ID A0A2K6L3J2_RHIBE Unreviewed; 1470 AA.
AC A0A2K6L3J2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
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:ENSRBIP00000018071.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000018071.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000018071.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000018071.1}
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; 61621.ENSRBIP00000018071; -.
DR Ensembl; ENSRBIT00000041930.1; ENSRBIP00000018071.1; ENSRBIG00000033020.1.
DR GeneTree; ENSGT00940000157895; -.
DR Proteomes; UP000233180; 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:UP000233180};
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 64..81
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 87..105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 287..310
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 334..356
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1068..1090
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1096..1117
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1147..1170
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1176..1197
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1204..1224
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1249..1268
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 34..86
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1033..1278
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1364..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1432..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1470 AA; 164302 MW; 733C964495614398 CRC64;
LDPGKPGCGR RGPPQDPAAG AAKGERRRRR GCAQHLADNR LKTTKYTLLS FLPKNLFEQF
HRPANVYFVF IALLNFVPAV NAFQPGLALA PVLFILAITA FRDLWEDYSR HRSDHKINHL
GCLVFSREEK KYVNRFWKEI HVGDFVHLRC NEIFPADILL LSSSDPDGLC HIETANLDGE
TNLKRRQVVR GFSELVSEFN PLTFTSVIEC EKPNNDLSRF RGCIIHDNGK KAGLYKENLL
LRGCTLRNTD AVVGIVIYAG HETKALLNNS GPRYKRSKLE RQMNGDVLWC VLLLVCMSLF
SAVGHGLWIW RYQEKKSLFY VPTSDGSSLS PVTAAVYSFL TMIIVLQVLI PISLYVSIEI
VKACQVYFIN QDVQLYDEET DSQLQCRALN ITEDLGQIQY IFSDKTGTLT ENKMVFRRCT
VSGVEYSHDA NAQRLARYQE ADSEEEEVVP RGGSVSQRSS IGSHQSVRVV HRTQSTKSHR
RTGSRAEAKR ASMLSKHTAF SSPMEKDITP DPKLLEKVSE CDKSLAVARH QEHPLAHLSP
ELSDVFDFFI ALTICNTVVV TCPDQPRTKV RVRFELKSPV KTIEDFLRRF TPSCLTSGCS
SIGSLAAHKS NHKSGSSFLS TPSSDGMLLR LERLDQPTSA ITSNGYSSQA DDWASELAQE
QEPERELRYE AESPDEAALV YAARAYNCVL VERLHDQVSV ELPHLGRLTF ELLHTLGFDS
IRKRMSVVIR HPLTDEINVY TKGADSVVMD LLQPCSSVDA RGRHQKKIRS KTQNYLNLYA
AEGLRTLCIA KRVLSKEEYA CWLQSHLEAE SSLENSEELL FQSAIRLETN LHLLGATGIE
DRLQDGVPET ISKLRQAGLQ IWVLTGDKQE TAVNIAYACK LLDHDEEVIT LNATSQEACA
ALLDQCLRYV QSRGLQRAPE KTKGKVSMRF SSLCPPSMST ASGRSPSLVI DGRSLAYALE
KNLEDKFLFL AKQCRSVLCC RSTPLQKSMV VKLVRSKLKA MTLAIGDGAN DVSMIQVADV
GVGISGQEGM QAVMASDFAV PKFRYLERLL ILHGHWCYSR LANMVLYFFY KNTMFVGLLF
WFQFFCGFSA SAMIDQWYLI FFNLLFSSLP PLVTGVLDRD VPANVLQNNP QLYKSGQNVE
EYRPQTFWFN MADATFQSLV CFSIPYLAYY DSNVDLFTWG TPIVTIALLT FLLHLGIETK
TWTWLNWITC GFSVLLFFAV ALIYNASCAT CYPPSNPYWT MQALLGDPVF YLICLMTPVA
ALLPRLFYRS IQGSVFPTQL QLARQLARKS PRRHRTPKET FAQGCLPEGS GTEHSAGRTV
SVPLSQPSWH TQQPACSPEA SGEPSTVDMS MALREHTLLE RLSAPAPRSS TPGDAVPGGC
PEESKVRAAS TGRVTPLSSL FSLPTFSLLN WISSWSLVSR LGSILQFSRT EQPADAQTGR
GLAVQPHSGR SGLQGPDHRL LIGASSRRSQ
//
