VSR1_ARATH
ID VSR1_ARATH Reviewed; 623 AA.
AC P93026; P94037; Q94AC0;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Vacuolar-sorting receptor 1;
DE Short=AtVSR1;
DE AltName: Full=BP80-like protein b;
DE Short=AtBP80b;
DE AltName: Full=Epidermal growth factor receptor-like protein 1;
DE Short=AtELP;
DE Short=AtELP1;
DE AltName: Full=Spot 3 protein;
DE Flags: Precursor;
GN Name=VSR1; Synonyms=BP80B, ELP, ELP1; OrderedLocusNames=At3g52850;
GN ORFNames=F8J2.20;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9159954; DOI=10.1104/pp.114.1.325;
RA Ahmed S.U., Bar-Peled M., Raikhel N.V.;
RT "Cloning and subcellular location of an Arabidopsis receptor-like protein
RT that shares common features with protein-sorting receptors of eukaryotic
RT cells.";
RL Plant Physiol. 114:325-336(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9306690; DOI=10.1104/pp.115.1.29;
RA Paris N., Rogers S.W., Jiang L., Kirsch T., Beevers L., Phillips T.E.,
RA Rogers J.C.;
RT "Molecular cloning and further characterization of a probable plant
RT vacuolar sorting receptor.";
RL Plant Physiol. 115:29-39(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Silique;
RA Stevens T.J., Prime T.A., Packman L.C., Dupree P.;
RT "Identification of a putative endosomal or Golgi protein from Arabidopsis
RT thaliana.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [5]
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 [6]
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 [7]
RP SUBCELLULAR LOCATION, AND TYROSINE-BASED INTERNALIZATION MOTIF.
RX PubMed=9707576; DOI=10.1073/pnas.95.17.9920;
RA Sanderfoot A.A., Ahmed S.U., Marty-Mazars D., Rapoport I., Kirchhausen T.,
RA Marty F., Raikhel N.V.;
RT "A putative vacuolar cargo receptor partially colocalizes with AtPEP12p on
RT a prevacuolar compartment in Arabidopsis roots.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9920-9925(1998).
RN [8]
RP SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=10561538; DOI=10.1016/s0005-2728(99)00087-0;
RA Laval V., Chabannes M., Carriere M., Canut H., Barre A., Rouge P.,
RA Pont-Lezica R., Galaud J.-P.;
RT "A family of Arabidopsis plasma membrane receptors presenting animal beta-
RT integrin domains.";
RL Biochim. Biophys. Acta 1435:61-70(1999).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=10397763; DOI=10.1091/mbc.10.7.2251;
RA Zheng H., von Mollard G.F., Kovaleva V., Stevens T.H., Raikhel N.V.;
RT "The plant vesicle-associated SNARE AtVTI1a likely mediates vesicle
RT transport from the trans-Golgi network to the prevacuolar compartment.";
RL Mol. Biol. Cell 10:2251-2264(1999).
RN [10]
RP FUNCTION, AND INTERACTION WITH ALEU.
RX PubMed=10871276; DOI=10.1083/jcb.149.7.1335;
RA Ahmed S.U., Rojo E., Kovaleva V., Venkataraman S., Dombrowski J.E.,
RA Matsuoka K., Raikhel N.V.;
RT "The plant vacuolar sorting receptor AtELP is involved in transport of
RT NH(2)-terminal propeptide-containing vacuolar proteins in Arabidopsis
RT thaliana.";
RL J. Cell Biol. 149:1335-1344(2000).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=12154135; DOI=10.1093/pcp/pcf085;
RA Li Y.-B., Rogers S.W., Tse Y.C., Lo S.W., Sun S.S.M., Jauh G.-Y., Jiang L.;
RT "BP-80 and homologs are concentrated on post-Golgi, probable lytic
RT prevacuolar compartments.";
RL Plant Cell Physiol. 43:726-742(2002).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=12493849; DOI=10.1093/jxb/erg018;
RA Laval V., Masclaux F., Serin A., Carriere M., Roldan C., Devic M.,
RA Pont-Lezica R.F., Galaud J.-P.;
RT "Seed germination is blocked in Arabidopsis putative vacuolar sorting
RT receptor (atbp80) antisense transformants.";
RL J. Exp. Bot. 54:213-221(2003).
RN [13]
RP FUNCTION, INTERACTION WITH ALEU AND CRA1, AND NOMENCLATURE.
RX PubMed=14657332; DOI=10.1073/pnas.2530568100;
RA Shimada T., Fuji K., Tamura K., Kondo M., Nishimura M., Hara-Nishimura I.;
RT "Vacuolar sorting receptor for seed storage proteins in Arabidopsis
RT thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:16095-16100(2003).
RN [14]
RP INTERACTION WITH EPSIN1.
RX PubMed=16905657; DOI=10.1105/tpc.105.039123;
RA Song J., Lee M.H., Lee G.-J., Yoo C.M., Hwang I.;
RT "Arabidopsis EPSIN1 plays an important role in vacuolar trafficking of
RT soluble cargo proteins in plant cells via interactions with clathrin, AP-1,
RT VTI11, and VSR1.";
RL Plant Cell 18:2258-2274(2006).
CC -!- FUNCTION: Vacuolar-sorting receptor (VSR) involved in clathrin-coated
CC vesicles sorting from Golgi apparatus to vacuoles. Required for the
CC sorting of 12S globulin, 2S albumin and maybe other seed storage
CC proteins to protein storage vacuoles (PSVs) in seeds. May also be
CC implicated in targeting N-terminal propeptide containing proteins to
CC lytic vacuoles. {ECO:0000269|PubMed:10871276,
CC ECO:0000269|PubMed:14657332}.
CC -!- SUBUNIT: Interacts with the N-terminal propeptide of ALEU and the C-
CC terminal part of the 12S globulin CRA1 in a calcium-dependent manner.
CC Binds to EPSIN1. {ECO:0000269|PubMed:10871276,
CC ECO:0000269|PubMed:14657332, ECO:0000269|PubMed:16905657}.
CC -!- INTERACTION:
CC P93026; Q8VY07: EPSIN1; NbExp=2; IntAct=EBI-1163008, EBI-1162785;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Golgi apparatus membrane; Single-pass type I membrane protein.
CC Cytoplasmic vesicle, clathrin-coated vesicle membrane; Single-pass type
CC I membrane protein. Prevacuolar compartment membrane; Single-pass type
CC I membrane protein. Note=Associated to the Golgi apparatus, mostly on
CC the trans-side, to clathrin-coated vesicles (CCVs) and to prevacuolar
CC compartments (PVCs). May also be associated with the plasma membrane.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots and dividing cells (at
CC protein level). Also expressed in seeds, seedlings, leaves, stems,
CC flowers, siliques and pollen. {ECO:0000269|PubMed:10561538,
CC ECO:0000269|PubMed:12493849, ECO:0000269|PubMed:9159954}.
CC -!- INDUCTION: Slightly induced by water deficit.
CC {ECO:0000269|PubMed:10561538}.
CC -!- DOMAIN: The tyrosine-based internalization signal may be involved in
CC trafficking at the trans Golgi network (TGN).
CC -!- SIMILARITY: Belongs to the VSR (BP-80) family. {ECO:0000305}.
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DR EMBL; U86700; AAB46988.1; -; mRNA.
DR EMBL; U79959; AAB72111.1; -; mRNA.
DR EMBL; Y07917; CAA69222.1; -; mRNA.
DR EMBL; AL132969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE79000.1; -; Genomic_DNA.
DR EMBL; AY048289; AAK82551.1; -; mRNA.
DR PIR; T47542; T47542.
DR RefSeq; NP_190853.1; NM_115145.2.
DR PDB; 4TJV; X-ray; 1.65 A; A=20-182.
DR PDB; 4TJX; X-ray; 1.90 A; A=20-182.
DR PDB; 7F2D; X-ray; 2.45 A; A=20-182.
DR PDB; 7F2I; X-ray; 2.35 A; A=20-182.
DR PDBsum; 4TJV; -.
DR PDBsum; 4TJX; -.
DR PDBsum; 7F2D; -.
DR PDBsum; 7F2I; -.
DR AlphaFoldDB; P93026; -.
DR SMR; P93026; -.
DR BioGRID; 9768; 32.
DR IntAct; P93026; 34.
DR STRING; 3702.AT3G52850.1; -.
DR TCDB; 9.B.87.1.13; the selenoprotein p receptor (selp-receptor) family.
DR PaxDb; P93026; -.
DR PRIDE; P93026; -.
DR ProteomicsDB; 242632; -.
DR EnsemblPlants; AT3G52850.1; AT3G52850.1; AT3G52850.
DR GeneID; 824451; -.
DR Gramene; AT3G52850.1; AT3G52850.1; AT3G52850.
DR KEGG; ath:AT3G52850; -.
DR Araport; AT3G52850; -.
DR TAIR; locus:2085136; AT3G52850.
DR eggNOG; ENOG502QSX2; Eukaryota.
DR HOGENOM; CLU_031082_1_0_1; -.
DR InParanoid; P93026; -.
DR OMA; YECKCGS; -.
DR OrthoDB; 1428226at2759; -.
DR PhylomeDB; P93026; -.
DR PRO; PR:P93026; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P93026; baseline and differential.
DR Genevisible; P93026; AT.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017119; C:Golgi transport complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0009940; F:amino-terminal vacuolar sorting propeptide binding; IDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006896; P:Golgi to vacuole transport; IDA:TAIR.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0007034; P:vacuolar transport; IMP:TAIR.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR003137; PA_domain.
DR Pfam; PF02225; PA; 1.
DR SMART; SM00179; EGF_CA; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01187; EGF_CA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cytoplasmic vesicle; Disulfide bond;
KW EGF-like domain; Glycoprotein; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..623
FT /note="Vacuolar-sorting receptor 1"
FT /id="PRO_0000036462"
FT TOPO_DOM 23..565
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..623
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 51..163
FT /note="PA"
FT DOMAIN 411..461
FT /note="EGF-like 1"
FT DOMAIN 464..511
FT /note="EGF-like 2"
FT DOMAIN 512..554
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255"
FT MOTIF 606..609
FT /note="Tyrosine-based internalization motif"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 415..433
FT /evidence="ECO:0000250"
FT DISULFID 422..442
FT /evidence="ECO:0000250"
FT DISULFID 444..460
FT /evidence="ECO:0000250"
FT DISULFID 468..488
FT /evidence="ECO:0000250"
FT DISULFID 475..496
FT /evidence="ECO:0000250"
FT DISULFID 498..510
FT /evidence="ECO:0000250"
FT DISULFID 540..553
FT /evidence="ECO:0000250"
FT CONFLICT 169
FT /note="V -> G (in Ref. 6; AAK82551)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="T -> A (in Ref. 2; AAB72111)"
FT /evidence="ECO:0000305"
FT STRAND 21..33
FT /evidence="ECO:0007829|PDB:4TJV"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:4TJV"
FT STRAND 38..49
FT /evidence="ECO:0007829|PDB:4TJV"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:4TJV"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:4TJV"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:4TJV"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:4TJV"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:4TJV"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:4TJV"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:4TJV"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:4TJV"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:4TJV"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:4TJV"
FT HELIX 153..164
FT /evidence="ECO:0007829|PDB:4TJV"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:4TJV"
SQ SEQUENCE 623 AA; 68992 MW; 5410A089BA1E58FA CRC64;
MKLGLFTLSF LLILNLAMGR FVVEKNNLKV TSPDSIKGIY ECAIGNFGVP QYGGTLVGTV
VYPKSNQKAC KSYSDFDISF KSKPGRLPTF VLIDRGDCYF TLKAWIAQQA GAAAILVADS
KAEPLITMDT PEEDKSDADY LQNITIPSAL ITKTLGDSIK SALSGGDMVN MKLDWTESVP
HPDERVEYEL WTNSNDECGK KCDTQIEFLK NFKGAAQILE KGGHTQFTPH YITWYCPEAF
TLSKQCKSQC INHGRYCAPD PEQDFTKGYD GKDVVVQNLR QACVYRVMND TGKPWVWWDY
VTDFAIRCPM KEKKYTKECA DGIIKSLGID LKKVDKCIGD PEADVENPVL KAEQESQIGK
GSRGDVTILP TLVVNNRQYR GKLEKGAVLK AMCSGFQEST EPAICLTEDL ETNECLENNG
GCWQDKAANI TACRDTFRGR LCECPTVQGV KFVGDGYTHC KASGALHCGI NNGGCWRESR
GGFTYSACVD DHSKDCKCPL GFKGDGVKNC EDVDECKEKT VCQCPECKCK NTWGSYECSC
SNGLLYMREH DTCIGSGKVG TTKLSWSFLW ILIIGVGVAG LSGYAVYKYR IRSYMDAEIR
GIMAQYMPLE SQPPNTSGHH MDI
