PTR3_YEAST
ID PTR3_YEAST Reviewed; 678 AA.
AC P43606; D6VTQ9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=SPS-sensor component PTR3;
DE AltName: Full=Peptide transport protein 3;
GN Name=PTR3; Synonyms=APF3, SSY3; OrderedLocusNames=YFR029W;
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=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
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 204511 / S288c / AB972;
RX PubMed=8686381;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<177::aid-yea896>3.0.co;2-a;
RA Eki T., Naitou M., Hagiwara H., Abe M., Ozawa M., Sasanuma S., Sasanuma M.,
RA Tsuchiya Y., Shibata T., Watanabe K., Ono A., Yamazaki M., Tashiro H.,
RA Hanaoka F., Murakami Y.;
RT "Fifteen open reading frames in a 30.8 kb region of the right arm of
RT chromosome VI from Saccharomyces cerevisiae.";
RL Yeast 12:177-190(1996).
RN [4]
RP FUNCTION.
RX PubMed=9701822; DOI=10.1046/j.1365-2958.1998.00931.x;
RA Barnes D., Lai W., Breslav M., Naider F., Becker J.M.;
RT "PTR3, a novel gene mediating amino acid-inducible regulation of peptide
RT transport in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 29:297-310(1998).
RN [5]
RP IDENTIFICATION.
RX PubMed=9483800;
RX DOI=10.1002/(sici)1097-0061(19980130)14:2<103::aid-yea203>3.0.co;2-c;
RA Joergensen M.U., Bruun M.B., Didion T., Kielland-Brandt M.C.;
RT "Mutations in five loci affecting GAP1-independent uptake of neutral amino
RT acids in yeast.";
RL Yeast 14:103-114(1998).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10409731; DOI=10.1128/mcb.19.8.5405;
RA Klasson H., Fink G.R., Ljungdahl P.O.;
RT "Ssy1p and Ptr3p are plasma membrane components of a yeast system that
RT senses extracellular amino acids.";
RL Mol. Cell. Biol. 19:5405-5416(1999).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11154269; DOI=10.1128/mcb.21.3.814-826.2001;
RA Forsberg H., Ljungdahl P.O.;
RT "Genetic and biochemical analysis of the yeast plasma membrane Ssy1p-Ptr3p-
RT Ssy5p sensor of extracellular amino acids.";
RL Mol. Cell. Biol. 21:814-826(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH SSY5.
RX PubMed=11489133; DOI=10.1046/j.1365-2958.2001.02538.x;
RA Bernard F., Andre B.;
RT "Genetic analysis of the signalling pathway activated by external amino
RT acids in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 41:489-502(2001).
RN [9]
RP FUNCTION.
RX PubMed=12502738; DOI=10.1101/gad.239202;
RA Andreasson C., Ljungdahl P.O.;
RT "Receptor-mediated endoproteolytic activation of two transcription factors
RT in yeast.";
RL Genes Dev. 16:3158-3172(2002).
RN [10]
RP MUTAGENESIS OF THR-435 AND GLN-439.
RX PubMed=15947203; DOI=10.1128/ec.4.6.1116-1124.2005;
RA Poulsen P., Wu B., Gaber R.F., Kielland-Brandt M.C.;
RT "Constitutive signal transduction by mutant Ssy5p and Ptr3p components of
RT the SPS amino acid sensor system in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 4:1116-1124(2005).
RN [11]
RP FUNCTION, PHOSPHORYLATION, INTERACTION WITH SSY1 AND SSY5, AND MUTAGENESIS
RP OF SER-321; THR-435; GLN-439; THR-525 AND THR-635.
RX PubMed=17984223; DOI=10.1128/mcb.00929-07;
RA Liu Z., Thornton J., Spirek M., Butow R.A.;
RT "Activation of the SPS amino acid-sensing pathway in Saccharomyces
RT cerevisiae correlates with the phosphorylation state of a sensor component,
RT Ptr3.";
RL Mol. Cell. Biol. 28:551-563(2008).
CC -!- FUNCTION: Component of the SPS-sensor system, which regulates the
CC expression of several amino acid-metabolizing enzymes and amino
CC acid- and peptide-permeases in response to extracellular amino acid
CC levels by controlling the activity of two transcription factors, STP1
CC and STP2. {ECO:0000269|PubMed:10409731, ECO:0000269|PubMed:11154269,
CC ECO:0000269|PubMed:11489133, ECO:0000269|PubMed:12502738,
CC ECO:0000269|PubMed:17984223, ECO:0000269|PubMed:9701822}.
CC -!- SUBUNIT: Homodimer. Component of the plasma membrane SPS (SSY1-PTR3-
CC SSY5) amino acid sensor complex. Interacts directly with SSY1 and SSY5.
CC {ECO:0000269|PubMed:11489133, ECO:0000269|PubMed:17984223}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10409731,
CC ECO:0000269|PubMed:11154269}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10409731, ECO:0000269|PubMed:11154269}; Cytoplasmic
CC side {ECO:0000269|PubMed:10409731, ECO:0000269|PubMed:11154269}.
CC -!- PTM: Hyperphosphorylated in response to extracellular amino acids and
CC dependent on the amino acid sensor component SSY1. Phosphorylation is
CC positively regulated by casein kinases YCK1 and YCK2, and negatively
CC regulated by phosphatase PP2A regulatory subunit RTS1.
CC {ECO:0000269|PubMed:17984223}.
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DR EMBL; D50617; BAA09268.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12469.1; -; Genomic_DNA.
DR PIR; S56284; S56284.
DR RefSeq; NP_116685.1; NM_001179994.1.
DR AlphaFoldDB; P43606; -.
DR BioGRID; 31184; 83.
DR IntAct; P43606; 1.
DR MINT; P43606; -.
DR STRING; 4932.YFR029W; -.
DR iPTMnet; P43606; -.
DR MaxQB; P43606; -.
DR PaxDb; P43606; -.
DR PRIDE; P43606; -.
DR EnsemblFungi; YFR029W_mRNA; YFR029W; YFR029W.
DR GeneID; 850587; -.
DR KEGG; sce:YFR029W; -.
DR SGD; S000001925; PTR3.
DR VEuPathDB; FungiDB:YFR029W; -.
DR eggNOG; ENOG502QUFR; Eukaryota.
DR HOGENOM; CLU_028479_0_0_1; -.
DR InParanoid; P43606; -.
DR OMA; TNFPIRC; -.
DR BioCyc; YEAST:G3O-30478-MON; -.
DR PRO; PR:P43606; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43606; protein.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:SGD.
DR GO; GO:0043200; P:response to amino acid; IMP:SGD.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome.
FT CHAIN 1..678
FT /note="SPS-sensor component PTR3"
FT /id="PRO_0000097093"
FT REGION 111..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 321
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:17984223"
FT MUTAGEN 435
FT /note="T->K: In PTR3-17; constitutively active, confers
FT increased STP1 processing in the absence of amino acids."
FT /evidence="ECO:0000269|PubMed:15947203,
FT ECO:0000269|PubMed:17984223"
FT MUTAGEN 439
FT /note="Q->R: In PTR3-5; constitutively active and
FT hyperphosphorylated, confers increased STP1 processing in
FT the absence of amino acids."
FT /evidence="ECO:0000269|PubMed:15947203,
FT ECO:0000269|PubMed:17984223"
FT MUTAGEN 525
FT /note="T->A,D,E: Loss of function. Abolishes
FT hyperphosphorylation of PTR3 and, consequently, results in
FT a failure to activate STP1."
FT /evidence="ECO:0000269|PubMed:17984223"
FT MUTAGEN 635
FT /note="T->A: No effect."
FT /evidence="ECO:0000269|PubMed:17984223"
SQ SEQUENCE 678 AA; 76286 MW; BF2B64842D669D6B CRC64;
MHSHRQKWGR QTDIARVLDD IEHDLYLPQR LSLDGATGTD ESHVQYGIVK DCSVLTCGCC
ISESLFNDLC RETSNKQTAC PICQRENVRL LSAIKPLRDL ARQIDFFRST TGQGESESDE
LPAIVKTSPS SSSLSLTPSR SSSTAGLEAD NKTLSDPTVK EKSSLLELFH IVASKMHNAN
TEVGSDHPLT TGTTRDQEEH TTKENYSSSL LEPNYDDHAN WKILDNASNT RTVPIDNNFS
LMSTDVTIPS TANYQTNSAH DLDEEKEYFF ANCFPMYRKK FQFNTHPKFL GTKSKLFINQ
SISPDCTKFA LITEHKWEIY SINPKDNSPQ LVSCGKSSGE YGPNFNQLTE QSSSSLSTTS
QASKKKKKNW SQRFCKLSND FLIISGSQNI LNVHDIHQNG KLIYTYVSRF PIRCIDIDPR
SQIIAYGITG KDRHTGAEQA LVVIQQITRN KVTLEPEFPP PITITLPYRD PINTIQLSHD
AKYLTCSTAL ESRFLIISLQ KINEPRLIMK SVRSIDTSLE SEGITDTKLF PGNPNLMCIT
STAFNSSPLV INTKITQING VRTVAQPSML IRVDEIGCKI HKCEISPRND AIAFLDRNGS
VYIMCAPTMM DNNEKRRTIL VETVANAYRA YESATLRFNP EGNKLYILDR KGTFFVEDFA
YGLPQSREIT KCKQIFHK
