ID VPS11_ARATH Reviewed; 932 AA.
AC Q9SJ40; Q8LG85;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 171.
DE RecName: Full=Vacuolar protein-sorting-associated protein 11 homolog;
DE Short=AtVPS11;
GN Name=VPS11; OrderedLocusNames=At2g05170; ORFNames=F5G3.7;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 651-932.
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, IDENTIFICATION IN THE C-VSP COMPLEX, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
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 [6]
RP INTERACTION WITH VPS39 AND VPS3, AND 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: Involved in regulating membrane fusion at the tonoplast and
CC the prevacuolar compartment. {ECO:0000269|PubMed:12589039}.
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 (PubMed:12589039,
CC PubMed:29463724). Interacts directly with VPS39 and VPS3
CC (PubMed:29463724). {ECO:0000269|PubMed:12589039,
CC ECO:0000269|PubMed:29463724}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:12589039};
CC Peripheral membrane protein {ECO:0000269|PubMed:12589039}. Prevacuolar
CC compartment membrane {ECO:0000269|PubMed:12589039}; Peripheral membrane
CC protein {ECO:0000269|PubMed:12589039}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, siliques and
CC flowers. {ECO:0000269|PubMed:12589039}.
CC -!- SIMILARITY: Belongs to the VPS11 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM60986.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC007018; AAD29055.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05900.1; -; Genomic_DNA.
DR EMBL; AF436824; AAL32006.1; -; mRNA.
DR EMBL; BT002698; AAO11614.1; -; mRNA.
DR EMBL; AY084412; AAM60986.1; ALT_INIT; mRNA.
DR PIR; F84465; F84465.
DR RefSeq; NP_027676.1; NM_126544.3.
DR AlphaFoldDB; Q9SJ40; -.
DR SMR; Q9SJ40; -.
DR BioGRID; 465; 2.
DR STRING; 3702.Q9SJ40; -.
DR PaxDb; 3702-AT2G05170-1; -.
DR ProteomicsDB; 242565; -.
DR EnsemblPlants; AT2G05170.1; AT2G05170.1; AT2G05170.
DR GeneID; 815065; -.
DR Gramene; AT2G05170.1; AT2G05170.1; AT2G05170.
DR KEGG; ath:AT2G05170; -.
DR Araport; AT2G05170; -.
DR TAIR; AT2G05170; VPS11.
DR eggNOG; KOG2114; Eukaryota.
DR HOGENOM; CLU_001287_0_1_1; -.
DR InParanoid; Q9SJ40; -.
DR OMA; ENECPAC; -.
DR OrthoDB; 5491867at2759; -.
DR PhylomeDB; Q9SJ40; -.
DR PRO; PR:Q9SJ40; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJ40; baseline and differential.
DR Genevisible; Q9SJ40; AT.
DR GO; GO:0033263; C:CORVET complex; IDA:UniProtKB.
DR GO; GO:0030897; C:HOPS complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0007033; P:vacuole organization; TAS:TAIR.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd16688; RING-H2_Vps11; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR016528; VPS11.
DR InterPro; IPR024763; VPS11_C.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR23323:SF24; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11 HOMOLOG; 1.
DR Pfam; PF00637; Clathrin; 1.
DR Pfam; PF12451; VPS11_C; 1.
DR Pfam; PF17122; zf-C3H2C3; 1.
DR PIRSF; PIRSF007860; VPS11; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50236; CHCR; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Membrane; Metal-binding; Reference proteome; Repeat; Vacuole;
KW Zinc; Zinc-finger.
FT CHAIN 1..932
FT /note="Vacuolar protein-sorting-associated protein 11
FT homolog"
FT /id="PRO_0000425971"
FT REPEAT 385..536
FT /note="CHCR 1"
FT REPEAT 548..756
FT /note="CHCR 2"
FT ZN_FING 842..877
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT COILED 795..841
FT /evidence="ECO:0000255"
FT CONFLICT 884
FT /note="V -> A (in Ref. 4; AAM60986)"
FT /evidence="ECO:0000305"
FT CONFLICT 892
FT /note="E -> Q (in Ref. 4; AAM60986)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 932 AA; 105713 MW; 75C906999A2E3B57 CRC64;
MYQLRKFDFF EEKYGGKIPE DVTGDIQCCS SGRGKVVIGS NDGSVSFLDR GVKFDSGFQA
HSSSVLFLQH LKQRNFLVTV GEDEQISPQQ SGMCLKVFDL DKVQEEGTSS SAPECIGILR
IFTNQFPEAK ITSFLVLEEV PPILLIAIGL DNGCIYCVKG DIARERITRF KLQVDGRSAI
TGLGFRMDGQ ALLLFAVTPE SVNLFSMQAQ PPKLQTLDHI GGSVNTVTMS DRSELIVGRP
EAVYFYEVDG RGPCWAFEGE KKFMGWFRGY LLCVIDDSKT GNTVFNVYDL RNRLIAYSIV
VDKVSNMLCE WGNIILIKAD KSLLCITEKD MESKLDMLFK KNLYTVAINL VQSQHADAAA
TANVMRKYGD HLYGKQDFDE AMLQYINTIG YLEPSFVIQK FLDAQRIYNL TNYLEKLHEK
GLASKDHTTL LLNCYTKLKD VEKLNTFIRK EDGIGELKFD VETAIRVCRA ANYHEHAMYV
AKKAGKHEWY LKILLEDLGN YDEALQYVSS LEPSQAGVTI EQYGKILIEH KPKETIDILM
RLCTEQGIPN GVFLSMLPSP VDFITVFVQH PHSLMHFLER YAEIVQDSPA QAEINNTLLE
LYLSRDLNFP SISLSENGLD KDLIDHSVAA AVSKADPEKK TNADSKDAME KDCTERQQKG
LELLKMAWPS DLEQPLYDVD LAVILCEMNS FKDGLLYLYE KMKFYKEVIA CYMQNHDHEG
LIACCKRLGD SSKGGDPSLW ADLLKYFGEI GEDCTKEVKE VLTYIERDDI LPPIIVLQTL
AKNPCLTLSV IKDYIARKLE QESKIIEEDR RAVEKYQETT KNMRKEIEDL RTNARIFQLS
KCTACTFTLD IPAVHFMCMH SFHQRCLGDN EKECPECAPE YRSVMEMKRS LEQNSKDQDL
FFQQVKGSKD GFSVIAEYFG KGIISKTRDA TS
//
