DTR1_YEAST
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 03-AUG-2022, entry version 155.
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; 50.
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; P38125; -.
DR PRIDE; P38125; -.
DR EnsemblFungi; YBR180W_mRNA; YBR180W; YBR180W.
DR GeneID; 852478; -.
DR KEGG; sce:YBR180W; -.
DR SGD; S000000384; DTR1.
DR VEuPathDB; FungiDB:YBR180W; -.
DR eggNOG; KOG0255; Eukaryota.
DR HOGENOM; CLU_008455_8_7_1; -.
DR InParanoid; P38125; -.
DR OMA; GMTWCSN; -.
DR BioCyc; YEAST:G3O-29124-MON; -.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0005275; F:amine transmembrane transporter activity; IMP:SGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
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 Gene3D; 1.20.1250.20; -; 1.
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 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
