ID A0A091FHA4_CORBR Unreviewed; 1121 AA.
AC A0A091FHA4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=N302_15308 {ECO:0000313|EMBL:KFO60830.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO60830.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO60830.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO60830.1};
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; KK718990; KFO60830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091FHA4; -.
DR STRING; 85066.A0A091FHA4; -.
DR Proteomes; UP000052976; 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; 2.
DR PANTHER; PTHR24092:SF33; PHOSPHOLIPID-TRANSPORTING ATPASE IH; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000052976};
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 56..74
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 282..305
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 336..355
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 952..974
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 986..1008
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1020..1044
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1050..1075
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 29..83
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 838..1090
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT COILED 608..639
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO60830.1"
FT NON_TER 1121
FT /evidence="ECO:0000313|EMBL:KFO60830.1"
SQ SEQUENCE 1121 AA; 128669 MW; 608FB5843945E6D9 CRC64;
CAGEENWVDS RTIYVGHHEP PPGAEAYIPQ RFPDNRIVSS KYTFWNFIPK NLFEQFRRIA
NFYFLIIFLV QLIIDTPTSP VTSGLPLLFV ITVTAIKQGY EDWLRHKADN AINQCPVHFI
QHGKLVRKQS RKLRVGDIVM VKEDEKFPCD LIFLSSSRGD GTCFVTTTSL DGESSHKTYY
AVQDTKAFRN EQEIDALHAT IECEQPQPDL YKFVGRINVY HDRNEPIARP LGSENLLLRG
ATLKNTEKIF GVAIYTGMET KMALNYQSKS QKRSAVEKSM NVFLVVYLCI LVSKALINTV
LKYAWQSEPF RDEPWYNQKT EPERKRNLFL QAFTDFLAFM VLFNYIIPVS MYVTVEMQKF
LGSYFITWDE EMFDEDTGEG PLVNTSDLNE ELGQIEYVFT DKTGTLTENN MEFVECCIEG
HVYVPHVICN GQILHDCTGI DMIDSSPGGS GKEREELFFR ALCLCHTVQV KDDDSVDGLK
KNRFSRRSCI YISSSPDEVA LVEGIQRLGY TYLRLKDNFM EILNRENNIE KFELLEVLSF
DSVRRRMSVI VKSSTGDIFL FCKGADSSIF PRVKEGKIDQ VRSRVERNAV EGLRTLCVAY
KKLTAEEYSN VQKLLQNAKL ALQDREKKLA EAYEKIERDF ILLGATAVED RLQEKAADTI
EALQKAGIKV WVLTGDKMET AAATCYACKL FRRNTQILEL TTKKIEEQNI LDVLFDLNKI
VVKPNGNLTR DTFSGLSTDM QDYGLIIDGA ALSLIMKTRP DGNSCSYREL FLEICRNCSA
VLCCRMAPLQ KAQIVKLIKL SDEHPITLAI GDGANDVSMI LEAHVGIGII GKEGRQAARN
SDYAIPKFKH LKKMLLVHGH FYYIRISELV QYFFYKNVCF IFPQFLYQFF CGFSQQTLYD
TAYLTLYNIS FTSLPILLYS LMEQHVSADI LKREPSLYRD VAKNALLRWR AFIYWTFLGV
FDAVVFFFGA YLLLDNTVVT SNGQVFGNWT FGTVVFTVLV FTVTFKLALD THYWTWINHF
MIWGSLVFYI IFSLLWGGII WPFLNYQRMY YVFMQMLSSG PAWLGIILLI TVSLLPDVLK
KVLCRQLWPT ATERIQTRHQ CLSVEQSTIF MLSQTSSSLS F
//
