ATCZ_SCHPO
ID ATCZ_SCHPO Reviewed; 1367 AA.
AC O36028;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Putative phospholipid-transporting ATPase C4F10.16c;
DE EC=7.6.2.1;
GN ORFNames=SPAC4F10.16c;
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: Catalyzes the hydrolysis of ATP coupled with the transport of
CC phospholipids. {ECO:0000250}.
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 {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
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; CAB11719.1; -; Genomic_DNA.
DR PIR; T38820; T38820.
DR RefSeq; NP_594759.1; NM_001020186.2.
DR AlphaFoldDB; O36028; -.
DR SMR; O36028; -.
DR BioGRID; 279941; 8.
DR STRING; 4896.SPAC4F10.16c.1; -.
DR PaxDb; O36028; -.
DR PRIDE; O36028; -.
DR EnsemblFungi; SPAC4F10.16c.1; SPAC4F10.16c.1:pep; SPAC4F10.16c.
DR GeneID; 2543523; -.
DR KEGG; spo:SPAC4F10.16c; -.
DR PomBase; SPAC4F10.16c; -.
DR VEuPathDB; FungiDB:SPAC4F10.16c; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_0_1_1; -.
DR InParanoid; O36028; -.
DR OMA; CETALDQ; -.
DR PhylomeDB; O36028; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-936837; Ion transport by P-type ATPases.
DR PRO; PR:O36028; -.
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; ISO:PomBase.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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:SF91; PTHR24092:SF91; 1.
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; Lipid transport; Magnesium; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1367
FT /note="Putative phospholipid-transporting ATPase C4F10.16c"
FT /id="PRO_0000343137"
FT TOPO_DOM 1..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..177
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..531
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..1091
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1092..1112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1113..1124
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1125..1145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1146..1174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1175..1197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1198..1212
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1213..1233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1234..1240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1241..1261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1262..1276
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1277..1297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1298..1367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 34..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 600
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1367 AA; 154282 MW; 4DCFD8A7479465EB CRC64;
MPSLINFDAI SSLKSSLHGL SICAFNHLHH VPQHNGSLAH EGPTNQTDYS SRHHESQFSQ
EAHAEQRSRD DEEANSFEGS CNNSDQSWTS RVTSKKNEAG TESGDASVRR IYVTSIPEEH
RHLPSQWFPS NKIRTTKYTP VSFIPKNLWN QFKNIANAFF LFVTLLQCIP LFCPEHLGLS
FIPLSVILLT TAIKDGIEDY RRCVLDKKFN NTLTWKLVGF NNANALGEHI GLWRKLKKFI
SHTVADMSYC LKNSGISSGL ATLTVDNISH RHSLESDSAF TLSSVSQDSL EIHEIGNSGP
SNSFSVIQEQ STGSSNAKFE RVCRKSLLVG DIVKVLADEA IPADLLILST ENSNGVCYVE
TKNLDGETNL KDKYALCSTK CCKSEYRCSA ASFWVECEQP HADLYSLNGV VKAPGAVQSP
SESTNGRKIH EEPFSISNVL LCGCTLRNSK WVIGLVLYTG SETRIQKNRG LTPSKRSRIT
RDLNWTIILN FLLLFAMCLF SGVLRSIYSA QNNSARVFEL SKNSNTAPAH GIISIFTSLI
LFQNLVPISL YITMDIVRSI QSYFIFSDRE MYDEKLDCPC SPKSWNISDD LGQIEYIFSD
KTGTLTQNIM SFKKCSINGI RYGKSHNEDT CIKKRRNLNY NENLSCKVDL DKKKMLETLS
LSDSPNPESI TFISSKFVDH LQSNENYIQT EACFEFFKAL ALCHSVVTDV QDETLIYNAQ
SPDEEALVKV ARDFGFTLLN TKNRRYTIRI RGENKNFRVL DIIPFTSTRK RMSVIIRDED
GIIHLICKGA DTVIFPRLSS GQNNIIEKTK KHLASFSSEG FRTLCIARRT IDKQDYLEWK
VNFNEANSAI HERNEKVSKV SEMIEQELEL LGGTAIEDKL QENVPETIAL LAIAGIKLWV
LTGDKVETAI NIGYSCNLLD PNMTIFRIDA NSFGALEEVE AFIRNTLCFN FGYMGTDEEF
RFLLKDHSPP SPKHAIVIDG DALNFVLSEQ VSFLFLMLCK QCKTVLCCRV SPSQKAAVVA
LVKKSLNVVT LAIGDGANDV SMIQEADVGV GIKGVEGQAA SMSADYAIGQ FSFLGRLLLV
HGRWDYKRMS QMISFFFYKN VIWTFILFWY QFYNEFDGNY IFDYTYVMLF NLLFTSLPVI
IAGCFDQDVD ASVSMKNPSL YQRGILGLEW NGKRFWSYML DGIYQSLVCF GVALFVFKFG
DFVSWTGRNI ECIEDIGLFI SSPTIFVINI FILMNQERLN LISLITWMFS IGVFWIWTFI
YSEVGPSYAF HKSASRTCQT FGFWCVTVLT IALCLLPRFS YICLQKLFYP RDIDLLRRRL
CAKSDDETSS SSSFATDIEM CEQCNDPLSS KKNSGIVTSV SFDDSNK
