ID G8BIW6_CANPC Unreviewed; 1753 AA.
AC G8BIW6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN OrderedLocusNames=CPAR2_403840 {ECO:0000313|CGD:CAL0000156625,
GN ECO:0000313|EMBL:CCE44581.1};
OS Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS parapsilosis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE44581.1, ECO:0000313|Proteomes:UP000005221};
RN [1] {ECO:0000313|Proteomes:UP000005221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2] {ECO:0000313|Proteomes:UP000005221}
RP GENOME REANNOTATION.
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA Berriman M., Butler G.;
RT "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT response of the pathogenic yeast Candida parapsilosis.";
RL BMC Genomics 12:628-628(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
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DR EMBL; HE605208; CCE44581.1; -; Genomic_DNA.
DR STRING; 578454.G8BIW6; -.
DR EnsemblFungi; CPAR2_403840-T; CPAR2_403840-T-p1; CPAR2_403840.
DR CGD; CAL0000156625; CPAR2_403840.
DR VEuPathDB; FungiDB:CPAR2_403840; -.
DR eggNOG; KOG0206; Eukaryota.
DR Proteomes; UP000005221; Chromosome 4.
DR GO; GO:0070867; C:mating projection tip membrane; IEA:EnsemblFungi.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IEA:EnsemblFungi.
DR GO; GO:0005802; C:trans-Golgi network; IEA:EnsemblFungi.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140345; F:phosphatidylcholine flippase activity; IEA:EnsemblFungi.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:EnsemblFungi.
DR GO; GO:0140346; F:phosphatidylserine flippase activity; IEA:EnsemblFungi.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 2.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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 NCBIfam; TIGR01652; ATPase-Plipid; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF174; PHOSPHOLIPID-TRANSPORTING ATPASE DNF3-RELATED; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000005221};
KW Translocase {ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT TRANSMEM 580..601
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 621..644
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1439..1464
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1470..1488
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1500..1525
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1545..1565
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 261..318
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1325..1575
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1753 AA; 198275 MW; 04F673A72EB0A607 CRC64;
MIEESSSSKE HNDGGENTND SYMPSSQPNS PQQPKDDMDN VATHASVQEA NSVDNSGNNN
NNNNNNNNNT LSVPNPSHTR RKRGLSLRSQ LFNKAFNLHQ EKSLPDNIDQ TTTATKPLDN
IELQPISTRL HTAPPQINVD ESPDPLPVYE SSSSFANKYE PYNVLESHLT KSTTHLTIDS
KRSSISSSSF LSKRQRLHNT SQNRFWRRLN KLKNKLLGVK VSQSTECGRI IPLSVNPNGV
NDYYQDEYYC PKSKSYIDER TNDPYINNLI TSSKYTVYSF LPKQLRAQFS KIANCYFMVV
AIMQMIPGWS TTGQYTTIIP LCIFMSISMA REGFDDWKRH GHDKEENSKL TTVIREDEEL
SNFDTHSINT ILTETISVVP GRVSNSAAGL PSLSANSSLS DLEDSLSSSE NLSFTNADAM
RRYNLKEMST KWKNVKVGDI VKISENEWFP ADVILIATSG DDLQEAFVET MALDGETNMK
SKFPHPEISK RARTAPGLKN LYTLITTEDP NIDLYNFEAS FYMNEQVYPL GPENVVYRGS
ILRNTESVLG IVVFTGEETK IRMNNIKNPR TKAPKLQKNI NYIVIFMVLV VVMLSAFSTM
AQRLKYNQNK SKAWYLYEED AGVAATLMGF IIMYNTLIPL SLYVTMEIIK VMQLCFLQFD
IDMYDPKTNT PADAKTATIL EELGQVSYIF SDKTGTLTDN KMIFRKLSVC GVSWLHDLDL
MVSERENPGD QDVVSLVQRQ SMHIPKSPSQ QGQNCAGANN ANNRFSTTSI VRESIDIRQS
GLSAKTWVST AQPHKVQDTL NTLQLIRHLQ TYPQTLFSRR AKFFLLSLAL CNTCSPIKQA
QKKFKISDSC SSLEEISDID DDASITYQST SPDEIALVQA ARDLGYVIFD RQSDKLKIRT
YPEGFDNDPV VEEYQVLDVI EFSSARKRMS VVVKFPDGRL ALICKGADNV ILEHLRNSKL
AQEKARDISI QSTERKMQEA DVVLQSRFSQ DLESRKSGFS LRQSLNLGEP RMNTIDNALM
GLDEEEEEEL ASIANQARKS LHLQQAKKYS LEDEDVSPNE QQTNTGGFHL QSIPSDKLVL
NDEFVIEKTL EHIEEFSIEG LRTLLYSFKW LTEREFNEWH TEYADAKTSL KDRAQLVEDV
GGKIEMNLEL LGATAIEDKL QDGVSEAIVK LRRAGIKMWM LTGDKRETAI NIGYSCRLIK
DYSSVTILSI DEGKQAVADK ITSFLKDIQG GKIAHSVLVI DGGTLTEIEN DTRLSSRFFE
LCVEVDSTVC CRASPSQKAN MVSSVRSLRK RAVTLAIGDG ANDIAMIQSA DIGVGITGRE
GLQAARSADY AIAQFRFLLK LLLVNGRYNY VRTSKFVLCT FYKELLFYLT QCIYQRNTLF
SGSSMYESWS LSMFNTLFTS LPVLCIGMFD KDLKPATLIA VPELYSKGRL YQAFNLRVFL
SWMILATLQS VGVEFLALYI WGFTGLRDNT TFALGSLVFS VLVIIINAKC TLMEMQNRQW
LAFASFIISV GGLAVWNVLI MFLYRSKEST IFFVSYGLTT WGLDQSWWAA LLLLVTVPLF
FDILIKVFKF MFSPSDDQIF QVYEKDMKWR KLFEQSAYKE LFQGWMFPRD PSTTKTHIFK
LLSKIGIHID LKPDKNIELA DNEEDEIYSQ SALNRKRAGT NPMDHELPAS GDGVGVYAND
LQPHDVVDAD GYEILPSGKR VKVKTRKERS WSLPKALRIK KRKSSMDSDE DVNAIIDNRL
KNLRDEEEGR QQD
//
