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Teneurin-1 (Ten-1) (Protein Odd Oz/ten-m homolog 1) (Tenascin-M1) (Ten-m1) (Teneurin transmembrane protein 1) [Cleaved into: Ten-1 intracellular domain (IDten-1) (Ten-1 ICD); Teneurin C-terminal-associated peptide (TCPA-1) (Ten-1 extracellular domain) (Ten-1 ECD)]

 TEN1_CHICK              Reviewed;        2705 AA.
Q9W6V6;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
12-SEP-2018, entry version 109.
RecName: Full=Teneurin-1;
Short=Ten-1;
AltName: Full=Protein Odd Oz/ten-m homolog 1;
AltName: Full=Tenascin-M1;
Short=Ten-m1;
AltName: Full=Teneurin transmembrane protein 1;
Contains:
RecName: Full=Ten-1 intracellular domain;
Short=IDten-1;
Short=Ten-1 ICD;
Contains:
RecName: Full=Teneurin C-terminal-associated peptide;
Short=TCPA-1;
AltName: Full=Ten-1 extracellular domain;
Short=Ten-1 ECD;
Name=TENM1; Synonyms=ODZ1, TNM1;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=10341219;
Minet A.D., Rubin B.P., Tucker R.P., Baumgartner S.,
Chiquet-Ehrismann R.;
"Teneurin-1, a vertebrate homologue of the Drosophila pair-rule gene
ten-m, is a neuronal protein with a novel type of heparin-binding
domain.";
J. Cell Sci. 112:2019-2032(1999).
[2]
PROTEOLYTIC PROCESSING, FUNCTION OF TEN-1 ICD, INTERACTION WITH MBD1
AND SORBS1, AND SUBCELLULAR LOCATION.
PubMed=15777793; DOI=10.1016/j.yexcr.2004.12.020;
Nunes S.M., Ferralli J., Choi K., Brown-Luedi M., Minet A.D.,
Chiquet-Ehrismann R.;
"The intracellular domain of teneurin-1 interacts with MBD1 and
CAP/ponsin resulting in subcellular codistribution and translocation
to the nuclear matrix.";
Exp. Cell Res. 305:122-132(2005).
[3]
PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
MUTAGENESIS OF 62-ARG--LYS-65.
PubMed=18366734; DOI=10.1186/1471-213X-8-30;
Kenzelmann D., Chiquet-Ehrismann R., Leachman N.T., Tucker R.P.;
"Teneurin-1 is expressed in interconnected regions of the developing
brain and is processed in vivo.";
BMC Dev. Biol. 8:30-30(2008).
-!- FUNCTION: Involved in neural development, regulating the
establishment of proper connectivity within the nervous system.
May function as a cellular signal transducer (By similarity).
{ECO:0000250}.
-!- FUNCTION: Teneurin C-terminal-associated peptide: Plays a role in
the regulation of neuroplasticity in the limbic system. Mediates a
rapid reorganization of actin- and tubulin-based cytoskeleton
elements with an increase in dendritic arborization and spine
density formation of neurons in the hippocampus and amygdala.
Induces BDNF transcription inhibition in neurons. Activates the
mitogen-activated protein (MAP) kinase 2 (MEK2) and extracellular
signal-regulated kinase (ERK) cascade (By similarity).
{ECO:0000250}.
-!- FUNCTION: Ten-1 intracellular domain: Induces gene transcription
activation. {ECO:0000269|PubMed:15777793}.
-!- SUBUNIT: Homodimer; disulfide-linked. Heterodimer with other
teneurins (By similarity). Ten-1 ICD interacts with SORBS1 (via
third SH3 domain). Interacts with MBD1 isoform 2. {ECO:0000250,
ECO:0000269|PubMed:15777793}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15777793,
ECO:0000269|PubMed:18366734}; Single-pass membrane protein
{ECO:0000269|PubMed:15777793, ECO:0000269|PubMed:18366734}.
-!- SUBCELLULAR LOCATION: Ten-1 intracellular domain: Nucleus. Nucleus
speckle. Nucleus matrix. Cytoplasm, cytoskeleton. Note=Colocalizes
with SORBS1 in the nucleus and to the cell periphery. Colocalizes
with MBD1 and PML in foci associated with the nuclear matrix.
-!- SUBCELLULAR LOCATION: Teneurin C-terminal-associated peptide:
Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in the neurons of the developing
visual system and in fetal brain. {ECO:0000269|PubMed:10341219}.
-!- DEVELOPMENTAL STAGE: Expressed in mitral cell, glomerular layer of
the olfactory bulb, hippocampus, posteromedial cortex piriformis,
nucleus rotundu, laminae 2 and 5 within the inner plexiform layer
of the retina, stratum griseum, nucleus laminaris and
magnocellularis in the hindbrain and Purkinje cells at embryonic
day (E) 17 (at protein level). At E14, it is concentrated in the
retina, the optic tectum and in specific nuclei in the dorsal
diencephalon, it is concentrated in the stratum griseum centrale.
Expression is seen in diencephalon, concentrated in the rotund
nucleus and in the neighboring ovoid nucleus. Similar expression
patterns are seen at E17. {ECO:0000269|PubMed:18366734}.
-!- DOMAIN: EGF-like domains 2 and 5 which have an odd number of
cysteines might enable the formation of intermolecular disulfide
bonds.
-!- DOMAIN: Cytoplasmic proline-rich regions could serve as docking
domains for intracellular SH3-containing proteins.
-!- PTM: Teneurin C-terminal-associated peptide: Derives from the
plasma membrane form by proteolytic processing. Further
proteolytic cleavage may be generated (By similarity).
{ECO:0000250}.
-!- PTM: Ten-1 intracellular domain: Derives from the plasma membrane
form by proteolytic cleavage and translocates to the nucleus.
{ECO:0000269|PubMed:15777793, ECO:0000269|PubMed:18366734}.
-!- MISCELLANEOUS: Teneurin C-terminal-associated peptide: Binds to
the plasma membrane and may be internalized by a receptor- and
caveolae-mediated endocytosis manner to reach cytosolic
compartments in a dynamin-dependent manner. {ECO:0000250}.
-!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
{ECO:0000305}.
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EMBL; AJ238613; CAB43098.1; -; mRNA.
RefSeq; NP_990193.1; NM_204862.1.
UniGene; Gga.4323; -.
ProteinModelPortal; Q9W6V6; -.
SMR; Q9W6V6; -.
MINT; Q9W6V6; -.
PaxDb; Q9W6V6; -.
PRIDE; Q9W6V6; -.
GeneID; 395668; -.
KEGG; gga:395668; -.
CTD; 10178; -.
eggNOG; ENOG410IT6U; Eukaryota.
eggNOG; ENOG4111K7T; LUCA.
HOGENOM; HOG000231701; -.
HOVERGEN; HBG080306; -.
InParanoid; Q9W6V6; -.
PhylomeDB; Q9W6V6; -.
PRO; PR:Q9W6V6; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
GO; GO:0048666; P:neuron development; IBA:GO_Central.
GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
GO; GO:0090316; P:positive regulation of intracellular protein transport; IDA:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
GO; GO:0006359; P:regulation of transcription by RNA polymerase III; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.120.10.30; -; 2.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR008969; CarboxyPept-like_regulatory.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR009471; Ten_N.
InterPro; IPR027688; TENM1/TENM4.
InterPro; IPR028916; Tox-GHH_dom.
InterPro; IPR006530; YD.
PANTHER; PTHR11219:SF9; PTHR11219:SF9; 2.
Pfam; PF06484; Ten_N; 2.
Pfam; PF15636; Tox-GHH; 1.
SMART; SM00181; EGF; 8.
SUPFAM; SSF49464; SSF49464; 1.
TIGRFAMs; TIGR01643; YD_repeat_2x; 2.
PROSITE; PS00022; EGF_1; 8.
PROSITE; PS01186; EGF_2; 7.
PROSITE; PS50026; EGF_3; 4.
PROSITE; PS51361; TENEURIN_N; 1.
1: Evidence at protein level;
Cell membrane; Cleavage on pair of basic residues; Complete proteome;
Cytoplasm; Cytoskeleton; Disulfide bond; EGF-like domain;
Glycoprotein; Membrane; Neuropeptide; Nucleus; Reference proteome;
Repeat; Repressor; Stress response; Transcription;
Transcription regulation; Transmembrane; Transmembrane helix.
CHAIN 1 2705 Teneurin-1.
/FTId=PRO_0000259500.
CHAIN 1 ? Ten-1 intracellular domain.
/FTId=PRO_0000421009.
CHAIN 2576 2705 Teneurin C-terminal-associated peptide.
{ECO:0000250}.
/FTId=PRO_0000421010.
TOPO_DOM 1 305 Cytoplasmic. {ECO:0000255}.
TRANSMEM 306 326 Helical. {ECO:0000255}.
TOPO_DOM 327 2705 Extracellular. {ECO:0000255}.
DOMAIN 1 299 Teneurin N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00694}.
DOMAIN 509 540 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 541 572 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 573 605 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 606 638 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 639 672 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 673 702 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 703 734 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 735 769 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1167 1192 NHL 1.
REPEAT 1202 1246 NHL 2.
REPEAT 1272 1316 NHL 3.
REPEAT 1331 1382 NHL 4.
REPEAT 1461 1504 NHL 5.
REPEAT 1514 1533 YD 1.
REPEAT 1550 1570 YD 2.
REPEAT 1588 1612 YD 3.
REPEAT 1613 1634 YD 4.
REPEAT 1635 1655 YD 5.
REPEAT 1825 1844 YD 6.
REPEAT 1845 1865 YD 7.
REPEAT 1866 1884 YD 8.
REPEAT 1885 1905 YD 9.
REPEAT 1913 1929 YD 10.
REPEAT 1930 1949 YD 11.
REPEAT 1950 1969 YD 12.
REPEAT 1972 1992 YD 13.
REPEAT 1995 2015 YD 14.
REPEAT 2065 2085 YD 15.
REPEAT 2093 2113 YD 16.
REPEAT 2133 2153 YD 17.
REPEAT 2154 2174 YD 18.
REPEAT 2176 2196 YD 19.
REPEAT 2208 2228 YD 20.
REPEAT 2230 2250 YD 21.
REPEAT 2276 2293 YD 22.
REPEAT 2294 2317 YD 23.
MOTIF 62 65 Nuclear localization signal (NLS).
MOTIF 271 278 Required for interaction with SORBS1
(Ten-1 ICD form).
COMPBIAS 173 181 Poly-Pro.
SITE 2575 2576 Cleavage. {ECO:0000305}.
CARBOHYD 414 414 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 878 878 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1057 1057 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1530 1530 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1547 1547 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1643 1643 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1679 1679 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1737 1737 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1761 1761 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1822 1822 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2125 2125 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2265 2265 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2582 2582 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 513 523 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 517 528 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 530 539 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 548 559 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 561 570 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 577 588 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 582 593 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 595 604 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 609 620 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 614 625 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 627 636 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 647 660 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 662 671 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 676 686 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 680 691 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 693 702 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 707 717 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 711 722 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 724 733 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 738 748 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 742 757 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 759 768 {ECO:0000255|PROSITE-ProRule:PRU00076}.
MUTAGEN 62 65 RKRK->AAAA: Inhibits translocation to the
nucleus (Ten-1 ICD form).
{ECO:0000269|PubMed:18366734}.
SEQUENCE 2705 AA; 302388 MW; 230F03D1999037D2 CRC64;
MEQMDCKPYQ PLSKVKHEVD LTYTSSSDES EDGRKQRQSY DSRETLNEYS QELRLNYNSQ
SRKRKNTDQS TQDMEFCETP HILCSGYQTD LHGVSEHSYP LEVGSDVDTE TEGGASPDHA
LRMWMRGMKS EHSSCLSSRA NSALSLTDTD HERKSDGEND MPGSPHNQFT FRPLPPPPPP
PHACTCTRKP PPAADSLQRR SMTTRSQPSP AAPTPPTSTQ DSVHLHNSWV LNSNIPLETR
HFLFKHGSGS SAIFSAASQN YPLTSNTVYS PPPRPLPRNT FSRPAFTFSK PYRCCNWKCT
ALSATAITVT LALLLAYVIA VHLFGLTWQL QPVEGQLYEN GVSKGNKGAE STDTTYSPIG
GKVSDKTEKK VFQKGRAIDT GEVEIGAQVM QTIPPGLFWR FQITIHHPVY LKFNISLAKD
SLLGIYGRRN IPPTHTQFDF VKLMDGKQLI KQEPKNSEEP QQAPRNLILT SLQETGFIEY
MDQGAWHMAF YNDGKKVEQV FVLTTAIEVL DDCSTNCNGN GECISGHCHC FPGFLGPDCA
KDSCPVLCSG NGEYEKGHCV CRNGWKGPEC DVPEEQCIDP TCFGHGTCIM GVCICVPGYK
GEICEEEDCL DPMCSGHGVC VQGECHCSAG WGGVNCETSL PICQEHCSGH GTFLLDVGLC
SCEPQWTGSD CSTELCTLDC GSHGVCSRGI CQCEEGWVGP TCEERTCHSH CAEHGQCKDG
KCECSPGWEG DHCTIDGCPG LCYGNGRCTL DQNGWHCVCQ VGWSGSGCNV VMEMACGDNL
DNDGDGLTDC VDPDCCQQNN CYASPLCQGS PDPLDLIQHS QPPFSQHPPR LFYDRIRFLI
GKESTHVIPG DISFESRRAS VIRGQVVAID GTPLVGVNVS FLHHDEYGYT ISRQDGSFDL
VAVGGISVTL VFDRSPFISE KRTLWLSWNR FVIVDKVVMQ RAESDIPSCD VSSFISPNPI
VLPSPLTAFG GSCPERGTVI PELQVVQEEI PIPSSFVKLS YLSSRTPGYK TLLRVILTHT
TIPSGMTKVH LIIAVEGRLL QKWFPAAANL VYTFAWNKTD IYGQKVSGLA EAMVSVGYEY
ETCPDFILWE KRTVILQGFE MDASNLGGWS INKHHVLNPQ SGIVHKGNGE NMFISQQPPV
ISTMMGNGHQ RSVSCSNCNG LALNSKLFAP VALTSGPDGS VYIGDFNFVR RIFPSGNSIG
ILELRNRDTR HSTSPAHKYY LAVDPVSESL YLSDTNTRRV YKAKSLIETK DLAKNVDVVA
GTGDQCLPFD QSHCGDGGKA SEASLNSPRG ITIDKHGFIY FVDGTMIRKI DENGMITTII
GSNGLTSTQP LSCDSGMDIT QVRLEWPTDL TVNPLDNSLY VLDNNIVLQI SESRRVRIIA
GRPIHCQVPG IDHFIVSKVA IHSTLESARA IAVSHSGIPY IRETDERKIN RIQQVTTNGE
ISIIAGAPSD CDCKIDPNCD CFSGDGGYAK DAKLKAPSSL AVSPDDTLYV ADLGNIRIRA
VSRNKAHLSD TNMYEIASPA DQELYQFTIN GTHLHTLNLI TRDYIYNFTY SGEGDVATIT
SSNGNSVHIR RDTSGLPLWV VVPGGQVYWL TISSNGVLKR VYAQGYNLAL MTYPGNTGLL
ATKSDENGWT TVYEYDSDGH LTNATFPTGE VSSFHSDVEK LTRVELDTSN RENMVTATNF
SATSTIYTLK QDNTQNIYRV SPDGSLRVTF ASGMEITLNT EPHILAGVVS PTLGKCNISL
PGEHNSNLIE WRQRREQTKG NISTFERRLR AHNRNLLSID FDHVTRTGKI YDDHRKFTLR
IMYDQTGRPV LWSPISKYNE VNITYSHSGL VTYIQRGTWT EKMEYDPSGN IISRTWADGK
IWSYTYLEKS VMLLLHSQRR YIFEYDQSDY LLSVTMPSMV RHALQTMLSV GYYRNIYTPP
DSGAAFIQDV TRDGRLLQTL YPGTGRRVLY KYSKQSRLSE ILYDTTQVTF TYEESSGVIK
TIHLMHDGFI CTIRYRQTGP LIGRQIFRFS EEGLVNARFD YSYNNFRVTS MQAMINETPL
PIDLYRYVDV SGRTEQFGKF SVINYDLNQV ITTTVMKHTK IFSANGQVIE VQYEILKSIA
YWMTIQYDNM GRMVICDIRV GVDANITRYF YEYDRDGQLQ TVSVNDKTQW RYSYDLNGNI
NLLSHGNSAR LTPLRYDLRD RITRLGEIQY KMDEDGFLRQ RGNEIFEYNS NGLLNKAYNK
VSGWTVQYCY DGLGRRVASK SSLGQHLQFF YADLSNPIRV THLYNHSSSE ITSLYYDLQG
HLIAMELSSG EEYYVACDNT GTPLAVFSSR GQVIKEILYT PYGEIYQDTN PDFQVVIGFH
GGLYDSLTKL VHLGQRDYDV IAGRWTTPNH HIWKHLNAVP QPFNLYSFEN NYPVGRIQDV
AKYTTDIGSW LELFGFQLHN VLPGFPKPEI EALETTYELL QLQTKTQEWD PGKTILGIQC
ELQKQLRNFI SLDQLPMTPR YSDGKCYEGV KQPRFAAIPS VFGKGIKFAI KDGIVTADII
GVANEDSRRI AAILNNAHYL ENLHFTIEGR DTHYFIKLGS LEEDLSLIGN TGGRRILENG
VNVTVSQMTS VINGRTRRFA DIQLQHGALC FNVRYGTTVE EEKNHVLEVA RQRAVAQAWT
KEQRRLQEGE EGIRAWTDGE KQQLLNTGRV QGYDGYFVLS VEQYLELSDS ANNIHFMRQS
EIGRR


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Genprice Inc, Invoices and accounting
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