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Database: UniProt
Entry: A0A1S3PXT6_SALSA
LinkDB: A0A1S3PXT6_SALSA
Original site: A0A1S3PXT6_SALSA 
ID   A0A1S3PXT6_SALSA        Unreviewed;      1136 AA.
AC   A0A1S3PXT6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-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=atp9b {ECO:0000313|RefSeq:XP_014032515.1};
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_014032515.1};
RN   [1] {ECO:0000313|RefSeq:XP_014032515.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014032515.1};
RG   RefSeq;
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   RefSeq; XP_014032515.1; XM_014177040.1.
DR   AlphaFoldDB; A0A1S3PXT6; -.
DR   GeneID; 106588231; -.
DR   OrthoDB; 275833at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa27.
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; cd07541; P-type_ATPase_APLT_Neo1-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:SF50; PHOSPHOLIPID-TRANSPORTING ATPASE IIB-RELATED; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 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        167..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        370..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        396..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        935..955
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        961..983
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1013..1033
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1039..1060
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1067..1088
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1100..1119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          111..170
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          901..1128
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          491..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..516
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1136 AA;  127971 MW;  09C0AA16C7584398 CRC64;
     MADSIPLNPM RKGSEKIAYY NTARHSRYSL EDEPSNLDEM PLMMSEEGFE NDESDYHTLP
     RARVNQRQRG LGWLLMGGWK ILCGSCCDCL ARMCRRTKEL KARTVWLGHP EKCEEKYPKN
     AIKNQKYNFF TFVPGVLYQQ FKFFLNLYFL VVACSQFVPA LKIGYLYTYW APLGFVMAVT
     MVREAVDEVR RYQRDKEMNS QLYSKLTVRG KVQVKSSDIQ VGDLIIVEKN QRIPADMIFL
     RTSEKTGSCF IRTDQLDGET DWKLKVAVVC TQRLPALGDL FSINAYVYAQ KPQLDIHSFE
     GNFTREDGDP QIHESLSIDH TLWASTIVAS GTVIGVVIYT GKETRSVLNT SSPKNKVGLL
     DLELNRLTKA LFLAQVVLSI VMVALQGFVG PWFRNLFRFI VLFSYIIPIS LRVNLDMGKS
     AYGWMIMKDE NIPGTVVRTS TIPEELGRLV YLLTDKTGTL TQNEMIFKRL HLGTVSYGTD
     TMDEIQSHIG QSYAQPSSQT QQSNSSTSST PSRKPQPAQA PKAVAPKAAA PKVRRSVSSR
     IHEAVKAIAL CHNVTPVYES RANGETESTA AEADQDFSDD NRTYQASSPD EVALVRWTES
     VGLTLVNRDL TSLQLKTPAG QVLTYYILQI FPFTSESKRM GIIIREETTG DITFYMKGAD
     VAMASIVQYN DWLEEECGNM AREGLRTLVV AKKSLSEEQY TDFENRFNQA KLSIHDRALK
     VAAVVESLER EMELLCLTGV EDQLQADVRP TLELLRNAGI KIWMLTGDKL ETATCIAKSS
     HLVSRSQDIH VFRSVSNRGE AHLELNAFRR KHDCALVISG DSLEVCLRYY EHEFVELACQ
     CPAVVCCRCS PTQKAQIVHL LKQHTANRTC AIGDGGNDVS MIQAADCGIG IEGKEGKQAS
     LAADFSITQF KHIGRLLMVH GRNSYKRSAA LGQFVMHRGM IISTMQAVFS SIFYFASVPL
     YQGFLMVGYS TIYTMFPVFS LVLDQDVKPE MALLYPELYK DLTKGRSLSF KTFLIWVLIS
     IYQGGILMYG ALVLFESEFV HVVAISFTAL ILTELLMVAL NIRTWHWLMV LAEFLSLGCY
     IASLAFLNEY FDLGFITTPA FLWKVSVITI VSCLPLYIIK YLKRKFSPPS YSKLSS
//
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