ID A0A1S3M6K2_SALSA Unreviewed; 1209 AA.
AC A0A1S3M6K2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=LOC106570854 {ECO:0000313|RefSeq:XP_013998898.1};
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_013998898.1};
RN [1] {ECO:0000313|RefSeq:XP_013998898.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013998898.1};
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_013998898.1; XM_014143423.1.
DR AlphaFoldDB; A0A1S3M6K2; -.
DR STRING; 8030.ENSSSAP00000056940; -.
DR PaxDb; 8030-ENSSSAP00000056940; -.
DR GeneID; 106570854; -.
DR KEGG; sasa:106570854; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000087266; Chromosome ssa15.
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; 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 63..93
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 281..303
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 331..350
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 874..895
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 907..927
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 956..978
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 998..1018
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1025..1043
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1069..1091
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 21..86
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 843..1097
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1209 AA; 137753 MW; 0680A7FCBA13DC53 CRC64;
MTLFGLDCAK KKERELERKL RANDREHNLS FRYATNAIKT SKYNAFTFLP LNLFEQFQRI
ANAYFLILLL LQVIPAISSL SWFTTVVPLV LVLSVTAAKD ATDDINRHRS DNQVNNRKVT
VLMDGELRSE KWMAVQVGDI IKLENNQFVT ADLLLLSSSE PLNLVYIETA ELDGETNLKV
KQALTVTGDM GDNIQSLAAF NGEVRCEPPN NRLDRFTGTL TNAGQKYSLD NNKILLRGCT
LRNTEWCFGL VLFGGPETKL MQNCGKTTFK RTSIDRLMNE LVLCIFGFLA FMCTILAIGN
RIWEQRWGSE FTAFLPRQDG VDTPFSSFLT FWSYVIILNT VVPISLYVSV EVIRLGNSFY
IDWDRKMYHA RSDTPAKART TTLNEELGQI KYVFSDKTGT LTQNIMIFNK CSINGKCYGD
VFDYTGQRLE INEHTETVDW SFNPLADHQF SFHDHSLVEA VKLENVEVHS FFRTLALCHT
VMAEEKTEGE LLYQAQSPDE GALVTAARNF GFVFRSRTPE SVTIVEMGKQ RSYELLAILD
FNNVRKRMSV IVRSPEGKLC LYCKGADTMV YERLHQSCTK LMDVTTEHLN EYAGEGLRTL
ALAYKDLDEE YFSRWKQCHH EASTALEDRE DKLDLLYEEI EKDLVLLGAT AIEDKLQDGV
PQTIEQLAKA DIKIWVLTGD KQETAENIGY SCNMLREEMN DIFIVSANNP DDVRQELRNV
LSTMKPGAEE EAIFMPERTL GNKPKVVRDE EVNGEYGLVI NGHSLAYALE RSMELLFLRT
ACLCKTVICC RVTPLQKAQV VELVKKYKQA VTLAIGDGAN DVSMIKAAHI GVGISGQEGM
QAVLSSDYSF AQFRFLERLL LVHGRWSYLR MCKFLRYFFY KNFTFTFVHF WYAFFCGFSA
QTVYDEWFIT LYNLVYTALP VLGMSLFDQD VNDIWSFQHP NLYVPGQLNQ YFSKTAFFKC
ALHSVYSSVV LFFIPYAAMY DTVRDDGRDI ADYQSFALLA QTCLVITVCI QLCLDMSYWT
AVNQFFVWGS LAMYFVVTFS MYSNGTHINF PASFPFIGTA RNSLNQPNVW LTILLTSILC
VLPVVAYRFL LIQLRPTIND KVMFKVRQAK ATPPLPARRA RMRRTSSRRS GYAFSHAQGY
GDLVTSNHFL RRPAITRSTA FTPLGRTMGF SPMGRSAGYS PTGNALNSRP QDVEVTSLQM
YRMVRDSAF
//
