ID A0A1S3SAH7_SALSA Unreviewed; 1151 AA.
AC A0A1S3SAH7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=LOC106608070 {ECO:0000313|RefSeq:XP_014061344.1};
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_014061344.1};
RN [1] {ECO:0000313|RefSeq:XP_014061344.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014061344.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014061344.1; XM_014205869.1.
DR AlphaFoldDB; A0A1S3SAH7; -.
DR GeneID; 106608070; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000087266; Chromosome ssa01.
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:SF225; PHOSPHOLIPID-TRANSPORTING ATPASE IA; 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; 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: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 98..117
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 295..318
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 338..362
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 851..871
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 877..895
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 924..946
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 961..982
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 989..1009
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1029..1053
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 40..101
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 811..1062
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1151 AA; 129714 MW; 40DA0DCAB16DA098 CRC64;
MPIERTISDL RSRLEGYEKI GEATSRTSIA DLEDARQIFI NQPQLTKFCT NHVSTAKYNV
LTFLPRFLYA QFRRAANSFF LFIALLQQIP DVSPTGRWTT LVPLILILLV AALKEIVEDL
KRHKADRVVN RKEAQILRNG AWEVVHWEKV EVGDGVTLNG REYIPADSIV LSSSEPHAMC
YIETSNLDGE TNLKIRQGLQ VTADDKYADS LSRLSGCMEC ESPNRHLYDF VGLIRLEGHS
PVPLGPEQIL LRGARLRNTQ WVNGMVVYTG HDTKLMQNST RPPLKLSSVE HITNTLILAL
FGCLLAISLV CSAGQTLWKT QHGDFAWYMD LNYGGAANFG LNFLTFIILF NNLIPISLLV
TLEVIKFIQA YFINWDMDMH YEPTDTSAVA RTSNLNEELG QVKYIFSDKT GTLTCNVMQF
KKCTIAGVAY GHNTDSPEEE GFGDPTLPEN LNNDHPTATI IQDFLTMMAV CHTAVPEKTE
DTIVYQASSP DEGALVRAAS SLGFVFSGRT PDSVIIHALG TEQRFELLNV LEFTSDRKRM
SVIMRTPSGR IRLYCKGADS VIYERLADSS KYKDITLNHL EQFATEGLRT LCYAVTNISD
ESYEQWAELY QRAATSLTNR ALKMEESYEL IERNLQLLGA TAIEDKLQDK VPETIETLLR
ADIKIWILTG DKQETAINIG HSCRLLRKNM GLLVVNEETL EGTRAALSHH CGMLGEALHR
ENDVALVMDG ETLKYALSFE VRQYFLDLAL SCKAVICCRV SPLQKSEVVD LVKRQVKVIT
LAVGDGANDV GMIQTAHVGV GISGNEGLQA ANSSDYSIAQ FKYLRNLLLV HGAWNYNRVS
KCILYCFYKN IVLYIIEIWF AIVNGFSGQI LFERWCIGLY NVIFTAMPPL ALGIFERCCK
KENMLKYPEL YKTSQNALGF NTKVFWAHCL NGLLHSVILF WLPLLIFQHD TVSWNGKTPD
YLLLGNMVYT FVVITVCLKA GLETSSWTLF SHIAIWGSVF LWVLFFWLYS TWWPVIAIAP
DMSGQAEMLF TSGVFWMSLL FIPVTSLLFD VAFRVVKRSF WKNLVDEVQE LEAKAQDPGV
VVHGKSLSER AQLLKNPFKK NSISSAYSTE SVPQNMLHGY AFSQEENGAV SQSDVIRSYD
TTKQRPAQPQ W
//
