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Database: UniProt
Entry: Q56ZQ3
LinkDB: Q56ZQ3
Original site: Q56ZQ3 
ID   VSR4_ARATH              Reviewed;         628 AA.
AC   Q56ZQ3; O80979;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   10-APR-2019, entry version 108.
DE   RecName: Full=Vacuolar-sorting receptor 4;
DE            Short=AtVSR4;
DE   AltName: Full=BP80-like protein a;
DE            Short=AtBP80a;
DE   AltName: Full=Epidermal growth factor receptor-like protein 2b;
DE            Short=AtELP2b;
DE   Flags: Precursor;
GN   Name=VSR4; Synonyms=BP80A, ELP2B; OrderedLocusNames=At2g14720;
GN   ORFNames=F26C24.14;
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=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 549-628.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   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
RT   beta-integrin domains.";
RL   Biochim. Biophys. Acta 1435:61-70(1999).
RN   [6]
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   [7]
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   [8]
RP   GENE FAMILY, AND 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 at low levels in seeds, seedlings,
CC       roots, stems, leaves, flowers and siliques.
CC       {ECO:0000269|PubMed:10561538, 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; AAC24185.1; -; Genomic_DNA.
DR   EMBL; AC005398; AAM15052.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06326.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06327.1; -; Genomic_DNA.
DR   EMBL; AY062744; AAL32822.1; -; mRNA.
DR   EMBL; BT008390; AAP37749.1; -; mRNA.
DR   EMBL; AK220910; BAD94353.1; -; mRNA.
DR   PIR; T02604; T02604.
DR   RefSeq; NP_179079.1; NM_127036.5.
DR   RefSeq; NP_849954.1; NM_179623.2.
DR   UniGene; At.22740; -.
DR   UniGene; At.75037; -.
DR   ProteinModelPortal; Q56ZQ3; -.
DR   SMR; Q56ZQ3; -.
DR   STRING; 3702.AT2G14720.2; -.
DR   PaxDb; Q56ZQ3; -.
DR   PRIDE; Q56ZQ3; -.
DR   EnsemblPlants; AT2G14720.1; AT2G14720.1; AT2G14720.
DR   EnsemblPlants; AT2G14720.2; AT2G14720.2; AT2G14720.
DR   GeneID; 815960; -.
DR   Gramene; AT2G14720.1; AT2G14720.1; AT2G14720.
DR   Gramene; AT2G14720.2; AT2G14720.2; AT2G14720.
DR   KEGG; ath:AT2G14720; -.
DR   Araport; AT2G14720; -.
DR   TAIR; locus:2046931; AT2G14720.
DR   eggNOG; ENOG410IFFK; Eukaryota.
DR   eggNOG; ENOG41105IF; LUCA.
DR   InParanoid; Q56ZQ3; -.
DR   OMA; HKQNHLL; -.
DR   OrthoDB; 1428226at2759; -.
DR   PhylomeDB; Q56ZQ3; -.
DR   PRO; PR:Q56ZQ3; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q56ZQ3; baseline and differential.
DR   Genevisible; Q56ZQ3; 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; IBA:GO_Central.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR   GO; GO:0005773; C:vacuole; 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; IGI: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 4.
FT                                /FTId=PRO_0000036466.
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;  69812 MW;  E8FD3D33194DCF0E CRC64;
     MKQLLCYLPW LLLLSLVVSP FNEARFVVEK 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 NKDCAESVIK SLGIDSRKID KCMGDPDADL DNPVLKEEQD
     AQVGKGTRGD VTILPTLVVN NRQYRGKLEK SAVLKALCSG FEESTEPAIC LSTDMETNEC
     LDNNGGCWQD KSANITACKD TFRGKVCVCP IVDGVRFKGD GYSHCEPSGP GRCTINNGGC
     WHEERDGHAF SACVDKDSVK CECPPGFKGD GVKKCEDINE CKEKKACQCP ECSCKNTWGS
     YECSCSGDLL YMRDHDTCIS KTGSQVKSAW AAVWLIMLSL GLAAAGAYLV YKYRLRQYMD
     SEIRAIMAQY MPLDSQPEVP NHTNDERA
//
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