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Database: UniProt
Entry: A0A2K6S9L7_SAIBB
LinkDB: A0A2K6S9L7_SAIBB
Original site: A0A2K6S9L7_SAIBB 
ID   A0A2K6S9L7_SAIBB        Unreviewed;       896 AA.
AC   A0A2K6S9L7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=ATPase phospholipid transporting 9A (putative) {ECO:0000313|Ensembl:ENSSBOP00000004069.1};
GN   Name=ATP9A {ECO:0000313|Ensembl:ENSSBOP00000004069.1};
OS   Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000004069.1, ECO:0000313|Proteomes:UP000233220};
RN   [1] {ECO:0000313|Ensembl:ENSSBOP00000004069.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   AlphaFoldDB; A0A2K6S9L7; -.
DR   STRING; 39432.ENSSBOP00000004069; -.
DR   Ensembl; ENSSBOT00000020215.1; ENSSBOP00000004069.1; ENSSBOG00000018293.1.
DR   GeneTree; ENSGT00940000159181; -.
DR   OMA; XVYFIAT; -.
DR   Proteomes; UP000233220; Unplaced.
DR   GO; GO:0031901; C:early endosome membrane; IEA:Ensembl.
DR   GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:Ensembl.
DR   GO; GO:0032588; C:trans-Golgi network membrane; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:1903542; P:negative regulation of exosomal secretion; IEA:Ensembl.
DR   GO; GO:2001135; P:regulation of endocytic recycling; IEA:Ensembl.
DR   GO; GO:1905279; P:regulation of retrograde transport, endosome to Golgi; IEA:Ensembl.
DR   CDD; cd07541; P-type_ATPase_APLT_Neo1-like; 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; IPR032631; P-type_ATPase_N.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR032630; P_typ_ATPase_c.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR24092:SF49; PHOSPHOLIPID-TRANSPORTING ATPASE IIA-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; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   PRINTS; PR00119; CATATPASE.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        42..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        275..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        305..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        695..715
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        721..743
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        773..793
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        799..820
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        827..847
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        853..879
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          23..83
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          661..888
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   896 AA;  101720 MW;  8F249F2386D3C0EF CRC64;
     CCEWLRCCGG GEPRPRTVWL GHPEKRDQRY PRNVINNQKY NFFTFLPGVL FNQFKYFFNL
     YFLLLACSQF VPEMRLGALY TYWVPLGFVL AVTVIREAVE EIRCYVRDKE VNSQVYSRLT
     ARGTVKVKSS NIQVGDLIIV EKNQRVPADM IFLRTSEKNG SCFLRTDQLD GETDWKLRLP
     VACTQRLPTA ADLLQIRSYV YAEEPNIDIH NFVGTFTRED SDPPISESLS IENTLWAGTV
     VASGTVVGVV LYTGRELRSV MNTSNPRSKI GLFDLEVNCL TKILFGALVV VSLVMVALQH
     FAGRWYLQII RFLLLFSNII PISLRVNLDM GKIVYSWVIR RDSKVPGTVV RSSTIPEQLG
     RISYLLTDKT GTLTQNEMVF KRLHLGTVAY GLDSMDEVQS HIFSIYTQVA LVQWTESVGL
     TLVGRDQSSM QLRTPGDQIL NFTILQIFPF TYESKRMGII VRDESTGEIT FYMKGADVVM
     AGIVQYNDWL EEECGNMARE GLRVLVVAKK SLAEEQYQDF EVWMLTGDKL ETATCTAKNA
     HLVTRNQDIH VFRLVTNRGE AHLELNAFRR KHDCALVISG DSLEVCLKYY EYEFMELACQ
     CPAVVCCRCA PTQKAQIVRL LQERTGKLTC AVGDGGNDVS MIQESDCGVG VEGKEGKQAS
     LAADFSITQF KHLGRLLMVH GRNSYKRSAA LSQFVIHRSL CISTMQAVFS SVFYFASVPL
     YQGFLIIGYS TIYTMFPVFS LVLDKDVKSE VAMLYPELYK DLLKGRPLSY KTFLIWVLIS
     IYQGSTIMYG ALLLFESEFV HIVAISFTSL ILTELLMVAL TIQTWHWLMT VAELLSLACY
     IASLVFLHEF IDVYFIATLS FLWKVSVITL VSCLPLYVLK YLRRRFSPPS YSKLTS
//
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