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Biliverdin reductase A (BVR A) (EC 1.3.1.24) (Biliverdin-IX alpha-reductase)

 BIEA_HUMAN              Reviewed;         296 AA.
P53004; A8K747; O95019; Q86UX0; Q96QL4; Q9BRW8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
10-OCT-2002, sequence version 2.
30-AUG-2017, entry version 169.
RecName: Full=Biliverdin reductase A;
Short=BVR A;
EC=1.3.1.24;
AltName: Full=Biliverdin-IX alpha-reductase;
Flags: Precursor;
Name=BLVRA; Synonyms=BLVR, BVR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-3.
PubMed=8950184; DOI=10.1016/S0167-4781(96)00099-1;
Komuro A., Tobe T., Nakano Y., Yamaguchi T., Tomita M.;
"Cloning and characterization of the cDNA encoding human biliverdin-IX
alpha reductase.";
Biochim. Biophys. Acta 1309:89-99(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=8631357; DOI=10.1111/j.1432-1033.1996.00372.x;
Maines M.D., Polevoda B.V., Huang T.-J., McCoubrey W.K. Jr.;
"Human biliverdin IXalpha reductase is a zinc-metalloprotein.
Characterization of purified and Escherichia coli expressed enzymes.";
Eur. J. Biochem. 235:372-381(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-3; VAL-37 AND
ARG-56.
NIEHS SNPs program;
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-3.
TISSUE=Brain, and Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 3-36; 48-74 AND 228-248.
TISSUE=Liver;
PubMed=8424666; DOI=10.1006/abbi.1993.1044;
Maines M.D., Trakshel G.M.;
"Purification and characterization of human biliverdin reductase.";
Arch. Biochem. Biophys. 300:320-326(1993).
[8]
PROTEIN SEQUENCE OF 3-22.
TISSUE=Liver;
PubMed=7929092;
Yamaguchi T., Komoda Y., Nakajima H.;
"Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from
human liver. Purification and characterization.";
J. Biol. Chem. 269:24343-24348(1994).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
INVOLVEMENT IN HBLVD.
PubMed=19580635; DOI=10.1111/j.1478-3231.2009.02029.x;
Gafvels M., Holmstrom P., Somell A., Sjovall F., Svensson J.O.,
Stahle L., Broome U., Stal P.;
"A novel mutation in the biliverdin reductase-A gene combined with
liver cirrhosis results in hyperbiliverdinaemia (green jaundice).";
Liver Int. 29:1116-1124(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174 AND SER-178, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-248 AND LYS-253, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 7-296 IN COMPLEX WITH NADP.
Structural genomics consortium (SGC);
"Crystal structure of human biliverdin reductase A.";
Submitted (FEB-2009) to the PDB data bank.
-!- FUNCTION: Reduces the gamma-methene bridge of the open
tetrapyrrole, biliverdin IX alpha, to bilirubin with the
concomitant oxidation of a NADH or NADPH cofactor.
-!- CATALYTIC ACTIVITY: Bilirubin + NAD(P)(+) = biliverdin + NAD(P)H.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
degradation.
-!- SUBUNIT: Monomer. {ECO:0000269|Ref.18}.
-!- INTERACTION:
Q8TBB1:LNX1; NbExp=3; IntAct=EBI-7410441, EBI-739832;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Liver.
-!- DISEASE: Hyperbiliverdinemia (HBLVD) [MIM:614156]: A condition
characterized by a green discoloration of the skin, urine, serum,
and other bodily fluids. It is due to increased biliverdin
resulting from inefficient conversion to bilirubin. Affected
individuals appear to have symptoms only in the context of
obstructive cholestasis and/or liver failure. In some cases, green
jaundice can resolve after resolution of obstructive cholestasis.
{ECO:0000269|PubMed:19580635}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Uses the reactants NADH or NADPH depending on the
pH; NADH is used at the acidic pH range (6-6.9) and NADPH at the
alkaline range (8.5-8.7). NADPH, however, is the probable reactant
in biological systems.
-!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Biliverdin
reductase subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/blvra/";
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EMBL; U34877; AAC35588.1; -; mRNA.
EMBL; X93086; CAA63635.1; -; mRNA.
EMBL; AK291862; BAF84551.1; -; mRNA.
EMBL; AY616754; AAT11126.1; -; Genomic_DNA.
EMBL; AC005189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC004939; AAD05025.1; -; Genomic_DNA.
EMBL; AC004985; AAP21879.1; -; Genomic_DNA.
EMBL; BC005902; AAH05902.1; -; mRNA.
EMBL; BC008456; AAH08456.1; -; mRNA.
CCDS; CCDS5472.1; -.
PIR; G02066; G02066.
PIR; S62624; S62624.
RefSeq; NP_000703.2; NM_000712.3.
RefSeq; NP_001240752.1; NM_001253823.1.
RefSeq; XP_011513776.1; XM_011515474.2.
RefSeq; XP_016868009.1; XM_017012520.1.
UniGene; Hs.488143; -.
PDB; 2H63; X-ray; 2.70 A; A/B/C/D=7-296.
PDBsum; 2H63; -.
ProteinModelPortal; P53004; -.
SMR; P53004; -.
BioGrid; 107113; 20.
DIP; DIP-42180N; -.
IntAct; P53004; 3.
MINT; MINT-1212210; -.
STRING; 9606.ENSP00000265523; -.
DrugBank; DB00157; NADH.
iPTMnet; P53004; -.
PhosphoSitePlus; P53004; -.
BioMuta; BLVRA; -.
DMDM; 23830892; -.
OGP; P53004; -.
REPRODUCTION-2DPAGE; IPI00294158; -.
EPD; P53004; -.
MaxQB; P53004; -.
PaxDb; P53004; -.
PeptideAtlas; P53004; -.
PRIDE; P53004; -.
Ensembl; ENST00000265523; ENSP00000265523; ENSG00000106605.
Ensembl; ENST00000402924; ENSP00000385757; ENSG00000106605.
GeneID; 644; -.
KEGG; hsa:644; -.
UCSC; uc003tir.4; human.
CTD; 644; -.
DisGeNET; 644; -.
GeneCards; BLVRA; -.
HGNC; HGNC:1062; BLVRA.
HPA; HPA019709; -.
HPA; HPA042865; -.
HPA; HPA054322; -.
MalaCards; BLVRA; -.
MIM; 109750; gene.
MIM; 614156; phenotype.
neXtProt; NX_P53004; -.
OpenTargets; ENSG00000106605; -.
Orphanet; 276405; Hyperbiliverdinemia.
PharmGKB; PA25373; -.
eggNOG; ENOG410IH7U; Eukaryota.
eggNOG; ENOG4111FZX; LUCA.
GeneTree; ENSGT00390000011072; -.
HOGENOM; HOG000231884; -.
HOVERGEN; HBG003218; -.
InParanoid; P53004; -.
KO; K00214; -.
OMA; PMTLSWA; -.
OrthoDB; EOG091G0E2N; -.
PhylomeDB; P53004; -.
TreeFam; TF342889; -.
BioCyc; MetaCyc:HS02928-MONOMER; -.
BRENDA; 1.3.1.24; 2681.
Reactome; R-HSA-189483; Heme degradation.
SIGNOR; P53004; -.
UniPathway; UPA00684; -.
ChiTaRS; BLVRA; human.
EvolutionaryTrace; P53004; -.
GenomeRNAi; 644; -.
PRO; PR:P53004; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000106605; -.
CleanEx; HS_BLVRA; -.
ExpressionAtlas; P53004; baseline and differential.
Genevisible; P53004; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0004074; F:biliverdin reductase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0042167; P:heme catabolic process; TAS:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
InterPro; IPR017094; Biliverdin_Rdtase_A.
InterPro; IPR015249; Biliverdin_Rdtase_cat.
InterPro; IPR016040; NAD(P)-bd_dom.
InterPro; IPR000683; Oxidoreductase_N.
Pfam; PF09166; Biliv-reduc_cat; 1.
Pfam; PF01408; GFO_IDH_MocA; 1.
PIRSF; PIRSF037032; Biliverdin_reductase_A; 1.
ProDom; PD040165; Biliverdin_Rdtase_cat; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Metal-binding; NAD; NADP; Oxidoreductase;
Phosphoprotein; Polymorphism; Reference proteome; Zinc.
PROPEP 1 2 {ECO:0000269|PubMed:7929092,
ECO:0000269|PubMed:8424666}.
/FTId=PRO_0000010852.
CHAIN 3 296 Biliverdin reductase A.
{ECO:0000269|PubMed:8631357}.
/FTId=PRO_0000010853.
NP_BIND 15 20 NAD or NADP.
NP_BIND 44 46 NAD or NADP.
NP_BIND 77 80 NAD or NADP.
COMPBIAS 11 16 Poly-Val.
METAL 280 280 Zinc. {ECO:0000255}.
METAL 281 281 Zinc. {ECO:0000255}.
METAL 292 292 Zinc. {ECO:0000255}.
METAL 293 293 Zinc. {ECO:0000255}.
BINDING 98 98 NAD or NADP; via carbonyl oxygen.
MOD_RES 174 174 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 230 230 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 248 248 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 253 253 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VARIANT 3 3 A -> T (in dbSNP:rs699512).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8950184,
ECO:0000269|Ref.4}.
/FTId=VAR_019230.
VARIANT 37 37 L -> V (in dbSNP:rs17245918).
{ECO:0000269|Ref.4}.
/FTId=VAR_019231.
VARIANT 56 56 Q -> R (in dbSNP:rs1050916).
{ECO:0000269|Ref.4}.
/FTId=VAR_014851.
CONFLICT 121 121 L -> S (in Ref. 6; AAH05902).
{ECO:0000305}.
CONFLICT 154 155 AG -> SD (in Ref. 2; CAA63635).
{ECO:0000305}.
CONFLICT 160 160 E -> D (in Ref. 2; CAA63635).
{ECO:0000305}.
STRAND 9 14 {ECO:0000244|PDB:2H63}.
HELIX 18 28 {ECO:0000244|PDB:2H63}.
HELIX 33 36 {ECO:0000244|PDB:2H63}.
STRAND 37 43 {ECO:0000244|PDB:2H63}.
STRAND 50 53 {ECO:0000244|PDB:2H63}.
HELIX 59 64 {ECO:0000244|PDB:2H63}.
STRAND 70 73 {ECO:0000244|PDB:2H63}.
HELIX 77 89 {ECO:0000244|PDB:2H63}.
STRAND 93 98 {ECO:0000244|PDB:2H63}.
HELIX 104 117 {ECO:0000244|PDB:2H63}.
STRAND 121 124 {ECO:0000244|PDB:2H63}.
HELIX 126 129 {ECO:0000244|PDB:2H63}.
HELIX 131 140 {ECO:0000244|PDB:2H63}.
STRAND 145 154 {ECO:0000244|PDB:2H63}.
HELIX 159 162 {ECO:0000244|PDB:2H63}.
HELIX 165 168 {ECO:0000244|PDB:2H63}.
HELIX 170 180 {ECO:0000244|PDB:2H63}.
STRAND 182 193 {ECO:0000244|PDB:2H63}.
STRAND 198 207 {ECO:0000244|PDB:2H63}.
STRAND 212 219 {ECO:0000244|PDB:2H63}.
STRAND 226 235 {ECO:0000244|PDB:2H63}.
HELIX 250 262 {ECO:0000244|PDB:2H63}.
HELIX 268 290 {ECO:0000244|PDB:2H63}.
SEQUENCE 296 AA; 33428 MW; 2CF2AA7F1CDDB707 CRC64;
MNAEPERKFG VVVVGVGRAG SVRMRDLRNP HPSSAFLNLI GFVSRRELGS IDGVQQISLE
DALSSQEVEV AYICSESSSH EDYIRQFLNA GKHVLVEYPM TLSLAAAQEL WELAEQKGKV
LHEEHVELLM EEFAFLKKEV VGKDLLKGSL LFTAGPLEEE RFGFPAFSGI SRLTWLVSLF
GELSLVSATL EERKEDQYMK MTVCLETEKK SPLSWIEEKG PGLKRNRYLS FHFKSGSLEN
VPNVGVNKNI FLKDQNIFVQ KLLGQFSEKE LAAEKKRILH CLGLAEEIQK YCCSRK


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Genprice Inc, Invoices and accounting
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