ATCX_SCHPO
ID ATCX_SCHPO Reviewed; 1402 AA.
AC Q09891; Q9USC3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Putative phospholipid-transporting ATPase C24B11.12c;
DE EC=7.6.2.1;
GN ORFNames=SPAC24B11.12c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX 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., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 633-855, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAA91777.1; -; Genomic_DNA.
DR EMBL; AB027875; BAA87179.1; -; Genomic_DNA.
DR PIR; T38339; S62557.
DR RefSeq; NP_592849.1; NM_001018250.2.
DR AlphaFoldDB; Q09891; -.
DR SMR; Q09891; -.
DR BioGRID; 278059; 30.
DR STRING; 4896.SPAC24B11.12c.1; -.
DR iPTMnet; Q09891; -.
DR MaxQB; Q09891; -.
DR PaxDb; Q09891; -.
DR PRIDE; Q09891; -.
DR EnsemblFungi; SPAC24B11.12c.1; SPAC24B11.12c.1:pep; SPAC24B11.12c.
DR GeneID; 2541560; -.
DR KEGG; spo:SPAC24B11.12c; -.
DR PomBase; SPAC24B11.12c; -.
DR VEuPathDB; FungiDB:SPAC24B11.12c; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; Q09891; -.
DR OMA; QALRCGR; -.
DR PhylomeDB; Q09891; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-936837; Ion transport by P-type ATPases.
DR PRO; PR:Q09891; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; ISO:PomBase.
DR GO; GO:0005886; C:plasma membrane; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central.
DR GO; GO:0034202; F:glycolipid floppase activity; IDA:PomBase.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0034203; P:glycolipid translocation; IDA:PomBase.
DR GO; GO:0045332; P:phospholipid translocation; ISO:PomBase.
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 InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR InterPro; IPR026871; PLip_transp_ATPase.
DR PANTHER; PTHR24092:SF153; PTHR24092:SF153; 2.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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;
KW ATP-binding; Cell membrane; Endoplasmic reticulum; Magnesium; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1402
FT /note="Putative phospholipid-transporting ATPase
FT C24B11.12c"
FT /id="PRO_0000046239"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1066..1086
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1101..1121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1151..1171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1193..1213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1218..1238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1260..1280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 569
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
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
