JEN1_YEAST
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 03-AUG-2022, entry version 172.
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; 40.
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; P36035; -.
DR PRIDE; P36035; -.
DR EnsemblFungi; YKL217W_mRNA; YKL217W; YKL217W.
DR GeneID; 853663; -.
DR KEGG; sce:YKL217W; -.
DR SGD; S000001700; JEN1.
DR VEuPathDB; FungiDB:YKL217W; -.
DR eggNOG; ENOG502QPK1; Eukaryota.
DR HOGENOM; CLU_001265_46_1_1; -.
DR InParanoid; P36035; -.
DR OMA; HEKFHRD; -.
DR BioCyc; YEAST:G3O-31974-MON; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0046943; F:carboxylic acid transmembrane transporter activity; IBA:GO_Central.
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:0046942; P:carboxylic acid transport; IBA:GO_Central.
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 Gene3D; 1.20.1250.20; -; 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 Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00891; 2A0112; 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
