ID A0A060VX38_ONCMY Unreviewed; 972 AA.
AC A0A060VX38;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=GSONMT00079915001 {ECO:0000313|EMBL:CDQ59427.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ59427.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ59427.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ59427.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-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; FR904326; CDQ59427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060VX38; -.
DR STRING; 8022.A0A060VX38; -.
DR PaxDb; 8022-A0A060VX38; -.
DR Proteomes; UP000193380; 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; cd07541; P-type_ATPase_APLT_Neo1-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:SF49; PHOSPHOLIPID-TRANSPORTING ATPASE IIA-RELATED; 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; 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:UP000193380};
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 65..87
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 99..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 298..322
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 328..351
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 845..865
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 871..893
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 918..935
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 45..105
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 811..949
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 972 AA; 109870 MW; 2681F5D52FCC03B4 CRC64;
MTDNIPLQPV RHKKRHDNKN RNGCCPWSRC CGMGDFRPRT VWLGHPEKRE QRYPRNVINN
QKYNFFTFLP GVLFNQFKYF FNLYFLLLAC SQFVNELRLG ALYTYWVPLG FVLIITIARE
AVEEIRCYCR DKEVNSQIYS KLSTRGTVKV KSSGIQVGDL IIVEKNQRVP ADMIFLRTSE
RNGSCFLRTD QLDGETDWKL RLPVACTQRL PTAADLLQIR SYVYAEEPNI DIHNFIGTFT
REDGDPPVNE SLSIENTLWA STVIASGTVV GVVIYTGKEL RSVMNTSNPR HKVGLFDLEV
NCLTKILFGA LVVVSLVMVA LQHFAGRWYL QIFRFLLLFS NIVPISLRVN LDMGKMVFSW
MIRRDSKIPG TVVRASTIPE QLGRISYLLT DKTGTLTQNE MVFRRLHLGT VAYGMDSMDE
VQSHVFSAYT QPSHDVPASR APAATKVRKT ISSRVHEAVK AIALVHCVTP VYEANGVTDQ
AEAEQHYEDT CRVYQAASPD EVSLVQWTES VGLTLVGRDH NSMQLRTPSG QILNFTILQI
FPFTYESKRM GIIVRDESTG EISFYMKGAD VVMAGIVQYN DWLEEECGNM AREGLRVLVV
SKKSLTEEQY QDFEARYIQA KLSVHDRSLK VATVIESLEM EMELLCLTGV EDQLQADVRP
TLEILRNAGI KVWMLTGDKL ETATCTAKNA HLVTRNQDIH IFRSVTTRGE AHLELNAFRR
KHDCALVISG DSLEVCLKFY EYEFMELACQ CPAVVCCRCA PTQKAQIVRL LQERTGKLTC
AVGDGGNDVS MIQEADCGVG VEGKEGKQAS LAADFSVTQF KHLGRLLMVH GRNSYKRSAG
LSQFVIHRSL CISTMQAVFS SVFYFASVPL YQGFLIIGYS TIYTMFPVFS LVLDKDVKSE
VAMLYPELYK DLLKGRPLSF KTFLIWVLIS IYQGTTLETA LPYGVGSMML PTNPHTFFLI
ASSRVYLCLC FL
//
