VSR3_ARATH
ID VSR3_ARATH Reviewed; 628 AA.
AC O80977;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Vacuolar-sorting receptor 3;
DE Short=AtVSR3;
DE AltName: Full=BP80-like protein a';
DE Short=AtBP80a';
DE AltName: Full=Epidermal growth factor receptor-like protein 2a;
DE Short=AtELP2a;
DE Flags: Precursor;
GN Name=VSR3; Synonyms=BP80A', ELP2A; OrderedLocusNames=At2g14740;
GN ORFNames=F26C24.12;
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 SUBCELLULAR LOCATION.
RX PubMed=11079568;
RX DOI=10.1002/1522-2683(20001001)21:16<3488::aid-elps3488>3.0.co;2-3;
RA Prime T.A., Sherrier D.J., Mahon P., Packman L.C., Dupree P.;
RT "A proteomic analysis of organelles from Arabidopsis thaliana.";
RL Electrophoresis 21:3488-3499(2000).
RN [4]
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 [5]
RP 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).
CC -!- FUNCTION: Vacuolar-sorting receptor (VSR) involved in clathrin-coated
CC vesicles sorting from Golgi apparatus to vacuoles. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}. Cytoplasmic vesicle,
CC clathrin-coated vesicle membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Prevacuolar compartment membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds, seedlings, roots, leaves,
CC flowers and siliques. {ECO:0000269|PubMed:12493849}.
CC -!- DOMAIN: The tyrosine-based internalization signal may be involved in
CC trafficking at the TGN. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VSR (BP-80) family. {ECO:0000305}.
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DR EMBL; AC004705; AAC24183.1; -; Genomic_DNA.
DR EMBL; AC005398; AAM15053.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06328.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06329.1; -; Genomic_DNA.
DR PIR; T02602; T02602.
DR RefSeq; NP_179081.1; NM_127038.2.
DR RefSeq; NP_849955.1; NM_179624.2.
DR AlphaFoldDB; O80977; -.
DR SMR; O80977; -.
DR BioGRID; 1321; 1.
DR STRING; 3702.AT2G14740.1; -.
DR PaxDb; O80977; -.
DR PRIDE; O80977; -.
DR ProteomicsDB; 242322; -.
DR EnsemblPlants; AT2G14740.1; AT2G14740.1; AT2G14740.
DR EnsemblPlants; AT2G14740.2; AT2G14740.2; AT2G14740.
DR GeneID; 815962; -.
DR Gramene; AT2G14740.1; AT2G14740.1; AT2G14740.
DR Gramene; AT2G14740.2; AT2G14740.2; AT2G14740.
DR KEGG; ath:AT2G14740; -.
DR Araport; AT2G14740; -.
DR TAIR; locus:2046911; AT2G14740.
DR eggNOG; ENOG502QSX2; Eukaryota.
DR HOGENOM; CLU_031082_1_0_1; -.
DR InParanoid; O80977; -.
DR OMA; GYTTCAA; -.
DR OrthoDB; 1428226at2759; -.
DR PhylomeDB; O80977; -.
DR PRO; PR:O80977; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80977; baseline and differential.
DR Genevisible; O80977; AT.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000137; C:Golgi cis cisterna; HDA: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:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; HDA: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; IBA:GO_Central.
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 InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR003137; PA_domain.
DR Pfam; PF12662; cEGF; 1.
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 2: Evidence at transcript level;
KW Calcium; Cytoplasmic vesicle; Disulfide bond; EGF-like domain;
KW Glycoprotein; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..628
FT /note="Vacuolar-sorting receptor 3"
FT /id="PRO_0000036465"
FT TOPO_DOM 25..569
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 591..628
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 56..168
FT /note="PA"
FT DOMAIN 416..466
FT /note="EGF-like 1"
FT DOMAIN 469..516
FT /note="EGF-like 2"
FT DOMAIN 517..559
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255"
FT MOTIF 610..613
FT /note="Tyrosine-based internalization motif"
FT /evidence="ECO:0000250"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 420..438
FT /evidence="ECO:0000250"
FT DISULFID 427..447
FT /evidence="ECO:0000250"
FT DISULFID 449..465
FT /evidence="ECO:0000250"
FT DISULFID 473..493
FT /evidence="ECO:0000250"
FT DISULFID 480..501
FT /evidence="ECO:0000250"
FT DISULFID 503..515
FT /evidence="ECO:0000250"
FT DISULFID 545..558
FT /evidence="ECO:0000250"
SQ SEQUENCE 628 AA; 69744 MW; 6862B7362E2779C3 CRC64;
MKQLLCYLPW LLLLTLLVSP LNDARFVVEK NSLSVTSPES IKGTHDSAIG NFGIPQYGGS
MAGTVVYPKE NQKSCKEFSD FSISFKSQPG ALPTFLLVDR GDCFFALKVW NAQKAGASAV
LVADNVDEPL ITMDTPEEDV SSAKYIENIT IPSALVTKGF GEKLKKAISG GDMVNLNLDW
REAVPHPDDR VEYELWTNSN DECGVKCDML MEFVKDFKGA AQILEKGGFT QFRPHYITWY
CPHAFTLSRQ CKSQCINKGR YCAPDPEQDF SSGYDGKDVV VENLRQLCVY KVANETGKPW
VWWDYVTDFQ IRCPMKEKKY NKECADSVIK SLGIDSKKLD KCMGDPDADL DNPVLKEEQD
AQVGKGSRGD VTILPTLVVN NRQYRGKLEK SAVLKALCSG FEETTEPAIC LSTDVESNEC
LDNNGGCWQD KSANITACKD TFRGRVCECP TVDGVQFKGD GYSHCEPSGP GRCTINNGGC
WHEERDGHAF SACVDKDSVK CECPPGFKGD GTKKCEDINE CKEKKACQCP ECSCKNTWGS
YECSCSGDLL YIRDHDTCIS KTGAQVRSAW AAVWLIMLSL GLAAAGAYLV YKYRLRQYMD
SEIRAIMAQY MPLDSQPEIP NHVNDERA
