ID A0A1S3NY25_SALSA Unreviewed; 1196 AA.
AC A0A1S3NY25;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=LOC106582021 {ECO:0000313|RefSeq:XP_014020156.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014020156.1};
RN [1] {ECO:0000313|RefSeq:XP_014020156.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014020156.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_014020156.1; XM_014164681.1.
DR AlphaFoldDB; A0A1S3NY25; -.
DR STRING; 8030.ENSSSAP00000120090; -.
DR PaxDb; 8030-ENSSSAP00000120090; -.
DR GeneID; 106582021; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000087266; Chromosome ssa21.
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: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 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:UP000087266};
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 295..318
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 349..368
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 911..931
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 961..983
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 995..1017
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1029..1053
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1059..1084
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 42..96
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 847..1099
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1115..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1196 AA; 135801 MW; E25473AA9B3885CA CRC64;
MDFSVLRNLI SRYCAGEEYW VDSRTVYIGH KEPPPAAEAY IPQRYPDNRI VSSKYTLWNF
IPKNLFEQFR RIANFYFLLI FLVQLIIDTP TSPVTSGLPL FFVITVTAIK QGYEDWLRHK
ADCSINECPV DMVQQGMVVR TQSSKLRVGD VVMVREDETF PCDLILLSTS RGDGTCYVTT
TSLDGESSHK TYYAVPDTMA FKTEQEVDSL HATIECEQPQ PDLYKFVGRI NIYKEREDSI
ARPLGAENLL LRGATLKNTE HIYAVAIYTG MDTKMALNYQ SKSQKRSAVE KSMNAFLVVY
LCILISKAVI NTVLKYAWQW SADRDEPWYN HRTEVDRERH VVIRAFTDFL AFMVLFNYII
PVSMYVTVEM QKFLGSYFIA WDKDMYDEEL GVGAQVNTSD LNEELGQVEY VFTDKTGTLT
ENNMEFIECC VDGHVYIPHA ICNGQILSAA SSIDMIDSSP GGYRREHEDL FFRALCLCHT
VQVKEEETVD SIKRGIHLGK PTSFYISSSP DEVALVEGMK RLGYTYLRLK DSHMEILNKD
DEIERFELLH VLNFDSVRRR MSVIVKSSSG EYLLFCKGAD TSIFPRVVSG KVEQVRARVE
QNAVEGLRTL CVAYRRLSPA EYEEACHQLS DAKLALKDRE QRLAQAYDLI ERDFTLLGAT
AVEDRLQEKA ADTIESLQKA GMKVWVLTGD KMETAAATCY ASKLFRRSTQ ILELTKKRTE
EQSLHDVLFD LSRTVLRQRS LSGLSVECQD YGLIIDGATL SAVLKPSPES SGSGNYREIF
LEISRNCSAV LCCRMAPLQK AQIVKLIKAS KEHPITLAIG DGANDVSMIL EAHVGIGIMG
KEGLQAARNS DYAIPKFKHL KKMLLVHGHF YYIRIAELVQ YFFYKNVCFI FPQFLYQFFC
GFSQQPLYDT AYLTLYNISF TSLPILLYSL IEKHVSIETL KRDPTLYRDV AKNALLRWPV
FLYWTCLGLF NACIFFFGAY FLFDNTTFTS NGQMFGNWTF GTLVFTVLVF TVTLKLALDT
HHWTWINHFV IWGSLLFYVI FSLLWGGIIW PFLNYQRMYY VFMQMLSSGP AWLGIILLIT
ISLLPDVVKK VLCRTLWPTA TERAQRVRAD GVCEGSVSPA TGPDPSPVAG GGGSESDMLC
PARTCEGERG GEGVRAARTY DSMMSHNPNY LLSQPLDHAP SDGEGCYGNW GVHLGH
//
