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Breast cancer type 1 susceptibility protein homolog (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BRCA1)

 BRCA1_PANTR             Reviewed;        1863 AA.
Q9GKK8; O46484;
21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
21-NOV-2003, sequence version 2.
25-OCT-2017, entry version 134.
RecName: Full=Breast cancer type 1 susceptibility protein homolog;
EC=2.3.2.27 {ECO:0000250|UniProtKB:P38398};
AltName: Full=RING-type E3 ubiquitin transferase BRCA1 {ECO:0000305};
Name=BRCA1;
Pan troglodytes (Chimpanzee).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pan.
NCBI_TaxID=9598;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLU-309; GLY-590; GLU-731 AND
GLU-1100.
TISSUE=Blood;
Takeda R., Hink R.L., Jogodka C., Walter N.A.R., Messier W.;
"Positive selection on the human BRCA1 gene may have resulted from
pressure for prolonged care for infants.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=15385441; DOI=10.1093/hmg/ddh301;
Pavlicek A., Noskov V.N., Kouprina N., Barrett J.C., Jurka J.,
Larionov V.;
"Evolution of the tumor suppressor BRCA1 locus in primates:
implications for cancer predisposition.";
Hum. Mol. Genet. 13:2737-2751(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 225-1365, AND VARIANTS GLU-731
AND GLU-1100.
PubMed=9462745; DOI=10.1038/ng0298-155;
Hacia J.G., Makalowski W., Edgemon K., Erdos M.R., Robbins C.M.,
Fodor S.P.A., Brody L.C., Collins F.S.;
"Evolutionary sequence comparisons using high-density oligonucleotide
arrays.";
Nat. Genet. 18:155-158(1998).
-!- FUNCTION: E3 ubiquitin-protein ligase that specifically mediates
the formation of 'Lys-6'-linked polyubiquitin chains and plays a
central role in DNA repair by facilitating cellular responses to
DNA damage. It is unclear whether it also mediates the formation
of other types of polyubiquitin chains. The E3 ubiquitin-protein
ligase activity is required for its tumor suppressor function. The
BRCA1-BARD1 heterodimer coordinates a diverse range of cellular
pathways such as DNA damage repair, ubiquitination and
transcriptional regulation to maintain genomic stability.
Regulates centrosomal microtubule nucleation. Required for normal
cell cycle progression from G2 to mitosis. Required for
appropriate cell cycle arrests after ionizing irradiation in both
the S-phase and the G2 phase of the cell cycle. Involved in
transcriptional regulation of P21 in response to DNA damage.
Required for FANCD2 targeting to sites of DNA damage. May function
as a transcriptional regulator. Inhibits lipid synthesis by
binding to inactive phosphorylated ACACA and preventing its
dephosphorylation. Contributes to homologous recombination repair
(HRR) via its direct interaction with PALB2, fine-tunes
recombinational repair partly through its modulatory role in the
PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA
breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1
activation and controls cell cycle G2/M checkpoints on DNA damage
via BRCA1-mediated ubiquitination of RBBP8. Acts as a
transcriptional activator (By similarity).
{ECO:0000250|UniProtKB:P38398}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000250|UniProtKB:P38398}.
-!- SUBUNIT: Heterodimer with BARD1. Part of the BRCA1-associated
genome surveillance complex (BASC), which contains BRCA1, MSH2,
MSH6, MLH1, ATM, BLM, PMS2 and the MRE11-RAD50-NBN protein (MRN)
complex. This association could be a dynamic process changing
throughout the cell cycle and within subnuclear domains. Component
of the BRCA1-A complex, at least composed of BRCA1, BARD1,
UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1.
Interacts (via the BRCT domains) with ABRAXAS1 (phosphorylated
form); this is important for recruitment to sites of DNA damage.
Can form a heterotetramer with two molecules of ABRAXAS1
(phosphorylated form). Component of the BRCA1-RBBP8 complex.
Interacts (via the BRCT domains) with RBBP8 ('Ser-327'
phosphorylated form); the interaction ubiquitinates RBBP8,
regulates CHEK1 activation, and involves RBBP8 in BRCA1-dependent
G2/M checkpoint control on DNA damage. Associates with RNA
polymerase II holoenzyme. Interacts with SMC1A, COBRA1, DCLRE1C,
CLSPN. CHEK1, CHEK2, BAP1, BRCC3, AURKA, UBXN1 and PCLAF.
Interacts (via BRCT domains) with BRIP1 (phosphorylated form).
Interacts with FANCD2 (ubiquitinated form). Interacts with H2AFX
(phosphorylated on 'Ser-140'). Interacts (via the BRCT domains)
with ACACA (phosphorylated form); the interaction prevents
dephosphorylation of ACACA. Part of a BRCA complex containing
BRCA1, BRCA2 and PALB2. Interacts directly with PALB2; the
interaction is essential for its function in HRR. Interacts
directly with BRCA2; the interaction occurs only in the presence
of PALB2 which serves as the bridging protein. Interacts (via the
BRCT domains) with LMO4; the interaction represses the
transcriptional activity of BRCA1. Interacts (via the BRCT
domains) with CCAR2 (via N-terminus); the interaction represses
the transcriptional activator activity of BRCA1 (By similarity).
Interacts with EXD2 (By similarity). Interacts (via C-terminus)
with DHX9; this interaction is direct and links BRCA1 to the RNA
polymerase II holoenzyme (By similarity).
{ECO:0000250|UniProtKB:P38398}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P38398}.
Chromosome {ECO:0000250|UniProtKB:P48754}. Cytoplasm
{ECO:0000250|UniProtKB:P38398}. Note=Localizes at sites of DNA
damage at double-strand breaks (DSBs); recruitment to DNA damage
sites is mediated by the BRCA1-A complex. Translocated to the
cytoplasm during UV-induced apoptosis.
{ECO:0000250|UniProtKB:P38398}.
-!- DOMAIN: The BRCT domains recognize and bind phosphorylated pSXXF
motif on proteins. The interaction with the phosphorylated pSXXF
motif of ABRAXAS1, recruits BRCA1 at DNA damage sites.
{ECO:0000250|UniProtKB:P38398}.
-!- DOMAIN: The RING-type zinc finger domain interacts with BAP1.
{ECO:0000250|UniProtKB:P38398}.
-!- PTM: Phosphorylation at Ser-308 by AURKA is required for normal
cell cycle progression from G2 to mitosis. Phosphorylated in
response to IR, UV, and various stimuli that cause checkpoint
activation, probably by ATM or ATR. Phosphorylation at Ser-988 by
CHEK2 regulates mitotic spindle assembly.
{ECO:0000250|UniProtKB:P38398}.
-!- PTM: Autoubiquitinated, undergoes 'Lys-6'-linked
polyubiquitination. 'Lys-6'-linked polyubiquitination does not
promote degradation. {ECO:0000250|UniProtKB:P38398}.
-----------------------------------------------------------------------
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EMBL; AF207822; AAG43492.1; -; mRNA.
EMBL; AY365046; AAR04849.1; -; Genomic_DNA.
EMBL; AF019075; AAC39583.1; -; Genomic_DNA.
RefSeq; NP_001038958.1; NM_001045493.1.
UniGene; Ptr.6298; -.
ProteinModelPortal; Q9GKK8; -.
SMR; Q9GKK8; -.
STRING; 9598.ENSPTRP00000015727; -.
PaxDb; Q9GKK8; -.
GeneID; 449497; -.
KEGG; ptr:449497; -.
CTD; 672; -.
eggNOG; ENOG410ITQ6; Eukaryota.
eggNOG; ENOG4111WR7; LUCA.
HOGENOM; HOG000230969; -.
HOVERGEN; HBG050730; -.
InParanoid; Q9GKK8; -.
KO; K10605; -.
Proteomes; UP000002277; Unplaced.
GO; GO:0070531; C:BRCA1-A complex; IBA:GO_Central.
GO; GO:0031436; C:BRCA1-BARD1 complex; ISS:UniProtKB.
GO; GO:0005694; C:chromosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0008274; C:gamma-tubulin ring complex; NAS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; ISS:UniProtKB.
GO; GO:0015631; F:tubulin binding; NAS:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0043009; P:chordate embryonic development; IBA:GO_Central.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; TAS:UniProtKB.
GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IBA:GO_Central.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0046600; P:negative regulation of centriole replication; NAS:UniProtKB.
GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISS:UniProtKB.
GO; GO:0035067; P:negative regulation of histone acetylation; IBA:GO_Central.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IBA:GO_Central.
GO; GO:0045739; P:positive regulation of DNA repair; NAS:UniProtKB.
GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
GO; GO:0085020; P:protein K6-linked ubiquitination; ISS:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; TAS:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0006359; P:regulation of transcription from RNA polymerase III promoter; TAS:UniProtKB.
CDD; cd00027; BRCT; 2.
Gene3D; 3.30.40.10; -; 1.
Gene3D; 3.40.50.10190; -; 2.
InterPro; IPR011364; BRCA1.
InterPro; IPR031099; BRCA1-associated.
InterPro; IPR025994; BRCA1_serine_dom.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR018957; Znf_C3HC4_RING-type.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
PANTHER; PTHR13763; PTHR13763; 1.
PANTHER; PTHR13763:SF0; PTHR13763:SF0; 1.
Pfam; PF00533; BRCT; 2.
Pfam; PF12820; BRCT_assoc; 1.
Pfam; PF00097; zf-C3HC4; 1.
PIRSF; PIRSF001734; BRCA1; 1.
PRINTS; PR00493; BRSTCANCERI.
SMART; SM00292; BRCT; 2.
SMART; SM00184; RING; 1.
SUPFAM; SSF52113; SSF52113; 2.
PROSITE; PS50172; BRCT; 2.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
2: Evidence at transcript level;
Acetylation; Activator; Cell cycle; Chromosome; Complete proteome;
Cytoplasm; DNA damage; DNA recombination; DNA repair; DNA-binding;
Fatty acid biosynthesis; Fatty acid metabolism; Isopeptide bond;
Lipid biosynthesis; Lipid metabolism; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation; Transferase;
Tumor suppressor; Ubl conjugation; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 1863 Breast cancer type 1 susceptibility
protein homolog.
/FTId=PRO_0000055833.
DOMAIN 1642 1736 BRCT 1. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 1756 1855 BRCT 2. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
ZN_FING 24 65 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 1397 1424 Interaction with PALB2. {ECO:0000250}.
COMPBIAS 651 654 Poly-Lys.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 308 308 Phosphoserine; by AURKA.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 398 398 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 423 423 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 551 551 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 694 694 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 708 708 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 725 725 Phosphoserine.
{ECO:0000250|UniProtKB:P48754}.
MOD_RES 753 753 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 840 840 Phosphoserine.
{ECO:0000250|UniProtKB:P48754}.
MOD_RES 988 988 Phosphoserine; by CHEK2.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1009 1009 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1143 1143 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1189 1189 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1191 1191 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1211 1211 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1217 1217 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1218 1218 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1280 1280 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1328 1328 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1336 1336 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1342 1342 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1387 1387 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1394 1394 Phosphothreonine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1423 1423 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1457 1457 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1524 1524 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
MOD_RES 1542 1542 Phosphoserine.
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 109 109 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 301 301 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 339 339 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 443 443 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 459 459 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 519 519 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 583 583 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 654 654 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 734 734 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 739 739 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 918 918 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 987 987 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
CROSSLNK 1079 1079 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38398}.
VARIANT 309 309 K -> E. {ECO:0000269|Ref.1}.
/FTId=VAR_018712.
VARIANT 590 590 S -> G. {ECO:0000269|Ref.1}.
/FTId=VAR_018713.
VARIANT 731 731 K -> E. {ECO:0000269|PubMed:9462745,
ECO:0000269|Ref.1}.
/FTId=VAR_018714.
VARIANT 1100 1100 G -> E. {ECO:0000269|PubMed:9462745,
ECO:0000269|Ref.1}.
/FTId=VAR_018715.
CONFLICT 427 427 E -> K (in Ref. 2; AAR04849).
{ECO:0000305}.
CONFLICT 925 925 I -> T (in Ref. 2; AAR04849).
{ECO:0000305}.
CONFLICT 1520 1520 R -> T (in Ref. 1; AAG43492).
{ECO:0000305}.
SEQUENCE 1863 AA; 207899 MW; 49673829CCFA756E CRC64;
MDLSALRVEE VQNVINAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK LLNQKKGPSQ
CPLCKNDITK RSLQESTRFS QLVEELLKII CAFQLDTGLE YANSYNFAKK ENNSPEHLKD
EVSIIQSMGY RNRAKRLLQS EPENPSLQET SLSVQLSNLG TVRTLRTKQR IQPQKKSVYI
ELGSDSSEDT VNKATYCSVG DQELLQITPQ GTRDEISLDS AKKAACEFSE TDVTNTEHHQ
PSNNDLNTTE KRATERHPEK YQGSSVSNLH VEPCGTNTHA SSLQHENSSL LLTKDRMNVE
KAEFCNKSKQ PGLARSQHNR WAGSKETCND RRTPSTEKKV DLNADPLCER KEWNKQKLPC
SENPRDTEDV PWITLNSSIQ KVNEWFSRSD ELLGSDDSHD GGSESNAKVA DVLDVLNEVD
EYSGSSEKID LLASDPHEAL ICKSERVHSK SVESNTEDKI FGKTYRRKAS LPNLSHVTEN
LIIGAFVTEP QIIQERPLTN KLKRKRRATS GLHPEDFIKK ADLAVQKTPE MINQGTNQME
QNGQVMNITN SGHENKTKGD SIQNEKNPNP IESLEKESAF KTKAEPISSS ISNMELELNI
HNSKAPKKNR LRRKSSTRHI HALELVVSRN LSPPNCTELQ IDSCSSSEEI KKKKYNQMPV
RHSRNLQLME DKEPATGVKK SNKPNEQTSK RHDSDTFPEL KLTNAPGSFT NCSNTSELKE
FVNPSLPREE KEEKLETVKV SNNAEDPKDL MLSGERVLQT ERSVESSSIS LVPGTDYGTQ
ESISLLEVST LGKAKTEPNK CVSQCAAFEN PKGLIHGCSK DTRNDTEGFK YPLGHEVNHS
RETSIEMEES ELDAQYLQNT FKVSKRQSFA LFSNPGNPEE ECATFSAHCR SLKKQSPKVT
FEREQKEQNQ GKNESNIKPV QTVNITAGFP VVCQKDKPVD YAKCSIKGGS RFCLSSQFRG
NETGLITPNK HGLLQNPYHI PPLFPIKSFV KTKCKKNLLE ENFEEHSMSP EREMGNENIP
STVSTISRNN IRENVFKEAS SSNINEVGSS TNEVGSSINE VGSSDENIQA ELGRNRGPKL
NAMLRLGVLQ PEVYKQSLPG SNCKHPEIKK QEYEEVVQTV NTDFSPCLIS DNLEQPMGSS
HASQVCSETP DDLLDDGEIK EDTSFAENDI KESSAVFSKS VQRGELSRSP SPFTHTHLAQ
GYRRGAKKLE SSEENLSSED EELPCFQHLL FGKVSNIPSQ STRHSTVATE CLSKNTEENL
LSLKNSLNDC SNQVILAKAS QEHHLSEETK CSASLFSSQC SELEDLTANT NTQDPFLIGS
SKQMRHQSES QGVGLSDKEL VSDDEERGTG LEENNQEEQS MDSNLGEAAS GCESETSVSE
DCSGLSSQSD ILTTQQRDTM QDNLIKLQQE MAELEAVLEQ HGSQPSNSYP SIISDSSALE
DLQNPEQSTS EKAVLTSQKS SEYPISQNPE GLSADKFEVS ADSSTSKNKE PGVERSSPSK
CPSLDDRWYM HSCSGSLQNR NYPSQEELIK VVDVEEQQLE ESGPHDLTET SYLPRQDLEG
TPYLESGISL FSDDPESDPS EDKAPESAHV GNIPSSTSAL KVPQLKVAES AQSPAAAHTT
NTAGYNAMEE SVSREKPELT ASTERVNKRM SMVVSGLTPE EFMLVYKFAR KHHITLTNLI
TEETTHVVMK TDAEFVCERT LKYFLGIAGG KWVVSYFWVT QSIKERKMLN EHDFEVRGDV
VNGRNHQGPK RARESQDRKI FRGLEICCYG PFTNMPTDQL EWMVQLCGAS VVKELSSFTL
GTGVHPIVVV QPDAWTEDNG FHAIGQMCEA PVVTREWVLD SVALYQCQEL DTYLIPQIPH
SHY


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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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