKB cofactor binding Inferred from physical interaction PubMed 15215199. Source: RGD endopeptidase inhibitor activity Inferred from electronic annotation. Source: InterPro lipid binding Inferred from direct assay PubMed 11305612. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

Chain

25 – 1663

1639

Complement C3

PRO_0000005937

Chain

25 – 666

642

Complement C3 beta chain

PRO_0000005938

Chain

568 – ?

Neutrophil chemotactic factor-2

PRO_0000395292

Chain

671 – 1663

993

Complement C3 alpha chain

PRO_0000005939

Chain

671 – 748

C3a anaphylatoxin

PRO_0000005940

Chain

671 – 747

Acylation stimulating protein By similarity

PRO_0000419937

Chain

749 – 1663

915

Complement C3b alpha' chain

PRO_0000005941

Chain

749 – 959

211

Complement C3c alpha' chain fragment 1

PRO_0000273950

Chain

960 – 1303

344

Complement C3dg fragment By similarity

PRO_0000273951

Chain

960 – 1001

Complement C3g fragment By similarity

PRO_0000273952

Chain

1002 – 1303

302

Complement C3d fragment By similarity

PRO_0000273953

Peptide

1304 – 1320

Complement C3f fragment By similarity

PRO_0000273954

Chain

1321 – 1663

343

Complement C3c alpha' chain fragment 2 By similarity

PRO_0000273955

Regions

Domain

693 – 728

Anaphylatoxin-like

Domain

1518 – 1661

144

NTR

Region

1424 – 1456

Properdin-binding By similarity

Sites

Site

747 – 748

Cleavage; by carboxypeptidases By similarity

Site

748 – 749

Cleavage; by C3 convertase

Site

959 – 960

Cleavage; by factor I Potential

Site

1303 – 1304

Cleavage; by factor I By similarity

Site

1320 – 1321

Cleavage; by factor I By similarity

Amino acid modifications

Modified residue

488

Phosphotyrosine By similarity

Glycosylation

939

N-linked (GlcNAc...) Probable

Glycosylation

1617

N-linked (GlcNAc...) Probable

Disulfide bond

558 ↔ 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

Cross-link

1010 ↔ 1013

Isoglutamyl cysteine thioester (Cys-Gln) By similarity

Experimental info

Sequence conflict

704

P → K in AAG00532. Ref.4

Sequence conflict

721 – 722

LK → KL AA sequence Ref.3

Secondary structure

1663

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P01026 [UniParc].

Last modified August 1, 1990. Version 3.
Checksum: 2F87CCB143CDD4BC
Show »

FASTA

1,663

186,460

        10         20         30         40         50         60 
MGPTSGSQLL VLLLLLASSL LALGSPMYSI ITPNVLRLES EETFILEAHD AQGDVPVTVT 

        70         80         90        100        110        120 
VQDFLKKQVL TSEKTVLTGA TGHLNRVFIK IPASKEFNAD KGHKYVTVVA NFGATVVEKA 

       130        140        150        160        170        180 
VLVSFQSGYL FIQTDKTIYT PGSTVFYRIF TVDNNLLPVG KTVVIVIETP DGVPIKRDIL 

       190        200        210        220        230        240 
SSHNQYGILP LSWNIPELVN MGQWKIRAFY EHAPKQTFSA EFEVKEYVLP SFEVLVEPTE 

       250        260        270        280        290        300 
KFYYIHGPKG LEVSITARFL YGKNVDGTAF VIFGVQDEDK KISLALSLTR VLIEDGSGEA 

       310        320        330        340        350        360 
VLSRKVLMDG VRPSSPEALV GKSLYVSVTV ILHSGSDMVE AERSGIPIVT SPYQIHFTKT 

       370        380        390        400        410        420 
PKFFKPAMPF DLMVFVTNPD GSPARRVPVV TQGSDAQALT QDDGVAKLSV NTPNNRQPLT 

       430        440        450        460        470        480 
ITVSTKKEGI PDARQATRTM QAQPYSTMHN SNNYLHLSVS RVELKPGDNL NVNFHLRTDA 

       490        500        510        520        530        540 
GQEAKIRYYT YLVMNKGKLL KAGRQVREPG QDLVVLSLPI TPEFIPSFRL VAYYTLIGAN 

       550        560        570        580        590        600 
GQREVVADSV WVDVKDSCVG TLVVKGDPRD NRQPAPGHQT TLRIEGNQGA RVGLVAVDKG 

       610        620        630        640        650        660 
VFVLNKKNKL TQSKIWDVVE KADIGCTPGS GKNYAGVFMD AGLTFKTNQG LQTDQREDPE 

       670        680        690        700        710        720 
CAKPAARRRR SVQLMERRMD KAGQYTDKGL RKCCEDGMRD IPMPYSCQRR ARLITQGESC 

       730        740        750        760        770        780 
LKAFMDCCNY ITKLREQHRR DHVLGLARSD VDEDIIPEED IISRSHFPES WLWTIEELKE 

       790        800        810        820        830        840 
PEKNGISTKV MNIFLKDSIT TWEILAVSLS DKKGICVADP YEITVMQDFF IDLRLPYSVV 

       850        860        870        880        890        900 
RNEQVEIRAV LFNYREQEKL KVRVELLHNP AFCSMATAKK RYYQTIEIPP KSSVAVPYVI 

       910        920        930        940        950        960 
VPLKIGLQEV EVKAAVFNHF ISDGVKKILK VVPEGMRVNK TVAVRTLDPE HLNQGGVQRE 

       970        980        990       1000       1010       1020 
DVNAADLSDQ VPDTDSETRI LLQGTPVAQM AEDAVDGERL KHLIVTPSGC GEQNMIGMTP 

      1030       1040       1050       1060       1070       1080 
TVIAVHYLDQ TEQWEKFGLE KRQEALELIK KGYTQQLAFK QPISAYAAFN NRPPSTWLTA 

      1090       1100       1110       1120       1130       1140 
MWSRSFSLAA NLIAIDSQVL CGAVKWLILE KQKPDGVFQE DGPVIHQEMI GGFRNTKEAD 

      1150       1160       1170       1180       1190       1200 
VSLTAFVLIA LQEARDICEG QVNSLPGSIN KAGEYLEASY LNLQRPYTVA IAGYALALMN 

      1210       1220       1230       1240       1250       1260 
KLEEPYLTKF LNTAKDRNRW EEPGQQLYNV EATSYALLAL LLLKDFDSVP PVVRWLNDER 

      1270       1280       1290       1300       1310       1320 
YYGGGYGSTQ ATFMVFQALA QYRADVPDHK DLNMDVSLHL PSRSSPTVFR LLWESGSLLR 

      1330       1340       1350       1360       1370       1380 
SEETKQNEGF SLTAKGKGQG TLSVVTVYHA KVKGKTTCKK FDLRVTIKPA PETAKKPQDA 

      1390       1400       1410       1420       1430       1440 
KSSMILDICT RYLGDVDATM SILDISMMTG FIPDTNDLEL LSSGVDRYIS KYEMDKAFSN 

      1450       1460       1470       1480       1490       1500 
KNTLIIYLEK ISHSEEDCLS FKVHQFFNVG LIQPGSVKVY SYYNLEESCT RFYHPEKDDG 

      1510       1520       1530       1540       1550       1560 
MLSKLCHNEM CRCAEENCFM HQSQDQVSLN ERLDKACEPG VDYVYKTKLT TIELSDDFDE 

      1570       1580       1590       1600       1610       1620 
YIMTIEQVIK SGSDEVQAGQ ERRFISHVKC RNALKLQKGK QYLMWGLSSD LWGEKPNTSY 

      1630       1640       1650       1660 
IIGKDTWVEH WPEAEERQDQ KNQKQCEDLG AFTETMVVFG CPN

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References

[1]	"Nucleotide and deduced amino acid sequence of rat complement C3." Misumi Y., Sohda M., Ikehara Y. Nucleic Acids Res. 18:2178-2178(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar. Tissue: Liver.
[2]	"Complement component C3-derived neutrophil chemotactic factors purified from exudate of rat carrageenin-induced inflammation." Nakagawa H., Komorita N. Biochem. Biophys. Res. Commun. 194:1181-1187(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 568-592 AND 671-687, FUNCTION. Tissue: Neutrophil.
[3]	"Purification, characterization, and amino acid sequence of rat anaphylatoxin (C3a)." Jacobs J.W., Rubin J.S., Hugli T.E., Bogardt R.A. Jr., Mariz I.K., Daniels J.S., Daughaday W.H., Bradshaw R.A. Biochemistry 17:5031-5038(1978) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 671-748.
[4]	"Nucleotide and deduced amino acid sequence of rat complement component C3a derived from Sprague-Dawley strain." Wahrmann M., Krieger S., Liewehr A. Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 671-748. Strain: Sprague-Dawley. Tissue: Liver.
[5]	"Structure at 1.44 A resolution of an N-terminally truncated form of the rat serum complement C3d fragment." Zanotti G., Bassetto A., Battistutta R., Folli C., Arcidiaco P., Stoppini M., Berni R. Biochim. Biophys. Acta 1478:232-238(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 960-969, X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF 1010-1286.
[6]	"Estrogen regulation of tissue-specific expression of complement C3." Sundstrom S.A., Komm B.S., Ponce-De-Leon H., Yi Z., Teuscher C., Lyttle C.R. J. Biol. Chem. 264:16941-16947(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1316-1595.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X52477 mRNA. Translation: CAA36716.1.
AF286158 mRNA. Translation: AAG00532.1.
M29866 mRNA. Translation: AAA40837.1.

IPI

IPI00480639.

PIR

C3RT. S15764.

RefSeq

NP_058690.2. NM_016994.2.

UniGene

Rn.11378.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QQF	X-ray	1.45	A	1010-1286	[»]
1QSJ	X-ray	1.90	A/B/C/D	1010-1286	[»]

ProteinModelPortal

P01026.

SMR

P01026. Positions 25-663, 672-1663.

ModBase

Search...

Protein family/group databases

MEROPS

I39.950.

PTM databases

PhosphoSite

P01026.

Proteomic databases

PRIDE

P01026.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

24232.

KEGG

rno:24232.

Organism-specific databases

CTD

718.

RGD

2232. C3.

Phylogenomic databases

HOVERGEN

HBG005110.

K03990.

Gene expression databases

Genevestigator

P01026.

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

EvolutionaryTrace

P01026.

NextBio

602683.

Entry information

Entry name

CO3_RAT

Accession

Primary (citable) accession number: P01026
Secondary accession number(s): Q9ET19, Q9QV57, Q9QV58

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 1, 1990
Last modified:	April 3, 2013
This is version 138 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 12 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents