ID C4R1N5_KOMPG Unreviewed; 1443 AA.
AC C4R1N5;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN OrderedLocusNames=PAS_chr2-1_0756 {ECO:0000313|EMBL:CAY69409.1};
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY69409.1, ECO:0000313|Proteomes:UP000000314};
RN [1] {ECO:0000313|EMBL:CAY69409.1, ECO:0000313|Proteomes:UP000000314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
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}.
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DR EMBL; FN392320; CAY69409.1; -; Genomic_DNA.
DR RefSeq; XP_002491689.1; XM_002491644.1.
DR STRING; 644223.C4R1N5; -.
DR EnsemblFungi; CAY69409; CAY69409; PAS_chr2-1_0756.
DR GeneID; 8198374; -.
DR KEGG; ppa:PAS_chr2-1_0756; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_0_1_1; -.
DR InParanoid; C4R1N5; -.
DR OMA; FKVAREC; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000000314; Chromosome 2.
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 GO; GO:0071705; P:nitrogen compound transport; IEA:UniProt.
DR GO; GO:0045332; P:phospholipid translocation; IEA:UniProt.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
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:SF150; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 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:UP000000314};
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 88..112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 118..137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 441..464
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 484..509
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1078..1097
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1109..1130
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1160..1179
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1199..1219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1226..1246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1266..1286
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 60..118
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1046..1295
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1443 AA; 163909 MW; AC1A11FA3FD99C1C CRC64;
MSFDTVVSGK HGGLTEKLRL IAYKYGIPGV PPPESVSNEL RAQSRKIYIN TPLPSDMYDE
KGHLKSHYAR NKIRTTKYTP TTFLPKNLFF QFTNIANSYF LLIVILGAFQ IFGVPNPVLS
AVPLIVIVVI TGVKDAFEDY RRSVSDRQLN DSRIHLLTGM ENHNVNKDSV TPWRRFKKLC
TRATRLTGRL MANIFRRNKS AASDSVENKR KDKESIRSLE SITTIPTNRN SLSKIPTKER
ITLSSMRKSF DNRSRRTAEV VQGTCSNPTV EPTFKPKFRT DFWKSVEVGN FVRVRNNEEV
PADIVIIATS DAEGTCFVET KNLDGETNLK NRTALHCGEG IRHAHDLERA QMMIEVEPPN
VHLYSFKGAC YFSTYDLQTG EKLEDRSEPI TNENVLLRGC ALRNTKWVIG VVVYTGPETK
VMLNSGITPT KKSRISKELN LSVIVNFVVL FVLCFVSAVV NGVFYNESDT SRIYFDFEPY
VDSAAGNGVV TFFVALIIYQ TLVPISLYIS IEIIKTVQAY FIYADVKMYY PKLDYPCVPK
SWNISDDLGQ IEYIFSDKTG TLTQNVMQFK KCTVAGKSYG LAYTEAQQGM DKRKGVNIVD
EVDKWRTKIS RDKQEMLDLL KDWTSNELDE NDLTFISSDF VKDLKTQKAS KDFSYNERLM
TALALCHTVV TEDDADKPGR PIFNAESPDE AALVSAARDI GIVFQERTRK GVLVSKFGNA
PSEFRLLEII PFNSTRKRMT TIMEIPPAYS PSRETEIMLY TKGADNVIYP RLRKDQDENI
VNQTALHLEQ FAEEGLRTLC VAEKKLESEY FKEWQQRYNA ACSSVSDNRE ALIDQLSEEI
ECNLTLLGGT AIEDRLQDGV PDSIAILAQA GIKLWVLTGD KVETAINIGF SCNLLTNEMK
LLVLQPQEKD NQDSDTLCKY FDGLISRYLS EEFNMNGSEE ELKEAKKVHT PAVDNYAIIV
DGAALAVIFN ESTGSLIRKF LLLCKQSKSV LCCRVSPAQK AQIVKMVKNL LGVMTLAIGD
GANDVAMIQA ANVGVGIAGE EGRQAAMSSD YAFGQFRFLT RLLLVHGRWS YKRLAEMIPC
FFYKNVTFTF TLFWYGIYNN FDGSYLFEYT YLMFYNLAFT SLPVIFLAIL DQDVSETVSL
LVPQLYRTGI LRLEWSQYKF FYYMLDGLYQ SVISFFFPYL VYHTGSFASA NARQIDHRFW
IGLFCAHISV VSCNIYVFLQ QYRWDYLSTI IVLLSILVIF FWTGVWSAGT ISGEFYKAAP
QVFGSTSFWA CFFVGVLVCV LPRFCYDNVK RVMKPRDIDI IRERVKLGDY RLFPERYDPT
DFNDVEVHRK MLSDNHSSLA SDSLDQANSA ELADLEKNDI EANLKNEIPK ESKGIQRALR
SIGHSIRHPT LTPPSRLDIL RKKSLENGSI TSLERIRTSH ELPGLTRAET LMSTYSYLSE
NRR
//
