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Major vault protein (MVP) (Lung resistance-related protein)

 MVP_HUMAN               Reviewed;         893 AA.
Q14764; Q96BG4; Q9BPW6; Q9BQT1; Q9UBD1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
23-MAY-2018, entry version 167.
RecName: Full=Major vault protein;
Short=MVP;
AltName: Full=Lung resistance-related protein;
Name=MVP; Synonyms=LRP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7585126; DOI=10.1038/nm0695-578;
Scheffer G.L., Wijngaard P.L.J., Flens M.J., Izquierdo M.A.,
Slovak M.L., Pinedo H.M., Meijer C.J.L.M., Clevers H.C., Scheper R.J.;
"The drug resistance-related protein LRP is the human major vault
protein.";
Nat. Med. 1:578-582(1995).
[2]
SEQUENCE REVISION TO C-TERMINUS.
Scheffer G.L.;
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-169.
PubMed=11071864; DOI=10.1006/bbrc.2000.3782;
Lange C., Walther W., Schwabe H., Stein U.;
"Cloning and initial analysis of the human multidrug resistance-
related MVP/LRP gene promoter.";
Biochem. Biophys. Res. Commun. 278:125-133(2000).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-65.
TISSUE=Lung cancer;
PubMed=11297743; DOI=10.1016/S0014-5793(01)02318-3;
Holzmann K., Ambrosch I., Elbling L., Micksche M., Berger W.;
"A small upstream open reading frame causes inhibition of human major
vault protein expression from a ubiquitous mRNA splice variant.";
FEBS Lett. 494:99-104(2001).
[6]
PROTEIN SEQUENCE OF 2-9; 68-82 AND 462-474, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Melanoma;
Quadroni M., Potts A., Barblan J., Bienvenut W.V.;
Submitted (JAN-2005) to UniProtKB.
[7]
ASSOCIATION WITH TEP1.
PubMed=10551828; DOI=10.1074/jbc.274.46.32712;
Kickhoefer V.A., Stephen A.G., Harrington L., Robinson M.O.,
Rome L.H.;
"Vaults and telomerase share a common subunit, TEP1.";
J. Biol. Chem. 274:32712-32717(1999).
[8]
INTERACTION WITH PTEN.
PubMed=12177006; DOI=10.1074/jbc.M207608200;
Yu Z., Fotouhi-Ardakani N., Wu L., Maoui M., Wang S., Banville D.,
Shen S.-H.;
"PTEN associates with the vault particles in HeLa cells.";
J. Biol. Chem. 277:40247-40252(2002).
[9]
PHOSPHORYLATION AT TYROSINE RESIDUES, IDENTIFICATION BY MASS
SPECTROMETRY, INTERACTION WITH PTPN11, SUBCELLULAR LOCATION, AND
FUNCTION.
PubMed=15133037; DOI=10.1074/jbc.M313955200;
Kolli S., Zito C.I., Mossink M.H., Wiemer E.A.C., Bennett A.M.;
"The major vault protein is a novel substrate for the tyrosine
phosphatase SHP-2 and scaffold protein in epidermal growth factor
signaling.";
J. Biol. Chem. 279:29374-29385(2004).
[10]
INTERACTION WITH ZNF540.
PubMed=16815308; DOI=10.1016/j.bbrc.2006.06.076;
Xiang Z., Yuan W., Luo N., Wang Y., Tan K., Deng Y., Zhou X., Zhu C.,
Li Y., Liu M., Wu X., Li Y.;
"A novel human zinc finger protein ZNF540 interacts with MVP and
inhibits transcriptional activities of the ERK signal pathway.";
Biochem. Biophys. Res. Commun. 347:288-296(2006).
[11]
FUNCTION, INTERACTION WITH SRC, TYROSINE PHOSPHORYLATION, SUBCELLULAR
LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16441665; DOI=10.1111/j.1742-4658.2006.05112.x;
Kim E., Lee S., Mian M.F., Yun S.U., Song M., Yi K.-S., Ryu S.H.,
Suh P.-G.;
"Crosstalk between Src and major vault protein in epidermal growth
factor-dependent cell signalling.";
FEBS J. 273:793-804(2006).
[12]
INDUCTION, AND FUNCTION.
PubMed=16418217; DOI=10.1242/jcs.02773;
Steiner E., Holzmann K., Pirker C., Elbling L., Micksche M.,
Sutterluety H., Berger W.;
"The major vault protein is responsive to and interferes with
interferon-gamma-mediated STAT1 signals.";
J. Cell Sci. 119:459-469(2006).
[13]
INTERACTION WITH APEX1.
PubMed=18809583; DOI=10.1128/MCB.00244-08;
Chattopadhyay R., Das S., Maiti A.K., Boldogh I., Xie J., Hazra T.K.,
Kohno K., Mitra S., Bhakat K.K.;
"Regulatory role of human AP-endonuclease (APE1/Ref-1) in YB-1-
mediated activation of the multidrug resistance gene MDR1.";
Mol. Cell. Biol. 28:7066-7080(2008).
[14]
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).
[15]
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).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND 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).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-444, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-444 AND LYS-704, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[21]
STRUCTURE BY NMR OF 113-221, AND INTERACTION WITH PARP4.
PubMed=16373071; DOI=10.1016/j.jmb.2005.11.064;
Kozlov G., Vavelyuk O., Minailiuc O., Banville D., Gehring K.,
Ekiel I.;
"Solution structure of a two-repeat fragment of major vault protein.";
J. Mol. Biol. 356:444-452(2006).
[22]
VARIANT GLU-87.
PubMed=28895081; DOI=10.1007/s12311-017-0883-4;
Kurihara M., Ishiura H., Sasaki T., Otsuka J., Hayashi T., Terao Y.,
Matsukawa T., Mitsui J., Kaneko J., Nishiyama K., Doi K.,
Yoshimura J., Morishita S., Shimizu J., Tsuji S.;
"Novel de novo KCND3 mutation in a Japanese patient with intellectual
disability, cerebellar ataxia, myoclonus, and dystonia.";
Cerebellum 17:237-242(2018).
-!- FUNCTION: Required for normal vault structure. Vaults are multi-
subunit structures that may act as scaffolds for proteins involved
in signal transduction. Vaults may also play a role in nucleo-
cytoplasmic transport. Down-regulates IFNG-mediated STAT1
signaling and subsequent activation of JAK. Down-regulates SRC
activity and signaling through MAP kinases.
{ECO:0000269|PubMed:15133037, ECO:0000269|PubMed:16418217,
ECO:0000269|PubMed:16441665}.
-!- SUBUNIT: The vault ribonucleoprotein particle is a huge (400 A x
670 A) cage structure of 12.9 MDa. It consists of a dimer of half-
vaults, with each half-vault comprising 39 identical major vault
protein (MVP) chains, PARP4 and one or more vault RNAs (vRNAs).
Interacts with TEP1. Interacts with PTEN and activated MAPK1. The
phosphorylated protein interacts with the SH2 domains of PTPN11
and SRC. Interacts with APEX1. May interact with ZNF540.
{ECO:0000269|PubMed:12177006, ECO:0000269|PubMed:15133037,
ECO:0000269|PubMed:16373071, ECO:0000269|PubMed:16441665,
ECO:0000269|PubMed:16815308, ECO:0000269|PubMed:18809583}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-2816254, EBI-2816254;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15133037,
ECO:0000269|PubMed:16441665}. Nucleus, nuclear pore complex
{ECO:0000269|PubMed:16441665}. Cytoplasm, perinuclear region
{ECO:0000269|PubMed:16441665}. Note=5% found in the nuclear pore
complex (PubMed:15133037). Translocates from the nucleus to the
cytoplasm upon EGF treatment (PubMed:16441665).
-!- TISSUE SPECIFICITY: Present in most normal tissues. Higher
expression observed in epithelial cells with secretory and
excretory functions, as well as in cells chronically exposed to
xenobiotics, such as bronchial cells and cells lining the
intestine. Overexpressed in many multidrug-resistant cancer cells.
-!- INDUCTION: Up-regulated by IFNG/IFN-gamma.
{ECO:0000269|PubMed:16418217}.
-!- DOMAIN: MVP 3 mediates interaction with PTEN.
-!- DOMAIN: MVP 4 mediates interaction with PARP4.
-!- PTM: Phosphorylated on Tyr residues after EGF stimulation.
{ECO:0000269|PubMed:15133037}.
-!- PTM: Dephosphorylated by PTPN11.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/LRPID120.html";
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EMBL; X79882; CAA56256.2; -; mRNA.
EMBL; BC015623; AAH15623.1; -; mRNA.
EMBL; AJ238512; CAB55354.1; -; Genomic_DNA.
EMBL; AJ238514; CAB55354.1; JOINED; Genomic_DNA.
EMBL; AJ238516; CAB55354.1; JOINED; Genomic_DNA.
EMBL; AJ238518; CAB55354.1; JOINED; Genomic_DNA.
EMBL; AJ238519; CAB55355.1; -; Genomic_DNA.
EMBL; AJ238514; CAB55355.1; JOINED; Genomic_DNA.
EMBL; AJ238516; CAB55355.1; JOINED; Genomic_DNA.
EMBL; AJ238518; CAB55355.1; JOINED; Genomic_DNA.
EMBL; AJ291365; CAC35313.1; -; Genomic_DNA.
EMBL; AJ291366; CAC35314.1; -; mRNA.
EMBL; AJ291367; CAC35316.1; -; mRNA.
CCDS; CCDS10656.1; -.
PIR; S57723; S57723.
RefSeq; NP_001280133.1; NM_001293204.1.
RefSeq; NP_001280134.1; NM_001293205.1.
RefSeq; NP_005106.2; NM_005115.4.
RefSeq; NP_059447.2; NM_017458.3.
UniGene; Hs.632177; -.
PDB; 1Y7X; NMR; -; A=113-221.
PDBsum; 1Y7X; -.
ProteinModelPortal; Q14764; -.
SMR; Q14764; -.
BioGrid; 115286; 96.
IntAct; Q14764; 41.
MINT; Q14764; -.
STRING; 9606.ENSP00000349977; -.
TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; Q14764; -.
PhosphoSitePlus; Q14764; -.
SwissPalm; Q14764; -.
BioMuta; MVP; -.
DMDM; 21542417; -.
OGP; Q14764; -.
REPRODUCTION-2DPAGE; IPI00000105; -.
EPD; Q14764; -.
PaxDb; Q14764; -.
PeptideAtlas; Q14764; -.
PRIDE; Q14764; -.
DNASU; 9961; -.
Ensembl; ENST00000357402; ENSP00000349977; ENSG00000013364.
Ensembl; ENST00000395353; ENSP00000378760; ENSG00000013364.
GeneID; 9961; -.
KEGG; hsa:9961; -.
CTD; 9961; -.
DisGeNET; 9961; -.
EuPathDB; HostDB:ENSG00000013364.18; -.
GeneCards; MVP; -.
HGNC; HGNC:7531; MVP.
HPA; CAB002752; -.
HPA; CAB022717; -.
HPA; HPA002321; -.
HPA; HPA064740; -.
MIM; 605088; gene.
neXtProt; NX_Q14764; -.
OpenTargets; ENSG00000013364; -.
PharmGKB; PA31332; -.
eggNOG; ENOG410IF6T; Eukaryota.
eggNOG; ENOG410ZCU8; LUCA.
GeneTree; ENSGT00390000008969; -.
HOGENOM; HOG000255109; -.
HOVERGEN; HBG003499; -.
InParanoid; Q14764; -.
KO; K17266; -.
OMA; VFPQNGL; -.
OrthoDB; EOG091G032A; -.
PhylomeDB; Q14764; -.
TreeFam; TF329353; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SignaLink; Q14764; -.
ChiTaRS; MVP; human.
EvolutionaryTrace; Q14764; -.
GeneWiki; Major_vault_protein; -.
GenomeRNAi; 9961; -.
PRO; PR:Q14764; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000013364; -.
CleanEx; HS_MVP; -.
ExpressionAtlas; Q14764; baseline and differential.
Genevisible; Q14764; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; IDA:UniProtKB.
GO; GO:0038127; P:ERBB signaling pathway; IDA:UniProtKB.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; IDA:UniProtKB.
GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0023057; P:negative regulation of signaling; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
CDD; cd08825; MVP_shoulder; 1.
InterPro; IPR021870; MVP_shoulder.
InterPro; IPR002499; Vault_N.
Pfam; PF11978; MVP_shoulder; 1.
Pfam; PF01505; Vault; 4.
PROSITE; PS51224; MVP; 8.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Isopeptide bond; mRNA transport;
Nuclear pore complex; Nucleus; Phosphoprotein; Polymorphism;
Protein transport; Reference proteome; Repeat; Ribonucleoprotein;
Translocation; Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
CHAIN 2 893 Major vault protein.
/FTId=PRO_0000158980.
REPEAT 2 56 MVP 1.
REPEAT 57 111 MVP 2.
REPEAT 112 164 MVP 3.
REPEAT 165 217 MVP 4.
REPEAT 218 272 MVP 5.
REPEAT 273 323 MVP 6.
REPEAT 324 379 MVP 7.
REPEAT 380 457 MVP 8.
REPEAT 458 520 MVP 9.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
MOD_RES 445 445 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 704 704 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 87 87 D -> E. {ECO:0000269|PubMed:28895081}.
/FTId=VAR_079710.
VARIANT 635 635 V -> I (in dbSNP:rs35916172).
/FTId=VAR_050179.
VARIANT 651 651 R -> Q (in dbSNP:rs3764944).
/FTId=VAR_050180.
STRAND 120 125 {ECO:0000244|PDB:1Y7X}.
STRAND 137 139 {ECO:0000244|PDB:1Y7X}.
STRAND 141 147 {ECO:0000244|PDB:1Y7X}.
HELIX 148 150 {ECO:0000244|PDB:1Y7X}.
STRAND 157 163 {ECO:0000244|PDB:1Y7X}.
STRAND 170 181 {ECO:0000244|PDB:1Y7X}.
STRAND 185 187 {ECO:0000244|PDB:1Y7X}.
STRAND 195 198 {ECO:0000244|PDB:1Y7X}.
STRAND 208 217 {ECO:0000244|PDB:1Y7X}.
SEQUENCE 893 AA; 99327 MW; 6FEE5545B0A3FE65 CRC64;
MATEEFIIRI PPYHYIHVLD QNSNVSRVEV GPKTYIRQDN ERVLFAPMRM VTVPPRHYCT
VANPVSRDAQ GLVLFDVTGQ VRLRHADLEI RLAQDPFPLY PGEVLEKDIT PLQVVLPNTA
LHLKALLDFE DKDGDKVVAG DEWLFEGPGT YIPRKEVEVV EIIQATIIRQ NQALRLRARK
ECWDRDGKER VTGEEWLVTT VGAYLPAVFE EVLDLVDAVI LTEKTALHLR ARRNFRDFRG
VSRRTGEEWL VTVQDTEAHV PDVHEEVLGV VPITTLGPHN YCVILDPVGP DGKNQLGQKR
VVKGEKSFFL QPGEQLEQGI QDVYVLSEQQ GLLLRALQPL EEGEDEEKVS HQAGDHWLIR
GPLEYVPSAK VEVVEERQAI PLDENEGIYV QDVKTGKVRA VIGSTYMLTQ DEVLWEKELP
PGVEELLNKG QDPLADRGEK DTAKSLQPLA PRNKTRVVSY RVPHNAAVQV YDYREKRARV
VFGPELVSLG PEEQFTVLSL SAGRPKRPHA RRALCLLLGP DFFTDVITIE TADHARLQLQ
LAYNWHFEVN DRKDPQETAK LFSVPDFVGD ACKAIASRVR GAVASVTFDD FHKNSARIIR
TAVFGFETSE AKGPDGMALP RPRDQAVFPQ NGLVVSSVDV QSVEPVDQRT RDALQRSVQL
AIEITTNSQE AAAKHEAQRL EQEARGRLER QKILDQSEAE KARKELLELE ALSMAVESTG
TAKAEAESRA EAARIEGEGS VLQAKLKAQA LAIETEAELQ RVQKVRELEL VYARAQLELE
VSKAQQLAEV EVKKFKQMTE AIGPSTIRDL AVAGPEMQVK LLQSLGLKST LITDGSTPIN
LFNTAFGLLG MGPEGQPLGR RVASGPSPGE GISPQSAQAP QAPGDNHVVP VLR


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201-12-1076 Human Lung resistance-related protein,LRP ELISA Kit 48T
YHB1916Hu Human Lung resistance-related protein,LRP ELISA Kit 96T
201-12-1076 Human Lung resistance-related protein(LRP)ELISA Kit 96T


 

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