VSR7_ARATH
ID VSR7_ARATH Reviewed; 625 AA.
AC Q8L7E3; O49438;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Vacuolar-sorting receptor 7;
DE Short=AtVSR7;
DE AltName: Full=BP80-like protein f;
DE Short=AtBP80f;
DE AltName: Full=Epidermal growth factor receptor-like protein 3;
DE Short=AtELP3;
DE Flags: Precursor;
GN Name=VSR7; Synonyms=BP80F, ELP3; OrderedLocusNames=At4g20110;
GN ORFNames=F18F4.210;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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 [5]
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 [6]
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: Golgi apparatus membrane {ECO:0000305}.
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=Q8L7E3-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in seedlings, roots, young
CC 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16619.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79011.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL021637; CAA16619.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161552; CAB79011.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84276.1; -; Genomic_DNA.
DR EMBL; AY136303; AAM96969.1; -; mRNA.
DR EMBL; BT000395; AAN15714.1; -; mRNA.
DR PIR; T04895; T04895.
DR RefSeq; NP_193744.1; NM_118130.4. [Q8L7E3-1]
DR AlphaFoldDB; Q8L7E3; -.
DR SMR; Q8L7E3; -.
DR STRING; 3702.AT4G20110.2; -.
DR PaxDb; Q8L7E3; -.
DR PRIDE; Q8L7E3; -.
DR ProteomicsDB; 242324; -. [Q8L7E3-1]
DR EnsemblPlants; AT4G20110.1; AT4G20110.1; AT4G20110. [Q8L7E3-1]
DR GeneID; 827757; -.
DR Gramene; AT4G20110.1; AT4G20110.1; AT4G20110. [Q8L7E3-1]
DR KEGG; ath:AT4G20110; -.
DR Araport; AT4G20110; -.
DR eggNOG; ENOG502QQUF; Eukaryota.
DR HOGENOM; CLU_031082_1_0_1; -.
DR InParanoid; Q8L7E3; -.
DR PhylomeDB; Q8L7E3; -.
DR PRO; PR:Q8L7E3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L7E3; baseline and differential.
DR Genevisible; Q8L7E3; AT.
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; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01187; EGF_CA; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..625
FT /note="Vacuolar-sorting receptor 7"
FT /id="PRO_0000036469"
FT TOPO_DOM 27..564
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 58..166
FT /note="PA"
FT DOMAIN 414..464
FT /note="EGF-like 1"
FT DOMAIN 467..513
FT /note="EGF-like 2"
FT DOMAIN 514..556
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255"
FT MOTIF 605..608
FT /note="Tyrosine-based internalization motif"
FT /evidence="ECO:0000250"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 418..436
FT /evidence="ECO:0000250"
FT DISULFID 425..445
FT /evidence="ECO:0000250"
FT DISULFID 447..463
FT /evidence="ECO:0000250"
FT DISULFID 471..491
FT /evidence="ECO:0000250"
FT DISULFID 478..499
FT /evidence="ECO:0000250"
FT DISULFID 501..512
FT /evidence="ECO:0000250"
FT DISULFID 542..555
FT /evidence="ECO:0000250"
FT CONFLICT 134
FT /note="P -> T (in Ref. 3; AAM96969/AAN15714)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="Y -> D (in Ref. 3; AAM96969/AAN15714)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 69800 MW; 962A2B3C7EE70DEA CRC64;
MGLVNGRASL TFLLAALTII AMVVEARFVV EKESISVLNP EEMRSKHDGS IANFGLPDYG
GFLIGSVVYP DSKTDGCSAF GKTFKPKFPR PTILLLDRGG CYFALKAWHA QQAGAAAVLV
ADNVDEPLLT MDSPEESKDA DGFIEKLTIP SVLIDKSFGD DLRQGFQKGK NIVIKLDWRE
SVPHPDKRVE YELWTNSNDE CGARCDEQMD FVKNFKGHAQ ILEKGGYTAF TPHYITWFCP
FQFINSPHCK SQCINHGRYC APDPEDNFRE GYEGKDVVLE NLRQLCVHRV ANESSRPWVW
WDYVTDFHSR CSMKEKKYSI DCAESVIKSL NLPIEKIKKC IGDPEADTEN QVLRTEQVSQ
IGRGNRGDVT ILPTLVINNA QYRGRLERTA VLKAICAGFN ETSEPAICLN TGLETNECLE
NNGGCWQDTK ANITACQDTF RGRLCECPVV KGVQYKGDGY TSCTPYGPAR CTMNNGGCWS
DTRNGLTFSA CSDSVSTGCK CPEGFQGDGL TCEDINECKE RSVCQCSGCR CKNSWGGYKC
SCSGDRLYIN DQDTCIERYG SKTAWWLTFL ILAIVAVAGL AGYIFYKYRF RSYMDSEIMT
IMSQYMPLES QRAREVPSEA EPFTL
