(data stored in ACNUC6288 zone)

SWISSPROT: B5RU83_DEBHA

ID   B5RU83_DEBHA            Unreviewed;      1312 AA.
AC   B5RU83;
DT   04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   OrderedLocusNames=DEHA2F02750g {ECO:0000313|EMBL:CAR66260.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAR66260.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAR66260.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phospholipid derivative(in) + ATP + H2O = a
CC         phospholipid derivative(out) + ADP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:14989, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16247, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|RuleBase:RU362033,
CC         ECO:0000256|SAAS:SAAS01116729};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362033};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU362033}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IV subfamily.
CC       {ECO:0000256|RuleBase:RU362033, ECO:0000256|SAAS:SAAS00533978}.
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DR   EMBL; CR382138; CAR66260.1; -; Genomic_DNA.
DR   RefSeq; XP_002770729.1; XM_002770683.1.
DR   STRING; 4959.XP_002770729.1; -.
DR   EnsemblFungi; CAR66260; CAR66260; DEHA2F02750g.
DR   GeneID; 8998863; -.
DR   KEGG; dha:DEHA2F02750g; -.
DR   HOGENOM; HOG000202528; -.
DR   InParanoid; B5RU83; -.
DR   KO; K14802; -.
DR   OMA; GMSCKLI; -.
DR   OrthoDB; 587717at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:1990530; C:Cdc50p-Drs2p complex; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005802; C:trans-Golgi network; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004012; F:phospholipid-translocating ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032456; P:endocytic recycling; IEA:EnsemblFungi.
DR   GO; GO:0006897; P:endocytosis; IEA:EnsemblFungi.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:EnsemblFungi.
DR   GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR   GO; GO:0000749; P:response to pheromone triggering conjugation with cellular fusion; IEA:EnsemblFungi.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IEA:EnsemblFungi.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006539; P-type_ATPase_IV.
DR   InterPro; IPR032631; P-type_ATPase_N.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR032630; P_typ_ATPase_c.
DR   PANTHER; PTHR24092; PTHR24092; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81660; SSF81660; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
DR   PRODOM; B5RU83.
DR   SWISS-2DPAGE; B5RU83.
KW   ATP-binding {ECO:0000256|RuleBase:RU362033,
KW   ECO:0000256|SAAS:SAAS00311808};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Magnesium {ECO:0000256|RuleBase:RU362033,
KW   ECO:0000256|SAAS:SAAS00311822};
KW   Membrane {ECO:0000256|RuleBase:RU362033,
KW   ECO:0000256|SAAS:SAAS00076974};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362033,
KW   ECO:0000256|SAAS:SAAS00311833};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Translocase {ECO:0000256|RuleBase:RU362033,
KW   ECO:0000256|SAAS:SAAS01101229};
KW   Transmembrane {ECO:0000256|RuleBase:RU362033,
KW   ECO:0000256|SAAS:SAAS00311809};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362033,
KW   ECO:0000256|SAAS:SAAS00311798}.
FT   TRANSMEM    448    470       Helical. {ECO:0000256|RuleBase:RU362033}.
FT   TRANSMEM    490    514       Helical. {ECO:0000256|RuleBase:RU362033}.
FT   TRANSMEM   1052   1073       Helical. {ECO:0000256|RuleBase:RU362033}.
FT   TRANSMEM   1094   1121       Helical. {ECO:0000256|RuleBase:RU362033}.
FT   TRANSMEM   1141   1161       Helical. {ECO:0000256|RuleBase:RU362033}.
FT   TRANSMEM   1173   1190       Helical. {ECO:0000256|RuleBase:RU362033}.
FT   TRANSMEM   1202   1222       Helical. {ECO:0000256|RuleBase:RU362033}.
FT   DOMAIN      181    247       PhoLip_ATPase_N. {ECO:0000259|Pfam:
FT                                PF16209}.
FT   DOMAIN      985   1236       PhoLip_ATPase_C. {ECO:0000259|Pfam:
FT                                PF16212}.
SQ   SEQUENCE   1312 AA;  148084 MW;  BE9419F63AECBA36 CRC64;
     MSYSNHRNKD ENGMNNLNNH TNPFSEPENL IDLDLDTRNS FNANVENSPY SHVTSQNQHA
     QPANPFEDNF IISDDEIERD DTIESLGHGS SSQRKVPLLS TANDKSQQRS GLFGGLLANR
     NDEYIGMENG PEERQFKDNN LNDGSSDFDI RKIYRKTKAK FSRSNAEAED AAAVNKGPRQ
     IYIMNQMLNS SFKYYGNHIS TTKYNFATFI PKFLFEQFSK YANLFFLFTS IIQQVPNVSP
     TNRYTTIGTL TIVLLVSAIK EIMEDLKRAG ADKELNNTKV LVLDASSGVF HSKKWIQVKV
     GDVVKINNEE PFPADLLLVS SSEPEGLCYI ETANLDGETN LKIKQAKSET SYLVNPRDLL
     SDLSRSEILS EQPNSSLYTY EGNLKNFGSV GDIPLSPDQL LLRGATLRNT QWIHGVVVFT
     GHETKLMRNA TAAPIKSTDV ERIINLQIIA LFSILIFLSF VSSIGNVIKI SVDSNELGYL
     MLGGTNKASL FFRNLLTYCI LFSNLVPISM FVTVEIIKFY QAYMIGSDLD MYYAETDTPT
     GVRTSSLVEE LGQIDYIFSD KTGTLTRNIM EFKCCSIGGK CYTEEITEDN QVQSHDGIEV
     GFYSFDNLHE HLKDTSSQQS AIINEFFTLL SACHTVIPET NDVDDTIKYQ AASPDEGALV
     QGAADLGYKF RVRKPKGISI RNTLTGVDSE YELLNICEFN STRKRMSAIF RCPDGVIRLF
     CKGADTVILE RLSDDGRPFV DATLSHLESF AAEGLRTLCI ASKIISEEQY ESWSTKYYEA
     STSLENRSEK LDEIAEVIEN DLFLLGATAI EDKLQDGVPE TIHTLQSAGI KIWVLTGDRQ
     ETAINIGMSC KLLSEDMNLL IINEETKNDT RLNLQEKISA IQEHQYDIED DTLESSLALV
     IDGHSLTFAL EPDLEDMFIQ LGSLCKAVIC CRVSPLQKAL VVKMVKRKKK DSLLLAIGDG
     ANDVSMIQAA HVGVGISGQE GMQAARSADV SIGQFKYLKK LLLVHGAWSY QRISNAILYS
     FYKNVTLYMT QFWFVFANCF SGQSIIESWT LTFYNVFFTV FPPFVMGVFD QFVNARLLDR
     YPQLYQLGQK KKFFNVPIFW GWIANGFYHS AIIFLCSIFI YQHGDQLSNG LVANNWTWGT
     AVFTTCTLTA LGKAALVVTM WTKYTLLAIP GSFLLWIGIF PAYATVAPMI NVSQEYRGVL
     KATYPSLTFW SMIFGVSVLC LLRDFAWKFF KRSYSPESYH YVQEIQKYNI QDYRPRMEQF
     QKAIRKVRQV QRIKKQRGFA FSQVDNQDQE KIVRLYDTTK KRGVFGELSE GN
//

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