ID   DTR1_YEAST              Reviewed;         572 AA.
AC   P38125; D6VQH4;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   08-NOV-2023, entry version 161.
DE   RecName: Full=Dityrosine transporter 1;
GN   Name=DTR1; OrderedLocusNames=YBR180W; ORFNames=YBR1242;
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=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
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   INDUCTION, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12455697; DOI=10.1128/ec.1.5.799-810.2002;
RA   Felder T., Bogengruber E., Tenreiro S., Ellinger A., Sa-Correia I.,
RA   Briza P.;
RT   "Dtrlp, a multidrug resistance transporter of the major facilitator
RT   superfamily, plays an essential role in spore wall maturation in
RT   Saccharomyces cerevisiae.";
RL   Eukaryot. Cell 1:799-810(2002).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15755916; DOI=10.1128/ec.4.3.536-544.2005;
RA   Iwamoto M.A., Fairclough S.R., Rudge S.A., Engebrecht J.;
RT   "Saccharomyces cerevisiae Sps1p regulates trafficking of enzymes required
RT   for spore wall synthesis.";
RL   Eukaryot. Cell 4:536-544(2005).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16554438; DOI=10.1242/jcs.02841;
RA   Nakanishi H., Morishita M., Schwartz C.L., Coluccio A., Engebrecht J.,
RA   Neiman A.M.;
RT   "Phospholipase D and the SNARE Sso1p are necessary for vesicle fusion
RT   during sporulation in yeast.";
RL   J. Cell Sci. 119:1406-1415(2006).
RN   [6]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17645731; DOI=10.1111/j.1600-0854.2007.00606.x;
RA   Morishita M., Mendonsa R., Wright J., Engebrecht J.;
RT   "Snc1p v-SNARE transport to the prospore membrane during yeast sporulation
RT   is dependent on endosomal retrieval pathways.";
RL   Traffic 8:1231-1245(2007).
RN   [8]
RP   SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX   PubMed=18676951; DOI=10.1128/ec.00151-08;
RA   Morishita M., Engebrecht J.;
RT   "Sorting signals within the Saccharomyces cerevisiae sporulation-specific
RT   dityrosine transporter, Dtr1p, C terminus promote Golgi-to-prospore
RT   membrane transport.";
RL   Eukaryot. Cell 7:1674-1684(2008).
CC   -!- FUNCTION: Prospore-specific dityrosine transporter responsible for
CC       translocation of dityrosine through the prospore membrane and required
CC       for the formation of the outermost layer of the spore.
CC       {ECO:0000269|PubMed:12455697}.
CC   -!- SUBCELLULAR LOCATION: Prospore membrane {ECO:0000269|PubMed:12455697,
CC       ECO:0000269|PubMed:15755916, ECO:0000269|PubMed:16554438,
CC       ECO:0000269|PubMed:17645731, ECO:0000269|PubMed:18676951}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:12455697,
CC       ECO:0000269|PubMed:15755916, ECO:0000269|PubMed:16554438,
CC       ECO:0000269|PubMed:17645731, ECO:0000269|PubMed:18676951}.
CC   -!- INDUCTION: During sporulation. {ECO:0000269|PubMed:12455697}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:18676951}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family.
CC       {ECO:0000305}.
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DR   EMBL; Z36049; CAA85141.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07294.1; -; Genomic_DNA.
DR   PIR; S46051; S46051.
DR   RefSeq; NP_009739.1; NM_001178528.1.
DR   AlphaFoldDB; P38125; -.
DR   BioGRID; 32878; 51.
DR   DIP; DIP-5179N; -.
DR   IntAct; P38125; 4.
DR   MINT; P38125; -.
DR   STRING; 4932.YBR180W; -.
DR   TCDB; 2.A.1.2.40; the major facilitator superfamily (mfs).
DR   PaxDb; 4932-YBR180W; -.
DR   PeptideAtlas; P38125; -.
DR   EnsemblFungi; YBR180W_mRNA; YBR180W; YBR180W.
DR   GeneID; 852478; -.
DR   KEGG; sce:YBR180W; -.
DR   AGR; SGD:S000000384; -.
DR   SGD; S000000384; DTR1.
DR   VEuPathDB; FungiDB:YBR180W; -.
DR   eggNOG; KOG0255; Eukaryota.
DR   HOGENOM; CLU_008455_8_7_1; -.
DR   InParanoid; P38125; -.
DR   OMA; FQAFGSC; -.
DR   OrthoDB; 1362470at2759; -.
DR   BioCyc; YEAST:G3O-29124-MONOMER; -.
DR   BioGRID-ORCS; 852478; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P38125; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38125; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR   GO; GO:0005275; F:amine transmembrane transporter activity; IMP:SGD.
DR   GO; GO:0015837; P:amine transport; IMP:SGD.
DR   GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR   GO; GO:0055085; P:transmembrane transport; IMP:SGD.
DR   CDD; cd17323; MFS_Tpo1_MDR_like; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR23502:SF21; DITYROSINE TRANSPORTER 1; 1.
DR   PANTHER; PTHR23502; MAJOR FACILITATOR SUPERFAMILY; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Reference proteome; Sporulation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..572
FT                   /note="Dityrosine transporter 1"
FT                   /id="PRO_0000173438"
FT   TOPO_DOM        1..110
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        132..149
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        171..184
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        206..207
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        229..240
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        262..267
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        289..366
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        367..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        388..398
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        420..446
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        447..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        470..472
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        473..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        494..520
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        521..541
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        542
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        543..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        564..572
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          49..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..572
FT                   /note="Required for the localization to the prospore
FT                   membrane"
FT   COMPBIAS        9..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   572 AA;  63407 MW;  8175C30520A266F4 CRC64;
     MGSEPFQKKN LGLQINSQES GTTRSTFHSL EDLGDDVINE SWDQVNQKRA NIDHDVFHEH
     PDSSPSLSAQ KAKTKEEEVA VKSSNSQSRD PSPDTQAHIP YTYFSKDQRL IIFGIIIFIG
     FLGPMSGNIY IPALPLLQRE YDVSATTINA TVSVFMAVFS VGPLFWGALA DFGGRKFLYM
     VSLSLMLIVN ILLAAVPVNI AALFVLRIFQ AFASSSVISL GAGTVTDVVP PKHRGKAIAY
     FMMGPNMGPI IAPIVAGLIL MKGNYWRWLF GFTSIMTGIA LILVTALLPE TLRCIVGNGD
     PKWGDKKDER ENNESPFFEG NKISHRRLFP DIGIRKPVNN DAFFQENFPK PPKAGLTLYW
     KMIKCPPIII TSVSTALLFS SYYAFSVTFS YYLEHDYRFT MLEIGAAYVC PGVAMLLGSQ
     SGGHLSDYLR SRWIKSHPKK KFPAEFRLLL NLIGILLTIC GTIGYGWAIF FHYHFVVLLV
     FSALTAFGMT WCSNTSMTYL TELFPKRAAG TVAVSSFFRN VGAAISSAII LQLCNAMGIG
     WCFTGLGLCS SISLIGILYL LIFQRKYTAK EF
//