VSR2_ARATH
ID VSR2_ARATH Reviewed; 625 AA.
AC O22925; Q1PEY7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Vacuolar-sorting receptor 2;
DE Short=AtVSR2;
DE AltName: Full=BP80-like protein c;
DE Short=AtBP80c;
DE AltName: Full=Epidermal growth factor receptor-like protein 4;
DE Short=AtELP4;
DE Flags: Precursor;
GN Name=VSR2; Synonyms=BP80C, ELP4; OrderedLocusNames=At2g30290;
GN ORFNames=T9D9.10;
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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O22925-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed only in flowers.
CC {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; AC002338; AAC16948.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08366.1; -; Genomic_DNA.
DR EMBL; DQ446580; ABE65874.1; -; mRNA.
DR PIR; F84706; F84706.
DR RefSeq; NP_180588.1; NM_128582.2. [O22925-1]
DR AlphaFoldDB; O22925; -.
DR SMR; O22925; -.
DR STRING; 3702.AT2G30290.2; -.
DR PaxDb; O22925; -.
DR PRIDE; O22925; -.
DR ProteomicsDB; 242633; -. [O22925-1]
DR EnsemblPlants; AT2G30290.1; AT2G30290.1; AT2G30290. [O22925-1]
DR GeneID; 817579; -.
DR Gramene; AT2G30290.1; AT2G30290.1; AT2G30290. [O22925-1]
DR KEGG; ath:AT2G30290; -.
DR Araport; AT2G30290; -.
DR eggNOG; ENOG502QSX2; Eukaryota.
DR HOGENOM; CLU_031082_1_0_1; -.
DR InParanoid; O22925; -.
DR OMA; KGFDEFD; -.
DR PhylomeDB; O22925; -.
DR PRO; PR:O22925; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22925; baseline and differential.
DR Genevisible; O22925; AT.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
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:0005802; C:trans-Golgi network; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..625
FT /note="Vacuolar-sorting receptor 2"
FT /id="PRO_0000036464"
FT TOPO_DOM 20..567
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..588
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 589..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 55..167
FT /note="PA"
FT DOMAIN 415..465
FT /note="EGF-like 1"
FT DOMAIN 468..515
FT /note="EGF-like 2"
FT DOMAIN 516..558
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255"
FT MOTIF 608..611
FT /note="Tyrosine-based internalization motif"
FT /evidence="ECO:0000250"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 419..437
FT /evidence="ECO:0000250"
FT DISULFID 426..446
FT /evidence="ECO:0000250"
FT DISULFID 448..464
FT /evidence="ECO:0000250"
FT DISULFID 472..492
FT /evidence="ECO:0000250"
FT DISULFID 479..500
FT /evidence="ECO:0000250"
FT DISULFID 502..514
FT /evidence="ECO:0000250"
FT DISULFID 544..557
FT /evidence="ECO:0000250"
SQ SEQUENCE 625 AA; 69875 MW; 008F9E254ADDCE5C CRC64;
MRTTNVWLVV IVWVTVGWSS CTGRFVVEKN NLRVTSPESI RGVYECALGN FGVPQYGGSM
SGAVVYPKTN QKACKNFDDF EISFRSRVAG LPTFVLVDRG DCYFTLKAWN AQRAGAATIL
VADNRPEQLI TMDAPEDETS DADYLQNITI PSALVSRSLG SAIKTAIAHG DPVHISLDWR
EALPHPNDRV AYELWTNSND ECGSKCDAQI RFLKRFKGAA QILEKGGYTR FTPHYITWYC
PEAFLASRQC KTQCINGGRY CAPDPEQDFS RGYNGKDVII QNLRQACFFR VTNESGKPWL
WWDYVTDFAI RCPMKEEKYN KKCADQVIQS LGVDVKKIDK CIGDIDANAE NPVLKEEQVA
QVGKGSRGDV TILPTIVINN RQYRGKLQRS AVLKALCSGF RETTEPPICL TEDIETNECL
QNNGGCWEDK TTNITACRDT FRGRVCQCPI VQGVKFLGDG YTHCEASGAL RCGINNGGCW
KQTQMGKTYS ACRDDHSKGC KCPPGFIGDG LKECKDVNEC EEKTACQCRD CKCKNTWGSY
ECSCSGSLLY IREHDICINR DARGDFSWGV IWIIIMGLGA AALGAYTVYK YRIRTYMDSE
IRAIMAQYMP LDNNPNTQLS SQLEL
