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Autophagy-related protein 18 (Cytoplasm to vacuole targeting protein 18) (Needed for premeiotic replication protein 1) (Swollen vacuole phenotype protein 1)

 ATG18_YEAST             Reviewed;         500 AA.
P43601; D6VTQ1;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
20-JUN-2018, entry version 167.
RecName: Full=Autophagy-related protein 18 {ECO:0000303|PubMed:14536056};
AltName: Full=Cytoplasm to vacuole targeting protein 18 {ECO:0000303|PubMed:11739783};
AltName: Full=Needed for premeiotic replication protein 1 {ECO:0000303|PubMed:11470404};
AltName: Full=Swollen vacuole phenotype protein 1 {ECO:0000303|PubMed:15103325};
Name=ATG18 {ECO:0000303|PubMed:14536056};
Synonyms=AUT10 {ECO:0000303|PubMed:11707261},
CVT18 {ECO:0000303|PubMed:11739783},
NMR1 {ECO:0000303|PubMed:11470404},
SVP1 {ECO:0000303|PubMed:15103325};
OrderedLocusNames=YFR021W {ECO:0000312|SGD:S000001917};
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7670463; DOI=10.1038/ng0795-261;
Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M.,
Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K.,
Yamazaki M., Tashiro H., Eki T.;
"Analysis of the nucleotide sequence of chromosome VI from
Saccharomyces cerevisiae.";
Nat. Genet. 10:261-268(1995).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION.
PubMed=11470404; DOI=10.1016/S0960-9822(01)00274-3;
Rabitsch K.P., Toth A., Galova M., Schleiffer A., Schaffner G.,
Aigner E., Rupp C., Penkner A.M., Moreno-Borchart A.C., Primig M.,
Esposito R.E., Klein F., Knop M., Nasmyth K.;
"A screen for genes required for meiosis and spore formation based on
whole-genome expression.";
Curr. Biol. 11:1001-1009(2001).
[4]
FUNCTION.
PubMed=11707261; DOI=10.1016/S0014-5793(01)03016-2;
Barth H., Meiling-Wesse K., Epple U.D., Thumm M.;
"Autophagy and the cytoplasm to vacuole targeting pathway both require
Aut10p.";
FEBS Lett. 508:23-28(2001).
[5]
FUNCTION.
PubMed=11739783; DOI=10.1091/mbc.12.12.3821;
Guan J., Stromhaug P.E., George M.D., Habibzadegah-Tari P., Bevan A.,
Dunn W.A. Jr., Klionsky D.J.;
"Cvt18/Gsa12 is required for cytoplasm-to-vacuole transport,
pexophagy, and autophagy in Saccharomyces cerevisiae and Pichia
pastoris.";
Mol. Biol. Cell 12:3821-3838(2001).
[6]
FUNCTION.
PubMed=11536337; DOI=10.1002/yea.764;
Georgakopoulos T., Koutroubas G., Vakonakis I., Tzermia M.,
Prokova V., Voutsina A., Alexandraki D.;
"Functional analysis of the Saccharomyces cerevisiae
YFR021w/YGR223c/YPL100w ORF family suggests relations to
mitochondrial/peroxisomal functions and amino acid signalling
pathways.";
Yeast 18:1155-1171(2001).
[7]
NOMENCLATURE.
PubMed=14536056; DOI=10.1016/S1534-5807(03)00296-X;
Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y.,
Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M.,
Ohsumi Y.;
"A unified nomenclature for yeast autophagy-related genes.";
Dev. Cell 5:539-545(2003).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATG9.
PubMed=14723849; DOI=10.1016/S1534-5807(03)00402-7;
Reggiori F., Tucker K.A., Stromhaug P.E., Klionsky D.J.;
"The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport
from the pre-autophagosomal structure.";
Dev. Cell 6:79-90(2004).
[10]
INTERACTION WITH PIP2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
73-ARG--ARG-76 AND 285-ARG-ARG-286.
PubMed=15103325; DOI=10.1038/sj.emboj.7600203;
Dove S.K., Piper R.C., McEwen R.K., Yu J.W., King M.C., Hughes D.C.,
Thuring J., Holmes A.B., Cooke F.T., Michell R.H., Parker P.J.,
Lemmon M.A.;
"Svp1p defines a family of phosphatidylinositol 3,5-bisphosphate
effectors.";
EMBO J. 23:1922-1933(2004).
[11]
FUNCTION.
PubMed=15194695; DOI=10.1074/jbc.M401066200;
Meiling-Wesse K., Barth H., Voss C., Eskelinen E.-L., Epple U.D.,
Thumm M.;
"Atg21 is required for effective recruitment of Atg8 to the
preautophagosomal structure during the Cvt pathway.";
J. Biol. Chem. 279:37741-37750(2004).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PIP2.
PubMed=15155809; DOI=10.1091/mbc.E04-02-0147;
Stromhaug P.E., Reggiori F., Guan J., Wang C.-W., Klionsky D.J.;
"Atg21 is a phosphoinositide binding protein required for efficient
lipidation and localization of Atg8 during uptake of aminopeptidase I
by selective autophagy.";
Mol. Biol. Cell 15:3553-3566(2004).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=16876790; DOI=10.1016/j.febslet.2006.07.041;
Krick R., Tolstrup J., Appelles A., Henke S., Thumm M.;
"The relevance of the phosphatidylinositolphosphat-binding motif FRRGT
of Atg18 and Atg21 for the Cvt pathway and autophagy.";
FEBS Lett. 580:4632-4638(2006).
[14]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VAC17, AND
MUTAGENESIS OF 285-ARG--ARG-286.
PubMed=17699591; DOI=10.1091/mbc.E07-04-0301;
Efe J.A., Botelho R.J., Emr S.D.;
"Atg18 regulates organelle morphology and Fab1 kinase activity
independent of its membrane recruitment by phosphatidylinositol 3,5-
bisphosphate.";
Mol. Biol. Cell 18:4232-4244(2007).
[15]
SUBCELLULAR LOCATION.
PubMed=18497569; DOI=10.4161/auto.6308;
Ma J., Bharucha N., Dobry C.J., Frisch R.L., Lawson S., Kumar A.;
"Localization of autophagy-related proteins in yeast using a versatile
plasmid-based resource of fluorescent protein fusions.";
Autophagy 4:792-800(2008).
[16]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=18769150; DOI=10.4161/auto.6801;
Krick R., Henke S., Tolstrup J., Thumm M.;
"Dissecting the localization and function of Atg18, Atg21 and
Ygr223c.";
Autophagy 4:896-910(2008).
[17]
IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=19037259; DOI=10.1038/emboj.2008.248;
Jin N., Chow C.Y., Liu L., Zolov S.N., Bronson R., Davisson M.,
Petersen J.L., Zhang Y., Park S., Duex J.E., Goldowitz D.,
Meisler M.H., Weisman L.S.;
"VAC14 nucleates a protein complex essential for the acute
interconversion of PI3P and PI(3,5)P(2) in yeast and mouse.";
EMBO J. 27:3221-3234(2008).
[18]
FUNCTION, INTERACTION WITH ATG2, PI3P-BINDING, AND SUBCELLULAR
LOCATION.
PubMed=18586673; DOI=10.1074/jbc.M803180200;
Obara K., Sekito T., Niimi K., Ohsumi Y.;
"The Atg18-Atg2 complex is recruited to autophagic membranes via
phosphatidylinositol 3-phosphate and exerts an essential function.";
J. Biol. Chem. 283:23972-23980(2008).
[19]
INTERACTION WITH ATG9, AND SUBCELLULAR LOCATION.
PubMed=18829864; DOI=10.1091/mbc.E08-05-0544;
He C., Baba M., Cao Y., Klionsky D.J.;
"Self-interaction is critical for Atg9 transport and function at the
phagophore assembly site during autophagy.";
Mol. Biol. Cell 19:5506-5516(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[21]
FUNCTION, AND DOMAIN.
PubMed=20154084; DOI=10.1074/jbc.M109.080374;
Nair U., Cao Y., Xie Z., Klionsky D.J.;
"Roles of the lipid-binding motifs of Atg18 and Atg21 in the cytoplasm
to vacuole targeting pathway and autophagy.";
J. Biol. Chem. 285:11476-11488(2010).
[22]
FUNCTION.
PubMed=22108003; DOI=10.4161/auto.7.12.18424;
Nair U., Thumm M., Klionsky D.J., Krick R.;
"GFP-Atg8 protease protection as a tool to monitor autophagosome
biogenesis.";
Autophagy 7:1546-1550(2011).
[23]
PIP2-BINDING.
PubMed=21536737; DOI=10.1101/gad.1998611;
Han B.K., Emr S.D.;
"Phosphoinositide [PI(3,5)P2] lipid-dependent regulation of the
general transcriptional regulator Tup1.";
Genes Dev. 25:984-995(2011).
[24]
SUBCELLULAR LOCATION.
PubMed=22889849; DOI=10.4161/auto.20681;
Taylor R. Jr., Chen P.H., Chou C.C., Patel J., Jin S.V.;
"KCS1 deletion in Saccharomyces cerevisiae leads to a defect in
translocation of autophagic proteins and reduces autophagosome
formation.";
Autophagy 8:1300-1311(2012).
[25]
FUNCTION OF THE ATG2-ATG8 COMPLEX.
PubMed=22728243; DOI=10.1016/j.febslet.2012.06.008;
Kobayashi T., Suzuki K., Ohsumi Y.;
"Autophagosome formation can be achieved in the absence of Atg18 by
expressing engineered PAS-targeted Atg2.";
FEBS Lett. 586:2473-2478(2012).
[26]
SUBCELLULAR LOCATION.
PubMed=22704557; DOI=10.1016/j.molcel.2012.05.027;
Baskaran S., Ragusa M.J., Boura E., Hurley J.H.;
"Two-site recognition of phosphatidylinositol 3-phosphate by PROPPINs
in autophagy.";
Mol. Cell 47:339-348(2012).
[27]
FUNCTION.
PubMed=22787281; DOI=10.1091/mbc.E12-05-0347;
Zieger M., Mayer A.;
"Yeast vacuoles fragment in an asymmetrical two-phase process with
distinct protein requirements.";
Mol. Biol. Cell 23:3438-3449(2012).
[28]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-264; THR-268; ARG-271;
ARG-285; ARG-286; SER-311; THR-313 AND HIS-315.
PubMed=22753491; DOI=10.1073/pnas.1205128109;
Krick R., Busse R.A., Scacioc A., Stephan M., Janshoff A., Thumm M.,
Kuhnel K.;
"Structural and functional characterization of the two
phosphoinositide binding sites of PROPPINs, a beta-propeller protein
family.";
Proc. Natl. Acad. Sci. U.S.A. 109:E2042-E2049(2012).
[29]
FUNCTION, AND INTERACTION WITH ATG9.
PubMed=24905091; DOI=10.4161/auto.28971;
Papinski D., Kraft C.;
"Atg1 kinase organizes autophagosome formation by phosphorylating
Atg9.";
Autophagy 10:1338-1340(2014).
-!- FUNCTION: The PI(3,5)P2 regulatory complex regulates both the
synthesis and turnover of phosphatidylinositol 3,5-bisphosphate
(PtdIns(3,5)P2). May negatively regulate FAB1 activity by
sequestering or masking VAC7 from FAB1. Necessary for proper
vacuole morphology. Plays an important role in osmotically-induced
vacuole fragmentation. Required for cytoplasm to vacuole transport
(Cvt) vesicle formation, pexophagy and starvation-induced
autophagy. Involved in correct ATG9 trafficking to the pre-
autophagosomal structure. Might also be involved in premeiotic DNA
replication. With ATG2, protects ATG8 from ATG4-mediated cleavage.
{ECO:0000269|PubMed:11470404, ECO:0000269|PubMed:11536337,
ECO:0000269|PubMed:11707261, ECO:0000269|PubMed:11739783,
ECO:0000269|PubMed:14723849, ECO:0000269|PubMed:15155809,
ECO:0000269|PubMed:15194695, ECO:0000269|PubMed:16876790,
ECO:0000269|PubMed:17699591, ECO:0000269|PubMed:18586673,
ECO:0000269|PubMed:18769150, ECO:0000269|PubMed:19037259,
ECO:0000269|PubMed:20154084, ECO:0000269|PubMed:22108003,
ECO:0000269|PubMed:22728243, ECO:0000269|PubMed:22787281,
ECO:0000269|PubMed:24905091}.
-!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex, composed
of ATG18, FIG4, FAB1, VAC14 and VAC7. VAC14 nucleates the assembly
of the complex and serves as a scaffold. Interacts with ATG2, ATG9
and VAC17. The ATG2-ATG18 complex is essential for autophagosome
formation. {ECO:0000269|PubMed:14723849,
ECO:0000269|PubMed:15103325, ECO:0000269|PubMed:15155809,
ECO:0000269|PubMed:17699591, ECO:0000269|PubMed:18586673,
ECO:0000269|PubMed:18829864, ECO:0000269|PubMed:19037259,
ECO:0000269|PubMed:24905091}.
-!- INTERACTION:
P53855:ATG2; NbExp=5; IntAct=EBI-22968, EBI-29212;
Q06708:VAC14; NbExp=5; IntAct=EBI-22968, EBI-27189;
-!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
{ECO:0000269|PubMed:14723849, ECO:0000269|PubMed:16876790,
ECO:0000269|PubMed:18497569, ECO:0000269|PubMed:18586673,
ECO:0000269|PubMed:18829864}; Peripheral membrane protein
{ECO:0000269|PubMed:14723849, ECO:0000269|PubMed:16876790,
ECO:0000269|PubMed:18497569, ECO:0000269|PubMed:18586673,
ECO:0000269|PubMed:18829864}. Vacuole membrane
{ECO:0000269|PubMed:15103325, ECO:0000269|PubMed:15155809,
ECO:0000269|PubMed:16876790, ECO:0000269|PubMed:17699591,
ECO:0000269|PubMed:18497569, ECO:0000269|PubMed:19037259};
Peripheral membrane protein {ECO:0000269|PubMed:15103325,
ECO:0000269|PubMed:15155809, ECO:0000269|PubMed:16876790,
ECO:0000269|PubMed:17699591, ECO:0000269|PubMed:18497569,
ECO:0000269|PubMed:19037259}. Endosome membrane
{ECO:0000269|PubMed:18769150}; Peripheral membrane protein
{ECO:0000269|PubMed:18769150}. Note=Requires VAC7 for vacuole
membrane localization. Under mid-log phase growth, localizes to
the vacuolar membrane; but when cells are starved, is almost
completely released from the vacuole membrane.
{ECO:0000269|PubMed:17699591}.
-!- DOMAIN: The 377 first amino acids might form a beta-propeller
domain involved in specific binding to phosphatidylinositol 3,5-
bisphosphate (PIP2), leading to the association of the protein to
the membrane. Association to the membrane can also occur through
binding to phosphatidylinositol 3-monophosphate (PI3P).
{ECO:0000269|PubMed:22753491}.
-!- DOMAIN: The FRRGT-motif is essential for the cytoplasm to vacuole
transport (Cvt) pathway, for the recruitment of ATG8 and ATG16 to
the PAS in nutrient-rich medium, and for its recruitment to and
dissociation from the PAS under starvation conditions.
{ECO:0000269|PubMed:16876790}.
-!- MISCELLANEOUS: Present with 1560 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the WD repeat SVP1 family. {ECO:0000305}.
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EMBL; D50617; BAA09260.1; -; Genomic_DNA.
EMBL; BK006940; DAA12461.1; -; Genomic_DNA.
PIR; S56276; S56276.
RefSeq; NP_444297.1; NM_001179986.1.
ProteinModelPortal; P43601; -.
BioGrid; 31174; 140.
ComplexPortal; CPX-3088; PAS complex.
ComplexPortal; CPX-361; ATG2-ATG18 complex.
DIP; DIP-5185N; -.
IntAct; P43601; 28.
MINT; P43601; -.
STRING; 4932.YFR021W; -.
TCDB; 9.A.15.1.1; the autophagy-related phagophore-formation transporter (apt) family.
iPTMnet; P43601; -.
MaxQB; P43601; -.
PaxDb; P43601; -.
PRIDE; P43601; -.
EnsemblFungi; BAA09260; BAA09260; BAA09260.
EnsemblFungi; YFR021W; YFR021W; YFR021W.
GeneID; 850577; -.
KEGG; sce:YFR021W; -.
EuPathDB; FungiDB:YFR021W; -.
SGD; S000001917; ATG18.
GeneTree; ENSGT00730000110845; -.
HOGENOM; HOG000217543; -.
InParanoid; P43601; -.
KO; K17908; -.
OMA; TICDLVF; -.
OrthoDB; EOG092C3UKJ; -.
BioCyc; YEAST:G3O-30472-MONOMER; -.
Reactome; R-SCE-1632852; Macroautophagy.
PRO; PR:P43601; -.
Proteomes; UP000002311; Chromosome VI.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005768; C:endosome; IDA:SGD.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
GO; GO:0070772; C:PAS complex; IDA:SGD.
GO; GO:0061908; C:phagophore; IDA:SGD.
GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
GO; GO:0005774; C:vacuolar membrane; IDA:UniProtKB.
GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:SGD.
GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:SGD.
GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
GO; GO:0030242; P:autophagy of peroxisome; IMP:SGD.
GO; GO:0045324; P:late endosome to vacuole transport; IMP:SGD.
GO; GO:0044805; P:late nucleophagy; IMP:SGD.
GO; GO:0016236; P:macroautophagy; IDA:SGD.
GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
GO; GO:0044090; P:positive regulation of vacuole organization; IMP:SGD.
GO; GO:0006497; P:protein lipidation; IBA:GO_Central.
GO; GO:0032258; P:protein localization by the Cvt pathway; IDA:SGD.
GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0006624; P:vacuolar protein processing; IDA:SGD.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF00400; WD40; 2.
SMART; SM00320; WD40; 2.
SUPFAM; SSF50978; SSF50978; 2.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Autophagy; Complete proteome; Endosome; Membrane; Phosphoprotein;
Protein transport; Reference proteome; Repeat; Transport; Vacuole;
WD repeat.
CHAIN 1 500 Autophagy-related protein 18.
/FTId=PRO_0000050874.
REPEAT 243 283 WD 1.
REPEAT 288 327 WD 2.
REGION 284 287 Necessary for proper localization to
vacuole membrane.
MOTIF 284 288 FRRGT-motif.
{ECO:0000303|PubMed:16876790}.
MOD_RES 354 354 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MUTAGEN 73 76 RRLR->SSLS: Slight reduction of PIP2
binding.
MUTAGEN 264 264 S->A: Impairs membrane-association.
{ECO:0000269|PubMed:22753491}.
MUTAGEN 268 268 T->A: Impairs membrane-association.
{ECO:0000269|PubMed:22753491}.
MUTAGEN 271 271 R->A: Impairs membrane-association.
{ECO:0000269|PubMed:22753491}.
MUTAGEN 285 286 RR->GG: Loss of recruitment to vacuole
membrane. {ECO:0000269|PubMed:22753491}.
MUTAGEN 285 286 RR->TT: 40-fold decrease of affinity to
PIP2. {ECO:0000269|PubMed:22753491}.
MUTAGEN 285 285 R->A: Impairs membrane-association.
{ECO:0000269|PubMed:22753491}.
MUTAGEN 286 286 R->A: Impairs membrane-association.
{ECO:0000269|PubMed:22753491}.
MUTAGEN 311 311 S->A: Impairs membrane-association.
{ECO:0000269|PubMed:22753491}.
MUTAGEN 313 313 T->A: Impairs membrane-association.
{ECO:0000269|PubMed:22753491}.
MUTAGEN 315 315 H->A: Impairs membrane-association.
{ECO:0000269|PubMed:22753491}.
SEQUENCE 500 AA; 55102 MW; 06B2DFAF842AE933 CRC64;
MSDSSPTINF INFNQTGTCI SLGTSKGFKI FNCEPFGKFY SEDSGGYAIV EMLFSTSLLA
LVGIGDQPAL SPRRLRIINT KKHSIICEVT FPTSILSVKM NKSRLVVLLQ EQIYIYDINT
MRLLHTIETN PNPRGLMAMS PSVANSYLVY PSPPKVINSE IKAHATTNNI TLSVGGNTET
SFKRDQQDAG HSDISDLDQY SSFTKRDDAD PTSSNGGNSS IIKNGDVIVF NLETLQPTMV
IEAHKGEIAA MAISFDGTLM ATASDKGTII RVFDIETGDK IYQFRRGTYA TRIYSISFSE
DSQYLAVTGS SKTVHIFKLG HSMSNNKLDS DDSNMEEAAA DDSSLDTTSI DALSDEENPT
RLAREPYVDA SRKTMGRMIR YSSQKLSRRA ARTLGQIFPI KVTSLLESSR HFASLKLPVE
TNSHVMTISS IGSPIDIDTS EYPELFETGN SASTESYHEP VMKMVPIRVV SSDGYLYNFV
MDPERGGDCL ILSQYSILMD


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VMP1_RAT ELISA Kit FOR Vacuole membrane protein 1; organism: Rat; gene name: Vmp1 96T
EIAAB34345 Homo sapiens,Human,REPA2,Replication factor A protein 2,Replication protein A 32 kDa subunit,Replication protein A 34 kDa subunit,RF-A protein 2,RP-A p32,RP-A p34,RPA2,RPA32,RPA34
EIAAB24949 Autophagy-related protein LC3 A,Autophagy-related ubiquitin-like modifier LC3 A,MAP1 light chain 3-like protein 1,MAP1A_MAP1B LC3 A,MAP1A_MAP1B light chain 3 A,Map1lc3a,Microtubule-associated protein
EIAAB24948 Autophagy-related protein LC3 A,Autophagy-related ubiquitin-like modifier LC3 A,MAP1 light chain 3-like protein 1,MAP1A_MAP1B LC3 A,MAP1A_MAP1B light chain 3 A,Map1lc3a,Microtubule-associated protein
orb80926 Human Autophagy Related 5 protein Autophagy Protein Human Recombinant produced in E.coli is non-glycosylated, polypeptide chain having molecular weight of 31.6 kDa. APG5 contains T7 tag at N-terminus 2
EIAAB34346 Mouse,Mus musculus,Replication factor A protein 2,Replication protein A 32 kDa subunit,Replication protein A 34 kDa subunit,RF-A protein 2,RP-A p32,RP-A p34,Rpa2,Rpa34
EIAAB24950 Autophagy-related protein LC3 A,Autophagy-related ubiquitin-like modifier LC3 A,Homo sapiens,Human,MAP1 light chain 3-like protein 1,MAP1A_MAP1B LC3 A,MAP1A_MAP1B light chain 3 A,MAP1LC3A,Microtubule-
EIAAB24952 Autophagy-related protein LC3 B,Autophagy-related ubiquitin-like modifier LC3 B,Bos taurus,Bovine,MAP1 light chain 3-like protein 2,MAP1A_MAP1B LC3 B,MAP1A_MAP1B light chain 3 B,MAP1ALC3,MAP1LC3,MAP1L
EIAAB24955 Autophagy-related protein LC3 C,Autophagy-related ubiquitin-like modifier LC3 C,Homo sapiens,Human,MAP1 light chain 3-like protein 3,MAP1A_MAP1B LC3 C,MAP1A_MAP1B light chain 3 C,MAP1LC3C,Microtubule-
EIAAB24954 Autophagy-related protein LC3 B,Autophagy-related ubiquitin-like modifier LC3 B,Homo sapiens,Human,MAP1 light chain 3-like protein 2,MAP1A_MAP1B LC3 B,MAP1A_MAP1B light chain 3 B,MAP1ALC3,MAP1LC3B,Mic
EIAAB34342 Homo sapiens,Human,REPA1,Replication factor A protein 1,Replication protein A 70 kDa DNA-binding subunit,RF-A protein 1,RP-A p70,RPA1,RPA70,Single-stranded DNA-binding protein
EIAAB24953 Autophagy-related protein LC3 B,Autophagy-related ubiquitin-like modifier LC3 B,MAP1 light chain 3-like protein 2,MAP1A_MAP1B LC3 B,MAP1A_MAP1B light chain 3 B,Map1alc3,Map1lc3,Map1lc3b,Microtubule-as
EIAAB24947 Autophagy-related protein LC3 A,Autophagy-related ubiquitin-like modifier LC3 A,Bos taurus,Bovine,MAP1 light chain 3-like protein 1,MAP1A_MAP1B LC3 A,MAP1A_MAP1B light chain 3 A,MAP1LC3A,Microtubule-a
EIAAB24951 Autophagy-related protein LC3 B,Autophagy-related ubiquitin-like modifier LC3 B,MAP1 light chain 3-like protein 2,MAP1A_MAP1B LC3 B,MAP1A_MAP1B light chain 3 B,Map1alc3,Map1lc3,Map1lc3b,Microtubule-as
EIAAB34348 Homo sapiens,Human,REPA3,Replication factor A protein 3,Replication protein A 14 kDa subunit,RF-A protein 3,RP-A p14,RPA14,RPA3
EIAAB34350 Homo sapiens,Human,Replication factor A protein 4,Replication protein A 30 kDa subunit,RF-A protein 4,RP-A p30,RPA4
EIAAB34343 Mouse,Mus musculus,Replication factor A protein 1,Replication protein A 70 kDa DNA-binding subunit,RF-A protein 1,RP-A p70,Rpa1
EIAAB34349 Mouse,Mus musculus,Replication factor A protein 3,Replication protein A 14 kDa subunit,RF-A protein 3,RP-A p14,Rpa3


 

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