NTT1_ENCCU
ID NTT1_ENCCU Reviewed; 559 AA.
AC Q8SRA2;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=ADP,ATP carrier protein 1;
DE AltName: Full=ADP/ATP translocase 1;
DE AltName: Full=Nucleotide transporter 1;
GN Name=NTT1; OrderedLocusNames=ECU08_1300;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18449191; DOI=10.1038/nature06903;
RA Tsaousis A.D., Kunji E.R.S., Goldberg A.V., Lucocq J.M., Hirt R.P.,
RA Embley T.M.;
RT "A novel route for ATP acquisition by the remnant mitochondria of
RT Encephalitozoon cuniculi.";
RL Nature 453:553-556(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
CC -!- FUNCTION: ATP transporter involved in the uptake of ATP from the host
CC cell cytoplasm. Provides the microsporidian cell with host ATP in
CC exchange for ADP. This is an obligate exchange system. This energy
CC acquiring activity is an important component of microsporidian
CC parasitism. {ECO:0000269|PubMed:18449191}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.4 uM for ATP uptake {ECO:0000269|PubMed:18449191};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18449191};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18449191}. Note=Only
CC found on the surface of parasites living inside host cells.
CC -!- SIMILARITY: Belongs to the ADP/ATP translocase tlc family.
CC {ECO:0000305}.
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DR EMBL; EU040266; ABW20407.1; -; Genomic_DNA.
DR EMBL; AL590448; CAD26436.1; -; Genomic_DNA.
DR RefSeq; NP_597260.1; NM_001041869.1.
DR AlphaFoldDB; Q8SRA2; -.
DR TCDB; 2.A.12.1.10; the atp:adp antiporter (aaa) family.
DR GeneID; 859682; -.
DR KEGG; ecu:ECU08_1300; -.
DR VEuPathDB; MicrosporidiaDB:ECU08_1300; -.
DR HOGENOM; CLU_023964_1_0_1; -.
DR InParanoid; Q8SRA2; -.
DR OMA; RKVIWPI; -.
DR OrthoDB; 1270398at2759; -.
DR Proteomes; UP000000819; Chromosome VIII.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IEA:InterPro.
DR InterPro; IPR004667; ADP_ATP_car_bac_type.
DR PANTHER; PTHR31187; PTHR31187; 1.
DR Pfam; PF03219; TLC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..559
FT /note="ADP,ATP carrier protein 1"
FT /id="PRO_0000382923"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 559 AA; 63516 MW; 9B15588ED28BCD5D CRC64;
MNEVENNNHS FPREDIPTED EIEEEANSRQ GILRYFRVAR AEYTKFALLG LMFGIIGFIY
SFMRILKDMF VMVRQEPTTI LFIKIFYILP VSMALVFLIQ YMLGTKTVSR IFSIFCGGFA
SLFFLCGAVF LIEEQVSPSK FLFRDMFIDG KMSSRSLNVF KSMFLTLNEP LATIVFISAE
MWGSLVLSYL FLSFLNESCT IRQFSRFIPP LIIITNVSLF LSATVAGAFF KLREKLAFQQ
NQVLLSGIFI FQGFLVVLVI FLKIYLERVT MKRPLFIVSS GSRRKKAKAN VSFSEGLEIM
SQSKLLLAMS LIVLFFNISY NMVESTFKVG VKVAAEYFNE EKGKYSGKFN RIDQYMTSVV
VICLNLSPFS SYVETRGFLL VGLITPIVTL MAIVLFLGSA LYNTSMEESG LGIVNGLFPG
GKPLYVLENY FGVIFMSLLK ITKYSAFDIC KEKLGMRINP TYRARFKSVY DGIFGKLGKS
IGSIYGLLMF EALDTEDLRK ATPITAGIIF IFIVMWVKAI IYLSRSYESA VQHNRDVDID
MTEKAKKSLE TPEEPKVVD
