ID A0A093NZQ2_PYGAD Unreviewed; 1080 AA.
AC A0A093NZQ2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
DE Flags: Fragment;
GN ORFNames=AS28_05381 {ECO:0000313|EMBL:KFW65527.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW65527.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW65527.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW65527.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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; KL224914; KFW65527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093NZQ2; -.
DR STRING; 9238.A0A093NZQ2; -.
DR Proteomes; UP000054081; 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:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
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; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR24092:SF57; PHOSPHOLIPID-TRANSPORTING ATPASE IF; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_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; SFLDS00003; Haloacid_Dehalogenase; 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|ARBA:ARBA00022840, 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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000054081};
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 49..64
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 271..294
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 325..344
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 832..853
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 885..905
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 935..957
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 969..992
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1004..1028
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1034..1060
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 16..72
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 816..1074
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW65527.1"
FT NON_TER 1080
FT /evidence="ECO:0000313|EMBL:KFW65527.1"
SQ SEQUENCE 1080 AA; 123499 MW; 5F76A7A46A56ADD5 CRC64;
DTRTIYIANR FPQHGHYVPQ KFADNRIISS KYTVWNFVPK NLFEQFRRVA NFYFLIIFLV
QLMIDTPTSP ITSGLPLFFV ITVTAIKQGY EDWLRHKADN EVNGAPVYVV RSGGLVKTRS
KNIRVGDIVR VAKDETFPVD LVLLSSDRVD GSCHVTTASL DGETNLKTHV AVPETAVLQS
VANLDKLVAV IECQQPEADL YRFVGRITVS QQTEEIVRPL GPESLLLRGA RLKNTKEIFG
VAVYTGMETK MALNYKSKSQ KRSAVEKSMN SFLIIYLIIL LFEAILSTIL KYAWQAEEKW
DEPWYNEKTE HERNSSKILR FISDFLAFLV LYNFIIPISL YVTVEMQKFL GSFFIGWDLD
LYHEETNQRA QVNTSDLNEE LGQVEYVFTD KTGTLTENEM QFRECSINGI KYQEVNGKLT
PEGFSEDSPD GNRHKEELFL KAVCLCHTVQ INADQTDGAD GPWHANGIAS PLEYYASSPD
EKALVEAASR VGVVFTGTSG DSMEVKSLGK SERYKLLHVL EFDPNRRRMS VIVESPSGEK
LLFTKGAESS ILPRSKSGEI DKTRIHVDEF ALKGLRTLCV AYRRFTPEEY QEIGKRLHEA
RTALQQREER LADAFNFIER DLELLGATGV EDKLQEKVQE TIEALRLAGI KVWVLTGDKH
ETAVSVSLSC GHFHRTMNIL ELVQHKLTSL FIVWATAYFI TKFNFFRHTN IKPTFLSLNR
IKEDHVIQHG LVVDGTSLSL ALREHEKLFM EVCKNCSAVL CCRMAPLQKA KVVRLLKTSP
EKPITLAIGD GANDVSMIQE AHVGIGIMGK EGRQAVRNSD YAIARFKFLS KLLFVHGHFY
YIRIATLVQY FFYKGSLQRN VCFITPQFLY QFFCLFSQQT LYDSVYLTLY NICFTSLPVL
IYSLFEQHVH PHVLQSKPVL YRDISKNAHL GFKPFLYWTI LGFFHAFVFF YGSYLLMGED
TSLLGNGQMF GNWTFGTLVF TVMVITVTMK MALETHFWTW INHFVTWGSI VFYFIFSLFY
GGIIWPFLHT QDMYFVFVQL LSSGSAWFAI ILIVVACLFL DVVKKVLYRH LQPTSTEKAQ
//
