NFT1_YEASX
ID NFT1_YEASX Reviewed; 1558 AA.
AC P0CE70; P36028; P36171; Q53ZY4; Q6Q5L3;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=ABC transporter NFT1;
DE AltName: Full=New full-length MRP-type transporter 1;
GN Name=NFT1;
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204278 / EG123 / SM1058, Sigma 1278B, and SK1;
RX PubMed=12796304; DOI=10.1128/ec.2.3.588-598.2003;
RA Mason D.L., Mallampalli M.P., Huyer G., Michaelis S.;
RT "A region within a lumenal loop of Saccharomyces cerevisiae Ycf1p directs
RT proteolytic processing and substrate specificity.";
RL Eukaryot. Cell 2:588-598(2003).
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; AY230264; AAO73540.1; -; Genomic_DNA.
DR EMBL; AY230265; AAO73541.1; -; Genomic_DNA.
DR EMBL; AY230266; AAO73542.1; -; Genomic_DNA.
DR AlphaFoldDB; P0CE70; -.
DR SMR; P0CE70; -.
DR IntAct; P0CE70; 3.
DR MINT; P0CE70; -.
DR VEuPathDB; FungiDB:YKR103W; -.
DR VEuPathDB; FungiDB:YKR104W; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1558
FT /note="ABC transporter NFT1"
FT /id="PRO_0000392614"
FT TOPO_DOM 1..29
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 51..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 125..130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 152..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 191..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 223..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 324..351
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..374
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 375..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 471..481
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..504
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 505..558
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 580..584
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 606..953
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 954..974
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 975..1013
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1014..1034
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1035..1082
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1083..1105
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1106..1109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1110..1132
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1133..1199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1200..1220
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1221..1222
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1223..1243
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1244..1558
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 311..621
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 651..892
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 961..1251
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1285..1538
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 410..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 686..693
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1319..1326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1558 AA; 176331 MW; C9F596EF39996A47 CRC64;
MIKNGTCPYW ERDDLSECAR REYIEFKFPL FILLTGMIYA FCKVFRAFYL RGKNHTNEAP
EFEEQGNGNH EYARFSVLRL KSAWESRSFC NVNNRSTFDK FKKFIEGAFI VLQLTIHLYI
LSSMPMDNKK FFHQGFLVQM FLWILLLVVI TLRLISASQS FRWVLACKRD LWAVSFYSYA
SLFTLSILPL RSVFIGKIKD KIMVKYIISE TFIDLALLLL LSTSSIEGTR YSFLVENENK
KLPPAPTVFG LLTFSRIDRL IWKAYKHCLG NADIWDLDIN NKSIAILANF EMSSKKGRLL
PNIICYFKAV FISQLFLAFV SSFLNFVPSL LMPRILSYVN DPKSKSWNLV SLYVSSMLVS
KIIATTCRGQ GLFLGEKGTM QLRTVLISNI YSKTLRRTIL KDSTTSLQKN ASTSFEENPD
SSEAEPRKKS SRKDNSVNNV MSIDAFKVSE AMNTFYLACE AVFMTVTALM ILYSLLGWSA
FAGTFALLAM IPLNFWCATF YGNYQADQLI LTDKRTSGIS EALNSIRVIK LLAWENLFYQ
KIINVRDGEI RLLKKKATIF FLNHLIWFFG PTLVSAITFS VFIKFQNQTL TPTIAFTALS
LFAILRTPMD QIASTVSLLI QSFISLERIQ DYLNESETRK YEILEQSNTK FGFEDASMEW
EAAETSFKLK NISIDFKLNS LNAIIGPTGS GKSSLLLGLL GELNLLSGKI YVPTVESRDD
LEIGKDGMTN SMAYCSQTPW LISGTIKDNV VFGEIFNKQK FDDVMKSCCL DKDIKAMTAG
IRTDVGDGGF SLSGGQQQRI ALARAIYSSS RYLILDDCLS AVDPETALYI YEECLCGPMM
KGRTCIITSH NISLVTKRAD WLVILDRGEV KSQGKPSDLI KSNEFLRESI NNDSKNTTHN
QIDLKRSTTS KKTKNGDPEG GNSQDEVCAE VENFEETKME GSVKFSAYKW LADYFGGLGV
VFVFTSSSIL IHGITLSQGF WLRYWLDTGS SGSKSTWLYR IVEGHSNIYF LLTYIIIGLV
SSFLTSGKVW IAIISGTNVT KKIFAKLLSS ILYAKLRFHN VTPTGRIMNR FSKDMDIIDQ
QLIPNFEGLS YSVVVCLWII LLIGYVTPQF LLFAIPLCAL YYTVCTLYLR ASRELKRIDN
INISPIHQLF AEAIKGVTTI RALADERRFI TQSLVAIDRS NAPFFYLNMA TEWITYRVDI
IGTLVLFSSS VMIIMKASYL DAGLAGILLS NAFSFTETAQ WIIKVFSSVE LLMSSVERIK
EYTDIPSESN GYISPPANWP QTGDVELKNL SLRYSPHSSK ALDNVSFKVK AGTKVGIVGR
TGAGKSSIIA AIYRLSDWEN GTITIDNKDI KHIPLERLRN SISCIPQDPT LFDGTVRSNL
DPFDRYSDVQ IYGVLSKVGL IEECDELCLI FEQEQPNFSS HKLRNRFIDL NTVVKSGGSN
LSQGQRQLLC LARSMLGARN IMLIDEATAS IDYISDAKIQ KTIRETMKNT TILTIAHRLR
SVIDYDKILV MEMGRVKEYD HPYTLISDRN TIFYRLCRQS GEFENLFELA KVSFDNKR
