ID A0A091XDS5_OPIHO Unreviewed; 1134 AA.
AC A0A091XDS5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=N306_13399 {ECO:0000313|EMBL:KFR11426.1};
OS Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC Opisthocomus.
OX NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR11426.1, ECO:0000313|Proteomes:UP000053605};
RN [1] {ECO:0000313|EMBL:KFR11426.1, ECO:0000313|Proteomes:UP000053605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR11426.1};
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; KK734915; KFR11426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091XDS5; -.
DR STRING; 30419.A0A091XDS5; -.
DR PhylomeDB; A0A091XDS5; -.
DR Proteomes; UP000053605; 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; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR24092:SF225; PHOSPHOLIPID-TRANSPORTING ATPASE IA; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_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|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:UP000053605};
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 281..305
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 325..348
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 837..857
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 863..881
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 910..928
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 948..967
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 979..999
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1019..1039
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 26..87
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 797..1048
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFR11426.1"
FT NON_TER 1134
FT /evidence="ECO:0000313|EMBL:KFR11426.1"
SQ SEQUENCE 1134 AA; 128075 MW; 5A8DFE0EA33333BA CRC64;
TGYEKTDDVS EKTSLADQEE LRTIFINQPQ LTKFCNNHVS TAKYNIITFL PRFLYSQFRR
AANAFFLFIA LLQQIPDVSP TGRYTTLVPL LFILAVAAVK EIIEDIKRHK ADNAVNKKQT
QVLRNGAWEI VHWEKVDVGD IVIIKGKEYI PADTVLLSSS EPQAMCYIET SNLDGETNLK
IRQGLPLTSD IKDIESLMRL SGRIECESPN RHLYDFVGNI RLDGHGTVPL GSDQILLRGA
QLRNTQWVHG IVVYTGHDTK LMQNSTSPPL KMSNVERITN IQILILFCIL IAMSLICSIG
SAIWNRRHTG RDWYLDLNYG GASNFGLNFL TFIILFNNLI PISLLVTLEV VKFIQAYFIN
WDIDMHYEPT DTAAMARTSN LNEELGQVKY IFSDKTGTLT CNVMQFKKCT VAGVAYGQGS
QNGEEKMFSD LSLLENLQSN HPTAPVICEF LTMMAVCHTA VPEREGDKII YQAASPDEGA
LVRAARHLRF VFTGRTPDSV IIESLGQEER YELLNVLEFT STRKRMSVIV RTPLGKLRLY
CKGADTVIYD RLAESSKYKE ITLKHLEQFA TEGLRTLCFA VAEISEGDYQ EWLDVYHRAS
TAIQNRALKL EESYELIEKN LQLLGATAIE DKLQDKVPET IETLMKADIK IWILTGDKQE
TAINIGHSCK LLRKNMGLIV INEGCLDGTR ETLSHHCSTL GDALRKENDF ALIIDGKSLK
YALTFGVRQY FLDLALSCKA VICCRVSPLQ KSEVVEMVKK QVKVVTLAIG DGANDVSMIQ
TAHVGVGISG NEGLQAANSS DYSIAQFKYL KNLLLVHGAW NYNRVAKCIL YCFYKNIVLY
IIEIWFAFVN GFSGQILFER WCIGLYNVMF TAMPPLTLGI FERSCRKENM LKYPELYKTS
QNALDFNTKV FWVHCLNGLF HSFILFWFPL KALQHGTVFG NGKTSDYLLL GNTVYTFVVL
TVCLKAGLET SYWTLFSHIA IWGSIALWVV FFGIYSSLWP VIPMAPDMSG EAAMMFSSGV
FWMGLLCIPM TALLFDVVYK VVKRATFKTL VDEVQELEAK SEDPGAVVHG KSLTERAQLL
KNVFKKNHVN LYRSDSLQQN LLHGYAFSQD ENGIVSQSEV IRAYDTTKQR PEEW
//
