BAP3_YEAST
ID BAP3_YEAST Reviewed; 604 AA.
AC P41815; D6VS34;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Valine amino-acid permease;
DE AltName: Full=Branched-chain amino-acid permease 3;
GN Name=BAP3; Synonyms=PAP1; OrderedLocusNames=YDR046C; ORFNames=YD9609.02C;
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] OF 11-575.
RX PubMed=8200527; DOI=10.1016/0378-1119(94)90617-3;
RA Mai B., Lipp M.;
RT "Cloning and chromosomal organization of a gene encoding a putative amino-
RT acid permease from Saccharomyces cerevisiae.";
RL Gene 143:129-133(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
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 [4]
RP FUNCTION IN L-CYSTEINE UPTAKE.
RX PubMed=10467005; DOI=10.1007/s002940050459;
RA During-Olsen L., Regenberg B., Gjermansen C., Kielland-Brandt M.C.,
RA Hansen J.;
RT "Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple
RT permeases.";
RL Curr. Genet. 35:609-617(1999).
RN [5]
RP FUNCTION.
RX PubMed=10654085; DOI=10.1007/s002940050506;
RA Regenberg B., During-Olsen L., Kielland-Brandt M.C., Holmberg S.;
RT "Substrate specificity and gene expression of the amino-acid permeases in
RT Saccharomyces cerevisiae.";
RL Curr. Genet. 36:317-328(1999).
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).
CC -!- FUNCTION: Involved in transport of isoleucine, leucine, valine,
CC cysteine, methionine, phenylalanine, tyrosine and tryptophan.
CC {ECO:0000269|PubMed:10467005, ECO:0000269|PubMed:10654085}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
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DR EMBL; X75076; CAA52970.1; -; Genomic_DNA.
DR EMBL; Z49209; CAA89077.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11894.1; -; Genomic_DNA.
DR PIR; S54032; S54032.
DR RefSeq; NP_010331.3; NM_001180354.3.
DR AlphaFoldDB; P41815; -.
DR SMR; P41815; -.
DR BioGRID; 32101; 167.
DR DIP; DIP-7900N; -.
DR IntAct; P41815; 11.
DR MINT; P41815; -.
DR STRING; 4932.YDR046C; -.
DR TCDB; 2.A.3.10.27; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; P41815; -.
DR PaxDb; P41815; -.
DR PRIDE; P41815; -.
DR EnsemblFungi; YDR046C_mRNA; YDR046C; YDR046C.
DR GeneID; 851616; -.
DR KEGG; sce:YDR046C; -.
DR SGD; S000002453; BAP3.
DR VEuPathDB; FungiDB:YDR046C; -.
DR eggNOG; KOG1286; Eukaryota.
DR GeneTree; ENSGT00940000176401; -.
DR HOGENOM; CLU_007946_12_0_1; -.
DR InParanoid; P41815; -.
DR OMA; QAFTWLA; -.
DR BioCyc; YEAST:G3O-29659-MON; -.
DR PRO; PR:P41815; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P41815; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:SGD.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; IDA:SGD.
DR GO; GO:0055085; P:transmembrane transport; IDA:SGD.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004762; Amino_acid_permease_fungi.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR TIGRFAMs; TIGR00913; 2A0310; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..604
FT /note="Valine amino-acid permease"
FT /id="PRO_0000054147"
FT TOPO_DOM 1..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..119
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..377
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..449
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..502
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..531
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38084"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38084"
FT CONFLICT 573..575
FT /note="VYD -> GLR (in Ref. 1; CAA52970)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 604 AA; 67365 MW; 49A16DE4BA6B6E8A CRC64;
MSDPIVTSSK MEKSAEFEVT DSALYNNFNT STTASLTPEI KEHSEESRNG LVHRFVDSFR
RAESQRLEED NDLEDGTKSM KSNNHLKKSM KSRHVVMMSL GTGIGTGLLV ANAKGLSLAG
PGSLVIGYVM VSFVTYFMVQ AAGEMGVTYP TLPGNFNAYN SIFISKSFGF ATTWLFCIQW
LTVLPLELIT SSMTVKYWND TINADVFIVI FYVFLLFIHF FGVKAYGETE FIFNSCKILM
VAGFIILSVV INCGGAGVDG YIGGKYWRDP GSFAEGSGAT RFKGICYILV SAYFSFGGIE
LFVLSINEQS NPRKSTPVAA KRSVYRILII YLLTMILIGF NVPHNNDQLM GSGGSATHAS
PYVLAASIHK VRVIPHIINA VILISVISVA NSALYAAPRL MCSLAQQGYA PKFLNYIDRE
GRPLRALVVC SLVGVVGFVA CSPQEEQAFT WLAAIAGLSE LFTWSGIMLS HIRFRKAMKV
QGRSLDEVGY KANTGIWGSY YGVFFNMLVF MAQFWVALSP IGNGGKCDAQ AFFESYLAAP
LWIFMYVGYM VYKRDFTFLN PLDKIDLDFH RRVYDPEIMR QEDEENKERL KNSSIFVRVY
KFWC
