UniProt: A0A2K5YHQ8

Database: UniProt
Entry: A0A2K5YHQ8_MANLE

LinkDB:  A0A2K5YHQ8_MANLE 
Original site:  A0A2K5YHQ8_MANLE

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Ontology (24)   
   GO (24)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (5)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (1)   
All databases (47)   

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ID   A0A2K5YHQ8_MANLE        Unreviewed;      1223 AA.
AC   A0A2K5YHQ8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   Name=ATP8B1 {ECO:0000313|Ensembl:ENSMLEP00000015088.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000015088.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000015088.1}
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   RefSeq; XP_011827134.1; XM_011971744.1.
DR   AlphaFoldDB; A0A2K5YHQ8; -.
DR   STRING; 9568.ENSMLEP00000015088; -.
DR   Ensembl; ENSMLET00000038543.1; ENSMLEP00000015088.1; ENSMLEG00000031684.1.
DR   GeneID; 105533322; -.
DR   KEGG; mleu:105533322; -.
DR   CTD; 5205; -.
DR   GeneTree; ENSGT00940000158002; -.
DR   OMA; GSIRLYC; -.
DR   OrthoDB; 275833at2759; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:1990531; C:phospholipid-translocating ATPase complex; IEA:Ensembl.
DR   GO; GO:0032420; C:stereocilium; IEA:Ensembl.
DR   GO; GO:0015247; F:aminophospholipid flippase activity; 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:1901612; F:cardiolipin binding; 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:0045176; P:apical protein localization; IEA:Ensembl.
DR   GO; GO:0015721; P:bile acid and bile salt transport; IEA:Ensembl.
DR   GO; GO:0008206; P:bile acid metabolic process; IEA:Ensembl.
DR   GO; GO:0060119; P:inner ear receptor cell development; IEA:Ensembl.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:2001225; P:regulation of chloride transport; IEA:Ensembl.
DR   GO; GO:0032534; P:regulation of microvillus assembly; IEA:Ensembl.
DR   GO; GO:1903729; P:regulation of plasma membrane organization; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR   GO; GO:0021650; P:vestibulocochlear nerve formation; IEA:Ensembl.
DR   GO; GO:0006855; P:xenobiotic transmembrane transport; IEA:Ensembl.
DR   CDD; cd02073; P-type_ATPase_APLT_Dnf-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; 1.
DR   PANTHER; PTHR24092:SF48; PHOSPHOLIPID-TRANSPORTING ATPASE IC; 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   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:UP000233140};
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        116..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        139..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        339..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        389..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1005..1028
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1040..1060
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1066..1085
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1117..1139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          67..145
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          977..1145
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..38
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1223 AA;  140665 MW;  0223E222AACB47BD CRC64;
     MSTERDSETT FDEDSQPNDE VVPYSDDETE DELDDQGSTV EPEQNRVNRE AEENQEPFRK
     ECTWQVKAND RKYHEQPHFM NTKFFCIKKS KYANNAIKTY KYNVLTFIPM NLFEQFKRAA
     NLYFLVLLIL QAIPQISTLA WYTTLVPLLL VLGVTAIKDL VDDVARHKMD KEINNRTCEV
     IKDGRFKVAK WKDIQVGDVI RLKKNDFVPA DILLLSSSEP NSLCYVETAE LDGETNLKFK
     MSLEITDQYL QREDTLATFD GFVECEEPNN RLDKFTGTLF WRNTSFPLDA DKILLRGCVI
     RNTDFCHGLV IFAGADTKIM KNSGKTRFKR TKIDYLMNYM VYTIFVVLSL LSAGLAIGHA
     YWEAQVGNYS WYLYDGKDDT PSYRGFLNFW GYIIVLNTMV PISLYVSVEV IRLGQSHFIN
     WDLQMYYAEK DTPAKARTTT LNEQLGQIHY IFSDKTGTLT QNIMTFKKCC INGQIYGDHR
     DASQHNHNKI EQVDFSWNTY ADRKLAFYDH YLIEQIQSGK EPEVRQFFFL LAVCHTVMVD
     RTDGQLNYQA ASPDEGALVN AARNFGFAFL ARTQNTITIS ELGTERTYNV LAILDFNSDR
     KRMSIIVRTP EGNIRLYCKG ADTVIYERLH RMNPTKQETQ DALDIFANET LRTLCLCYKE
     IEEKEFAQWN KKFMAASVAS TNRDEALDKV YEEIEKDLIL LGATAIEDKL QDGVPETISK
     LAKADIKIWV LTGDKKETAE NIGFACELLT EDTTICYGED INSLLHARME NQRNRGGVYA
     KFAPPVQEPF FPPGGNRALI ITGSWLNEIL LEKKTKRSKI LKLKFPRTEE ERRMRTQSKR
     RLEAKKEQRQ KNFVDLACEC SAVICCRVTP KQKAMVVDLV KRYKKAITLA IGDGANDVNM
     IKTAHIGVGI SGQEGMQAVM SSDYSFAQFR YLQRLLLVHG RWSYIRMCKF LRYFFYKNFA
     FTLVHFWYSF FNGYSAQDVS DKLSLRFPGL YIVGQRDLLF NYKRFFVSLL HGVLTSMILF
     FIPLGAYLQT VGQDGEAPSD YQSFAVTIAS ALVITVNFQI GLDTSYWTFV NAFSIFGSIA
     LYFGIMFDFH SAGIHVLFPS IFQFTGTASN ALRQPYIWLT IILTVAVCLL PVVAIRFLSM
     TIWPSESDKI QKHRKRLKAE EQWQRRQQVF RRGVSSRRSA YAFSHQRGYA DLISSGRSIR
     KKRSPLDAIV ADGTAEYRRT GDS
//

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