PKR1_YEAST
ID PKR1_YEAST Reviewed; 122 AA.
AC Q03880; D6VZU6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=V-type ATPase assembly factor PKR1;
GN Name=PKR1; OrderedLocusNames=YMR123W; ORFNames=YM8564.05;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16926153; DOI=10.1074/jbc.m606451200;
RA Davis-Kaplan S.R., Compton M.A., Flannery A.R., Ward D.M., Kaplan J.,
RA Stevens T.H., Graham L.A.;
RT "PKR1 encodes an assembly factor for the yeast V-type ATPase.";
RL J. Biol. Chem. 281:32025-32035(2006).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Functions together with the other V-type ATPase assembly
CC factors in the endoplasmic reticulum to efficiently assemble the V-type
CC ATPase membrane sector V(0). {ECO:0000269|PubMed:16926153}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16926153}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16926153}.
CC -!- MISCELLANEOUS: Present with 5750 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PKR1 family. {ECO:0000305}.
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DR EMBL; Z49273; CAA89272.1; -; Genomic_DNA.
DR EMBL; AY558408; AAS56734.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10020.1; -; Genomic_DNA.
DR PIR; S54492; S54492.
DR RefSeq; NP_013842.1; NM_001182624.1.
DR AlphaFoldDB; Q03880; -.
DR BioGRID; 35300; 477.
DR DIP; DIP-4436N; -.
DR IntAct; Q03880; 5.
DR MINT; Q03880; -.
DR STRING; 4932.YMR123W; -.
DR PaxDb; Q03880; -.
DR PRIDE; Q03880; -.
DR TopDownProteomics; Q03880; -.
DR EnsemblFungi; YMR123W_mRNA; YMR123W; YMR123W.
DR GeneID; 855153; -.
DR KEGG; sce:YMR123W; -.
DR SGD; S000004730; PKR1.
DR VEuPathDB; FungiDB:YMR123W; -.
DR eggNOG; ENOG502S6V3; Eukaryota.
DR HOGENOM; CLU_068499_1_0_1; -.
DR InParanoid; Q03880; -.
DR OMA; LWESIFV; -.
DR BioCyc; YEAST:G3O-32816-MON; -.
DR PRO; PR:Q03880; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03880; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IMP:SGD.
DR InterPro; IPR013945; Pkr1.
DR PANTHER; PTHR28251; PTHR28251; 1.
DR Pfam; PF08636; Pkr1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..122
FT /note="V-type ATPase assembly factor PKR1"
FT /id="PRO_0000203297"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..46
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 82..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 122 AA; 13962 MW; 5CAA6929D55F2C40 CRC64;
MANFFVRLWE SVFEPGTSPQ LIIATHVSFV ALLLTLIWLI YATNGNIHFY ALFCISLLLW
ITVIWFINEL SHVKLKDNDE LDKDANKKDD SAIKEDSEDK QESGKSTSTA RRTQAQSRSR
KA
