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Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (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]

 CO3_PIG                 Reviewed;        1661 AA.
P01025; O97940; Q9GKP1;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
31-OCT-2012, sequence version 2.
25-OCT-2017, entry version 96.
RecName: Full=Complement C3;
Contains:
RecName: Full=Complement C3 beta chain;
Contains:
RecName: Full=C3-beta-c;
Short=C3bc;
Contains:
RecName: Full=Complement C3 alpha chain;
Contains:
RecName: Full=C3a anaphylatoxin;
Contains:
RecName: Full=Acylation stimulating protein;
Short=ASP;
AltName: Full=C3adesArg;
Contains:
RecName: Full=Complement C3b alpha' chain;
Contains:
RecName: Full=Complement C3c alpha' chain fragment 1;
Contains:
RecName: Full=Complement C3dg fragment;
Contains:
RecName: Full=Complement C3g fragment;
Contains:
RecName: Full=Complement C3d fragment;
Contains:
RecName: Full=Complement C3f fragment;
Contains:
RecName: Full=Complement C3c alpha' chain fragment 2;
Flags: Precursor;
Name=C3;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=11419349; DOI=10.1046/j.1365-2052.2001.0647f.x;
Wimmers K., Mekchay S., Ponsuksili S., Hardge T., Yerle M.,
Schellander K.;
"Polymorphic sites in exon 15 and 30 of the porcine C3 gene.";
Anim. Genet. 32:46-47(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Liver;
PubMed=12927082; DOI=10.1186/1297-9686-35-S1-S83;
Mekchay S., Ponsuksili S., Schellander K., Wimmers K.;
"Association of the porcine C3 gene with haemolytic complement
activity in the pig.";
Genet. Sel. Evol. 35:S83-S96(2003).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
TISSUE=Liver;
PubMed=12557058;
Wimmers K., Mekchay S., Schellander K., Ponsuksili S.;
"Molecular characterization of the pig C3 gene and its association
with complement activity.";
Immunogenetics 54:714-724(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 607-799.
TISSUE=Adipose tissue;
Miner J.L., Toombs C.F.;
"Porcine acylation stimulating protein.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[5]
PROTEIN SEQUENCE OF 670-746.
PubMed=956663;
Corbin N.C., Hugli T.E.;
"The primary structure of porcine C3a anaphylatoxin.";
J. Immunol. 117:990-995(1976).
-!- 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 (By
similarity). {ECO:0000250}.
-!- FUNCTION: 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. In chronic inflammation, acts as a
chemoattractant for neutrophils (By similarity). {ECO:0000250}.
-!- FUNCTION: C3-beta-c: Acts as a chemoattractant for neutrophils in
chronic inflammation. {ECO:0000250}.
-!- FUNCTION: Acylation stimulating protein: adipogenic hormone that
stimulates triglyceride (TG) synthesis and glucose transport in
adipocytes, regulating fat storage and playing a role in post-
prandial TG clearance. Appears to stimulate TG synthesis via
activation of the PLC, MAPK and AKT signaling pathways. Ligand for
C5AR2. Promotes the phosphorylation, ARRB2-internalization and
recycling of C5AR2 (By similarity). {ECO:0000250}.
-!- SUBUNIT: 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). {ECO:0000250}.
-!- INTERACTION:
C7EYC8:gC (xeno); NbExp=2; IntAct=EBI-11688674, EBI-11688666;
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: 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 carboxylases to release the C-
termianl arginine residue generating the acylation stimulating
protein (ASP). Levels of ASP are increased in adipocytes in the
postprandial period and by insulin and dietary chylomicrons (By
similarity). {ECO:0000250}.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000250|UniProtKB:P01024}.
-----------------------------------------------------------------------
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EMBL; AF154933; AAG40565.1; -; mRNA.
EMBL; AJ494748; CAD38823.2; -; Genomic_DNA.
EMBL; AF110278; AAC99785.1; -; mRNA.
PIR; A01259; A01259.
RefSeq; NP_999174.1; NM_214009.1.
UniGene; Ssc.61; -.
ProteinModelPortal; P01025; -.
SMR; P01025; -.
IntAct; P01025; 1.
STRING; 9823.ENSSSCP00000014399; -.
MEROPS; I39.950; -.
PeptideAtlas; P01025; -.
PRIDE; P01025; -.
GeneID; 397072; -.
KEGG; ssc:397072; -.
CTD; 718; -.
InParanoid; P01025; -.
KO; K03990; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0031715; F:C5L2 anaphylatoxin chemotactic receptor binding; ISS:UniProtKB.
GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IDA:AgBase.
GO; GO:0045745; P:positive regulation of G-protein coupled receptor protein signaling pathway; ISS:UniProtKB.
GO; GO:0010828; P:positive regulation of glucose transport; ISS:UniProtKB.
GO; GO:0010884; P:positive regulation of lipid storage; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0010866; P:regulation of triglyceride biosynthetic process; ISS:UniProtKB.
CDD; cd03583; NTR_complement_C3; 1.
Gene3D; 1.20.91.20; -; 1.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 2.60.40.690; -; 1.
InterPro; IPR009048; A-macroglobulin_rcpt-bd.
InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
InterPro; IPR011626; A2M_comp.
InterPro; IPR002890; A2M_N.
InterPro; IPR011625; A2M_N_2.
InterPro; IPR000020; Anaphylatoxin/fibulin.
InterPro; IPR018081; Anaphylatoxin_comp_syst.
InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
InterPro; IPR035711; Complement_C3-like.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR001599; Macroglobln_a2.
InterPro; IPR019742; MacrogloblnA2_CS.
InterPro; IPR019565; MacrogloblnA2_thiol-ester-bond.
InterPro; IPR001134; Netrin_domain.
InterPro; IPR018933; Netrin_module_non-TIMP.
InterPro; IPR035815; NTR_complement_C3.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
InterPro; IPR008993; TIMP-like_OB-fold.
PANTHER; PTHR11412:SF81; PTHR11412:SF81; 1.
Pfam; PF00207; A2M; 1.
Pfam; PF07678; A2M_comp; 1.
Pfam; PF01835; A2M_N; 1.
Pfam; PF07703; A2M_N_2; 1.
Pfam; PF07677; A2M_recep; 1.
Pfam; PF01821; ANATO; 1.
Pfam; PF01759; NTR; 1.
Pfam; PF10569; Thiol-ester_cl; 1.
PRINTS; PR00004; ANAPHYLATOXN.
SMART; SM01360; A2M; 1.
SMART; SM01359; A2M_N_2; 1.
SMART; SM01361; A2M_recep; 1.
SMART; SM00104; ANATO; 1.
SMART; SM00643; C345C; 1.
SUPFAM; SSF47686; SSF47686; 1.
SUPFAM; SSF48239; SSF48239; 1.
SUPFAM; SSF49410; SSF49410; 1.
SUPFAM; SSF50242; SSF50242; 1.
PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
PROSITE; PS50189; NTR; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Complement alternate pathway;
Complement pathway; Complete proteome; Direct protein sequencing;
Disulfide bond; Fatty acid metabolism; Glycoprotein; Immunity;
Inflammatory response; Innate immunity; Lipid metabolism;
Phosphoprotein; Reference proteome; Secreted; Signal; Thioester bond.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 1661 Complement C3.
/FTId=PRO_0000419922.
CHAIN 23 665 Complement C3 beta chain. {ECO:0000250}.
/FTId=PRO_0000419923.
CHAIN 567 665 C3-beta-c. {ECO:0000250}.
/FTId=PRO_0000430432.
CHAIN 670 1661 Complement C3 alpha chain. {ECO:0000250}.
/FTId=PRO_0000419924.
CHAIN 670 746 C3a anaphylatoxin.
/FTId=PRO_0000419925.
CHAIN 670 745 Acylation stimulating protein.
{ECO:0000250}.
/FTId=PRO_0000419926.
CHAIN 747 1661 Complement C3b alpha' chain.
{ECO:0000250}.
/FTId=PRO_0000419927.
CHAIN 747 953 Complement C3c alpha' chain fragment 1.
{ECO:0000250}.
/FTId=PRO_0000419928.
CHAIN 954 1302 Complement C3dg fragment. {ECO:0000250}.
/FTId=PRO_0000419929.
CHAIN 954 1000 Complement C3g fragment. {ECO:0000250}.
/FTId=PRO_0000419930.
CHAIN 1001 1302 Complement C3d fragment. {ECO:0000250}.
/FTId=PRO_0000419931.
PEPTIDE 1303 1319 Complement C3f fragment. {ECO:0000250}.
/FTId=PRO_0000419932.
CHAIN 1320 1661 Complement C3c alpha' chain fragment 2.
{ECO:0000250}.
/FTId=PRO_0000419933.
DOMAIN 691 726 Anaphylatoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00022}.
DOMAIN 1516 1659 NTR. {ECO:0000255|PROSITE-
ProRule:PRU00295}.
REGION 1422 1454 Properdin-binding. {ECO:0000250}.
SITE 745 746 Cleavage; by carboxypeptidases.
{ECO:0000250}.
SITE 746 747 Cleavage; by C3 convertase.
{ECO:0000250}.
SITE 1301 1302 Cleavage; by factor I. {ECO:0000250}.
SITE 1318 1319 Cleavage; by factor I. {ECO:0000250}.
MOD_RES 38 38 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 70 70 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 670 670 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 966 966 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 1319 1319 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 1571 1571 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
CARBOHYD 937 937 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1615 1615 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 557 814 Interchain (between beta and alpha
chains). {ECO:0000255|PROSITE-
ProRule:PRU00022, ECO:0000255|PROSITE-
ProRule:PRU00295}.
DISULFID 625 660 {ECO:0000250}.
DISULFID 691 718 {ECO:0000250}.
DISULFID 692 725 {ECO:0000250}.
DISULFID 705 726 {ECO:0000250}.
DISULFID 871 1511 {ECO:0000250}.
DISULFID 1099 1156 {ECO:0000250}.
DISULFID 1356 1487 {ECO:0000250}.
DISULFID 1387 1456 {ECO:0000250}.
DISULFID 1504 1509 {ECO:0000250}.
DISULFID 1516 1588 {ECO:0000250}.
DISULFID 1535 1659 {ECO:0000250}.
DISULFID 1635 1644 {ECO:0000250}.
CROSSLNK 1008 1011 Isoglutamyl cysteine thioester (Cys-Gln).
{ECO:0000250}.
CONFLICT 679 679 D -> N (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 687 688 DV -> EL (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 698 698 D -> N (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 713 716 QHGD -> HQGN (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 724 724 D -> N (in Ref. 5; AA sequence).
{ECO:0000305}.
SEQUENCE 1661 AA; 186807 MW; 4899D0914BE3310C CRC64;
MGSTSGPRLL LLLLTSLPLA LGDPIYTIIT PNVLRLESEE MVVLEAHEGQ GDIRVSVTVH
DFPAKRQVLS SETTTLNNAN NYLSTVNIKI PASKEFKSEK GHKFVTVQAL FGNVQVEKVV
LVSLQSGYLF IQTDKTIYTP GSTVLYRIFT VDHKLLPVGQ TIVVTIETPE GIDIKRDSLS
SHNQFGILAL SWNIPELVNM GQWKIRAHYE DAPQQVFSAE FEVKEYVLPS FEVQVEPSEK
FYYIDDPNGL TVNIIARFLY GESVDGTAFV IFGVQDGDQR ISLSQSLTRV PIIDGTGEAT
LSQGVLLNGV HYSSVNDLVG KSIYVSVTVI LNSGSDMVEA ERTGIPIVTS PYQIHFTKTP
KFFKPAMPFD LMVYVTNPDG SPARHIPVVT EDFKVRSLTQ EDGVAKLSIN TPDNRNSLPI
TVRTEKDGIP AARQASKTMH VLPYNTQGNS KNYLHLSLPR VELKPGENLN VNFHLRTDPG
YQDKIRYFTY LIMNKGKLLK VGRQPRESGQ VVVVLPLTIT TDFIPSFRLV AYYTLIAANG
QREVVADSVW VDVKDSCVGT LVVKGGGKQD KQHRPGQQMT LEIQGERGAR VGLVAVDKGV
FVLNKKNKLT QRRIWDVVEK ADIGCTPGSG KDFAGVFTDA GLAFKSSKGL QTPQRADLEC
PKPAARKRRS VQLMEKRMDK LGQYSKDVRR CCEHGMRDNP MKFSCQRRAQ FIQHGDACVK
AFLDCCEYIA KLRQQHSRNK PLGLARSDLD EEIIPEEDII SRSQFPESWL WTIEEFKEPD
KNGISTKTMN VFLKDSITTW EILAVSLSDK KGICVADPYE VVVKQDFFID LRLPYSVVRN
EQVEIRAILY NYREAEDLKV RVELLYNPAF CSLATAKKRH QQTLTVPAKS SVPVPYIIVP
LKTGLQEVEV KAAVYNHFIS DGVKKTLKVV PEGMRVNKTV VTRTLDPEHK GQQGVQREEI
PPADLSDQVP DTESETKILL QGTPVAQMVE DAIDGDRLKH LIQTPSGCGE QNMIGMTPTV
IAVHYLDSTE QWEKFGLEKR QEALELIKKG YTQQLAFRQK NSAFAAFQDR LSSTLLTAYV
VKVFAMAANL IAIDSQVLCG AVKWLILEKQ KPDGVFEENG PVIHQEMIGG FKNTEEKDVS
LTAFVLIALQ EAKDICEPQV NSLLRSINKA RDFLADYYLE LKRPYTVAIA GYALALSDKL
DEPFLNKLLS TAKERNRWEE PGQKLHNVEA TSYALLALLV VKDFDSVPPI VRWLNEQRYY
GGGYGSTQAT FMVFQALAQY QKDVPDHKDL NLDVSIHLPS RSAPVRHRIL WESASLLRSE
ETKENEGFTL IAEGKGQGTL SVVTMYHGKA KGKTTCKKFD LKVSIHPAPE PVKKPQEAKS
SMVLDICTRY LGNQDATMSI LDISMMTGFS PDTEDLKLLS TGVDRYISKY ELNKALSNKN
TLIIYLDKIS HTLEDCISFK VHQYFNVGLI QPGSVKVYSY YNLDESCTRF YHPEKEDGML
NKLCHKEMCR CAEENCFMHH DEEEVTLDDR LERACEPGVD YVYKTRLLKK ELSDDFDDYI
MVIEQIIKSG SDEVQVGQER RFISHIKCRE ALKLKEGGHY LVWGVSSDLW GEKPNISYII
GKDTWVELWP DGDVCQDEEN QKQCQDLANF SENMVVFGCP N


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