YOOC_SCHPO
ID YOOC_SCHPO Reviewed; 1258 AA.
AC O94296;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Probable phospholipid-transporting ATPase C887.12;
DE EC=7.6.2.1;
GN ORFNames=SPBC887.12;
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 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 -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of phospholipids. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAA21897.1; -; Genomic_DNA.
DR PIR; T40737; T40737.
DR RefSeq; NP_596486.1; NM_001022406.2.
DR AlphaFoldDB; O94296; -.
DR SMR; O94296; -.
DR BioGRID; 277753; 1.
DR STRING; 4896.SPBC887.12.1; -.
DR iPTMnet; O94296; -.
DR MaxQB; O94296; -.
DR PaxDb; O94296; -.
DR PRIDE; O94296; -.
DR EnsemblFungi; SPBC887.12.1; SPBC887.12.1:pep; SPBC887.12.
DR GeneID; 2541239; -.
DR KEGG; spo:SPBC887.12; -.
DR PomBase; SPBC887.12; -.
DR VEuPathDB; FungiDB:SPBC887.12; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_3_0_1; -.
DR InParanoid; O94296; -.
DR OMA; QFWYSFQ; -.
DR PhylomeDB; O94296; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-936837; Ion transport by P-type ATPases.
DR PRO; PR:O94296; -.
DR Proteomes; UP000002485; Chromosome II.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; 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; ISO:PomBase.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; 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 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; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Endoplasmic reticulum; Golgi apparatus; Magnesium; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1258
FT /note="Probable phospholipid-transporting ATPase C887.12"
FT /id="PRO_0000314112"
FT TOPO_DOM 1..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..208
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..451
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..974
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 975..995
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 996..998
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 999..1019
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1020..1051
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1052..1072
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1073..1086
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 1087..1107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1108..1115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1116..1136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1137..1148
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 1149..1169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1170..1258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1258 AA; 142379 MW; 9128B7BFD692B022 CRC64;
MARDVDNKQN AKRISRDEDE DEFAGESMVG RTLDNPFLGE DEFEDIFGSE SQYISSSGQN
STNPFLADTR IENSPLGSES KANQLNKQGT NVNHIEIPLR DFNDPTQPES FLPPPKNTFT
SRIKKIKNLF KKEKKQVKPE DLGPRQIILN DYSANHFLHN AVSTCKYSAF TFLPKFLKEQ
FSKYANLFFL FTAVVQQIPG ITPVNRYTTI GPMLIVLSVS GIKEIMEDIK RKKQDQELNE
SPCYVLQGTG FVEKQWKDVV VGDIVKIVSE TFFPADLVLL SSSEPEGLCY IETANLDGET
NLKIKQALPE TAGLLKPVEL GQLSGEVKSE QPNNNLYTFD ATLKLLPSDR ELPLSPDQLL
LRGAQLRNTP WVYGIVVFTG HESKLMKNTT ETPIKRTSVE KQVNSQILFL LCIFVFLCFA
SSLGALIHRS VYGSALSYVK YTSNRAGMFF KGLLTFWILY SNLVPISLFV TFELVRYIQA
QLISSDLDMY NEETDTPAAC RTSSLVEELG QVGYIFSDKT GTLTRNQMEF RQCTIAGVAY
ADVIPEDRQF TSEDLDSDMY IYDFDTLKEN LKHSENASLI HQFLLVLSIC HTVIPEYDES
TNSIKYQASS PDEGALVKGA ASIGYKFLAR KPHLVTVSIF GKDESYELLH ICEFNSTRKR
MSIVFRCPDG KIRLYVKGAD TVIMERLASD NPYLQTTIHH LEDYATVGLR TLCIAMREVP
EDEYQRWSTV FETAASSLVD RAQKLMDAAE EIEKDLILLG ATAIEDRLQD GVPDTISTLQ
TAGIKIWVLT GDRQETAINI GMSCKLIDED MGLVIVNEET KEATAESVMA KLSSIYRNEA
TTGNVESMAL VIDGVSLTYA LDFSLERRFF ELASLCRAVI CCRVSPLQKA LIVKMVKRNT
GEVLLAIGDG ANDVPMIQAA HVGVGISGME GLQAVRSSDF SISQFCYLKK LLLVHGSWCY
QRLSKLILYS FYKNIALYMT QFWYAFCNAF SGQVIFESWS ISLYNVLFTV LPPVVIGIFD
QFVSAGQLFQ YPQLYQLGQR SEFFNLKRFW SWITNGFYHS LLLFLCSIAV FYYDGPNKDG
LASGHWVWGT TLYAAILATV LGKAALISNH WTQYTVIATL GSFLLWIVFM PIYAVAAPAI
GFSKEYYGII PHLYGNLKFW ASLLVLPTIA LMRDFVWKYS SRMYYPEEYH YVQEIQKYNV
TDYRPRIVGF HKAIRKIRQM QRMRKQRGYA FSQGEEDQSR ILDAYDTTHT RGAYGEMR
