PMR1/YGL167C Summary Help

Standard Name PMR1
Systematic Name YGL167C
Alias BSD1 1 , LDB1 2 , SSC1 3
Feature Type ORF, Verified
Description High affinity Ca2+/Mn2+ P-type ATPase; required for Ca2+ and Mn2+ transport into Golgi; involved in Ca2+ dependent protein sorting and processing; D53A mutant (Mn2+ transporting) is rapamycin sensitive, Q783A mutant (Ca2+ transporting) is rapamycin resistant; Mn2+ transport into Golgi lumen appears to be required for rapamycin sensitivity; mutations in human homolog ATP2C1 cause acantholytic skin condition Hailey-Hailey disease (4, 5, 6, 7, 8 and see Summary Paragraph)
Name Description Plasma Membrane ATPase Related
Chromosomal Location
ChrVII:190468 to 187616 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: -104 cM
Gene Ontology Annotations All PMR1 GO evidence and references
  View Computational GO annotations for PMR1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 2 genes
Classical genetics
reduction of function
Large-scale survey
935 total interaction(s) for 517 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 23
  • Affinity Capture-RNA: 1
  • Co-localization: 2
  • Co-purification: 1
  • PCA: 1

Genetic Interactions
  • Dosage Growth Defect: 1
  • Dosage Lethality: 14
  • Dosage Rescue: 9
  • Negative Genetic: 611
  • Phenotypic Enhancement: 13
  • Phenotypic Suppression: 78
  • Positive Genetic: 83
  • Synthetic Growth Defect: 66
  • Synthetic Lethality: 15
  • Synthetic Rescue: 17

Expression Summary
Length (a.a.) 950
Molecular Weight (Da) 104,570
Isoelectric Point (pI) 5.45
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVII:190468 to 187616 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: -104 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..2853 190468..187616 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | TCDB | UniProtKB
Primary SGDIDS000003135

PMR1 encodes the major Golgi membrane P-type ATPase ion pump responsible for transporting calcium [Ca(2+)] and manganese [Mn(2+)] ions into the Golgi apparatus (9, 10, 3, 11). Both ions are necessary for proper processing and trafficking of polypeptides through the secretory pathway, but each plays a distinct role. Ca(2+) is required to sustain protein sorting while Mn(2+) is required for protein glycosylation. In addition, Pmr1p provides a major route for cellular detoxification of Mn(2+). Excess levels of cytosolic Mn(2+) are transported into the Golgi and then exit the cell via secretory pathway vesicles (10, 12, 13 and references therein).

Two different regions in this protein have been demonstrated to play important roles in Pmr1p selectivity and function, an N-terminal EF hand-like motif is necessary for ion binding and transport activity in vitro. Single point mutations in this motif can change the affinity of the protein for Ca(2+), Mn(2+), or both. (14). Second, putative cation translocating regions have been localized to transmembrane helices 4 and 6. Specific mutations in these regions can also alter the ion selectivity of Pmr1p (10). A null mutation of the HUR1 gene, which overlaps PMR1, was reported to cause sensitivity to hydroxyurea (15); however, a precise deletion within PMR1 that does not include any of the HUR1 coding sequence confers hydroxyurea sensitivity (16).

Pmr1p is the prototype of a family of transporters known as SPCA (Secretory Pathway Ca2+-ATPases) with members found in fungi, C. elegans, D. melanogaster, and mammals (13 and refereneces therein). Defects in the human ortholog of PMR1, ATP2C1, are associated with Hailey-Hailey disease (aka benign familial pemphigus), a severe blistering skin disorder (reviewed in 17). Although hSPCA1 (the protein encoded by ATP2C1) and Pmr1p are only 49% homologous, when expressed in yeast, ATP2C1 fully complements the pmr1 mutant phenotype (18).

Last updated: 2006-11-21 Contact SGD

References cited on this page View Complete Literature Guide for PMR1
1) Lapinskas PJ, et al.  (1995) Mutations in PMR1 suppress oxidative damage in yeast cells lacking superoxide dismutase. Mol Cell Biol 15(3):1382-8
2) Olivero I, et al.  (2003) The ldb1 mutant of Saccharomyces cerevisiae is defective in Pmr1p, the yeast secretory pathway/Golgi Ca(2+)/Mn(2+)-ATPase. FEMS Microbiol Lett 219(1):137-42
3) Rudolph HK, et al.  (1989) The yeast secretory pathway is perturbed by mutations in PMR1, a member of a Ca2+ ATPase family. Cell 58(1):133-45
4) Vashist S, et al.  (2002) Two distinctly localized p-type ATPases collaborate to maintain organelle homeostasis required for glycoprotein processing and quality control. Mol Biol Cell 13(11):3955-66
5) Mandal D, et al.  (2003) Packing interactions between transmembrane helices alter ion selectivity of the yeast Golgi Ca2+/Mn2+-ATPase PMR1. J Biol Chem 278(37):35292-8
6) Kellermayer R, et al.  (2003) Extracellular Ca(2+) sensing contributes to excess Ca(2+) accumulation and vacuolar fragmentation in a pmr1Delta mutant of S. cerevisiae. J Cell Sci 116(Pt 8):1637-46
7) Marie Mauro T  (2004) Yeast researchers consider Hailey-Hailey disease. J Invest Dermatol 123(6):xxii-xxiii
8) Devasahayam G, et al.  (2007) Golgi Manganese Transport Is Required for Rapamycin Signaling in Saccharomyces cerevisiae. Genetics 177(1):231-8
9) Antebi A and Fink GR  (1992) The yeast Ca(2+)-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution. Mol Biol Cell 3(6):633-54
10) Mandal D, et al.  (2000) Manganese selectivity of pmr1, the yeast secretory pathway ion pump, is defined by residue gln783 in transmembrane segment 6. Residue Asp778 is essential for cation transport. J Biol Chem 275(31):23933-8
11) Sorin A, et al.  (1997) PMR1, a Ca2+-ATPase in yeast Golgi, has properties distinct from sarco/endoplasmic reticulum and plasma membrane calcium pumps. J Biol Chem 272(15):9895-901
12) Durr G, et al.  (1998) The medial-Golgi ion pump Pmr1 supplies the yeast secretory pathway with Ca2+ and Mn2+ required for glycosylation, sorting, and endoplasmic reticulum-associated protein degradation. Mol Biol Cell 9(5):1149-62
13) Culotta VC, et al.  (2005) Manganese transport and trafficking: lessons learned from Saccharomyces cerevisiae. Eukaryot Cell 4(7):1159-65
14) Wei Y, et al.  (1999) An N-terminal EF hand-like motif modulates ion transport by Pmr1, the yeast Golgi Ca(2+)/Mn(2+)-ATPase. Biochemistry 38(44):14534-41
15) Zewail A, et al.  (2003) Novel functions of the phosphatidylinositol metabolic pathway discovered by a chemical genomics screen with wortmannin. Proc Natl Acad Sci U S A 100(6):3345-50
16) Jordan PW, et al.  (2007) Novel roles for selected genes in meiotic DNA processing. PLoS Genet 3(12):e222
17) Kellermayer R  (2005) Hailey-Hailey disease as an orthodisease of PMR1 deficiency in Saccharomyces cerevisiae. FEBS Lett 579(10):2021-5
18) Ton VK, et al.  (2002) Functional expression in yeast of the human secretory pathway Ca(2+), Mn(2+)-ATPase defective in Hailey-Hailey disease. J Biol Chem 277(8):6422-7