PUTX_EMENI
ID PUTX_EMENI Reviewed; 550 AA.
AC P18696; C8VP33; Q5BCJ8; Q92202;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Proline-specific permease;
DE AltName: Full=Proline transport protein;
GN Name=prnB; ORFNames=AN1732;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=pabaA1;
RX PubMed=2664423; DOI=10.1111/j.1365-2958.1989.tb00219.x;
RA Sophianopoulou V., Scazzocchio C.;
RT "The proline transport protein of Aspergillus nidulans is very similar to
RT amino acid transporters of Saccharomyces cerevisiae.";
RL Mol. Microbiol. 3:705-714(1989).
RN [2]
RP SEQUENCE REVISION.
RA Tazebay U.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Required for high-affinity proline transport.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- INDUCTION: By L-proline.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF85456.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA64018.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X79797; CAA56191.1; -; Genomic_DNA.
DR EMBL; AACD01000027; EAA64018.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001307; CBF85456.1; ALT_SEQ; Genomic_DNA.
DR PIR; S04547; S04547.
DR RefSeq; XP_659336.1; XM_654244.1.
DR AlphaFoldDB; P18696; -.
DR SMR; P18696; -.
DR STRING; 162425.CADANIAP00008377; -.
DR EnsemblFungi; EAA64018; EAA64018; AN1732.2.
DR GeneID; 2875279; -.
DR KEGG; ani:AN1732.2; -.
DR eggNOG; KOG1286; Eukaryota.
DR HOGENOM; CLU_007946_12_1_1; -.
DR InParanoid; P18696; -.
DR OrthoDB; 621852at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 2: Evidence at transcript level;
KW Amino-acid transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..550
FT /note="Proline-specific permease"
FT /id="PRO_0000054159"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..72
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..152
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..484
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..550
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 550 AA; 60810 MW; 04BC14762005E5E8 CRC64;
MSPPSAKSME EGRTPSVQYG YGDPKTLEGE IEEHTATKRG LSSRQLQLLA IGGCIGTGLF
VGTSTVLTQT GPAPLLMSYI VMASIVWFVM NVLGEMTTYL PIRGVSVPYL IGRFTEPSIG
FASGYNYWYS FAMLLASEVT ASGLIIEYWN PPVSVGLWIA IVLVVILALN VFAVEWYGES
EFWFAGLKIL AIIGLIILGV VLFFGGGPNH DRLGFRYWQD PGAFNPYLVP GDTGKFLGFW
TALIKSGFSF IFSPELITTA AGEVEAPRRN IPKATKRFIY RVFTFYILGS LVIGVTVAYN
DPTLEAGVES GGSGAGASPF VVAIQNAGIG GLNHVVNAAI LISAWSSGNA WCYAGSRTLY
SLAGEGQAPK IFTRTNRTGV PYVAVLATWT IGLLSFLNLS SSGQTVFYWF TNITTVGGFI
NWVLIGIAYL RFRKALQFHG MLDMLPFKTP LQPYGTYYVM FIISILTLTN GYAVFFPGRF
TASDFLVSYI VFAIFLALYA GHKIWYRTPW LTKVSEVDIF TGKDEIDRLC ENDMERQPRN
WLERVWWWIF
