ID A0A2K6NER8_RHIRO Unreviewed; 1481 AA.
AC A0A2K6NER8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-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=ATP10A {ECO:0000313|Ensembl:ENSRROP00000002756.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000002756.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000002756.1}
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 STRING; 61622.ENSRROP00000002756; -.
DR Ensembl; ENSRROT00000012343.1; ENSRROP00000002756.1; ENSRROG00000010879.1.
DR GeneTree; ENSGT00940000157895; -.
DR OMA; VWSYQES; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140351; F:glycosylceramide flippase activity; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140345; F:phosphatidylcholine flippase activity; IEA:Ensembl.
DR GO; GO:1903527; P:positive regulation of membrane tubulation; IEA:Ensembl.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF81; PHOSPHOLIPID-TRANSPORTING ATPASE VA; 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; SFLDG00002; C1.7:_P-type_atpase_like; 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 Lipid transport {ECO:0000256|ARBA:ARBA00023055};
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:UP000233200};
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}; Transport {ECO:0000256|ARBA:ARBA00023055}.
FT TRANSMEM 75..92
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 98..116
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 298..321
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 345..367
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1079..1101
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1107..1128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1158..1181
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1187..1208
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1215..1235
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1260..1279
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 45..97
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1044..1289
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1298..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1443..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1481 AA; 165753 MW; 148B5FF6B096B28C CRC64;
PPGRRRRREG RTRTVRSNLL PPPGAEDPAA GAAKGERRRR RGCAQHLADN RLKTTKYTLL
SFLPKNLFEQ FHRPANVYFV FIALLNFVPA VNAFQPGLAL APVLFILAIT AFRDLWEDYS
RHRSDHKINH LGCLVFSREE KKYVNRFWKE IHVGDFVRLR CNEIFPADIL LLSSSDPDGL
CHIETANLDG ETNLKRRQVV RGFSELVSEF NPLTFTSVIE CEKPNNDLSR FRGCIIHDNG
KKAGLYKENL LLRGCTLRNT DAVVGIVIYA GHETKALLNN SGPRYKRSKL ERQMNGDVLW
CVLLLVCMSL FSAVGHGLWI WRYQEKKSLF YVPTSDGSSL SPVTAAVYSF LTMIIVLQVL
IPISLYVSIE IVKACQVYFI NQDVQLYDEE TDSQLQCRAL NITEDLGQIQ YIFSDKTGTL
TENKMVFRRC TVSGVEYSHD ANAQRLARYQ EADSEEEEVV PRGGSVSQRS SIGSHQSVRV
VHRTQSTKSH RRTGSRAEAK RASMLSKHTA FSSPMEKDIT PDPKLLEKVS ECDKSLAVAR
HQEHPLAHLS PELSDVFDFF IALTICNTVV VTCPDQPRTK VRVRFELKSP VKTIEDFLRR
FTPSCLTSGC SSIGSLAAHK SNHKSGSGFL STPSSDGMLL RLERLDQPTS AITSNGYSSQ
ADDWASELAQ EQEPERELRY EAESPDEAAL VYAARAYNCV LVERLHDQVS VELPHLGRLT
FELLHTLGFD SIRKRMSVVI RHPLTDEINV YTKGADSVVM DLLQPCSSVD ARGRHQKKIR
SKTQNYLNLY GAEGLRTLCI AKRVLSKEEY ACWLQSHLEA ESSLENSEEL LFQSAIRLET
NLHLLGATGI EDRLQDGVPE TISKLRQAGL QIWVLTGDKQ ETAVNIAYAC KLLDHDEEVI
TLNATSQEAC AALLDQCLRY VQSRGLQRAP EKTKGKVSMR FSSLCPPSMS TASGRSPSLV
IDGRSLAYAL EKNLEDKFLF LAKQCRSVLC CRSTPLQKSM VVKLVRSKLK AMTLAIGDGA
NDVSMIQVAD VGVGISGQEG MQAVMASDFA VPKFRYLERL LILHGHWCYS RLANMVLYFF
YKNTMFVGLL FWFQFFCGFS ASAMIDQWYL IFFNLLFSSL PPLVTGVLDR DVPANVLQNN
PQLYKSGQNV EEYRPQTFWF NMADATFQSL VCFSIPYLAY YDSNVDLFTW GTPIVTIALL
TFLLHLGIET KTWTWLNWIT CGFSVLLFFA VALIYNASCA TCYPPSNPYW TMQALLGDPV
FYLICLMTPV AALLPRLFYR SIQGSVFPTQ LQLARQLARK SPRRHRTPKE TFAQGCLPEG
SGTEHSAGRT VSVPLSQPSW HTQQPACSPE ASGEPSTVDM SMALREHTLL ERLSAPAPRS
STPGDAVPGG CPEESKVRVA STGRVTPLSS LFSLPTFSLL NWISSWSLVS RLGSILQFSR
TEQPADAQTG RGLAVQPHSG RSGLQGPDHR LLIGASSRRS Q
//
