ID   ATCX_SCHPO              Reviewed;        1402 AA.
AC   Q09891;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-JUN-2009, entry version 70.
DE   RecName: Full=Putative phospholipid-transporting ATPase C24B11.12c;
DE            EC=3.6.3.1;
GN   ORFNames=SPAC24B11.12c;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(In) = ADP +
CC       phosphate + phospholipid(Out).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       family. Type IV subfamily.
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DR   EMBL; CU329670; CAA91777.1; -; Genomic_DNA.
DR   PIR; T38339; S62557.
DR   RefSeq; NP_592849.1; -.
DR   GeneID; 2541560; -.
DR   KEGG; spo:SPAC24B11.12c; -.
DR   NMPDR; fig|4896.1.peg.2819; -.
DR   GeneDB_Spombe; SPAC24B11.12c; -.
DR   OMA; Q09891; FIRIRAN.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000589-MON; -.
DR   BRENDA; 3.6.3.1; 653.
DR   ArrayExpress; Q09891; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:GeneDB_SPombe.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015662; F:ATPase activity, coupled to transmembrane m...; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004012; F:phospholipid-translocating ATPase activity; IEA:EC.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-reg.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_phosphor_site.
DR   InterPro; IPR006539; ATPase_P-typ_Plipid-transl.
DR   InterPro; IPR013200; HAD-SF_hydro-like_3.
DR   PANTHER; PTHR11939; ATPase_P; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF08282; Hydrolase_3; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Hydrolase; Magnesium; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Transmembrane.
FT   CHAIN         1   1402       Putative phospholipid-transporting ATPase
FT                                C24B11.12c.
FT                                /FTId=PRO_0000046239.
FT   TRANSMEM    109    129       Potential.
FT   TRANSMEM    135    155       Potential.
FT   TRANSMEM    457    477       Potential.
FT   TRANSMEM    501    521       Potential.
FT   TRANSMEM   1066   1086       Potential.
FT   TRANSMEM   1101   1121       Potential.
FT   TRANSMEM   1151   1171       Potential.
FT   TRANSMEM   1193   1213       Potential.
FT   TRANSMEM   1218   1238       Potential.
FT   TRANSMEM   1260   1280       Potential.
FT   ACT_SITE    569    569       4-aspartylphosphate intermediate (By
FT                                similarity).
SQ   SEQUENCE   1402 AA;  159356 MW;  E8495A7598B3020B CRC64;
     MESVEEKSKQ RRWLPNFKAL RLKVYRLADR LNIPLADAAR VELEEYDGSD PQSLRGLQKL
     PRTLYFGLPL PDSELDDTGE AKRWFPRNKI RTAKYTPIDF IPKNIFLQFQ NVANLFFLFL
     VILQSISIFG EQVNPGLAAV PLIVVVGITA VKDAIEDFRR TMLDIHLNNT PTLRLSHYQN
     PNIRTEYISY FRRFKKRISA LFRVFLAKQE EKKRAKRLND AVPLEDMAGS ESRPSYDSIF
     RESFEAKRSF EDSKGKVPLS ALDGTATILQ SRPMDIIDYE AEATGECHFK KTYWKDVRVG
     DFVKVMDNDE IPADIVIINS SDPEGICYIE TKNLDGETNL KMRHALTCGK NVVDEASCER
     CRFWIESEPP HANLYEYNGA CKSFVHSEAG GSDTSQTVSE PISLDSMLLR GCVLRNTKWV
     IGVVVFTGDD TKIMLNSGAP PLKRSRITRN LNWNVYLNFI ILFSMCFVCA VVEGIAWRGH
     SRSSYYFEFG SIGGSPAKDG VVTFFTGVIL FQNLVPISLY ISIEIVKTIQ AIFIYFDKDM
     YYKKLKYACT PKSWNISDDL GQVEYIFSDK TGTLTQNVME FKKCTINGVA YGEAFTEAMA
     GMAKREGKDT EELTLQKQSF IERDRMQMIS QMRNMHDNKY LVDDNLTFIS SQFVHDLAGK
     AGEEQSLACY EFFLALALCH SVVADRVGDR IVYKAQSPDE AALVGTARDV GFVFLDQRRD
     IMVTRALGET QRFKLMDTIE FSSARKRMSV IVKGPDNRYV LICKGADSII FERLEPNEQV
     ELRKTTSEHL RIFALEGLRT LCIAKRELTE EEYYEWKEKY DIAASAIENR EEQIEEVADL
     IESHLTLLGG TAIEDRLQEG VPDSIALLAQ AGIKLWVLTG DKMETAINIG FSCNLLDAGM
     DMIKFDVDQE VSTPELEVIL ADYLYRYFGL SGSVEELEAA KKDHDTPSGS HALVIDGSVL
     KRVLDGPMRT KFLLLCKRCK AVLCCRVSPA QKADVVQLVR ESLEVMTLAI GDGANDVAMI
     QKADIGVGIV GEEGRAAAMS ADYAIGQFRF LSKLVLVHGR WDYNRVAEMV NNFFYKSVVW
     TFTLFWYQIY NNFDANYLFD YTYVMLFNLI FSSLPVIVMG VYDQDVNADL SLRIPQLYKR
     GILQLNSARK IFIGYMLDGF YQSVICFFFS FLVINNVTTA AQNGRDTMAV QDLGVYVAAP
     TIMVVDTYVI LNQSNWDVFS IGLWALSCLT FWFWTGVYSQ SLYTYEFYKS ASRIFRTPNF
     WAVLCGTIVS CLFPKFLFMT TQKLFWPYDV DIIRESYRTK RLHELDEEEE IENAEQSPDW
     ASSTLQVPFN ASSSSLATPK KEPLRLDTNS LTLTSSMPRS FTPSYTPSFL EGSPVFSDEI
     LNRGEYMPHR GSISSSEQPL RP
//