| Tag |
Content |
LipidDB ID |
LipidDB-9606-00532 |
Entry Name |
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UniProt Accession |
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Theoretical PI |
6.17 |
Molecular Weight |
129755.75 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
Probable phospholipid-transporting ATPase IH |
Protein Synonyms/Alias |
3.6.3.1; ATPase IS; ATPase class VI type 11A; P4-ATPase flippase complex alpha subunit ATP11A; |
Gene Name |
ATP11A |
Gene Synonyms/Alias |
ATPIH; ATPIS; KIAA1021; |
Created Date |
30-MAY-2000 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
3 | Canonical | *****MDCSLVRTLV | [1] | S-Palmitoylation | 14 | Canonical | RTLVHRYCAGEENWV | [1] | S-Palmitoylation | 302 | Canonical | AFLIVYLCILISKAL | [1] | S-Palmitoylation | 610 | Canonical | VEGLRTLCVAYKRLI | [1] | S-Palmitoylation | 1114 | Canonical | RVQTKSQCLSVEQST | [1] | S-Palmitoylation |
|
Organism |
Homo sapiens (Human) |
NCBI Taxa ID |
9606 |
Reference |
[1] Predicted from GPS-Lipid
|
Functional Description |
Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (Probable). May be involved in the uptake of farnesyltransferase inhibitor drugs, such as lonafarnib. |
Sequence Annotation |
Topological domain: 1 61 Cytoplasmic.
Transmembrane: 62 82 Helical.
Topological domain: 83 88 Extracellular.
Transmembrane: 89 110 Helical.
Topological domain: 111 296 Cytoplasmic.
Transmembrane: 297 318 Helical.
Topological domain: 319 349 Extracellular.
Transmembrane: 350 372 Helical.
Topological domain: 373 881 Cytoplasmic.
Transmembrane: 882 902 Helical.
Topological domain: 903 914 Extracellular.
Transmembrane: 915 934 Helical.
Topological domain: 935 964 Cytoplasmic.
Transmembrane: 965 986 Helical.
Topological domain: 987 1000 Extracellular.
Transmembrane: 1001 1023 Helical.
Topological domain: 1024 1029 Cytoplasmic.
Transmembrane: 1030 1050 Helical.
Topological domain: 1051 1068 Extracellular.
Transmembrane: 1069 1093 Helical.
Topological domain: 1094 1134 Cytoplasmic.
Active site: 414 414 4-aspartylphosphate intermediate.
Metal binding site: 825 825 Magnesium.
Metal binding site: 829 829 Magnesium.
|
Protein Length |
1134 AA. |
Protein Sequence
(Canonical) |
MDCSLVRTLV HRYCAGEENW VDSRTIYVGH REPPPGAEAY IPQRYPDNRI VSSKYTFWNF 60
IPKNLFEQFR RVANFYFLII FLVQLIIDTP TSPVTSGLPL FFVITVTAIK QGYEDWLRHK 120
ADNAMNQCPV HFIQHGKLVR KQSRKLRVGD IVMVKEDETF PCDLIFLSSN RGDGTCHVTT 180
ASLDGESSHK THYAVQDTKG FHTEEDIGGL HATIECEQPQ PDLYKFVGRI NVYSDLNDPV 240
VRPLGSENLL LRGATLKNTE KIFGVAIYTG METKMALNYQ SKSQKRSAVE KSMNAFLIVY 300
LCILISKALI NTVLKYMWQS EPFRDEPWYN QKTESERQRN LFLKAFTDFL AFMVLFNYII 360
PVSMYVTVEM QKFLGSYFIT WDEDMFDEET GEGPLVNTSD LNEELGQVEY IFTDKTGTLT 420
ENNMEFKECC IEGHVYVPHV ICNGQVLPES SGIDMIDSSP SVNGREREEL FFRALCLCHT 480
VQVKDDDSVD GPRKSPDGGK SCVYISSSPD EVALVEGVQR LGFTYLRLKD NYMEILNREN 540
HIERFELLEI LSFDSVRRRM SVIVKSATGE IYLFCKGADS SIFPRVIEGK VDQIRARVER 600
NAVEGLRTLC VAYKRLIQEE YEGICKLLQA AKVALQDREK KLAEAYEQIE KDLTLLGATA 660
VEDRLQEKAA DTIEALQKAG IKVWVLTGDK METAAATCYA CKLFRRNTQL LELTTKRIEE 720
QSLHDVLFEL SKTVLRHSGS LTRDNLSGLS ADMQDYGLII DGAALSLIMK PREDGSSGNY 780
RELFLEICRS CSAVLCCRMA PLQKAQIVKL IKFSKEHPIT LAIGDGANDV SMILEAHVGI 840
GVIGKEGRQA ARNSDYAIPK FKHLKKMLLV HGHFYYIRIS ELVQYFFYKN VCFIFPQFLY 900
QFFCGFSQQT LYDTAYLTLY NISFTSLPIL LYSLMEQHVG IDVLKRDPTL YRDVAKNALL 960
RWRVFIYWTL LGLFDALVFF FGAYFVFENT TVTSNGQIFG NWTFGTLVFT VMVFTVTLKL 1020
ALDTHYWTWI NHFVIWGSLL FYVVFSLLWG GVIWPFLNYQ RMYYVFIQML SSGPAWLAIV 1080
LLVTISLLPD VLKKVLCRQL WPTATERVQT KSQCLSVEQS TIFMLSQTSS SLSF 1134
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FASTA
(Canonical) |
>LipidDB-9606-00532|P98196
MDCSLVRTLVHRYCAGEENWVDSRTIYVGHREPPPGAEAYIPQRYPDNRIVSSKYTFWNF
IPKNLFEQFRRVANFYFLIIFLVQLIIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHK
ADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTT
ASLDGESSHKTHYAVQDTKGFHTEEDIGGLHATIECEQPQPDLYKFVGRINVYSDLNDPV
VRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNAFLIVY
LCILISKALINTVLKYMWQSEPFRDEPWYNQKTESERQRNLFLKAFTDFLAFMVLFNYII
PVSMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLT
ENNMEFKECCIEGHVYVPHVICNGQVLPESSGIDMIDSSPSVNGREREELFFRALCLCHT
VQVKDDDSVDGPRKSPDGGKSCVYISSSPDEVALVEGVQRLGFTYLRLKDNYMEILNREN
HIERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPRVIEGKVDQIRARVER
NAVEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATA
VEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRRNTQLLELTTKRIEE
QSLHDVLFELSKTVLRHSGSLTRDNLSGLSADMQDYGLIIDGAALSLIMKPREDGSSGNY
RELFLEICRSCSAVLCCRMAPLQKAQIVKLIKFSKEHPITLAIGDGANDVSMILEAHVGI
GVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLY
QFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRDVAKNALL
RWRVFIYWTLLGLFDALVFFFGAYFVFENTTVTSNGQIFGNWTFGTLVFTVMVFTVTLKL
ALDTHYWTWINHFVIWGSLLFYVVFSLLWGGVIWPFLNYQRMYYVFIQMLSSGPAWLAIV
LLVTISLLPDVLKKVLCRQLWPTATERVQTKSQCLSVEQSTIFMLSQTSSSLSF
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Gene Ontology |
GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW GO:0005765; C:lysosomal membrane; IDA:UniProtKB GO:0016020; C:membrane; IDA:UniProtKB GO:0005886; C:plasma membrane; IEA:UniProtKB-KW GO:0055037; C:recycling endosome; IDA:UniProtKB GO:0005524; F:ATP binding; IEA:UniProtKB-KW GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro GO:0000287; F:magnesium ion binding; IEA:InterPro GO:0004012; F:phospholipid-translocating ATPase activity; IEA:UniProtKB-EC GO:0045332; P:phospholipid translocation; NAS:UniProtKB |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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