VSR6_ARATH
ID VSR6_ARATH Reviewed; 631 AA.
AC Q9FYH7; F4I7T2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Vacuolar-sorting receptor 6;
DE Short=AtVSR6;
DE AltName: Full=BP80-like protein d;
DE Short=AtBP80d;
DE AltName: Full=Epidermal growth factor receptor-like protein 6;
DE Short=AtELP6;
DE Flags: Precursor;
GN Name=VSR6; Synonyms=BP80D, ELP6; OrderedLocusNames=At1g30900;
GN ORFNames=F17F8.23;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 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 [4]
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 BP80E.
CC {ECO:0000305|PubMed:12493849}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF98196.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC000107; AAF98196.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31291.1; -; Genomic_DNA.
DR PIR; G86434; G86434.
DR RefSeq; NP_174375.1; NM_102827.2.
DR AlphaFoldDB; Q9FYH7; -.
DR SMR; Q9FYH7; -.
DR STRING; 3702.AT1G30900.1; -.
DR PaxDb; Q9FYH7; -.
DR PRIDE; Q9FYH7; -.
DR ProteomicsDB; 242323; -.
DR EnsemblPlants; AT1G30900.1; AT1G30900.1; AT1G30900.
DR GeneID; 839974; -.
DR Gramene; AT1G30900.1; AT1G30900.1; AT1G30900.
DR KEGG; ath:AT1G30900; -.
DR Araport; AT1G30900; -.
DR TAIR; locus:2015726; AT1G30900.
DR eggNOG; ENOG502QQUF; Eukaryota.
DR HOGENOM; CLU_031082_1_0_1; -.
DR InParanoid; Q9FYH7; -.
DR OMA; VPAMGRF; -.
DR OrthoDB; 1428226at2759; -.
DR PRO; PR:Q9FYH7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FYH7; baseline and differential.
DR Genevisible; Q9FYH7; 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..631
FT /note="Vacuolar-sorting receptor 6"
FT /id="PRO_0000036468"
FT TOPO_DOM 26..563
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585..631
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 57..165
FT /note="PA"
FT DOMAIN 413..463
FT /note="EGF-like 1"
FT DOMAIN 494..540
FT /note="EGF-like 2"
FT REGION 610..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 604..607
FT /note="Tyrosine-based internalization motif"
FT /evidence="ECO:0000250"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 417..435
FT /evidence="ECO:0000250"
FT DISULFID 424..444
FT /evidence="ECO:0000250"
FT DISULFID 446..462
FT /evidence="ECO:0000250"
FT DISULFID 498..511
FT /evidence="ECO:0000250"
FT DISULFID 530..539
FT /evidence="ECO:0000250"
SQ SEQUENCE 631 AA; 70258 MW; 6BC20BF63461327D CRC64;
MSLIHKGATL ALFLALTMVV NGVFGRFIVE KSSVTILNPL AMRSKHDAAI ANFGVPNYGG
YMIGSVVYAG QGAYGCDSFD KTFKPKFPRP TILIIDRGEC YFALKVWNGQ QSGVAAVLVA
DNVDEPLITM DSPEESKEAD DFIEKLNIPS ALIDFSFANT LKQALKKGEE VVLKIDWSES
LPHPDERVEY ELWTNTNDEC GARCDEQMNF VKNFKGHAQI LEKGGYSLFT PHYITWFCPK
DYVSSNQCKS QCINQGRYCA PDPEQDFGDG YDGKDIVFEN LRQLCVHKVA KENNRSWVWW
DYVTDFHIRC SMKEKKYSKE CAERVVESLG LPLDKIKKCI GDPDANVENE VLKAEQALQV
GQGDRGDVTI LPTLIVNNAQ YRGKLERNAV LKAICSGFKE RTEPGICLSG DIETNECLEA
NGGCWEDKKS NVTACKDTFR GRVCECPVVN GVQYKGDGYT SCEPYGPARC SINQGGCWSE
TKKGLTFSAC SNLETSGCRC PPGFKGDGLK CEDIDECKEQ SACQCDGCNC KNKWGGFECK
CSGNRLYMKE QDTCIERSGS RIGWFPTFVI LAAVASICVG GYVFYKYRLR SYMDSEIMAI
MSQYMPLESQ NTTDPMTGES QHQQLRLTSA A
