ID A0A672GWW9_SALFA Unreviewed; 1237 AA.
AC A0A672GWW9;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS Salarias fasciatus (Jewelled blenny) (Blennius fasciatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Blenniimorphae; Blenniiformes; Blennioidei; Blenniidae;
OC Salariinae; Salarias.
OX NCBI_TaxID=181472 {ECO:0000313|Ensembl:ENSSFAP00005021535.1, ECO:0000313|Proteomes:UP000472267};
RN [1] {ECO:0000313|Ensembl:ENSSFAP00005021535.1}
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; A0A672GWW9; -.
DR Ensembl; ENSSFAT00005022452.1; ENSSFAP00005021535.1; ENSSFAG00005010518.1.
DR InParanoid; A0A672GWW9; -.
DR Proteomes; UP000472267; Unplaced.
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; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; 1.
DR PANTHER; PTHR24092:SF79; PHOSPHOLIPID-TRANSPORTING ATPASE VB; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 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:UP000472267};
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 73..90
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 96..115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 291..316
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 343..365
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 989..1013
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1051..1075
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1081..1102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1114..1136
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1156..1173
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 40..96
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 940..1175
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1237 AA; 140016 MW; 0CA224999EA1D01F CRC64;
MTKRSLLTLV RDALRGQRAR DRDLRNLVSN LPYEGLERSK QPNRYFQSNG IKTTKYTLLT
FVPMNLYEQF HRLANIYFVG LVILNFFPVV NAFQPQVALI PICVILALTA LKDAWEDFRR
YQSDRKLNNT PCLVYSRREK QFAERCWKDV QVGDFVKVAC NEIIPADLLL LHTSDPNGVC
HIETANLDGE TNLKQRTVVH GVCHPEFDPE SFNSRVVCEK PNNNLNHFKC YVEKPDEEKV
GAGIESLLLR GCTVRNTDHA AGFVVYAGHE TKSMLNNSGP RYKRSKLERK LNVDVLFCVI
LLFAMCLIGS LGHYLWRLSL PDVPPYLVAD GNGHLDSPSL SSFYMFFTMI ILLQILIPIS
LYVSIELVKM GQIFFITNDV DLYDEETDSR VQCKALNITE DLGQVEYIFS DKTGTLTENK
MLFRRCSIMG TEFPHKENGT SHTQWNYHLQ PASEAPADGP VAETEVIPDR KLLQQITRGE
NSSRKTDPYL DFFLALAICN TVVVSMATAR RRRVSTSSVL DTLTSLVKKK DSLSCIFTSC
RSKPKTEDSV IEESHFHPPA DKKEGTDAIS RHRKCSLHVL SQSDVSAVTS ADLRYEAESP
DEAALVYAAK AYGFVLLART PNSVTVRLPS GDELVFEVLD TLTFDSNRKR MSVLVKHPVT
KEYVLYTKGA DYAIMELLGT PYAGTEHFKG KQKNVATDTQ HHVDCYAKEG LRTLCFAKKI
VSEKMYEDWL VGRQRALAAI DNREELIMET AGQLETNLSL LGATGIEDRL QESVPDTIVA
LREAGIQVWV LTGDKPETAV NIGYACRLLE EEDLVINMSC KNKLTCTAIL DCTLEEVKRY
NDDPRNVDTT QNISVVIDGP TLTMALSPDL RDRFMELARR CRSVLCCRVT PLQKSRVVKL
VREKLKVMTL AVGDGANDVN MIQAADIGIG ISGQEGMQAV MASDFAISRF KHLKKLLLVH
GHWCYTRLAN MIIYFFYKNV AYVNLLFWYQ FFCGFSGTAM IDYWLMIFFN LFFTSVPPIM
FGIMDRDVSA EVLLGVPELY RTGQGKGEYN FLTFWISILD AFYQSLVCFF VPYLVYQGSD
VDIFTFGTPL NTSSLFVILL HLSIEIKAWT VVHWVVMLGS VLLYFVVTLA FSAICVTCNP
PSNPYWILQS QMADPTFYLI CILTTVVALL PRYQQRYPDC ARRQPCFYQL YVIICSYFTH
LSAGHSSRKL SSSTHFPADF IIDTTSETIN IGLKKTN
//
