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Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc) (Neutrophil chemotactic factor-2) (ENCF-2); Complement C3 alpha chain; C3a anaphylatoxin (Neutrophil chemotactic factor-1) (ENCF-1); 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_RAT                 Reviewed;        1663 AA.
P01026; Q9ET19; Q9QV57; Q9QV58;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 3.
20-JUN-2018, entry version 170.
RecName: Full=Complement C3;
Contains:
RecName: Full=Complement C3 beta chain;
Contains:
RecName: Full=C3-beta-c;
Short=C3bc;
AltName: Full=Neutrophil chemotactic factor-2;
Short=ENCF-2;
Contains:
RecName: Full=Complement C3 alpha chain;
Contains:
RecName: Full=C3a anaphylatoxin;
AltName: Full=Neutrophil chemotactic factor-1;
Short=ENCF-1;
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Liver;
PubMed=2336397; DOI=10.1093/nar/18.8.2178;
Misumi Y., Sohda M., Ikehara Y.;
"Nucleotide and deduced amino acid sequence of rat complement C3.";
Nucleic Acids Res. 18:2178-2178(1990).
[2]
PROTEIN SEQUENCE OF 568-592 AND 671-687, IDENTIFICATION OF C3A
ANAPHYLATOXIN AND C3-BETA-C, AND FUNCTION.
TISSUE=Neutrophil;
PubMed=8352775; DOI=10.1006/bbrc.1993.1947;
Nakagawa H., Komorita N.;
"Complement component C3-derived neutrophil chemotactic factors
purified from exudate of rat carrageenin-induced inflammation.";
Biochem. Biophys. Res. Commun. 194:1181-1187(1993).
[3]
PROTEIN SEQUENCE OF 671-748.
PubMed=309768; DOI=10.1021/bi00616a027;
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.;
"Purification, characterization, and amino acid sequence of rat
anaphylatoxin (C3a).";
Biochemistry 17:5031-5038(1978).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 671-748.
STRAIN=Sprague-Dawley; TISSUE=Liver;
Wahrmann M., Krieger S., Liewehr A.;
"Nucleotide and deduced amino acid sequence of rat complement
component C3a derived from Sprague-Dawley strain.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[5]
PROTEIN SEQUENCE OF 960-969, AND X-RAY CRYSTALLOGRAPHY (1.44
ANGSTROMS) OF 1010-1286.
PubMed=10825534; DOI=10.1016/S0167-4838(00)00040-6;
Zanotti G., Bassetto A., Battistutta R., Folli C., Arcidiaco P.,
Stoppini M., Berni R.;
"Structure at 1.44 A resolution of an N-terminally truncated form of
the rat serum complement C3d fragment.";
Biochim. Biophys. Acta 1478:232-238(2000).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1316-1595.
PubMed=2674144;
Sundstrom S.A., Komm B.S., Ponce-De-Leon H., Yi Z., Teuscher C.,
Lyttle C.R.;
"Estrogen regulation of tissue-specific expression of complement C3.";
J. Biol. Chem. 264:16941-16947(1989).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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.
{ECO:0000269|PubMed:8352775}.
-!- 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 (PubMed:8352775).
{ECO:0000269|PubMed:8352775}.
-!- FUNCTION: C3-beta-c: Acts as a chemoattractant for neutrophils in
chronic inflammation. {ECO:0000269|PubMed:8352775}.
-!- FUNCTION: 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).
{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}.
-!- 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 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). {ECO:0000250}.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000250|UniProtKB:P01024}.
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EMBL; X52477; CAA36716.1; -; mRNA.
EMBL; AF286158; AAG00532.1; -; mRNA.
EMBL; M29866; AAA40837.1; -; mRNA.
PIR; S15764; C3RT.
RefSeq; NP_058690.2; NM_016994.2.
UniGene; Rn.11378; -.
PDB; 1QQF; X-ray; 1.45 A; A=1010-1286.
PDB; 1QSJ; X-ray; 1.90 A; A/B/C/D=1010-1286.
PDBsum; 1QQF; -.
PDBsum; 1QSJ; -.
ProteinModelPortal; P01026; -.
SMR; P01026; -.
BioGrid; 246419; 1.
STRING; 10116.ENSRNOP00000066885; -.
MEROPS; I39.950; -.
CarbonylDB; P01026; -.
iPTMnet; P01026; -.
PhosphoSitePlus; P01026; -.
PaxDb; P01026; -.
PRIDE; P01026; -.
GeneID; 24232; -.
KEGG; rno:24232; -.
CTD; 718; -.
RGD; 2232; C3.
eggNOG; KOG1366; Eukaryota.
eggNOG; ENOG410XRED; LUCA.
HOVERGEN; HBG005110; -.
InParanoid; P01026; -.
KO; K03990; -.
PhylomeDB; P01026; -.
EvolutionaryTrace; P01026; -.
PRO; PR:P01026; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0031715; F:C5L2 anaphylatoxin chemotactic receptor binding; ISS:UniProtKB.
GO; GO:0048037; F:cofactor binding; IPI:RGD.
GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
GO; GO:0008289; F:lipid binding; IDA:RGD.
GO; GO:0007596; P:blood coagulation; IMP:RGD.
GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
GO; GO:0006956; P:complement activation; IDA:RGD.
GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
GO; GO:0006958; P:complement activation, classical pathway; TAS:RGD.
GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0048639; P:positive regulation of developmental growth; IDA:RGD.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:RGD.
GO; GO:0045745; P:positive regulation of G-protein coupled receptor protein signaling pathway; ISS:UniProtKB.
GO; GO:0010828; P:positive regulation of glucose transmembrane 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.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0043627; P:response to estrogen; IEP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0032026; P:response to magnesium ion; IEP:RGD.
GO; GO:0032570; P:response to progesterone; IEP:RGD.
GO; GO:0002507; P:tolerance induction; IEP:RGD.
CDD; cd03583; NTR_complement_C3; 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;
3D-structure; Chemotaxis; 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 24
CHAIN 25 1663 Complement C3.
/FTId=PRO_0000005937.
CHAIN 25 666 Complement C3 beta chain.
/FTId=PRO_0000005938.
CHAIN 568 666 C3-beta-c.
/FTId=PRO_0000395292.
CHAIN 671 1663 Complement C3 alpha chain.
/FTId=PRO_0000005939.
CHAIN 671 748 C3a anaphylatoxin.
/FTId=PRO_0000005940.
CHAIN 671 747 Acylation stimulating protein.
{ECO:0000250}.
/FTId=PRO_0000419937.
CHAIN 749 1663 Complement C3b alpha' chain.
/FTId=PRO_0000005941.
CHAIN 749 959 Complement C3c alpha' chain fragment 1.
/FTId=PRO_0000273950.
CHAIN 960 1303 Complement C3dg fragment. {ECO:0000250}.
/FTId=PRO_0000273951.
CHAIN 960 1001 Complement C3g fragment. {ECO:0000250}.
/FTId=PRO_0000273952.
CHAIN 1002 1303 Complement C3d fragment. {ECO:0000250}.
/FTId=PRO_0000273953.
PEPTIDE 1304 1320 Complement C3f fragment. {ECO:0000250}.
/FTId=PRO_0000273954.
CHAIN 1321 1663 Complement C3c alpha' chain fragment 2.
{ECO:0000250}.
/FTId=PRO_0000273955.
DOMAIN 693 728 Anaphylatoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00022}.
DOMAIN 1518 1661 NTR. {ECO:0000255|PROSITE-
ProRule:PRU00295}.
REGION 1424 1456 Properdin-binding. {ECO:0000250}.
SITE 747 748 Cleavage; by carboxypeptidases.
{ECO:0000250}.
SITE 748 749 Cleavage; by C3 convertase.
SITE 959 960 Cleavage; by factor I. {ECO:0000255}.
SITE 1303 1304 Cleavage; by factor I. {ECO:0000250}.
SITE 1320 1321 Cleavage; by factor I. {ECO:0000250}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 303 303 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 671 671 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 968 968 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 1321 1321 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 1573 1573 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
CARBOHYD 939 939 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 1617 1617 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 558 816 Interchain (between beta and alpha
chains). {ECO:0000255|PROSITE-
ProRule:PRU00022, ECO:0000255|PROSITE-
ProRule:PRU00295}.
DISULFID 626 661 {ECO:0000250}.
DISULFID 693 720 {ECO:0000250}.
DISULFID 694 727 {ECO:0000250}.
DISULFID 707 728 {ECO:0000250}.
DISULFID 873 1513 {ECO:0000250}.
DISULFID 1101 1158 {ECO:0000250}.
DISULFID 1358 1489 {ECO:0000250}.
DISULFID 1389 1458 {ECO:0000250}.
DISULFID 1506 1511 {ECO:0000250}.
DISULFID 1518 1590 {ECO:0000250}.
DISULFID 1537 1661 {ECO:0000250}.
CROSSLNK 1010 1013 Isoglutamyl cysteine thioester (Cys-Gln).
{ECO:0000250}.
CONFLICT 704 704 P -> K (in Ref. 4; AAG00532).
{ECO:0000305}.
CONFLICT 721 722 LK -> KL (in Ref. 3; AA sequence).
{ECO:0000305}.
HELIX 1013 1031 {ECO:0000244|PDB:1QQF}.
HELIX 1034 1037 {ECO:0000244|PDB:1QQF}.
HELIX 1039 1041 {ECO:0000244|PDB:1QQF}.
HELIX 1042 1057 {ECO:0000244|PDB:1QQF}.
HELIX 1076 1089 {ECO:0000244|PDB:1QQF}.
TURN 1090 1092 {ECO:0000244|PDB:1QQF}.
HELIX 1097 1111 {ECO:0000244|PDB:1QQF}.
HELIX 1127 1134 {ECO:0000244|PDB:1QQF}.
HELIX 1139 1158 {ECO:0000244|PDB:1QQF}.
TURN 1159 1161 {ECO:0000244|PDB:1QQF}.
HELIX 1165 1180 {ECO:0000244|PDB:1QQF}.
HELIX 1186 1198 {ECO:0000244|PDB:1QQF}.
HELIX 1206 1213 {ECO:0000244|PDB:1QQF}.
TURN 1216 1218 {ECO:0000244|PDB:1QQF}.
HELIX 1226 1242 {ECO:0000244|PDB:1QQF}.
TURN 1246 1248 {ECO:0000244|PDB:1QSJ}.
HELIX 1249 1258 {ECO:0000244|PDB:1QQF}.
HELIX 1269 1285 {ECO:0000244|PDB:1QQF}.
SEQUENCE 1663 AA; 186460 MW; 2F87CCB143CDD4BC CRC64;
MGPTSGSQLL VLLLLLASSL LALGSPMYSI ITPNVLRLES EETFILEAHD AQGDVPVTVT
VQDFLKKQVL TSEKTVLTGA TGHLNRVFIK IPASKEFNAD KGHKYVTVVA NFGATVVEKA
VLVSFQSGYL FIQTDKTIYT PGSTVFYRIF TVDNNLLPVG KTVVIVIETP DGVPIKRDIL
SSHNQYGILP LSWNIPELVN MGQWKIRAFY EHAPKQTFSA EFEVKEYVLP SFEVLVEPTE
KFYYIHGPKG LEVSITARFL YGKNVDGTAF VIFGVQDEDK KISLALSLTR VLIEDGSGEA
VLSRKVLMDG VRPSSPEALV GKSLYVSVTV ILHSGSDMVE AERSGIPIVT SPYQIHFTKT
PKFFKPAMPF DLMVFVTNPD GSPARRVPVV TQGSDAQALT QDDGVAKLSV NTPNNRQPLT
ITVSTKKEGI PDARQATRTM QAQPYSTMHN SNNYLHLSVS RVELKPGDNL NVNFHLRTDA
GQEAKIRYYT YLVMNKGKLL KAGRQVREPG QDLVVLSLPI TPEFIPSFRL VAYYTLIGAN
GQREVVADSV WVDVKDSCVG TLVVKGDPRD NRQPAPGHQT TLRIEGNQGA RVGLVAVDKG
VFVLNKKNKL TQSKIWDVVE KADIGCTPGS GKNYAGVFMD AGLTFKTNQG LQTDQREDPE
CAKPAARRRR SVQLMERRMD KAGQYTDKGL RKCCEDGMRD IPMPYSCQRR ARLITQGESC
LKAFMDCCNY ITKLREQHRR DHVLGLARSD VDEDIIPEED IISRSHFPES WLWTIEELKE
PEKNGISTKV MNIFLKDSIT TWEILAVSLS DKKGICVADP YEITVMQDFF IDLRLPYSVV
RNEQVEIRAV LFNYREQEKL KVRVELLHNP AFCSMATAKK RYYQTIEIPP KSSVAVPYVI
VPLKIGLQEV EVKAAVFNHF ISDGVKKILK VVPEGMRVNK TVAVRTLDPE HLNQGGVQRE
DVNAADLSDQ VPDTDSETRI LLQGTPVAQM AEDAVDGERL KHLIVTPSGC GEQNMIGMTP
TVIAVHYLDQ TEQWEKFGLE KRQEALELIK KGYTQQLAFK QPISAYAAFN NRPPSTWLTA
MWSRSFSLAA NLIAIDSQVL CGAVKWLILE KQKPDGVFQE DGPVIHQEMI GGFRNTKEAD
VSLTAFVLIA LQEARDICEG QVNSLPGSIN KAGEYLEASY LNLQRPYTVA IAGYALALMN
KLEEPYLTKF LNTAKDRNRW EEPGQQLYNV EATSYALLAL LLLKDFDSVP PVVRWLNDER
YYGGGYGSTQ ATFMVFQALA QYRADVPDHK DLNMDVSLHL PSRSSPTVFR LLWESGSLLR
SEETKQNEGF SLTAKGKGQG TLSVVTVYHA KVKGKTTCKK FDLRVTIKPA PETAKKPQDA
KSSMILDICT RYLGDVDATM SILDISMMTG FIPDTNDLEL LSSGVDRYIS KYEMDKAFSN
KNTLIIYLEK ISHSEEDCLS FKVHQFFNVG LIQPGSVKVY SYYNLEESCT RFYHPEKDDG
MLSKLCHNEM CRCAEENCFM HQSQDQVSLN ERLDKACEPG VDYVYKTKLT TIELSDDFDE
YIMTIEQVIK SGSDEVQAGQ ERRFISHVKC RNALKLQKGK QYLMWGLSSD LWGEKPNTSY
IIGKDTWVEH WPEAEERQDQ KNQKQCEDLG AFTETMVVFG CPN


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GENTAUR France SARL
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Tel 01 43 25 01 50

Fax 01 43 25 01 60
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BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

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GENTAUR GmbH
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Support Karolina Elandt
Tel: 0035929830070
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San Jose, CA 95123
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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