VPS51_ARATH
ID VPS51_ARATH Reviewed; 780 AA.
AC Q0WQ75; O04247;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Vacuolar protein sorting-associated protein 51 homolog {ECO:0000303|PubMed:24757006};
DE AltName: Full=Protein UNHINGED {ECO:0000303|PubMed:24757006};
GN Name=VPS51 {ECO:0000303|PubMed:24757006};
GN Synonyms=UNH {ECO:0000303|PubMed:24757006};
GN OrderedLocusNames=At4g02030 {ECO:0000312|Araport:AT4G02030};
GN ORFNames=T10M13.4 {ECO:0000312|EMBL:CAB80696.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH VPS52, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=24757006; DOI=10.1242/dev.099333;
RA Pahari S., Cormark R.D., Blackshaw M.T., Liu C., Erickson J.L.,
RA Schultz E.A.;
RT "Arabidopsis UNHINGED encodes a VPS51 homolog and reveals a role for the
RT GARP complex in leaf shape and vein patterning.";
RL Development 141:1894-1905(2014).
CC -!- FUNCTION: Acts as component of the GARP complex that is involved in
CC retrograde transport from early and late endosomes to the trans-Golgi
CC network (TGN). The GARP complex is required for the maintenance of
CC protein retrieval from endosomes to the TGN, acid hydrolase sorting,
CC lysosome function, endosomal cholesterol traffic and autophagy. VPS51
CC participates in retrograde transport of acid hydrolase receptors,
CC likely by promoting tethering and SNARE-dependent fusion of endosome-
CC derived carriers to the TGN. Acts as component of the EARP complex that
CC is involved in endocytic recycling. The EARP complex associates with
CC Rab4-positive endosomes and promotes recycling of internalized
CC transferrin receptor (TFRC) to the plasma membrane (By similarity).
CC Required for vacuolar targeting and cellular trafficking. Involved in
CC the regulation of vascular tissue patterning, probably by regulating
CC PIN1 expression pattern, thus modulating auxin flux. Important to
CC prevent PIN1 accumulation within margin cells, possibly by targeting
CC PIN1 to the lytic vacuole. Regulates PIN1 and ATHB8 expression pattern
CC in secondary veins (PubMed:24757006). {ECO:0000250|UniProtKB:Q9UID3,
CC ECO:0000269|PubMed:24757006}.
CC -!- SUBUNIT: Component of the Golgi-associated retrograde protein (GARP)
CC complex, composed by VPS51, VPS52, VPS53 and VPS54. Component of the
CC endosome-associated retrograde protein (EARP) complex, composed of
CC VPS51, VPS52, VPS53 and VPS50 (By similarity). Interacts with VPS52
CC (PubMed:24757006). {ECO:0000250|UniProtKB:Q9UID3,
CC ECO:0000269|PubMed:24757006}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:24757006}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q9UID3}. Prevacuolar compartment
CC {ECO:0000269|PubMed:24757006}. Note=Localizes to the trans-Golgi
CC network as part of the GARP complex, while it localizes to recycling
CC endosomes as part of the EARP complex. {ECO:0000250|UniProtKB:Q9UID3}.
CC -!- TISSUE SPECIFICITY: Expressed in primary and lateral roots, shoots of
CC seedlings and flowers. {ECO:0000269|PubMed:24757006}.
CC -!- DEVELOPMENTAL STAGE: In leaves, first observed at low levels in a
CC diffuse pattern 3.5 days after germination (DAG), spreads throughout
CC much of the lamina by 4 DAG and becomes increasingly restricted to
CC presumptive veins from 5 to 8 DAG. Confined in epidermal cells of the
CC proximal margins in mature leaves. {ECO:0000269|PubMed:24757006}.
CC -!- DISRUPTION PHENOTYPE: Leaf vascular tissue patterning defects: simpler
CC leaf venation with distal non-meeting of the secondary veins and fewer
CC higher order veins, a narrower leaf with prominent serrations, and
CC reduced root and shoot growth. Normal early endocytic events, but
CC disrupted cellular trafficking. Reduced vacuolar targeting resulting in
CC expanded expression of PIN1 in leaf margins and altered expression
CC pattern of PIN1 and ATHB8 in secondary veins.
CC {ECO:0000269|PubMed:24757006}.
CC -!- SIMILARITY: Belongs to the VPS51 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC78695.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80696.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF001308; AAC78695.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161493; CAB80696.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82113.1; -; Genomic_DNA.
DR EMBL; AK228828; BAF00724.1; -; mRNA.
DR PIR; T01504; T01504.
DR RefSeq; NP_192112.2; NM_116434.4.
DR AlphaFoldDB; Q0WQ75; -.
DR SMR; Q0WQ75; -.
DR STRING; 3702.AT4G02030.2; -.
DR iPTMnet; Q0WQ75; -.
DR PRIDE; Q0WQ75; -.
DR EnsemblPlants; AT4G02030.1; AT4G02030.1; AT4G02030.
DR GeneID; 828155; -.
DR Gramene; AT4G02030.1; AT4G02030.1; AT4G02030.
DR KEGG; ath:AT4G02030; -.
DR Araport; AT4G02030; -.
DR eggNOG; KOG2346; Eukaryota.
DR OMA; HTIEPRT; -.
DR PhylomeDB; Q0WQ75; -.
DR PRO; PR:Q0WQ75; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q0WQ75; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:1990745; C:EARP complex; ISS:UniProtKB.
DR GO; GO:0000938; C:GARP complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0048193; P:Golgi vesicle transport; IBA:GO_Central.
DR GO; GO:0010305; P:leaf vascular tissue pattern formation; IMP:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0007041; P:lysosomal transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0007034; P:vacuolar transport; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
DR InterPro; IPR014812; Vps51.
DR PANTHER; PTHR15954; PTHR15954; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endosome; Golgi apparatus; Lipid transport; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..780
FT /note="Vacuolar protein sorting-associated protein 51
FT homolog"
FT /id="PRO_0000440166"
FT REGION 270..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 780 AA; 88516 MW; 100D4B9A65B9DD3D CRC64;
MATEAAPMDE KAKRMRDLLS SFYAPDPSIS TSGSSINASF DNINSTSFDA DQYMDLMIKK
SNLEVLLQRH VQMAAEIKNL DTDLQMLVYE NYNKFISATD TIKRMKSNIF GMEGNMDQLL
QKIMSVQSKS DGVNTSLFEK REHIEKLHRT RNLLRKVQFI YDLPARLQKC IKSEAYGDAV
RFYTGAMPIL KVYGDTSFQD CRRASEEAIE IIIKNLQTKL FSDSESIQAR AEAAVLLKQL
DVPVDSLKAK LLEKLEQSLD GLQIKPEEAS TLVEDDDSSN DTESNDQHPA KIHEDAVRGF
SEAIRAYREI FPDSEERLFK LARALTAMHF EYMELYIKKR VSAADFLGIF RIVWEDVVLM
DEVLPEAALS DLSAEAAQVT LKQFVARMFS HLQQDISDTL LKFDINQKEA VEGELLKVVL
EASQKAVLQG TTNIFQDFRQ LLDEKTGIFI KMKDLISGWI QKGSQDFFRS LEAQFLVLSG
KTSSSNDIEG KSSDKIHAGL ILVLAQLSVF IEQKVIPRVT EEIAASFSGG NSQAFENGPA
FIPGELCRVF HAASEKLLQH YIDTRTQKVS VLLRKRFKTP NWVKHKEPRE VHMYVDMFLH
ELEEVGKEVK QVLPQGTFRK HKRTDSNGSN TTTSSRSNTL HNDKMARSNS QRARSQLFET
HLAKLFKQKV EIFTKVEFTQ ESVVTTTVKL CLKSLQEYVR LQTFNRSGFQ QIQLDIQFLK
APLKEAVEDE AAIDFLLDEV IVAASERCLD VIPLEPPILD KLIQAKLAKS KEHNNNTVSS
