UniProt: A0A2K6LTI8

Database: UniProt
Entry: A0A2K6LTI8_RHIBE

LinkDB:  A0A2K6LTI8_RHIBE 
Original site:  A0A2K6LTI8_RHIBE

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (14)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (1)   
All databases (25)   

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ID   A0A2K6LTI8_RHIBE        Unreviewed;      1010 AA.
AC   A0A2K6LTI8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   Name=ATP11A {ECO:0000313|Ensembl:ENSRBIP00000026819.1};
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:ENSRBIP00000026819.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000026819.1, 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:ENSRBIP00000026819.1}
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; A0A2K6LTI8; -.
DR   Ensembl; ENSRBIT00000050741.1; ENSRBIP00000026819.1; ENSRBIG00000037242.1.
DR   GeneTree; ENSGT00940000157849; -.
DR   Proteomes; UP000233180; Unplaced.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProt.
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   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; 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:SF33; PHOSPHOLIPID-TRANSPORTING ATPASE IH; 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   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        171..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        225..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        761..779
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        791..811
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        841..863
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        875..897
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        909..933
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        939..964
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          727..979
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1010 AA;  115303 MW;  706F8771DACCDE52 CRC64;
     MNQCPVHFIQ HGKLVRKQSR KLRVGDIVMV KEDETFPCDL IFLSSNRGDG TCHVTTASLD
     GESSHKTHYA VQDTKGFHTE EDIGGLHATI ECEQPQPDLY KFVGRINVYS DLNDPVVRPL
     GSENLLLRGA TLKNTEKIFG VAIYTGMETK MALNYQSKSQ KRSAVEKSMN AFLIVYLCIL
     ISKALINTVL KYVWQSEPFR DEPWYNQKTE SERQRNLFLR AFTDFLAFMV LFNYIIPVSM
     YVTVEMQKFL GSYFITWDED MFDEETGEGP LVNTSDLNEE LGQVEYIFTD KTGTLTENNM
     EFKECCIEGH VYVPHVICNG QVLPESSGID MIDSSPSVNG REREELFFRA LCLCHTVQVK
     DNDSVDGPRK SPDGGASCVY ISSSPDEVAL VEGVQRLGFT YLRLKDNYME LLNRENHVER
     FELLEILSFD SVRRRMSVIV KSATGEIYLF CKGADSSIFP RVIEGKVDQI RARVERNAVE
     GLRTLCVAYK RLIQEEYEGI CKLLQAAKVA LQDREKKLAE AYEQIEKDLI LLGATAVEDR
     LQEKAADTIE ALQKAGIKVW VLTGDKMETA AATCYACKLF RRNTQLLELT TKRIEEQSLH
     DVLFELSKTV LRHSGSLTRD NFSGLSADMQ DYGLIIDGAA LSLIMKPRED GSSSNYRELF
     LEICRSCSAV LCCRMAPLQK AQIVKLIKFS KEHPITLAVG DGANDVSMIL EAHVGIGVIG
     KEGRQAARNS DYAIPKFKHL KKMLLVHGHF YYIRISELVQ YFFYKNVCFI FPQFLYQFFC
     GFSQQTLYDT AYLTLYNISF TSLPILLYSL MEQHIGIDVL KRDPTLYRDV AKNALLRWRV
     FIYWTLLGLF DALVFFFGAY FMFENTTVTS NGQIFGNWTF GTLVFTVMVF TVTLKLALDT
     HYWTWINHFV IWGSLLFYVV FSLLWGGVIW PFLNYQRMYY VFIQMLSSGP AWLAIVLLVT
     ISLLPDVLKK VLCRQLWPTA TERVQTKSQC LSVEQSTIFM LSQTSSSLSF
//

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