INVA4_ARATH
ID INVA4_ARATH Reviewed; 664 AA.
AC Q39041; Q7DLW9; Q8GX36;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Acid beta-fructofuranosidase 4, vacuolar {ECO:0000303|PubMed:9332372};
DE Short=At beta fruct4 {ECO:0000303|PubMed:9332372};
DE Short=AtBETAFRUCT4 {ECO:0000303|PubMed:9332372};
DE EC=3.2.1.26 {ECO:0000255|PROSITE-ProRule:PRU10067};
DE AltName: Full=Acid invertase 4 {ECO:0000303|PubMed:9332372};
DE Short=AI 4 {ECO:0000303|PubMed:9332372};
DE AltName: Full=Acid sucrose hydrolase 4 {ECO:0000305};
DE AltName: Full=Vacuolar invertase 4 {ECO:0000303|PubMed:14871666};
DE Short=Inv-V4 {ECO:0000303|PubMed:14871666};
DE Short=VAC-INV 4 {ECO:0000303|PubMed:16481625};
DE Short=VI 4 {ECO:0000303|PubMed:14871666};
DE Flags: Precursor;
GN Name=BFRUCT4 {ECO:0000303|PubMed:9332372};
GN Synonyms=BETAFRUCT4 {ECO:0000303|PubMed:9332372};
GN OrderedLocusNames=At1g12240 {ECO:0000312|Araport:AT1G12240};
GN ORFNames=T28K15.3 {ECO:0000312|EMBL:AAG12569.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=9332372; DOI=10.1016/s0378-1119(97)00268-0;
RA Haouazine-Takvorian N., Tymowska-Lalanne Z., Takvorian A., Tregear J.,
RA Lejeune B., Lecharny A., Kreis M.;
RT "Characterization of two members of the Arabidopsis thaliana gene family,
RT At beta fruct3 and At beta fruct4, coding for vacuolar invertases.";
RL Gene 197:239-251(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 413-636.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12773619; DOI=10.1073/pnas.1230987100;
RA Rojo E., Zouhar J., Carter C., Kovaleva V., Raikhel N.V.;
RT "A unique mechanism for protein processing and degradation in Arabidopsis
RT thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7389-7394(2003).
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=14871666; DOI=10.1016/j.bbapap.2003.09.017;
RA Rausch T., Greiner S.;
RT "Plant protein inhibitors of invertases.";
RL Biochim. Biophys. Acta 1696:253-261(2004).
RN [8]
RP DEVELOPMENTAL STAGE, AND INDUCTION BY GIBBERELLIN.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=15056893; DOI=10.1271/bbb.68.602;
RA Mitsuhashi W., Sasaki S., Kanazawa A., Yang Y.-Y., Kamiya Y., Toyomasu T.;
RT "Differential expression of acid invertase genes during seed germination in
RT Arabidopsis thaliana.";
RL Biosci. Biotechnol. Biochem. 68:602-608(2004).
RN [9]
RP INDUCTION BY VIRULENT P.SYRINGAE.
RX PubMed=16807755; DOI=10.1007/s00425-006-0303-3;
RA Bonfig K.B., Schreiber U., Gabler A., Roitsch T., Berger S.;
RT "Infection with virulent and avirulent P. syringae strains differentially
RT affects photosynthesis and sink metabolism in Arabidopsis leaves.";
RL Planta 225:1-12(2006).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=16481625; DOI=10.1073/pnas.0511015103;
RA Sergeeva L.I., Keurentjes J.J., Bentsink L., Vonk J., van der Plas L.H.W.,
RA Koornneef M., Vreugdenhil D.;
RT "Vacuolar invertase regulates elongation of Arabidopsis thaliana roots as
RT revealed by QTL and mutant analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:2994-2999(2006).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=20207708; DOI=10.1104/pp.110.154443;
RA Naegele T., Henkel S., Hoermiller I., Sauter T., Sawodny O., Ederer M.,
RA Heyer A.G.;
RT "Mathematical modeling of the central carbohydrate metabolism in
RT Arabidopsis reveals a substantial regulatory influence of vacuolar
RT invertase on whole plant carbon metabolism.";
RL Plant Physiol. 153:260-272(2010).
RN [12]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF 7-LEU-LEU-8; 9-PRO-ILE-10;
RP 14-GLU--GLU-16; 18-LEU--TYR-21 AND 21-TYR--LEU-24, AND DOMAIN.
RC STRAIN=cv. Columbia;
RX PubMed=21899678; DOI=10.1111/j.1600-0854.2011.01276.x;
RA Jung C., Lee G.J., Jang M., Lee M., Lee J., Kang H., Sohn E.J., Hwang I.;
RT "Identification of sorting motifs of AtbetaFruct4 for trafficking from the
RT ER to the vacuole through the Golgi and PVC.";
RL Traffic 12:1774-1792(2011).
RN [13]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF ALA-2; 3-SER-SER-4; SER-3; SER-4;
RP ASP-5; ALA-6; 7-LEU-LEU-8; LEU-7; LEU-8; PRO-9; ILE-10; SER-11; ALA-12 AND
RP 21-TYR--LEU-24, AND DOMAIN.
RX PubMed=23737500; DOI=10.1093/pcp/pct075;
RA Xiang L., Van den Ende W.;
RT "Trafficking of plant vacuolar invertases: from a membrane-anchored to a
RT soluble status. Understanding sorting information in their complex N-
RT terminal motifs.";
RL Plant Cell Physiol. 54:1263-1277(2013).
CC -!- FUNCTION: Possible role in the continued mobilization of sucrose to
CC sink organs (PubMed:20207708). Regulates root elongation
CC (PubMed:16481625). {ECO:0000269|PubMed:16481625,
CC ECO:0000269|PubMed:20207708}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside
CC residues in beta-D-fructofuranosides.; EC=3.2.1.26;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10067};
CC -!- ACTIVITY REGULATION: Inhibited by C/VIF1 and C/VIF2.
CC {ECO:0000269|PubMed:14871666}.
CC -!- PATHWAY: Glycan biosynthesis; sucrose metabolism. {ECO:0000305}.
CC -!- SUBUNIT: May be present in two forms, a 70 kDa monomer and a
CC heterodimer of the 30 kDa and 38 kDa subunits. The ratio of the levels
CC of the two forms within cells appears to be regulated developmentally
CC (By similarity). {ECO:0000250|UniProtKB:P29001}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:12773619}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:21899678,
CC ECO:0000269|PubMed:23737500}; Single-pass type II membrane protein.
CC Golgi apparatus membrane {ECO:0000269|PubMed:21899678,
CC ECO:0000269|PubMed:23737500}; Single-pass type II membrane protein.
CC Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:21899678}; Single-pass type II membrane protein.
CC Prevacuolar compartment membrane {ECO:0000269|PubMed:21899678}; Single-
CC pass type II membrane protein. Vacuole membrane
CC {ECO:0000269|PubMed:21899678}; Single-pass type II membrane protein.
CC Vacuole lumen {ECO:0000269|PubMed:21899678,
CC ECO:0000269|PubMed:23737500}. Note=Located in the lytic vacuole but not
CC in the protein storage vacuole. Remains inserted into membranes on its
CC way to the lytic vacuole, following the classical sorting pathway from
CC the endoplasmic reticulum. Released into the lumen of the vacuole from
CC the tonoplast through a proteolytic processing.
CC {ECO:0000269|PubMed:21899678, ECO:0000269|PubMed:23737500}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in stems, roots and flowers, and,
CC to a lower extent, in mature leaves. {ECO:0000269|PubMed:9332372}.
CC -!- DEVELOPMENTAL STAGE: Expressed during germination et seedling growth.
CC {ECO:0000269|PubMed:15056893}.
CC -!- INDUCTION: Induced by gibberellin (e.g. gibberellic acid GA) that
CC accumulates in seeds after red light treatment (PubMed:15056893).
CC Accumulates upon infection with virulent but not with avirulent
CC P.syringae (PubMed:16807755). Degraded in a VPEgamma-dependent manner
CC during senescence (PubMed:12773619). {ECO:0000269|PubMed:12773619,
CC ECO:0000269|PubMed:15056893, ECO:0000269|PubMed:16807755}.
CC -!- DOMAIN: The LCPYTRL domain (18-24) is critical for trafficking from the
CC trans-Golgi network to the prevacuolar compartment and from the
CC prevacuolar compartment to the central vacuole (PubMed:21899678). The
CC PRRRRP domain (36-41) is involved in sorting to the vacuole
CC (PubMed:23737500). At least two Arg are needed for correct delivery and
CC the presence of two neighboring Pro seems to contribute to the sorting
CC efficiency (PubMed:23737500). {ECO:0000269|PubMed:21899678,
CC ECO:0000269|PubMed:23737500}.
CC -!- DISRUPTION PHENOTYPE: Reduced carbon fixation rates during the day, but
CC increased respiration during the night (PubMed:20207708). Shorter roots
CC (PubMed:16481625). {ECO:0000269|PubMed:16481625,
CC ECO:0000269|PubMed:20207708}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC43067.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X97749; CAA66330.1; -; mRNA.
DR EMBL; Y11559; CAA72321.1; -; Genomic_DNA.
DR EMBL; AC022522; AAG12569.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28855.1; -; Genomic_DNA.
DR EMBL; AY046009; AAK76683.1; -; mRNA.
DR EMBL; AY142666; AAN13204.1; -; mRNA.
DR EMBL; AK118459; BAC43067.1; ALT_INIT; mRNA.
DR PIR; E86257; E86257.
DR PIR; S71276; S71276.
DR RefSeq; NP_563901.1; NM_101096.3.
DR AlphaFoldDB; Q39041; -.
DR SMR; Q39041; -.
DR BioGRID; 23017; 2.
DR IntAct; Q39041; 2.
DR STRING; 3702.AT1G12240.1; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR iPTMnet; Q39041; -.
DR PaxDb; Q39041; -.
DR PRIDE; Q39041; -.
DR ProteomicsDB; 247030; -.
DR EnsemblPlants; AT1G12240.1; AT1G12240.1; AT1G12240.
DR GeneID; 837777; -.
DR Gramene; AT1G12240.1; AT1G12240.1; AT1G12240.
DR KEGG; ath:AT1G12240; -.
DR Araport; AT1G12240; -.
DR TAIR; locus:2201966; AT1G12240.
DR eggNOG; KOG0228; Eukaryota.
DR HOGENOM; CLU_001528_6_1_1; -.
DR InParanoid; Q39041; -.
DR OMA; WIGGTIN; -.
DR OrthoDB; 405663at2759; -.
DR PhylomeDB; Q39041; -.
DR BioCyc; ARA:AT1G12240-MON; -.
DR UniPathway; UPA00238; -.
DR PRO; PR:Q39041; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39041; baseline and differential.
DR Genevisible; Q39041; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; IDA:UniProtKB.
DR GO; GO:0005775; C:vacuolar lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; ISS:TAIR.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; ISS:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0071370; P:cellular response to gibberellin stimulus; IEP:UniProtKB.
DR GO; GO:0080022; P:primary root development; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR021792; Beta-fructofuranosidase_N.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR018053; Glyco_hydro_32_AS.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF11837; DUF3357; 1.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Glycosidase; Golgi apparatus; Hydrolase; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Vacuole; Zymogen.
FT PROPEP 1..108
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P80065"
FT /id="PRO_0000417019"
FT CHAIN 109..664
FT /note="Acid beta-fructofuranosidase 4, vacuolar"
FT /id="PRO_0000417020"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 44..64
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..664
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 7..8
FT /note="Critical for endoplasmic reticulum export"
FT /evidence="ECO:0000269|PubMed:21899678"
FT MOTIF 9..10
FT /note="Critical for endoplasmic reticulum export"
FT /evidence="ECO:0000269|PubMed:21899678"
FT MOTIF 14..16
FT /note="Critical for trafficking from the trans-Golgi
FT network to the prevacuolar compartment and from the
FT prevacuolar compartment to the central vacuole"
FT /evidence="ECO:0000269|PubMed:21899678"
FT ACT_SITE 135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 132..135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 194..195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 258..259
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 510..558
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT MUTAGEN 2
FT /note="Missing: No effect on localization."
FT /evidence="ECO:0000269|PubMed:23737500"
FT MUTAGEN 3..4
FT /note="Missing: Endoplasmic reticulum localization."
FT /evidence="ECO:0000269|PubMed:23737500"
FT MUTAGEN 3
FT /note="Missing: Partial retention in the endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:23737500"
FT MUTAGEN 4
FT /note="Missing: Partial retention in the endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:23737500"
FT MUTAGEN 5
FT /note="Missing: Endoplasmic reticulum localization."
FT /evidence="ECO:0000269|PubMed:23737500"
FT MUTAGEN 6
FT /note="Missing: No effect on localization."
FT /evidence="ECO:0000269|PubMed:23737500"
FT MUTAGEN 7..8
FT /note="LL->AA: Reduced vacuolar trafficking."
FT /evidence="ECO:0000269|PubMed:21899678"
FT MUTAGEN 7..8
FT /note="Missing: Endoplasmic reticulum localization."
FT /evidence="ECO:0000269|PubMed:23737500"
FT MUTAGEN 7
FT /note="Missing: Partial retention in the endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:23737500"
FT MUTAGEN 8
FT /note="Missing: Partial retention in the endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:23737500"
FT MUTAGEN 9..10
FT /note="PI->AA: Reduced vacuolar trafficking."
FT /evidence="ECO:0000269|PubMed:21899678"
FT MUTAGEN 9
FT /note="P->A: Partial retention in the endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:23737500"
FT MUTAGEN 10
FT /note="Missing: Endoplasmic reticulum localization."
FT /evidence="ECO:0000269|PubMed:23737500"
FT MUTAGEN 11
FT /note="Missing: Endoplasmic reticulum localization."
FT /evidence="ECO:0000269|PubMed:23737500"
FT MUTAGEN 12
FT /note="Missing: No effect on localization."
FT /evidence="ECO:0000269|PubMed:23737500"
FT MUTAGEN 14..16
FT /note="EEE->AAA: Reduced vacuolar trafficking."
FT /evidence="ECO:0000269|PubMed:21899678"
FT MUTAGEN 18..21
FT /note="LCPY->AAAA: Reduced vacuolar trafficking."
FT /evidence="ECO:0000269|PubMed:21899678"
FT MUTAGEN 21..24
FT /note="YTRL->AAAA: Reduced vacuolar trafficking."
FT /evidence="ECO:0000269|PubMed:21899678"
FT MUTAGEN 21..24
FT /note="Missing: No effect on localization."
FT /evidence="ECO:0000269|PubMed:23737500"
SQ SEQUENCE 664 AA; 73844 MW; 85948869AEDABD8B CRC64;
MASSDALLPI SAREEEPLCP YTRLPMADPN QETHGPRRRR PFKGLLAVSF GLLFIAFYVA
LIATHDGSRS NDEGIDETET ITSRARLAGV SEKRNDGLWK LSGDRNTPAF EWNNSMLSWQ
RTAFHFQPEQ NWMNDPNGPL FYKGWYHFFY QYNPNAAVWG DIVWGHAVSR DLIHWVHLPI
AMVADQWYDS NGVWTGSATF LPDGSIVMLY TGSTDKAVQV QNLAYPEDPN DPLLLKWVKF
PGNPVLVPPP GILPKDFRDP TTAWKTSEGK WRITIGSKLN KTGISLVYDT IDFKTYEKLD
TLLHRVPNTG MWECVDFYPV SKTAGNGLDT SVNGPDVKHI VKASMDDTRF DHYAVGTYFD
SNGTWIPDDP TIDVGMTASL RYDYGKFYAS KSFYDQNKGR RVLWSWIGES DSEASDVQKG
WSSLQGIPRT VVLDTKTGKN LVQWPVEEIK SLRLSSKQFD LEVGPGSVVP VDVGSAAQLD
IEAEFEINKE SLDKIIGNAS VVAEAEEFSC EKSGGSTVRG ALGPFGFSVL ATESLSEQTP
VYFYVAKGKD SELKTFFCTD TSRSSVANDV VKPIYGSVVP VLKGEKLTMR ILVDHSIVEA
FGQGGRTCIT SRVYPTTAIY GAAKLFLFNN ALDATVTASF TVWQMNSAFI HPYSDEAVRA
LSRT
