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VSR4_ARATH
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   25-MAY-2022, entry version 121.
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; 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=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   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., Hayashizaki Y.,
RA   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 beta-
RT   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., 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 at low levels in seeds, seedlings, roots,
CC       stems, leaves, flowers and siliques. {ECO:0000269|PubMed:10561538,
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; 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   AlphaFoldDB; Q56ZQ3; -.
DR   SMR; Q56ZQ3; -.
DR   STRING; 3702.AT2G14720.2; -.
DR   PaxDb; Q56ZQ3; -.
DR   PRIDE; Q56ZQ3; -.
DR   ProteomicsDB; 242742; -.
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; ENOG502QSX2; Eukaryota.
DR   HOGENOM; CLU_031082_1_0_1; -.
DR   InParanoid; Q56ZQ3; -.
DR   OMA; GINSCDD; -.
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; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; 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:0000325; C:plant-type vacuole; 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; 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; 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 4"
FT                   /id="PRO_0000036466"
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;  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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