VSR5_ARATH
ID VSR5_ARATH Reviewed; 618 AA.
AC O64758;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Vacuolar-sorting receptor 5;
DE Short=AtVSR5;
DE AltName: Full=BP80-like protein e;
DE Short=AtBP80e;
DE AltName: Full=Epidermal growth factor receptor-like protein 5;
DE Short=AtELP5;
DE Flags: Precursor;
GN Name=VSR5; Synonyms=BP80E, ELP5; OrderedLocusNames=At2g34940;
GN ORFNames=F19I3.17;
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 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 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 in seedlings, roots, leaves, flowers and
CC siliques. {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 -!- CAUTION: Was originally erroneously termed BP80D.
CC {ECO:0000305|PubMed:12493849}.
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; AC004238; AAC12834.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09042.1; -; Genomic_DNA.
DR EMBL; BT004565; AAO42811.1; -; mRNA.
DR PIR; T00476; T00476.
DR RefSeq; NP_181040.1; NM_129047.4.
DR AlphaFoldDB; O64758; -.
DR SMR; O64758; -.
DR BioGRID; 3405; 2.
DR STRING; 3702.AT2G34940.1; -.
DR iPTMnet; O64758; -.
DR PaxDb; O64758; -.
DR PRIDE; O64758; -.
DR ProteomicsDB; 242754; -.
DR EnsemblPlants; AT2G34940.1; AT2G34940.1; AT2G34940.
DR GeneID; 818059; -.
DR Gramene; AT2G34940.1; AT2G34940.1; AT2G34940.
DR KEGG; ath:AT2G34940; -.
DR Araport; AT2G34940; -.
DR TAIR; locus:2044782; AT2G34940.
DR eggNOG; ENOG502QQUF; Eukaryota.
DR HOGENOM; CLU_031082_1_0_1; -.
DR InParanoid; O64758; -.
DR OMA; DCKCKNN; -.
DR OrthoDB; 1428226at2759; -.
DR PhylomeDB; O64758; -.
DR PRO; PR:O64758; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64758; baseline and differential.
DR Genevisible; O64758; 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: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 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..618
FT /note="Vacuolar-sorting receptor 5"
FT /id="PRO_0000036467"
FT TOPO_DOM 24..563
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585..618
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 58..164
FT /note="PA"
FT DOMAIN 412..462
FT /note="EGF-like 1"
FT DOMAIN 465..511
FT /note="EGF-like 2"
FT DOMAIN 512..554
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255"
FT MOTIF 604..607
FT /note="Tyrosine-based internalization motif"
FT /evidence="ECO:0000250"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 416..434
FT /evidence="ECO:0000250"
FT DISULFID 423..443
FT /evidence="ECO:0000250"
FT DISULFID 445..461
FT /evidence="ECO:0000250"
FT DISULFID 469..489
FT /evidence="ECO:0000250"
FT DISULFID 476..497
FT /evidence="ECO:0000250"
FT DISULFID 499..510
FT /evidence="ECO:0000250"
FT DISULFID 540..553
FT /evidence="ECO:0000250"
SQ SEQUENCE 618 AA; 69257 MW; 8143C14A37A5A4CE CRC64;
MSPSNKGTVL ALILALTMVV VNGFSSRFFV EKSSLTVLNS WEMGAKHDAA IANFGLPKYG
GFMIGSVVYA GQDAYGCNSF NKTFNTKSPY PKILLIDRGV CNFALKIWNG QQSGAAAVLL
ADNIVEPLIT MDTPQDEDPD FIDKVKIPSA LILRSFGDSL KKALKRGEEV ILKMDWSESI
PNPDERVEYE LWANTNDECG VHCDKQIDFI KNFKGMAQIL EKGGYTLFRP HYISWVCPKE
LLLSKQCRTQ CINQGRYCAL DTKQEFEDGY NGKDVVYENL RQLCVHKVAK EKNTSWVWWD
YVTDFNIRCS MKEKKYSREC AETIVESLGL SLEKIKKCIG DPDADVENEV LKAEEAFQLG
QENRGIVTIF PTLMINNAQY RGKLERTAVL KAICSGFKER TEPSICLNSD IETNECLIEN
GGCWQDKRSN VTACKDTFRG RVCECPVVDG VQYKGDGYTS CKPYGPARCS MNNGDCWSET
RKGLTFSSCS DSETSGCRCP LGFLGDGLKC EDIDECKEKS ACKCDGCKCK NNWGGYECKC
SNNSIYMKEE DTCIERRSGS RSRGLFTIVV LTAIAGISLG AYIFYKYHLQ SYMDSEIVSI
MSQYIPLDSQ SINQDSFK
