ID A0A672VAV6_STRHB Unreviewed; 1164 AA.
AC A0A672VAV6;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS Strigops habroptila (Kakapo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Strigops.
OX NCBI_TaxID=2489341 {ECO:0000313|Ensembl:ENSSHBP00005023628.1, ECO:0000313|Proteomes:UP000472266};
RN [1] {ECO:0000313|Ensembl:ENSSHBP00005023628.1, ECO:0000313|Proteomes:UP000472266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jarvis E.D., Howard J., Rhie A., Phillippy A., Korlach J., Digby A.,
RA Iorns D., Eason D., Robertson B., Raemaekers T., Howe K., Lewin H.,
RA Damas J., Hastie A., Tracey A., Chow W., Fedrigo O.;
RT "Strigops habroptila (kakapo) genome, bStrHab1, primary haplotype, v2.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSHBP00005023628.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A672VAV6; -.
DR Ensembl; ENSSHBT00005028137.1; ENSSHBP00005023628.1; ENSSHBG00005019815.1.
DR GeneTree; ENSGT00940000161917; -.
DR Proteomes; UP000472266; Chromosome 3.
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; 1.
DR PANTHER; PTHR24092:SF52; PHOSPHOLIPID-TRANSPORTING ATPASE FETA; 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|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:UP000472266};
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 67..89
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 267..290
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 310..336
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 867..885
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 897..917
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 946..966
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 986..1004
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1016..1039
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1059..1080
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 18..73
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 833..1087
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1095..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1164 AA; 132800 MW; D7BBC06CFCFD09BC CRC64;
MFCSWEDLQL LWGCPDKRCF KNNSIKTSKY NFFTFLPLNL FEQFQRIANA YFLFLLILQL
IPQISSLAWF TTVVPLVLVL AVSGVKDAID DFNRHKSDKH VNNRPVQVLI NGMLKNEKWM
NVQVGDIIKL ENNNFVTADL LLLSSSEPHS LTYIETAELD GETNLKVKQA LTVTAELGED
LQKLTEFNGE VKCEAPNNKL DKFTGTLTLQ GEKYALDNEK MLLRGCIIRN TEWCFGLVIY
AGPDTKLMQN SGKTTFKRTS IDRLMNVLVL LIFAFLGLMC LILAIGNGIW EYDKGYYFQV
YLPWAEGVNS ASYSGFLMFW SYVIILNTVV PISLYVSVEI IRLGNSFYID WDRKMYYPPK
DTPAQARTTT LNEELGQIEY IFSDKTGTLT QNIMCFNKCS INGKSYGDVY DMSGQRIEIN
EKTEKVDFSY NQLADPKFVF YDHSLVEAVK LSDVPTHRFF RLLSLCHTVM PEEKKEGNLV
YQAQSPDEGA LVTAARNFGF VFRARTPETI TVVEMGETKV YKLLAILDFN NVRKRMSVIV
RSPEGDLTLY CKGADTILYE LLHSSCDSLK EETTEHLNEF AGEGLRTLVV AYKNLDEEYF
QDWIRRHHEA STALEGREDK LSELYEEIEK DLMLLGATAI EDKLQDGVPQ TIETLARANI
KIWVLTGDKQ ETAMNIGYSC NLLNDDMDDV FIIEGSTSDD VLKELRNARK KMKPDSFLDS
NEINIQFEKS SKKPKILPDE QANGVYGLVI TGHSLAYALE ENLELELVRT ACMCKVVICC
RVTPLQKAQV VELVKKYKKA VTLAIGDGAN DVSMIKTAHI GVGISGQEGM QAVLSSDFSF
AQFRYLQRLL LVHGRWSYIR MCKFLKYFFY KNFAFTLVHF WYGFFSGFSA QTVYDEWFIT
LYNLVYTSLP VLGMSLFDQD VDDRWSLLFP QLYVPGQQNL YFNKMVFVKC MFQGIYSSLI
LFFIPYGAMY NTVRSDGKAI ADYQSFALMV QTCLLIVVSV QIGLDTSYWT VVNQFFIWGS
LSVYFAITFT MYSDGMYLIF TASFPFVGTA RNTLSQPNVW LAIFLSIALC VLPVVGFRFL
KTQLRPTPSD KVLLKIKEAK KRPPPPSPRR RLRRTSTRRS GYAFAHQHGF GALIMSGRNM
RPKSPFATTG TFSPNSDKYK HKGL
//
