PNT1_YEAST
ID PNT1_YEAST Reviewed; 423 AA.
AC P38969; D6W2W6; Q08730;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Pentamidine resistance factor, mitochondrial;
DE Flags: Precursor;
GN Name=PNT1; OrderedLocusNames=YOR266W;
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 [GENOMIC DNA].
RC STRAIN=S21R;
RX PubMed=7695273; DOI=10.1128/aac.38.12.2850;
RA Ludewig G., Staben C.;
RT "Characterization of the PNT1 pentamidine resistance gene of Saccharomyces
RT cerevisiae.";
RL Antimicrob. Agents Chemother. 38:2850-2856(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9153759;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<483::aid-yea105>3.0.co;2-u;
RA Poirey R., Jauniaux J.-C.;
RT "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals
RT 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1
RT and VPH1.";
RL Yeast 13:483-487(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
RX PubMed=7634332; DOI=10.1016/0092-8674(95)90431-x;
RA Archer J.E., Vega L.R., Solomon F.;
RT "Rbl2p, a yeast protein that binds to beta-tubulin and participates in
RT microtubule function in vivo.";
RL Cell 82:425-434(1995).
RN [7]
RP FUNCTION.
RX PubMed=10490599; DOI=10.1128/mcb.19.10.6598;
RA He S., Fox T.D.;
RT "Mutations affecting a yeast mitochondrial inner membrane protein, pnt1p,
RT block export of a mitochondrially synthesized fusion protein from the
RT matrix.";
RL Mol. Cell. Biol. 19:6598-6607(1999).
RN [8]
RP INTERACTION WITH COX18.
RX PubMed=11950926; DOI=10.1091/mbc.01-12-0580;
RA Saracco S.A., Fox T.D.;
RT "Cox18p is required for export of the mitochondrially encoded Saccharomyces
RT cerevisiae Cox2p C-tail and interacts with Pnt1p and Mss2p in the inner
RT membrane.";
RL Mol. Biol. Cell 13:1122-1131(2002).
RN [9]
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 [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
CC -!- FUNCTION: Probably involved in mitochondrial export. Confers resistance
CC to the anti-pneumocystis carinii drug pentamidine. May act by the
CC removal of pentamidine, or its damage targets, from the matrix by an
CC active-transport mechanism. {ECO:0000269|PubMed:10490599}.
CC -!- SUBUNIT: Interacts with COX18. This interaction may be essential for
CC its insertion into mitochondrial inner membrane.
CC {ECO:0000269|PubMed:11950926}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16823961}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 1460 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U15217; AAA86313.1; -; Genomic_DNA.
DR EMBL; Z75174; CAA99489.1; -; Genomic_DNA.
DR EMBL; AY692772; AAT92791.1; -; Genomic_DNA.
DR EMBL; U30184; AAB08526.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11032.1; -; Genomic_DNA.
DR PIR; S67163; S67163.
DR RefSeq; NP_014909.3; NM_001183685.3.
DR AlphaFoldDB; P38969; -.
DR BioGRID; 34655; 125.
DR DIP; DIP-4099N; -.
DR IntAct; P38969; 4.
DR MINT; P38969; -.
DR STRING; 4932.YOR266W; -.
DR MaxQB; P38969; -.
DR PaxDb; P38969; -.
DR PRIDE; P38969; -.
DR EnsemblFungi; YOR266W_mRNA; YOR266W; YOR266W.
DR GeneID; 854440; -.
DR KEGG; sce:YOR266W; -.
DR SGD; S000005792; PNT1.
DR VEuPathDB; FungiDB:YOR266W; -.
DR eggNOG; ENOG502S645; Eukaryota.
DR HOGENOM; CLU_061833_0_0_1; -.
DR InParanoid; P38969; -.
DR OMA; EKWGVNN; -.
DR BioCyc; YEAST:G3O-33756-MON; -.
DR PRO; PR:P38969; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P38969; protein.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0032979; P:protein insertion into mitochondrial inner membrane from matrix; IMP:SGD.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..423
FT /note="Pentamidine resistance factor, mitochondrial"
FT /id="PRO_0000022080"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 406..423
FT /note="NISLLKYNSELVATKDIQ -> IYHC (in Ref. 1; AAA86313)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 48934 MW; 471441CD7D402741 CRC64;
MDSRVALVRK YIAPSVIKSD SIQLHGLVKA PLFKALNSRY KLGSLQIVQD VDWNAKTTPS
DSPEPLAATL NSNRSLPMTK FPKQEILEQV KLDTKVGKWR KFMTGWFRIG LYLLKSYKTG
IQNTLKVFWD TRNEEQKFSI KNGALANLVR EIEMHEINTR LSSSSLPTSS SAKAPLRPLS
INRKTLVELI RRDQIWKLPV FFTLVFIFEE VSVLIFTFFP RVCPYNCLTP GGYKKLSNSY
IKGTTSTQGN YGLGPLEFTK QGTIKYEPPY AVPIENLYNF LTSFPQSMIS NWKLYIYKKL
KLQKLLCNEI EKIYQYLFID DWLLLQSILN TDVEKTKIAL SDRELVNCIL ERKLYHMGDD
LNEMVNDTLG KEILLKRLFL YWTLRYNDTI SLNGKHTFSE KWGVNNISLL KYNSELVATK
DIQ
