PMR1/YGL167C Protein Information Help

Standard Name Pmr1p
Systematic Name Ygl167cp
Alias Bsd1p 1 , Ldb1p 2 , Ssc1p 3
ORF Classification 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; mutations in human homolog ATP2C1 cause acantholytic skin condition Hailey-Hailey disease (4, 5, 6, 7)
Name Description Plasma Membrane ATPase Related
Experimental Data
Molecules/cell 6900 8
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 950
Molecular Weight (Da) 104,570
Isoelectric Point (pI) 5.45

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Pmr1p (InterPro)
Transmembrane Domains There are 7 total predicted transmembrane domains (TMHMM)
Physical Interactions There are 25 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000126200 | P13586
MIPS: YGL167C
NCBI: 114301 | 1322768 | 172199 | 6321271 | 832923 | 971386 | NP_011348.1
GenBank/EMBL/DDBJ: DAA07946.1 | M25488 | X64319 | X85757 | Z72690
External Classifications EC: 3.6.3.8 [Calcium-transporting ATPase] TC: 3.A.3.2
Amino Acid Sequence (or in FASTA format)
 
       1  MSDNPFNASL LDEDSNRERE ILDATAEALS KPSPSLEYCT LSVDEALEKL
      51  DTDKNGGLRS SNEANNRRSL YGPNEITVED DESLFKKFLS NFIEDRMILL
     101  LIGSAVVSLF MGNIDDAVSI TLAIFIVVTV GFVQEYRSEK SLEALNKLVP
     151  AECHLMRCGQ ESHVLASTLV PGDLVHFRIG DRIPADIRII EAIDLSIDES
     201  NLTGENEPVH KTSQTIEKSS FNDQPNSIVP ISERSCIAYM GTLVKEGHGK
     251  GIVVGTGTNT SFGAVFEMMN NIEKPKTPLQ LTMDKLGKDL SLVSFIVIGM
     301  ICLVGIIQGR SWLEMFQISV SLAVAAIPEG LPIIVTVTLA LGVLRMAKRK
     351  AIVRRLPSVE TLGSVNVICS DKTGTLTSNH MTVSKLWCLD SMSNKLNVLS
     401  LDKNKKTKNS NGNLKNYLTE DVRETLTIGN LCNNASFSQE HAIFLGNPTD
     451  VALLEQLANF EMPDIRNTVQ KVQELPFNSK RKLMATKILN PVDNKCTVYV
     501  KGAFERILEY STSYLKSKGK KTEKLTEAQK ATINECANSM ASEGLRVFGF
     551  AKLTLSDSST PLTEDLIKDL TFTGLIGMND PPRPNVKFAI EQLLQGGVHI
     601  IMITGDSENT AVNIAKQIGI PVIDPKLSVL SGDKLDEMSD DQLANVIDHV
     651  NIFARATPEH KLNIVRALRK RGDVVAMTGD GVNDAPALKL SDIGVSMGRI
     701  GTDVAKEASD MVLTDDDFST ILTAIEEGKG IFNNIQNFLT FQLSTSVAAL
     751  SLVALSTAFK LPNPLNAMQI LWINILMDGP PAQSLGVEPV DHEVMKKPPR
     801  KRTDKILTHD VMKRLLTTAA CIIVGTVYIF VKEMAEDGKV TARDTTMTFT
     851  CFVFFDMFNA LACRHNTKSI FEIGFFTNKM FNYAVGLSLL GQMCAIYIPF
     901  FQSIFKTEKL GISDILLLLL ISSSVFIVDE LRKLWTRKKN EEDSTYFSNV
     951  *

external links for Pmr1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Aspergillus (AspGD) BioPIXIE MIPS YeastRC Public Image Repository
Candida (CGD) CYC2008 (complexes) Pfam domains
Candida (CandidaDB) Complexome TCDB
YGOB DIP YeastRC Structure Prediction (Seattle)
YOGY GeneMANIA

References cited on this page View Complete Literature Guide for Pmr1p
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) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41