ID A8NE20_COPC7 Unreviewed; 1502 AA.
AC A8NE20;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=CC1G_12291 {ECO:0000313|EMBL:EAU88889.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU88889.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU88889.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAU88889.2}.
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DR EMBL; AACS02000002; EAU88889.2; -; Genomic_DNA.
DR RefSeq; XP_001832922.2; XM_001832870.2.
DR STRING; 240176.A8NE20; -.
DR GeneID; 6009411; -.
DR KEGG; cci:CC1G_12291; -.
DR VEuPathDB; FungiDB:CC1G_12291; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; A8NE20; -.
DR OMA; CDRPDTN; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:RHEA.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF153; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000001861};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT TRANSMEM 94..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 116..134
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 407..432
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 452..475
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1145..1165
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1177..1197
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1218..1246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1258..1278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1290..1311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1331..1351
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 55..119
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1110..1360
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 187..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1416..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1502 AA; 168143 MW; 0ED1391873463AB8 CRC64;
MKRARKVAEW YDKWAAWKVE DLFSKKREPG PRRTVFINEN LPDSYRDSKG RVKKDHIYAT
NQVITSKYTI LTFIPRNLLE QFRRIANMYG PPTFVSRVEF FLFIAVLQFF SRFRTISPGL
VILPLLIVLS ITAAKDGYED IKRHQSDRQV NHTLVRVLCG GGWINPNVME KKAKTFVRGL
VPSRMRKRGS KVKNVNPKGE ELAGVTSNDP APETPGVEFD DPEETTTHSS HHLPHVFHHG
TNKEDTDRPH WRKNAWEDLA VGDFVKIMDN ESLPADILIC STSEDENVAF VETKNLDGET
NLKSRNAVPA LTHIRSAADC ASPHNSFRVD CDRPDVNMYR LNAAVRVGQD MFPVDMQNVL
LRGTVLRNTK WVIGVVIYTG EDTRIVMNAG GTPSKRSKVE RQMNPQVFIN LLVLAVMAIV
CGVVDSILQH RYLGSEAPWL YDADRPGDNP SVNGVITFFF ALITFQNIVP ISLYISIEFV
RTCQAAFIYF DKQIFYEKTE QPTIARSWNL SDDLGQVEYI FSDKTGTLTQ NAMVFQKCSI
GGKVYNGDPS PEDELPADDL KAASAIKELP DIAIPKKLAG LSTEKELKIL SSTHVQLTDS
GSAGTSSVKR DSKLAGAENV PHPLEATALK ARVHFHDAEL AQDLRDAVSA EPGTPGASHA
RTLNGFFSVL SLCHTVLANV DPTTGTIEYK SQSPDEAALV QAAADMGFVF RGREREVLLL
QTPFSTLTAE TQSPRSSSSS KEKQSISSEP RMEGLERYEL LNILEFTSAR KRMSVIVRKL
DSDDSRLFLL CKGADNVIFE RLKPGYAEDL KEETEKHLDE FAAQGLRTLT LAYKVIPEDV
YQSWSERYHE ATVSLDDREE KVERVSDEIE HDLRLLGATA IEDRLQDGVP ETIADLKEAG
IKIWVATGDK LETAIAIGHS TNLIGRDSNI IVIRGGNEGR PVYDQIMYAI EEFFPGSGIV
DEQGKVRDID DAPAKSPKSA RRNSLFSNPP QSPGAGGGPL RRFDTGISSI VGAGNGERPG
GFVLVIDGGA LSVALSDAEH KNILLQLAML CEGVICCRVS PLQKALIVRL VKDGIGAMTL
AIGDGANDVS MIQAADVGVG ISGEEGLQAV NSSDYAIAQF RFLKRLLLVH GHWSYYRNGN
MILNFFYKNI VCIGVLWWFQ IYSGWSSNYV LEYTYLLFWN SFWTIAPVIA IGLFDRLADD
DLLMQFPELY RFGREGRWFG FGLFTVFMLD GVMQSAIIFF LILYAYVLVS SRKDGWDVTQ
YEFSTTMAFS AVFTANFFNG LNTNTWTAWV FFAVFFGDAF IWIYTAIYNS ISPGWFVTPV
WGNNNLLFES AYYWLCLPLT ILLCLLPRYI YKAYRAGYHP DDIDHLRYAR KFHPDIDLRH
ELSDEKGEGV ALGALRRSTS MHSRTTARTE SIASMPRPSM DYRSSSRTDM STGVTSHHRG
FDFSMEEGGV AIQRMQTNLS ERRQSRPSLA PVPESPQKRK MLTLPRSLLR RKGSNAQDAS
QS
//
