VPS18_ARATH
ID VPS18_ARATH Reviewed; 988 AA.
AC F4IDS7; Q9LN91; Q9LN97;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Vacuolar sorting protein 18 {ECO:0000303|PubMed:12589039};
GN Name=VPS18 {ECO:0000303|PubMed:12589039};
GN OrderedLocusNames=At1g12470 {ECO:0000312|Araport:AT1G12470};
GN ORFNames=F5O11.22 {ECO:0000312|EMBL:AAF79641.1},
GN T12C24.2 {ECO:0000312|EMBL:AAF88074.1};
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 [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 [2]
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 [3]
RP IDENTIFICATION.
RX PubMed=12589039; DOI=10.1091/mbc.e02-08-0509;
RA Rojo E., Zouhar J., Kovaleva V., Hong S., Raikhel N.V.;
RT "The AtC-VPS protein complex is localized to the tonoplast and the
RT prevacuolar compartment in arabidopsis.";
RL Mol. Biol. Cell 14:361-369(2003).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29463724; DOI=10.1073/pnas.1717839115;
RA Takemoto K., Ebine K., Askani J.C., Krueger F., Gonzalez Z.A., Ito E.,
RA Goh T., Schumacher K., Nakano A., Ueda T.;
RT "Distinct sets of tethering complexes, SNARE complexes, and Rab GTPases
RT mediate membrane fusion at the vacuole in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E2457-E2466(2018).
CC -!- FUNCTION: Essential protein required during embryogenesis. Believed to
CC act as a core component of the putative HOPS endosomal tethering
CC complex and of the class C core vacuole/endosome tethering (CORVET)
CC complex. CORVET is required for vacuolar transport of SYP22. HOPS is
CC required for the central vacuole formation. Involved in root
CC development (PubMed:29463724). Plays a role in vesicle-mediated protein
CC trafficking to lysosomal compartments including the endocytic membrane
CC transport pathways (By similarity). {ECO:0000250|UniProtKB:Q9P253,
CC ECO:0000269|PubMed:29463724}.
CC -!- SUBUNIT: Core component of at least two putative endosomal tethering
CC complexes, the homotypic fusion and vacuole protein sorting (HOPS)
CC complex and the class C core vacuole/endosome tethering (CORVET)
CC complex. Their common core is composed of the class C Vps proteins
CC VPS11, VCL1, VPS18 and VPS33, which in HOPS further associates with
CC VPS39 and VPS41 and in CORVET with VPS3. {ECO:0000269|PubMed:29463724}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q9P253};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9P253}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q9P253}. Vacuole membrane
CC {ECO:0000269|PubMed:29463724}; Peripheral membrane protein
CC {ECO:0000269|PubMed:29463724}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9P253}. Cytoplasm
CC {ECO:0000269|PubMed:29463724}. Note=Co-localizes with VPS39 at
CC subdomains of the vacuolar membrane, and with VPS3 and RABF2B at
CC punctate compartments in the cytoplasm, with faintly dispersed
CC distribution in the cytosol. Sometimes observed at the vertex zone, the
CC ring-shaped edge of vacuole-vacuole contact sites. Co-localizes with
CC RABG3F. {ECO:0000269|PubMed:29463724}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality (PubMed:29463724).
CC Heterozygous mutants produce some yellowish seeds with developmentally
CC retarded or abnormally shaped embryos. Conditional dexamethasone (DEX)-
CC inducible mutants exhibit abnormal root morphology (PubMed:29463724).
CC {ECO:0000269|PubMed:29463724}.
CC -!- SIMILARITY: Belongs to the VPS18 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79641.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF88074.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC025416; AAF79641.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC025417; AAF88074.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28887.1; -; Genomic_DNA.
DR PIR; B86259; B86259.
DR RefSeq; NP_172709.2; NM_101119.7.
DR AlphaFoldDB; F4IDS7; -.
DR SMR; F4IDS7; -.
DR STRING; 3702.AT1G12470.1; -.
DR PaxDb; F4IDS7; -.
DR PRIDE; F4IDS7; -.
DR ProteomicsDB; 242704; -.
DR EnsemblPlants; AT1G12470.1; AT1G12470.1; AT1G12470.
DR GeneID; 837804; -.
DR Gramene; AT1G12470.1; AT1G12470.1; AT1G12470.
DR KEGG; ath:AT1G12470; -.
DR Araport; AT1G12470; -.
DR TAIR; locus:2034735; AT1G12470.
DR eggNOG; KOG2034; Eukaryota.
DR HOGENOM; CLU_003488_1_0_1; -.
DR InParanoid; F4IDS7; -.
DR OMA; HVQRESR; -.
DR OrthoDB; 87842at2759; -.
DR PRO; PR:F4IDS7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4IDS7; baseline and differential.
DR GO; GO:0033263; C:CORVET complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0030897; C:HOPS complex; IDA:UniProtKB.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0048284; P:organelle fusion; IBA:GO_Central.
DR GO; GO:0010015; P:root morphogenesis; IMP:UniProtKB.
DR GO; GO:0007033; P:vacuole organization; IBA:GO_Central.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR007810; Pep3_Vps18.
DR InterPro; IPR001841; Znf_RING.
DR Pfam; PF00637; Clathrin; 1.
DR Pfam; PF05131; Pep3_Vps18; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50236; CHCR; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Endosome; Membrane; Metal-binding;
KW Protein transport; Reference proteome; Transport; Vacuole; Zinc;
KW Zinc-finger.
FT CHAIN 1..988
FT /note="Vacuolar sorting protein 18"
FT /id="PRO_0000444308"
FT REPEAT 589..749
FT /note="CHCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01006"
FT ZN_FING 836..886
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT COILED 785..819
FT /evidence="ECO:0000255"
SQ SEQUENCE 988 AA; 112320 MW; 203CC559284BBE49 CRC64;
MDQGRQVFSV DLLERYATKN RGMITCMAAG NDVIVLGTSK GWIIRYDFGV GSSNDIDLAV
GRTGEQSIHK VFVDPGGSHC IATVTGVGGA ETFYTHAKWL KPRVLSRLKG LLVNAVAWNR
QQITEVSTKE IILGTQDGQL FEMAVDEKDK REKYIKFLFE LEELPEAFKA LQMETANISS
GMRYYVMAVT PTRLYSFTGI GTLESVFASY KERAVHFMEL PGEIPNSELH FFIKQRRAVH
FAWLSGTGIY HGGLNFGAQH SYPNGDENFV ENKALLDYSK LSDGTEAVKP GSMALSEYHF
LLLIGNKVKV VNRISEQIIE ELQFDITSDS VSRGIIGLCS DASANVFYAY DQNSIFQVSV
IDEGRDMWKV YLDLKVYAAA LANCRDPLQR DQVYLVQAES AFTDKEYLRA ASFYAKINYV
ISFEEVTLKF ISINEPEALR TFLLHKLDNL SKDDKCQITM ISTWATELYL DKINRLLLED
DTAIENRDSE YHSVIQEFRA FMSDCKDELD EATTVKILES YGRVEELVYF ANLKEQYEIV
VLHYIQQGEA KKALEVLQKS SVSVELQYQF APELIMLDAY ETVESWMANK NLNPRRLITA
MMRYSSGPHA KNETHEVIKY LEFCVHRLHN EDPGIHSLLL SLYAKQEDDG ALLRFLQCKF
GKGRENGPEF FYDPKYALRL CLKERRTRAC VHIYSMMSMH EEAVALALQI DPELAMAEAD
KVEDDEDLRK KLWLMVAKHV VKQEKGAKRE NIRKAIAFLK ETDGLLKIED ILPFFPDFAL
IDDFKEAICS SLEDYNKQIE QLKEEMNDAT RGADNIRNDI SALTQRYAVI DRDEECGVCK
RKILMMSGDF RMAQGYSSAG PLAPFYVFPC GHSFHAQCLI THVTSCAHEE QAEHILDLQK
QLTLLGSETR RDINGNRSDE PITSTTTADK LRSELDDAIA SECPFCGELM INEITLPFIK
PEDSQYSTSW DLRSETNLAN QRTISLPV
