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NTT2_ENCCU
ID   NTT2_ENCCU              Reviewed;         553 AA.
AC   Q8SUF9;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=ADP,ATP carrier protein 2;
DE   AltName: Full=ADP/ATP translocase 2;
DE   AltName: Full=Nucleotide transporter 2;
GN   Name=NTT2; OrderedLocusNames=ECU10_0540;
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, DEVELOPMENTAL
RP   STAGE, FUNCTION, AND 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=19.8 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   -!- DEVELOPMENTAL STAGE: Expressed in all stages of development including
CC       spores. {ECO:0000269|PubMed:18449191}.
CC   -!- SIMILARITY: Belongs to the ADP/ATP translocase tlc family.
CC       {ECO:0000305}.
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DR   EMBL; EU040267; ABW20408.1; -; Genomic_DNA.
DR   EMBL; AL590449; CAD25773.1; -; Genomic_DNA.
DR   RefSeq; NP_586169.1; NM_001042002.1.
DR   AlphaFoldDB; Q8SUF9; -.
DR   TCDB; 2.A.12.1.11; the atp:adp antiporter (aaa) family.
DR   PRIDE; Q8SUF9; -.
DR   GeneID; 859818; -.
DR   KEGG; ecu:ECU10_0540; -.
DR   VEuPathDB; MicrosporidiaDB:ECU10_0540; -.
DR   HOGENOM; CLU_023964_1_0_1; -.
DR   InParanoid; Q8SUF9; -.
DR   OMA; FLMTAIY; -.
DR   OrthoDB; 1270398at2759; -.
DR   Proteomes; UP000000819; Chromosome X.
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..553
FT                   /note="ADP,ATP carrier protein 2"
FT                   /id="PRO_0000382925"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        477..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        507..527
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        406
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        532
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   553 AA;  62160 MW;  5091200D1F656BF5 CRC64;
     MSEIGSSVPV NENRPLLTED EVEAQANSST VWPLSRIRVA RCEWKLWGSL AFIFGASAYI
     YSFSRVMKDS FVLSRQLPIA ISFLKTCFVL PISVIVTGIV QKLLVTRTIS KVFDYTLIAF
     SFLYLLIGMV LLPFAEKIQP GLYFSRDIFA DDKMAYKGFE FLFAIFLIFN EWTTSFVYVC
     AELFGSLVVQ FMFLAFANEA LTIRQSTRMM PLFYVISNIL LLLSSESTSF YSKKVREWDY
     KKTCLITNSF FAVFGAMIAV TYLVKKYAEN TILKKQLFIR TEGVAKKKGR KSSAGFSESM
     KLMAQSKFLV AMVMNALFYY AGTNLIESSW KNGISVAADA NNMEKRAYSA SIVSGEQRVV
     GALVAIILLT PISTLVQTHG WITMAIVPPL VTLVSSLVIF GSAFFNYSNY PEGKTSVILS
     SLVKGYKPNF YLECNIGIYC VSGMKIAKYA FYDISKEAIS LQIDPLYRPR LKAVYDGLCG
     KLGKSIGSLY AMFWSVMGYN DVRAAAPITL GMWLIISPIW IYSVIYLNRK YNQSIQTSSP
     IDLDLFSGKK DLE
 
 
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