ID A0A1S3LUB7_SALSA Unreviewed; 1238 AA.
AC A0A1S3LUB7;
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=LOC106568528 {ECO:0000313|RefSeq:XP_013994424.1,
GN ECO:0000313|RefSeq:XP_013994425.1};
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_013994425.1};
RN [1] {ECO:0000313|RefSeq:XP_013994424.1, ECO:0000313|RefSeq:XP_013994425.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013994424.1,
RC ECO:0000313|RefSeq:XP_013994425.1};
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_013994424.1; XM_014138949.1.
DR RefSeq; XP_013994425.1; XM_014138950.1.
DR STRING; 8030.ENSSSAP00000086609; -.
DR PaxDb; 8030-ENSSSAP00000086609; -.
DR GeneID; 106568528; -.
DR KEGG; sasa:106568528; -.
DR OMA; GSIRLYC; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000087266; Chromosome ssa13.
DR Bgee; ENSSSAG00000066100; Expressed in pharyngeal gill and 5 other cell types or tissues.
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:SF48; PHOSPHOLIPID-TRANSPORTING ATPASE IC; 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 326..350
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 370..395
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 937..958
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 970..990
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1020..1044
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1056..1075
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1087..1113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1133..1154
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 68..132
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 906..1160
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..36
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1238 AA; 141614 MW; C189D8737F7D9ABC CRC64;
MSRERADSQG SLGPDDEVMP YSDDETDDEL DPGSDEERPQ VEEAKSTESG WRVKANDRAF
CNLPEFQKKY FLCLKKSKYA GNGIKTYKYN ALTFIPLNLF EQFKRAANLY FLALLILQII
PEITTLPWYT TLVPLVLVLG ITAIKDLVDD LARHRMDNEI NNRKCEVLLD GRFQVSKWMN
IHVGDVVRLK KNDHIPADIL LLSSSNPNSL CYVETAELDG ETNLKFKMGL RATDERLQGE
HQLAQFDAVI VCEEPNNRLD KFTGTMRWRK DRFPLDVGKM MLRGCRIRNT DACHGLVIFA
GADTKIMRNG GKTRFKRTKI DELMNYMVYT IFVILVLLCA GLAIGNTFWY EAVGRKAWYL
NDGKDQTASY RGFLSFWGYI IVLNTMVPIS LYVSVEVIRL GQSKFINWDL QMYYQEKDTP
AKARTTTLNE QLGQIEYIFS DKTGTLTQNI MAFKKCTIAG RTFGDPANVE GVSLDRGKPV
DFTWNKYADR KFEYLDHSLV ACIRSKKDKD TLEFFKLLSL CHTVMVEQKE DELVYQAASP
DEGALVTAAR NFGFVFLSRT QDTITISEMD QEMTYEMLAL LDFNSDRKRM SIILRFPDGR
IRLYCKGADT VIYERLSPNS KHKEVTQTAL DIFANETLRT LCLCYKDISK QEFDAWAKKH
KAASVAMGNK EAALDRVYEQ IESNLMMIGA TAIEDKLQDG VPETIAKLAK ADIKIWVLTG
DKKETAENIG YSCKLLTDGM QIHYGEDVNE KLRIRQANRR DQPPAFGRTR KKVPDPFFPE
PGRNALIITG GWLNEILYEK KKKRRRLRLK RLGKRPASAT PQDAAQPIDD WEKETRQVDF
VNMACECEAV ICCRVTPKQK ANVVSLVKKY KKAVTLSIGD GANDVNMIKT ADIGVGISGQ
EGMQAVMSSD YAFAQFRYLE RLLLVHGRWS YIRMCKFLRF FFFKNFAFTL VHFWYSFFSG
FSAQVAYEDW FITLYNVMYS SLPVLLVGLL DQDVNDKLSR KFPKLYLPGQ QGALFNYKNF
FISLFHGIFT SLVIFFIPYG AFLQTMGQDG EAPSDYQSLA VVMASSLIFT VNMQISLETS
YWTFVNCFAV LCSIAIYFGI MFDIHSAGIH VIFPSTFTFT GVASNALKQP YLWLTIILTV
GISLLPVICI QFLYKTIWPS VGDKVQRNRK KYEMEEEEQE KSTPFQRGRR SRRSAYAFSH
SRGYADLIAS GRSIRRRPPT ARPNPRDSIR EIPQAENI
//
