VPS45_ARATH
ID VPS45_ARATH Reviewed; 569 AA.
AC O49048; O80650;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Vacuolar protein sorting-associated protein 45 homolog {ECO:0000303|PubMed:10888666, ECO:0000303|PubMed:9625693};
DE Short=AtVPS45 {ECO:0000303|PubMed:10888666, ECO:0000303|PubMed:9625693};
DE AltName: Full=Protein BFA-VISUALIZED ENDOCYTIC TRAFFICKING DEFECTIVE 2 {ECO:0000303|PubMed:23737757};
GN Name=VPS45 {ECO:0000303|PubMed:10888666, ECO:0000303|PubMed:9625693};
GN Synonyms=BEN2 {ECO:0000303|PubMed:23737757};
GN OrderedLocusNames=At1g77140 {ECO:0000312|Araport:AT1G77140};
GN ORFNames=T14N5.2 {ECO:0000312|EMBL:AAC34344.1};
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9625693; DOI=10.1104/pp.117.2.407;
RA Bassham D.C., Raikhel N.V.;
RT "An Arabidopsis VPS45p homolog implicated in protein transport to the
RT vacuole.";
RL Plant Physiol. 117:407-415(1998).
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 INTERACTION WITH SYP21; SYP22; SYP31; SYP41; SYP42; SYP61; VTI11 AND VTI12,
RP AND SUBCELLULAR LOCATION.
RX PubMed=10888666; DOI=10.1091/mbc.11.7.2251;
RA Bassham D.C., Sanderfoot A.A., Kovaleva V., Zheng H., Raikhel N.V.;
RT "AtVPS45 complex formation at the trans-Golgi network.";
RL Mol. Biol. Cell 11:2251-2265(2000).
RN [6]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19251905; DOI=10.1104/pp.108.134361;
RA Zouhar J., Rojo E., Bassham D.C.;
RT "AtVPS45 is a positive regulator of the SYP41/SYP61/VTI12 SNARE complex
RT involved in trafficking of vacuolar cargo.";
RL Plant Physiol. 149:1668-1678(2009).
RN [7]
RP FUNCTION, MUTAGENESIS OF ASP-129, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=23737757; DOI=10.1371/journal.pgen.1003540;
RA Tanaka H., Kitakura S., Rakusova H., Uemura T., Feraru M.I., De Rycke R.,
RA Robert S., Kakimoto T., Friml J.;
RT "Cell polarity and patterning by PIN trafficking through early endosomal
RT compartments in Arabidopsis thaliana.";
RL PLoS Genet. 9:e1003540-e1003540(2013).
CC -!- FUNCTION: Involved in the protein transport to the vacuole, probably at
CC the level of vesicle fusion at the trans-Golgi network (TGN) and not in
CC transport from the TGN to the prevacuolar compartment, by promoting the
CC recycling of vacuolar sorting receptors back to the TGN
CC (PubMed:19251905). Involved in early endosomal vesicle trafficking,
CC particularly at the trans-Golgi-network/early endosome (TGN/EE) thus
CC residing in early endocytic route (PubMed:23737757). Together with
CC BIG5/BEN1 required for polar PIN-FORMED (PIN) proteins localization,
CC for their dynamic repolarization, and consequently for auxin activity
CC gradient formation and auxin-related developmental processes (e.g.
CC embryonic patterning, organogenesis and vasculature venation
CC patterning) (PubMed:23737757). Necessary for pollen germination and for
CC cell expansion (PubMed:19251905). Binds syntaxins.
CC {ECO:0000269|PubMed:19251905, ECO:0000269|PubMed:23737757}.
CC -!- SUBUNIT: Interacts with both SYP41 or SYP42 and VTI12, but in different
CC domains of the trans-Golgi network (PubMed:10888666). Does not interact
CC on the pervacuolar compartment with VTI11, SYP21 or SYP22, or on the
CC cis-Golgi with SYP31 (PubMed:10888666). Interacts at the trans-Golgi
CC network (TGN) with the SYP41/SYP61/VTI12 SNARE complex
CC (PubMed:19251905). {ECO:0000269|PubMed:10888666,
CC ECO:0000269|PubMed:19251905}.
CC -!- INTERACTION:
CC O49048; O65359: SYP41; NbExp=6; IntAct=EBI-1750377, EBI-1750331;
CC O49048; Q9SWH4: SYP42; NbExp=4; IntAct=EBI-1750377, EBI-1750405;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:10888666}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10888666}. Early endosome
CC {ECO:0000269|PubMed:23737757}. Note=Binds to trans-Golgi network
CC membranes through interaction with other proteins.
CC {ECO:0000269|PubMed:10888666}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots, lower expression in
CC leaves, stems and flowers.
CC -!- DISRUPTION PHENOTYPE: Male gametophytic lethal and stunted growth
CC associated with defects in vacuole formation leading to reduced cell
CC expansion and autophagy-related defects in nutrient turnover
CC (PubMed:19251905). Blocked transport of vacuolar cargo proteins with C-
CC terminal vacuolar sorting determinants (PubMed:19251905).
CC {ECO:0000269|PubMed:19251905}.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR EMBL; AF036234; AAC39472.1; -; mRNA.
DR EMBL; AC004260; AAC34344.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35940.1; -; Genomic_DNA.
DR EMBL; AY050370; AAK91388.1; -; mRNA.
DR EMBL; AY101517; AAM26638.1; -; mRNA.
DR PIR; T00445; T00445.
DR PIR; T52056; T52056.
DR RefSeq; NP_565150.1; NM_106364.2.
DR AlphaFoldDB; O49048; -.
DR SMR; O49048; -.
DR BioGRID; 29269; 5.
DR IntAct; O49048; 5.
DR STRING; 3702.AT1G77140.1; -.
DR iPTMnet; O49048; -.
DR PaxDb; O49048; -.
DR PRIDE; O49048; -.
DR ProteomicsDB; 242739; -.
DR DNASU; 844050; -.
DR EnsemblPlants; AT1G77140.1; AT1G77140.1; AT1G77140.
DR GeneID; 844050; -.
DR Gramene; AT1G77140.1; AT1G77140.1; AT1G77140.
DR KEGG; ath:AT1G77140; -.
DR Araport; AT1G77140; -.
DR TAIR; locus:2196025; AT1G77140.
DR eggNOG; KOG1299; Eukaryota.
DR HOGENOM; CLU_013933_3_1_1; -.
DR InParanoid; O49048; -.
DR OMA; VHQLNNA; -.
DR OrthoDB; 651641at2759; -.
DR PhylomeDB; O49048; -.
DR PRO; PR:O49048; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O49048; baseline and differential.
DR Genevisible; O49048; AT.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0009846; P:pollen germination; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:2000012; P:regulation of auxin polar transport; IMP:UniProtKB.
DR GO; GO:2000067; P:regulation of root morphogenesis; IMP:UniProtKB.
DR GO; GO:0031338; P:regulation of vesicle fusion; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.40.50.2060; -; 1.
DR Gene3D; 3.90.830.10; -; 1.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR Pfam; PF00995; Sec1; 1.
DR PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 1: Evidence at protein level;
KW Auxin signaling pathway; Endosome; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..569
FT /note="Vacuolar protein sorting-associated protein 45
FT homolog"
FT /id="PRO_0000206315"
FT MUTAGEN 129
FT /note="D->N: In ben2; abnormal subcellular localization
FT with impaired association with the trans-Golgi-network and
FT early endosome (TGN/EE). Reduced accumulation of
FT endocytosed proteins (e.g. PIN2) in agglomerated
FT intracellular endosomal compartments leading to an altered
FT auxin gradient and subsequent growth defects (e.g.
FT disrupted roots architecture and shoot growth)."
FT /evidence="ECO:0000269|PubMed:23737757"
FT CONFLICT 362
FT /note="T -> I (in Ref. 1; AAC39472)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 64942 MW; 844F24C9A21E9C1D CRC64;
MVLVTSVRDY INRMLQDISG MKVLILDSET VSNVSIVYSQ SELLQKEVFL VEMIDSISVS
KESMSHLKAV YFIRPTSDNI QKLRYQLANP RFGEYHLFFS NLLKDTQIHI LADSDEQEVV
QQVQEYYADF VSGDPYHFTL NMASNHLYMI PAVVDPSGLQ RFSDRVVDGI AAVFLALKRR
PVIRYQRTSD TAKRIAHETA KLMYQHESAL FDFRRTESSP LLLVIDRRDD PVTPLLNQWT
YQAMVHELIG LQDNKVDLKS IGSLPKDQQV EVVLSSEQDA FFKSNMYENF GDIGMNIKRM
VDDFQQVAKS NQNIQTVEDM ARFVDNYPEY KKMQGNVSKH VTLVTEMSKL VEARKLMTVS
QTEQDLACNG GQGAAYEAVT DLLNNESVSD IDRLRLVMLY ALRYEKENPV QLMQLFNKLA
SRSPKYKPGL VQFLLKQAGV EKRTGDLFGN RDLLNIARNM ARGLKGVENV YTQHQPLLFQ
TMESITRGRL RDVDYPFVGD HFQQGRPQEV VIFMVGGTTY EESRSVALQN ATNSGVRFIL
GGTAVLNSKR FLKDLEEAQR ISRSGSHMV
