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P01026

- CO3_RAT

UniProt

P01026 - CO3_RAT

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Protein
Complement C3
Gene
C3
Organism
Rattus norvegicus (Rat)
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.1 Publication
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.1 Publication
Neutrophil chemotactic factor-2 acts as a chemoattractant for neurophils.1 Publication
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 By similarity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei747 – 7482Cleavage; by carboxypeptidases By similarity
Sitei748 – 7492Cleavage; by C3 convertase
Sitei959 – 9602Cleavage; by factor I Reviewed prediction
Sitei1303 – 13042Cleavage; by factor I By similarity
Sitei1320 – 13212Cleavage; by factor I By similarity

GO - Molecular functioni

  1. C5L2 anaphylatoxin chemotactic receptor binding Source: UniProtKB
  2. cofactor binding Source: RGD
  3. endopeptidase inhibitor activity Source: InterPro
  4. lipid binding Source: RGD
  5. protein binding Source: RGD

GO - Biological processi

  1. blood coagulation Source: RGD
  2. chemotaxis Source: UniProtKB-KW
  3. complement activation Source: RGD
  4. complement activation, alternative pathway Source: UniProtKB-KW
  5. complement activation, classical pathway Source: RGD
  6. fatty acid metabolic process Source: UniProtKB-KW
  7. inflammatory response Source: UniProtKB-KW
  8. positive regulation of ERK1 and ERK2 cascade Source: RGD
  9. positive regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
  10. positive regulation of developmental growth Source: RGD
  11. positive regulation of glucose transport Source: UniProtKB
  12. positive regulation of lipid storage Source: UniProtKB
  13. positive regulation of protein phosphorylation Source: UniProtKB
  14. regulation of triglyceride biosynthetic process Source: UniProtKB
  15. response to estradiol Source: RGD
  16. response to estrogen Source: RGD
  17. response to glucocorticoid Source: RGD
  18. response to magnesium ion Source: RGD
  19. response to progesterone Source: RGD
  20. tolerance induction Source: RGD
Complete GO annotation...

Keywords - Biological processi

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

Protein family/group databases

MEROPSiI39.950.

Names & Taxonomyi

Protein namesi
Gene namesi
Name:C3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2232. C3.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424
Add
BLAST
Chaini25 – 16631639Complement C3
PRO_0000005937Add
BLAST
Chaini25 – 666642Complement C3 beta chain
PRO_0000005938Add
BLAST
Chaini568 – ?Neutrophil chemotactic factor-2PRO_0000395292
Chaini671 – 1663993Complement C3 alpha chain
PRO_0000005939Add
BLAST
Chaini671 – 74878C3a anaphylatoxin
PRO_0000005940Add
BLAST
Chaini671 – 74777Acylation stimulating protein By similarity
PRO_0000419937Add
BLAST
Chaini749 – 1663915Complement C3b alpha' chain
PRO_0000005941Add
BLAST
Chaini749 – 959211Complement C3c alpha' chain fragment 1
PRO_0000273950Add
BLAST
Chaini960 – 1303344Complement C3dg fragment By similarity
PRO_0000273951Add
BLAST
Chaini960 – 100142Complement C3g fragment By similarity
PRO_0000273952Add
BLAST
Chaini1002 – 1303302Complement C3d fragment By similarity
PRO_0000273953Add
BLAST
Peptidei1304 – 132017Complement C3f fragment By similarity
PRO_0000273954Add
BLAST
Chaini1321 – 1663343Complement C3c alpha' chain fragment 2 By similarity
PRO_0000273955Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi558 ↔ 816Interchain (between beta and alpha chains) By similarity
Disulfide bondi626 ↔ 661 By similarity
Disulfide bondi693 ↔ 720 By similarity
Disulfide bondi694 ↔ 727 By similarity
Disulfide bondi707 ↔ 728 By similarity
Disulfide bondi873 ↔ 1513 By similarity
Glycosylationi939 – 9391N-linked (GlcNAc...) Inferred
Cross-linki1010 ↔ 1013Isoglutamyl cysteine thioester (Cys-Gln) By similarity
Disulfide bondi1101 ↔ 1158 By similarity
Disulfide bondi1358 ↔ 1489 By similarity
Disulfide bondi1389 ↔ 1458 By similarity
Disulfide bondi1506 ↔ 1511 By similarity
Disulfide bondi1518 ↔ 1590 By similarity
Disulfide bondi1537 ↔ 1661 By similarity
Glycosylationi1617 – 16171N-linked (GlcNAc...) Inferred

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 By similarity.
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

PRIDEiP01026.

PTM databases

PhosphoSiteiP01026.

Expressioni

Gene expression databases

GenevestigatoriP01026.

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.

Protein-protein interaction databases

BioGridi246419. 1 interaction.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1013 – 103119
Helixi1034 – 10374
Helixi1039 – 10413
Helixi1042 – 105716
Helixi1076 – 108914
Turni1090 – 10923
Helixi1097 – 111115
Helixi1127 – 11348
Helixi1139 – 115820
Turni1159 – 11613
Helixi1165 – 118016
Helixi1186 – 119813
Helixi1206 – 12138
Turni1216 – 12183
Helixi1226 – 124217
Turni1246 – 12483
Helixi1249 – 125810
Helixi1269 – 128517

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QQFX-ray1.45A1010-1286[»]
1QSJX-ray1.90A/B/C/D1010-1286[»]
ProteinModelPortaliP01026.
SMRiP01026. Positions 25-663, 672-1663.

Miscellaneous databases

EvolutionaryTraceiP01026.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini693 – 72836Anaphylatoxin-like
Add
BLAST
Domaini1518 – 1661144NTR
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1424 – 145633Properdin-binding By similarity
Add
BLAST

Sequence similaritiesi

Contains 1 NTR domain.

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG005110.
KOiK03990.
PhylomeDBiP01026.

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]

Sequencei

Sequence statusi: Complete.

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

P01026-1 [UniParc]FASTAAdd to Basket

« Hide

MGPTSGSQLL VLLLLLASSL LALGSPMYSI ITPNVLRLES EETFILEAHD     50
AQGDVPVTVT VQDFLKKQVL TSEKTVLTGA TGHLNRVFIK IPASKEFNAD 100
KGHKYVTVVA NFGATVVEKA VLVSFQSGYL FIQTDKTIYT PGSTVFYRIF 150
TVDNNLLPVG KTVVIVIETP DGVPIKRDIL SSHNQYGILP LSWNIPELVN 200
MGQWKIRAFY EHAPKQTFSA EFEVKEYVLP SFEVLVEPTE KFYYIHGPKG 250
LEVSITARFL YGKNVDGTAF VIFGVQDEDK KISLALSLTR VLIEDGSGEA 300
VLSRKVLMDG VRPSSPEALV GKSLYVSVTV ILHSGSDMVE AERSGIPIVT 350
SPYQIHFTKT PKFFKPAMPF DLMVFVTNPD GSPARRVPVV TQGSDAQALT 400
QDDGVAKLSV NTPNNRQPLT ITVSTKKEGI PDARQATRTM QAQPYSTMHN 450
SNNYLHLSVS RVELKPGDNL NVNFHLRTDA GQEAKIRYYT YLVMNKGKLL 500
KAGRQVREPG QDLVVLSLPI TPEFIPSFRL VAYYTLIGAN GQREVVADSV 550
WVDVKDSCVG TLVVKGDPRD NRQPAPGHQT TLRIEGNQGA RVGLVAVDKG 600
VFVLNKKNKL TQSKIWDVVE KADIGCTPGS GKNYAGVFMD AGLTFKTNQG 650
LQTDQREDPE CAKPAARRRR SVQLMERRMD KAGQYTDKGL RKCCEDGMRD 700
IPMPYSCQRR ARLITQGESC LKAFMDCCNY ITKLREQHRR DHVLGLARSD 750
VDEDIIPEED IISRSHFPES WLWTIEELKE PEKNGISTKV MNIFLKDSIT 800
TWEILAVSLS DKKGICVADP YEITVMQDFF IDLRLPYSVV RNEQVEIRAV 850
LFNYREQEKL KVRVELLHNP AFCSMATAKK RYYQTIEIPP KSSVAVPYVI 900
VPLKIGLQEV EVKAAVFNHF ISDGVKKILK VVPEGMRVNK TVAVRTLDPE 950
HLNQGGVQRE DVNAADLSDQ VPDTDSETRI LLQGTPVAQM AEDAVDGERL 1000
KHLIVTPSGC GEQNMIGMTP TVIAVHYLDQ TEQWEKFGLE KRQEALELIK 1050
KGYTQQLAFK QPISAYAAFN NRPPSTWLTA MWSRSFSLAA NLIAIDSQVL 1100
CGAVKWLILE KQKPDGVFQE DGPVIHQEMI GGFRNTKEAD VSLTAFVLIA 1150
LQEARDICEG QVNSLPGSIN KAGEYLEASY LNLQRPYTVA IAGYALALMN 1200
KLEEPYLTKF LNTAKDRNRW EEPGQQLYNV EATSYALLAL LLLKDFDSVP 1250
PVVRWLNDER YYGGGYGSTQ ATFMVFQALA QYRADVPDHK DLNMDVSLHL 1300
PSRSSPTVFR LLWESGSLLR SEETKQNEGF SLTAKGKGQG TLSVVTVYHA 1350
KVKGKTTCKK FDLRVTIKPA PETAKKPQDA KSSMILDICT RYLGDVDATM 1400
SILDISMMTG FIPDTNDLEL LSSGVDRYIS KYEMDKAFSN KNTLIIYLEK 1450
ISHSEEDCLS FKVHQFFNVG LIQPGSVKVY SYYNLEESCT RFYHPEKDDG 1500
MLSKLCHNEM CRCAEENCFM HQSQDQVSLN ERLDKACEPG VDYVYKTKLT 1550
TIELSDDFDE YIMTIEQVIK SGSDEVQAGQ ERRFISHVKC RNALKLQKGK 1600
QYLMWGLSSD LWGEKPNTSY IIGKDTWVEH WPEAEERQDQ KNQKQCEDLG 1650
AFTETMVVFG CPN 1663
Length:1,663
Mass (Da):186,460
Last modified:August 1, 1990 - v3
Checksum:i2F87CCB143CDD4BC
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti704 – 7041P → K in AAG00532. 1 Publication
Sequence conflicti721 – 7222LK → KL AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52477 mRNA. Translation: CAA36716.1.
AF286158 mRNA. Translation: AAG00532.1.
M29866 mRNA. Translation: AAA40837.1.
PIRiS15764. C3RT.
RefSeqiNP_058690.2. NM_016994.2.
UniGeneiRn.11378.

Genome annotation databases

GeneIDi24232.
KEGGirno:24232.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52477 mRNA. Translation: CAA36716.1 .
AF286158 mRNA. Translation: AAG00532.1 .
M29866 mRNA. Translation: AAA40837.1 .
PIRi S15764. C3RT.
RefSeqi NP_058690.2. NM_016994.2.
UniGenei Rn.11378.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P01026.
SMRi P01026. Positions 25-663, 672-1663.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 246419. 1 interaction.

Protein family/group databases

MEROPSi I39.950.

PTM databases

PhosphoSitei P01026.

Proteomic databases

PRIDEi P01026.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 24232.
KEGGi rno:24232.

Organism-specific databases

CTDi 718.
RGDi 2232. C3.

Phylogenomic databases

HOVERGENi HBG005110.
KOi K03990.
PhylomeDBi P01026.

Miscellaneous databases

EvolutionaryTracei P01026.
NextBioi 602683.

Gene expression databases

Genevestigatori P01026.

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 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.

Entry informationi

Entry nameiCO3_RAT
AccessioniPrimary (citable) accession number: P01026
Secondary accession number(s): Q9ET19, Q9QV57, Q9QV58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1990
Last modified: June 11, 2014
This is version 146 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi