VPS70_YEAST
ID VPS70_YEAST Reviewed; 811 AA.
AC P47161; D6VWU5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Vacuolar protein sorting-associated protein 70;
DE EC=3.4.-.-;
GN Name=VPS70; OrderedLocusNames=YJR126C; ORFNames=J2050;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=12134085; DOI=10.1091/mbc.02-01-0005;
RA Bonangelino C.J., Chavez E.M., Bonifacino J.S.;
RT "Genomic screen for vacuolar protein sorting genes in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 13:2486-2501(2002).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Involved in vacuolar protein sorting.
CC {ECO:0000269|PubMed:12134085}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 112 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
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DR EMBL; Z49626; CAA89657.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08911.1; -; Genomic_DNA.
DR PIR; S57149; S57149.
DR RefSeq; NP_012660.1; NM_001181784.1.
DR AlphaFoldDB; P47161; -.
DR SMR; P47161; -.
DR BioGRID; 33882; 67.
DR DIP; DIP-4989N; -.
DR IntAct; P47161; 1.
DR STRING; 4932.YJR126C; -.
DR MaxQB; P47161; -.
DR PaxDb; P47161; -.
DR PRIDE; P47161; -.
DR EnsemblFungi; YJR126C_mRNA; YJR126C; YJR126C.
DR GeneID; 853590; -.
DR KEGG; sce:YJR126C; -.
DR SGD; S000003887; VPS70.
DR VEuPathDB; FungiDB:YJR126C; -.
DR eggNOG; KOG2195; Eukaryota.
DR GeneTree; ENSGT01030000234598; -.
DR HOGENOM; CLU_005688_2_0_1; -.
DR InParanoid; P47161; -.
DR OMA; QGSTEWV; -.
DR BioCyc; YEAST:G3O-31747-MON; -.
DR Reactome; R-SCE-8963693; Aspartate and asparagine metabolism.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR Reactome; R-SCE-9013026; RHOB GTPase cycle.
DR Reactome; R-SCE-9013106; RHOC GTPase cycle.
DR Reactome; R-SCE-9696273; RND1 GTPase cycle.
DR PRO; PR:P47161; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47161; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006623; P:protein targeting to vacuole; HMP:SGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.930.40; -; 1.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR InterPro; IPR034308; VPS70.
DR PANTHER; PTHR10404; PTHR10404; 1.
DR PANTHER; PTHR10404:SF46; PTHR10404:SF46; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF47672; SSF47672; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Zinc.
FT CHAIN 1..811
FT /note="Vacuolar protein sorting-associated protein 70"
FT /id="PRO_0000174138"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 522
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 607
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 811 AA; 92018 MW; 932818225880E49B CRC64;
MRMIQRERKR EKEEGQLKER TVVNMADPDD NEAEATGLQQ YSGETTRDDN EESMNDSFTL
TSRNRGRSNT ISSIVSGYEI MKEHMDKEKF MYLILASLLL YMGFVAAFAP RTSLSRDFRR
FHSSRLTNAE VYRIYLNSLQ QENRAKEHVY KYAGYMSNGA SDSSTFKYTL DEFLDMGYKP
KVEKYYPWIG EPVDTNVAPL ENGKVVYEAS MIEDRVKGDP ASHARKRQKG FHQYSKNGSV
TARYVFCNYG SISDYKLLLK KNIDIEDKIH IVRSGKILPG LKVKNAELYG ASSVIIYTDP
FDDGKVTEEN GFLHYPYGPA RNPSYIRRDS VNYFSDTPGD PTTPGYPSKD SDTEHMSPVG
RVPRIPSVPM SARDVQPILE RLNGRGFQIG PGSNIKDFGS FTGPSSSIDK VHLHNELTYN
IKEMSSVEVS IPGIFTEGEI IIGAHRDSLA SSSAGDANSG SAILLEIARG MSKLLKHGWK
PLRPIKLISW DGERSGLLGS TDYAEAHAAI LRRRALVYLN LDNAISGTNF HCKANPLLQD
VIYEAAKLTE FNGHEDWSLF DHWKYTSNAT ISLLDGLSSY TSFQYHLGVP AAHFQFNAND
TSGAVYHSNS VFDSPTWLEK FTNSDYKLHN TMAMFVGLTT LMLSENELAR FNTHVYLKKI
YNWYIAWHSN LSSAFPQDDE VNSLAKRVLD LLKVATQEDS IQFDQQNGIL YKECREALPV
WAFYKKIKSY IKLQRSNSKS KQIDQLFITH RGLKDREWMK YSLLAPSKFE GSVGEVLPGL
HEGLADIDRN EVIQWLTILL SQFSNVRYLL Q
