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Database: UniProt
Entry: O80977
LinkDB: O80977
Original site: O80977 
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   16-JAN-2019, entry version 125.
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; 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   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.,
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   -!- 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
CC       in trafficking at the TGN. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the VSR (BP-80) family. {ECO:0000305}.
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   UniGene; At.40502; -.
DR   ProteinModelPortal; O80977; -.
DR   SMR; O80977; -.
DR   BioGrid; 1321; 1.
DR   STRING; 3702.AT2G14740.1; -.
DR   PaxDb; O80977; -.
DR   PRIDE; O80977; -.
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; ENOG410IFFK; Eukaryota.
DR   eggNOG; ENOG41105IF; LUCA.
DR   HOGENOM; HOG000241019; -.
DR   InParanoid; O80977; -.
DR   OMA; RAKPGAM; -.
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; IDA:TAIR.
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:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0005802; C:trans-Golgi network; 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; 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; IPR013032; EGF-like_CS.
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; Complete proteome; 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     24       {ECO:0000255}.
FT   CHAIN        25    628       Vacuolar-sorting receptor 3.
FT                                /FTId=PRO_0000036465.
FT   TOPO_DOM     25    569       Lumenal. {ECO:0000255}.
FT   TRANSMEM    570    590       Helical. {ECO:0000255}.
FT   TOPO_DOM    591    628       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       56    168       PA.
FT   DOMAIN      416    466       EGF-like 1.
FT   DOMAIN      469    516       EGF-like 2.
FT   DOMAIN      517    559       EGF-like 3; calcium-binding.
FT                                {ECO:0000255}.
FT   MOTIF       610    613       Tyrosine-based internalization motif.
FT                                {ECO:0000250}.
FT   CARBOHYD    148    148       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    294    294       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    434    434       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    420    438       {ECO:0000250}.
FT   DISULFID    427    447       {ECO:0000250}.
FT   DISULFID    449    465       {ECO:0000250}.
FT   DISULFID    473    493       {ECO:0000250}.
FT   DISULFID    480    501       {ECO:0000250}.
FT   DISULFID    503    515       {ECO:0000250}.
FT   DISULFID    545    558       {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
//
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