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Database: UniProt
Entry: A0A674BLC9_SALTR
LinkDB: A0A674BLC9_SALTR
Original site: A0A674BLC9_SALTR 
ID   A0A674BLC9_SALTR        Unreviewed;      1151 AA.
AC   A0A674BLC9;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   Name=ATP8A1 {ECO:0000313|Ensembl:ENSSTUP00000072255.1};
OS   Salmo trutta (Brown trout).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000072255.1, ECO:0000313|Proteomes:UP000472277};
RN   [1] {ECO:0000313|Ensembl:ENSSTUP00000072255.1}
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; A0A674BLC9; -.
DR   Ensembl; ENSSTUT00000076672.1; ENSSTUP00000072255.1; ENSSTUG00000025920.1.
DR   GeneTree; ENSGT00940000157110; -.
DR   OrthoDB; 275833at2759; -.
DR   Proteomes; UP000472277; 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; 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:SF150; 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:UP000472277};
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;  129694 MW;  0DB6FF667E2C9654 CRC64;
     MPIERTISDL RSRLEGYEKI GEATSRTSIA DLEDARQIFI NQPQLTKFCT NHVSTAKYNV
     LTFLPRFLYA QFRRAANSFF LFIALLQQIP DVSPTGRWTT LVPLILILLV AALKEIVEDL
     KRHKADRVVN RKEAQVLRNG AWEVVHWEKV TVGDVVRASD GDHLPADLVL LASSEPHAMC
     YIETSNLDGE TNLKIRQGLQ VTADDKDADS LSRLSGCMEC ESPNRHLYDF VGVIRLEGHS
     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 PDSVIIHTLG TEQRFELLNV LEFTSDRKRM
     SVIMRTPSGR IRLYCKGADS VIYERLADSS KYKDITLNHL EQFATEGLRT LCYAVTNISD
     ESYEQWAELY QRAATSLTNR ALKMEESYEL IERNLQLLGA TAIEDKLQDK VPETIETLLR
     ADIKIWILTG DKQETAINIG HSCRLLRKNM GLLVVNEETL EGTRTALSHH 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 LEAKAQDPGA
     VVHGKSLSER AQLLKNPFKK NRILSAYSTE SVPQNMLHGY AFSQEENGAV SQSDVIRSYD
     TTKQRPAQPQ W
//
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