VSR1_PEA
ID VSR1_PEA Reviewed; 623 AA.
AC P93484;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Vacuolar-sorting receptor 1;
DE AltName: Full=80 kDa proaleurein-binding protein;
DE AltName: Full=BP-80;
DE Flags: Precursor;
GN Name=BP80;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-41; 178-197 AND 394-417,
RP FUNCTION, SUBCELLULAR LOCATION, AND VARIANT LEU-25.
RC TISSUE=Seed;
RX PubMed=9306690; DOI=10.1104/pp.115.1.29;
RA Paris N., Rogers S.W., Jiang L., Kirsch T., Beevers L., Phillips T.E.,
RA Rogers J.C.;
RT "Molecular cloning and further characterization of a probable plant
RT vacuolar sorting receptor.";
RL Plant Physiol. 115:29-39(1997).
RN [2]
RP INTERACTION WITH ALEUREIN, TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=8159760; DOI=10.1073/pnas.91.8.3403;
RA Kirsch T., Paris N., Butler J.M., Beevers L., Rogers J.C.;
RT "Purification and initial characterization of a potential plant vacuolar
RT targeting receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3403-3407(1994).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=10449584; DOI=10.2307/3870979;
RA Hinz G., Hillmer S., Baeumer M., Hohl I.;
RT "Vacuolar storage proteins and the putative vacuolar sorting receptor BP-80
RT exit the Golgi apparatus of developing pea cotyledons in different
RT transport vesicles.";
RL Plant Cell 11:1509-1524(1999).
RN [4]
RP FUNCTION.
RX PubMed=10760239; DOI=10.2307/3871064;
RA Cao X., Rogers S.W., Butler J., Beevers L., Rogers J.C.;
RT "Structural requirements for ligand binding by a probable plant vacuolar
RT sorting receptor.";
RL Plant Cell 12:493-506(2000).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11149919; DOI=10.1083/jcb.152.1.41;
RA Hillmer S., Movafeghi A., Robinson D.G., Hinz G.;
RT "Vacuolar storage proteins are sorted in the cis-cisternae of the pea
RT cotyledon Golgi apparatus.";
RL J. Cell Biol. 152:41-50(2001).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=12154135; DOI=10.1093/pcp/pcf085;
RA Li Y.-B., Rogers S.W., Tse Y.C., Lo S.W., Sun S.S.M., Jauh G.-Y., Jiang L.;
RT "BP-80 and homologs are concentrated on post-Golgi, probable lytic
RT prevacuolar compartments.";
RL Plant Cell Physiol. 43:726-742(2002).
CC -!- FUNCTION: Vacuolar-sorting receptor (VSR) involved in clathrin-coated
CC vesicles sorting from Golgi apparatus to vacuoles. Seems to binds
CC preferentially proteins containing a N-terminal NPIR motif.
CC {ECO:0000269|PubMed:10760239, ECO:0000269|PubMed:9306690}.
CC -!- SUBUNIT: Interacts with the N-terminal propeptide of aleurein
CC (proaleurein). {ECO:0000269|PubMed:8159760}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Golgi apparatus membrane; Single-pass type I membrane protein.
CC Cytoplasmic vesicle, clathrin-coated vesicle membrane; Single-pass type
CC I membrane protein. Prevacuolar compartment membrane; Single-pass type
CC I membrane protein. Note=Associated to the Golgi apparatus, mostly on
CC the trans-side, to clathrin-coated vesicles (CCVs) and to prevacuolar
CC compartments (PVCs). May also be associated with the plasma membrane.
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; U79958; AAB72110.1; -; mRNA.
DR PIR; T06794; T06794.
DR AlphaFoldDB; P93484; -.
DR SMR; P93484; -.
DR PRIDE; P93484; -.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Calcium; Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Glycoprotein; Golgi apparatus; Membrane;
KW Protein transport; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:9306690"
FT CHAIN 23..623
FT /note="Vacuolar-sorting receptor 1"
FT /id="PRO_0000036463"
FT TOPO_DOM 23..564
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..623
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 54..163
FT /note="PA"
FT DOMAIN 411..461
FT /note="EGF-like 1"
FT DOMAIN 464..511
FT /note="EGF-like 2"
FT DOMAIN 512..554
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 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 415..433
FT /evidence="ECO:0000250"
FT DISULFID 422..442
FT /evidence="ECO:0000250"
FT DISULFID 444..460
FT /evidence="ECO:0000250"
FT DISULFID 468..488
FT /evidence="ECO:0000250"
FT DISULFID 475..496
FT /evidence="ECO:0000250"
FT DISULFID 498..510
FT /evidence="ECO:0000250"
FT DISULFID 540..553
FT /evidence="ECO:0000250"
FT VARIANT 25
FT /note="V -> L"
FT /evidence="ECO:0000269|PubMed:9306690"
FT CONFLICT 191
FT /note="W -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="T -> Y (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 623 AA; 68896 MW; 10CC0895BD80B184 CRC64;
MKCWRLSAIL FLGFMLTSLS TARFVVEKNS LSVTSPEKIK GKHDSAIGNF GIPQYGGSMA
GNVVYPKDNS KGCKDFDSSF KSRPGALPTI LLLDRGSCFF ALKVWNAQKA GASAVLVADD
IEEPLITMDT PEEDVSSAKY IENITIPSAL IGKSFGEKLK DAISGGDMVN VNLDWREAVP
HPDDRVEYEL WTNSNDECGV KCDMLIEFLK DFKGAAQILE KGGYTQFTPH YITWYCPHAF
TLSKQCKSQC INHGRYCAPD PEQDFNTGYD GKDVVVENLR QLCVFKVAKE TEKSWVWWDY
VTDFQIRCPM KEKKYNKECA NSVIKSLGLD VEKIDKCMGD PNADTENSIL KEEQDAQIGK
GTRGDVTILP TLVVNNRQYR GKLEKGAVLK AICSGFEETT DPAVCLSNDV ETNECLTNNG
GCWQDKTANI AACKDTFRGR VCECPLVDGV QFKGDGYTTC EVSGHGRCKI NNGGCWHDAR
NGHAFSACLD DGGVKCQCPA GFKGDGVKNC EDIDECKDKK ACQCPECSCK NTWGSYNCSC
SGDLLYIKDQ DTCISKTASQ AKSTWAAFWV VLIALAMIAG GGFLVYKYRI RQYMDSEIRA
IMAQYMPLDS QEEGPNHVNH QRG
