YD56_SCHPO
ID YD56_SCHPO Reviewed; 1033 AA.
AC Q10309;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Putative phospholipid-transporting ATPase C6C3.06c;
DE EC=7.6.2.1;
GN ORFNames=SPAC6C3.06c;
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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; CAA93618.1; -; Genomic_DNA.
DR PIR; T39030; T39030.
DR RefSeq; NP_593720.1; NM_001019151.2.
DR AlphaFoldDB; Q10309; -.
DR SMR; Q10309; -.
DR BioGRID; 279357; 17.
DR STRING; 4896.SPAC6C3.06c.1; -.
DR iPTMnet; Q10309; -.
DR SwissPalm; Q10309; -.
DR MaxQB; Q10309; -.
DR PaxDb; Q10309; -.
DR PRIDE; Q10309; -.
DR EnsemblFungi; SPAC6C3.06c.1; SPAC6C3.06c.1:pep; SPAC6C3.06c.
DR GeneID; 2542915; -.
DR KEGG; spo:SPAC6C3.06c; -.
DR PomBase; SPAC6C3.06c; -.
DR VEuPathDB; FungiDB:SPAC6C3.06c; -.
DR eggNOG; KOG0210; Eukaryota.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; Q10309; -.
DR OMA; IAITTWH; -.
DR PhylomeDB; Q10309; -.
DR Reactome; R-SPO-936837; Ion transport by P-type ATPases.
DR PRO; PR:Q10309; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0000139; C:Golgi membrane; ISO:PomBase.
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; IBA:GO_Central.
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:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0045332; P:phospholipid translocation; ISO:PomBase.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1033
FT /note="Putative phospholipid-transporting ATPase C6C3.06c"
FT /id="PRO_0000046319"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 768..788
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 843..863
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 913..933
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 939..959
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 965..985
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 992..1012
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 408
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 770
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 774
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1033 AA; 116588 MW; D57C467427D0C6D6 CRC64;
MDSRLNRIQS KMKLWIKDKN LSNPSIPLKV LNKSFRSSRQ SSVSNGHGLY SLDRDETESL
MSSHEASNAG ISLDSSFRVI QVGQPEPQYG NNAVTNTKYD LFTFLPKCLY EQFRYFYNMY
FLLVSLSQLI PPLKIGYLST YIAPLIFVLL ITLTKEAVDD LKRRRRDSYA NNEIYTVNDS
PCAAQNIQAG DVVYIAKDQR IPADMILLET TVGNEAFIRT DQLDGETDWK LRIPCSNQHT
EGIVHADAPI KSVHHFYGTF TLNNQKRPIS VDHTLWANTV LASDGVYGVV VYTGKDTRQS
MNSSKAKTKV GLLEKEINFY SKILCTFVLV LSIGLTFSHG IKTDWYISVF RYLILFSSII
PINLRVNLDL AKIVHSKNTE SDPNLPGVVV RSSNIPEELG RIEYVLTDKT GTLTQNEMEM
KKLHVGTMGF SAESMDVVQA CIQNYSTPIP LSEDSKTLVR NLVLALSLCH NVTPSKGHDG
VVSYQAASPD EVAIVKWTST LGLVLTNRTR DAITLNNNVY KILNIFPFKS ETKRMGIIVQ
SPDEKITFYL KGADSIMQNF VKPSFWLEEE CGNLAREGLR TLVVAKKDLS AEEYSAFSLA
HSDASLSFSN SRDKKMEEIV SRYLENDMDL LGLTGVEDKL QKDVKITLEL LRNAGIHVWM
LTGDKVETAR CIAISSRLVS RGQYIHTINQ LSSREEAHNH LLTLRNKPDS CLIIDGESME
FCIGYLQNEF IDIVSDLSSV VICRCTPTQK ANMTRLIQEK KQASVCCIGD GGNDVGMIQV
ANVGIGIVGK EGQQASLAAD YSVKEFSHVS RLLLWHGRIS YKQTSKLAMF VIHRGLLISV
CQVVYSVISA FEPIALFQGL LLVGYSTMYT MLPVFSIVYD RDVSEKLVFL FPELYKEMRE
QKCFSYKNFI SCVLISVYQG LIIQLFTFYL IGFEEEGKML AVCFSCLIFN ELIMVALQIN
TWEQTIVMSE LLTLMMYILS VPFLTNYFEL KFLLGLKFYW VSALILFISL LPVWCGKALK
RKLKPSSYAK LQR
