TCPA_CLAP2
ID TCPA_CLAP2 Reviewed; 542 AA.
AC M1WCQ0;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=MFS thioclapurine efflux transporter tcpA {ECO:0000303|PubMed:27390873};
DE AltName: Full=Thioclapurine biosynthesis protein A {ECO:0000303|PubMed:27390873};
GN Name=tcpA {ECO:0000303|PubMed:27390873}; ORFNames=CPUR_02675;
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1;
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
RN [2]
RP FUNCTION, AND INDUCTION.
RX PubMed=27390873; DOI=10.1371/journal.pone.0158945;
RA Dopstadt J., Neubauer L., Tudzynski P., Humpf H.U.;
RT "The epipolythiodiketopiperazine gene cluster in Claviceps purpurea:
RT dysfunctional cytochrome P450 enzyme prevents formation of the previously
RT unknown clapurines.";
RL PLoS ONE 11:E0158945-E0158945(2016).
CC -!- FUNCTION: MFS efflux transporter probably involved in thioclapurine
CC export (PubMed:27390873). {ECO:0000305|PubMed:27390873}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by the thioclapurine
CC cluster-specific transcription factor tcpZ (PubMed:27390873).
CC {ECO:0000269|PubMed:27390873}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; CAGA01000011; CCE28984.1; -; Genomic_DNA.
DR AlphaFoldDB; M1WCQ0; -.
DR SMR; M1WCQ0; -.
DR EnsemblFungi; CCE28984; CCE28984; CPUR_02675.
DR VEuPathDB; FungiDB:CPUR_02675; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_000960_22_1_1; -.
DR OrthoDB; 627633at2759; -.
DR PhylomeDB; M1WCQ0; -.
DR Proteomes; UP000016801; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..542
FT /note="MFS thioclapurine efflux transporter tcpA"
FT /id="PRO_0000437733"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 542 AA; 57747 MW; D0DC095336420CF7 CRC64;
MATVGTEEKN PIGSASNTAE PNVTEPQKQY ASGFKLTIIV ISLCLSLFLC GLDQTIITTA
VPIITNDFKA IEDVGWYTTA YLLTTSSFQI AYGKLYTTLS VKMILLMALA IFELGSIICA
AAPNSTTLIV GRAIAGLGAA GIFPGSTLVL VHAAPMERRP ALLGITTGMF GIASLCGPFI
GGAFADGASW RWCFIINVPL GVITAVIVTF FVFTPVDPLY AEWTFKDKLA YAKIPEILVL
VAALVCLVLG LQWGGTTYAW SDGRIIALLV VFAVLTTAFL VLQVLLPKSR TIPTSIVKNR
NIWFASIFAL CSSGAMFIAV TYLPIYFQAI KNASALSSGV NVMPLILGFL VMSIISGVIT
NTTGYYNPSM FLCTILASVG AGLVSTFDVG TPQPKWIGYQ ALLGFGIGFG LQQPIVCAQH
VLDERDVPFG VAFINMMQML GGAIFVAVSQ NVFLNGLANG IAEALPGFNT HKIIEGGLTD
FKNLFTSDQL PKAIPVYAHV LGQVFLIATG LCVGTLLGSL GVQWRSVKKA KVTEDQADVE
RK
