PTR2_SCHPO
ID PTR2_SCHPO Reviewed; 618 AA.
AC Q9P380; P46031; Q9UU13;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable peptide transporter ptr2;
DE AltName: Full=Peptide permease ptr2;
GN Name=ptr2; ORFNames=SPBC13A2.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7919993; DOI=10.2307/3869826;
RA Steiner H., Song W., Naider F., Becker J.M., Stacey G.;
RT "An Arabidopsis peptide transporter is a member of a new class of membrane
RT transport proteins.";
RL Plant Cell 6:1289-1299(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 215-395, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; TYR-23; SER-25; SER-33;
RP THR-35; SER-44; THR-45; SER-51; SER-53; THR-54; SER-594 AND THR-618, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Uptake of small peptides. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:10759889}; Multi-
CC pass membrane protein {ECO:0000305|PubMed:10759889}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:7919993) reported to be isolated from
CC an A.thaliana cv. Landsberg erecta cDNA library.
CC {ECO:0000305|PubMed:7919993}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA53173.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U01171; AAA53173.1; ALT_FRAME; mRNA.
DR EMBL; CU329671; CAB99397.1; -; Genomic_DNA.
DR EMBL; AB027874; BAA87178.1; -; Genomic_DNA.
DR RefSeq; NP_596417.1; NM_001022336.2.
DR AlphaFoldDB; Q9P380; -.
DR SMR; Q9P380; -.
DR BioGRID; 276734; 51.
DR STRING; 4896.SPBC13A2.04c.1; -.
DR TCDB; 2.A.17.2.1; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR iPTMnet; Q9P380; -.
DR MaxQB; Q9P380; -.
DR PaxDb; Q9P380; -.
DR PRIDE; Q9P380; -.
DR EnsemblFungi; SPBC13A2.04c.1; SPBC13A2.04c.1:pep; SPBC13A2.04c.
DR GeneID; 2540201; -.
DR KEGG; spo:SPBC13A2.04c; -.
DR PomBase; SPBC13A2.04c; ptr2.
DR VEuPathDB; FungiDB:SPBC13A2.04c; -.
DR eggNOG; KOG1237; Eukaryota.
DR HOGENOM; CLU_004790_4_2_1; -.
DR InParanoid; Q9P380; -.
DR OMA; YYAVAFS; -.
DR PhylomeDB; Q9P380; -.
DR Reactome; R-SPO-427975; Proton/oligopeptide cotransporters.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR PRO; PR:Q9P380; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:PomBase.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031520; C:plasma membrane of cell tip; IDA:PomBase.
DR GO; GO:0005774; C:vacuolar membrane; EXP:PomBase.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0042937; F:tripeptide transmembrane transporter activity; ISO:PomBase.
DR GO; GO:0140206; P:dipeptide import across plasma membrane; IMP:PomBase.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; EXP:PomBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0140207; P:tripeptide import across plasma membrane; ISO:PomBase.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000109; POT_fam.
DR InterPro; IPR018456; PTR2_symporter_CS.
DR PANTHER; PTHR11654; PTHR11654; 1.
DR Pfam; PF00854; PTR2; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS01022; PTR2_1; 1.
DR PROSITE; PS01023; PTR2_2; 1.
PE 1: Evidence at protein level;
KW Membrane; Peptide transport; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..618
FT /note="Probable peptide transporter ptr2"
FT /id="PRO_0000064319"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 26..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 23
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 35
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 45
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 618
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 38
FT /note="T -> Q (in Ref. 1; AAA53173)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="R -> S (in Ref. 1; AAA53173)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="S -> T (in Ref. 1; AAA53173)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="S -> T (in Ref. 1; AAA53173)"
FT /evidence="ECO:0000305"
FT CONFLICT 609..610
FT /note="TA -> NC (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 618 AA; 68499 MW; 33C10E3C63B98474 CRC64;
MSSIEEQITK SDSDFIISED QSYLSKEKKA DGSATINTAD EQSSTDELQK SMSTGVLVNG
DLYPSPTEEE LATLPRVCGT IPWKAFIIII VELCERFAYY GLTVPFQNYM QFGPKDATPG
ALNLGESGAD GLSNFFTFWC YVTPVGAALI ADQFLGRYNT IVCSAVIYFI GILILTCTAI
PSVIDAGKSM GGFVVSLIII GLGTGGIKSN VSPLMAEQLP KIPPYVKTKK NGSKVIVDPV
VTTSRAYMIF YWSINVGSLS VLATTSLEST KGFVYAYLLP LCVFVIPLII LAVSKRFYKH
TPPSGSIFVR VGQVFFLAAQ NKFNLEKTKP SCTTTVGRVT LKDQWDDLFI DELKRALRAC
KTFLFYPIYW VCYGQMTNNL ISQAGQMQTG NVSNDLFQAF DSIALIIFIP ICDNIIYPLL
RKYNIPFKPI LRITLGFMFA TASMIYAAVL QAKIYQRGPC YANFTDTCVS NDISVWIQIP
AYVLIAFSEI FASITGLEFA FTKAPPSMKS IITALFLFTN AFGAILSICI SSTAVNPKLT
WMYTGIAVTA FIAGIMFWVC FHHYDAMEDE QNQLEFKRND ALTKKDVEKE VHDSYSMADE
SQYNLEKATA EEEIMKST
