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Database: UniProt
Entry: O22925
LinkDB: O22925
Original site: O22925 
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   16-JAN-2019, entry version 124.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   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-
CC       coated vesicles sorting from Golgi apparatus to vacuoles.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC       Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC       Prevacuolar compartment membrane {ECO:0000250}; Single-pass type I
CC       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
CC       in trafficking at the TGN. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the VSR (BP-80) family. {ECO:0000305}.
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   UniGene; At.52975; -.
DR   ProteinModelPortal; O22925; -.
DR   SMR; O22925; -.
DR   STRING; 3702.AT2G30290.2; -.
DR   PaxDb; O22925; -.
DR   PRIDE; O22925; -.
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; ENOG410JXEQ; Eukaryota.
DR   eggNOG; ENOG411041H; LUCA.
DR   HOGENOM; HOG000241019; -.
DR   InParanoid; O22925; -.
DR   OMA; TVGWSFL; -.
DR   OrthoDB; 1428226at2759; -.
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:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
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; Complete proteome; Cytoplasmic vesicle;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Golgi apparatus;
KW   Membrane; Protein transport; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    625       Vacuolar-sorting receptor 2.
FT                                /FTId=PRO_0000036464.
FT   TOPO_DOM     20    567       Lumenal. {ECO:0000255}.
FT   TRANSMEM    568    588       Helical. {ECO:0000255}.
FT   TOPO_DOM    589    625       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       55    167       PA.
FT   DOMAIN      415    465       EGF-like 1.
FT   DOMAIN      468    515       EGF-like 2.
FT   DOMAIN      516    558       EGF-like 3; calcium-binding.
FT                                {ECO:0000255}.
FT   MOTIF       608    611       Tyrosine-based internalization motif.
FT                                {ECO:0000250}.
FT   CARBOHYD    147    147       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    293    293       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    433    433       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    419    437       {ECO:0000250}.
FT   DISULFID    426    446       {ECO:0000250}.
FT   DISULFID    448    464       {ECO:0000250}.
FT   DISULFID    472    492       {ECO:0000250}.
FT   DISULFID    479    500       {ECO:0000250}.
FT   DISULFID    502    514       {ECO:0000250}.
FT   DISULFID    544    557       {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
//
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