ID   JEN1_YEAST              Reviewed;         616 AA.
AC   P36035; D6VWY6;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Carboxylic acid transporter protein homolog;
GN   Name=JEN1; OrderedLocusNames=YKL217W;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 204510 / AB320;
RA   Davis E.S., Brennan M.B.;
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7941750; DOI=10.1002/yea.320100511;
RA   Tzermia M., Horaitis O., Alexandraki D.;
RT   "The complete sequencing of a 24.6 kb segment of yeast chromosome XI
RT   identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open
RT   reading frames including homologues to the threonine dehydratases, membrane
RT   transporters, hydantoinases and the phospholipase A2-activating protein.";
RL   Yeast 10:663-679(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [4]
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   [5]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-9 AND LYS-338, ACETYLATION
RP   [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=SUB592;
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA   Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
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   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-4; SER-11; SER-584 AND SER-606, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA   Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA   van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT   "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT   phosphorylation in assembly of the ATP synthase.";
RL   Mol. Cell. Proteomics 6:1896-1906(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-66; THR-70; SER-603
RP   AND SER-606, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Essential to lactate transport.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR   EMBL; U24155; AAB60291.1; -; Genomic_DNA.
DR   EMBL; X75951; CAA53556.1; -; Genomic_DNA.
DR   EMBL; Z28217; CAA82062.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA08952.1; -; Genomic_DNA.
DR   PIR; S38060; S38060.
DR   RefSeq; NP_012705.1; NM_001179782.1.
DR   AlphaFoldDB; P36035; -.
DR   SMR; P36035; -.
DR   BioGRID; 33948; 44.
DR   DIP; DIP-8064N; -.
DR   STRING; 4932.YKL217W; -.
DR   TCDB; 2.A.1.12.2; the major facilitator superfamily (mfs).
DR   iPTMnet; P36035; -.
DR   PaxDb; 4932-YKL217W; -.
DR   PeptideAtlas; P36035; -.
DR   EnsemblFungi; YKL217W_mRNA; YKL217W; YKL217W.
DR   GeneID; 853663; -.
DR   KEGG; sce:YKL217W; -.
DR   AGR; SGD:S000001700; -.
DR   SGD; S000001700; JEN1.
DR   VEuPathDB; FungiDB:YKL217W; -.
DR   eggNOG; ENOG502QPK1; Eukaryota.
DR   HOGENOM; CLU_001265_46_1_1; -.
DR   InParanoid; P36035; -.
DR   OMA; ILWFSVC; -.
DR   OrthoDB; 1332396at2759; -.
DR   BioCyc; YEAST:G3O-31974-MONOMER; -.
DR   BioGRID-ORCS; 853663; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P36035; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36035; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0015355; F:secondary active monocarboxylate transmembrane transporter activity; IMP:SGD.
DR   GO; GO:0097079; F:selenite:proton symporter activity; IMP:SGD.
DR   GO; GO:0015136; F:sialic acid transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0035879; P:plasma membrane lactate transport; IMP:SGD.
DR   GO; GO:0006849; P:plasma membrane pyruvate transport; IMP:SGD.
DR   GO; GO:0097080; P:plasma membrane selenite transport; IMP:SGD.
DR   CDD; cd17316; MFS_SV2_like; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR004742; SA_transporter.
DR   NCBIfam; TIGR00891; 2A0112; 1.
DR   PANTHER; PTHR23508; CARBOXYLIC ACID TRANSPORTER PROTEIN HOMOLOG; 1.
DR   PANTHER; PTHR23508:SF10; CARBOXYLIC ACID TRANSPORTER PROTEIN HOMOLOG; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Isopeptide bond; Membrane; Phosphoprotein; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12872131,
FT                   ECO:0007744|PubMed:17761666, ECO:0007744|PubMed:22814378"
FT   CHAIN           2..616
FT                   /note="Carboxylic acid transporter protein homolog"
FT                   /id="PRO_0000050460"
FT   TOPO_DOM        2..140
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..176
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        198..205
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        227..230
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..263
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        285..296
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..317
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        318..363
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..384
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        385..402
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        403..423
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        424..432
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        433..453
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        454..457
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        458..478
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        479..489
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        490..510
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        511..535
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        536..556
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        557..616
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:17761666,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17761666"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17761666"
FT   MOD_RES         61
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         70
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         584
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17761666"
FT   MOD_RES         603
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         606
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17761666,
FT                   ECO:0007744|PubMed:19779198"
FT   CROSSLNK        9
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
FT   CROSSLNK        338
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
SQ   SEQUENCE   616 AA;  69376 MW;  47926F50842ACD5B CRC64;
     MSSSITDEKI SGEQQQPAGR KLYYNTSTFA EPPLVDGEGN PINYEPEVYN PDHEKLYHNP
     SLPAQSIQDT RDDELLERVY SQDQGVEYEE DEEDKPNLSA ASIKSYALTR FTSLLHIHEF
     SWENVNPIPE LRKMTWQNWN YFFMGYFAWL SAAWAFFCVS VSVAPLAELY DRPTKDITWG
     LGLVLFVRSA GAVIFGLWTD KSSRKWPYIT CLFLFVIAQL CTPWCDTYEK FLGVRWITGI
     AMGGIYGCAS ATAIEDAPVK ARSFLSGLFF SAYAMGFIFA IIFYRAFGYF RDDGWKILFW
     FSIFLPILLI FWRLLWPETK YFTKVLKARK LILSDAVKAN GGEPLPKANF KQKMVSMKRT
     VQKYWLLFAY LVVLLVGPNY LTHASQDLLP TMLRAQLGLS KDAVTVIVVV TNIGAICGGM
     IFGQFMEVTG RRLGLLIACT MGGCFTYPAF MLRSEKAILG AGFMLYFCVF GVWGILPIHL
     AELAPADARA LVAGLSYQLG NLASAAASTI ETQLADRYPL ERDASGAVIK EDYAKVMAIL
     TGSVFIFTFA CVFVGHEKFH RDLSSPVMKK YINQVEEYEA DGLSISDIVE QKTECASVKM
     IDSNVSKTYE EHIETV
//