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Reviewed, UniProtKB/Swiss-Prot Q29449 (AT8A1_BOVIN)

Last modified June 16, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Probable phospholipid-transporting ATPase IA
    EC=3.6.3.1
Alternative name(s):
    Chromaffin granule ATPase II
    ATPase class I type 8A member 1
Gene names
Name: ATP8A1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length1149 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

May play a role in the transport of aminophospholipids from the outer to the inner leaflet of various membranes and the maintenance of asymmetric distribution of phospholipids, mainly in secretory vesicles.

Catalytic activity

ATP + H2O + phospholipid(In) = ADP + phosphate + phospholipid(Out).

Subcellular location

Cytoplasmic vesicle › secretory vesicle › chromaffin granule membrane; Multi-pass membrane protein.

Tissue specificity

Kidney.

Sequence similarities

Belongs to the cation transport ATPase (P-type) family. Type IV subfamily.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11491149Probable phospholipid-transporting ATPase IA
PRO_0000046359

Regions

Topological domain1 – 6565Cytoplasmic Potential
Transmembrane66 – 8621 Potential
Topological domain87 – 926Extracellular Potential
Transmembrane93 – 11523 Potential
Topological domain116 – 297182Cytoplasmic Potential
Transmembrane298 – 31922 Potential
Topological domain320 – 34425Extracellular Potential
Transmembrane345 – 36622 Potential
Topological domain367 – 842476Cytoplasmic Potential
Transmembrane843 – 86321 Potential
Topological domain864 – 87512Extracellular Potential
Transmembrane876 – 89520 Potential
Topological domain896 – 92530Cytoplasmic Potential
Transmembrane926 – 94722 Potential
Topological domain948 – 96114Extracellular Potential
Transmembrane962 – 98423 Potential
Topological domain985 – 9906Cytoplasmic Potential
Transmembrane991 – 101121 Potential
Topological domain1012 – 102918Extracellular Potential
Transmembrane1030 – 105526 Potential
Topological domain1056 – 114994Cytoplasmic Potential
Nucleotide binding726 – 7338ATP Potential
Nucleotide binding1080 – 10878ATP Potential

Sites

Active site40914-aspartylphosphate intermediate By similarity
Metal binding7861Magnesium By similarity
Metal binding7901Magnesium By similarity

Amino acid modifications

Modified residue91Phosphoserine By similarity
Modified residue251Phosphoserine By similarity
Modified residue281Phosphothreonine By similarity
Modified residue291Phosphoserine By similarity
Modified residue2691Phosphotyrosine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q29449-1 [UniParc].

Last modified January 1, 1999. Version 2.
Checksum: 0EE71C958E8C5BE1

FASTA1,149130,026
        10         20         30         40         50         60 
MPTMRRTVSE IRSRAEGYEK TDDVSEKTSL ADQEEIRTIF INQPQLTKFC NNHVSTAKYN 

        70         80         90        100        110        120 
IITFLPRFLY SQFRRAANSF FLFIALLQQI PDVSPTGRYT TLVPLLFILA VAAIKEIIED 

       130        140        150        160        170        180 
IKRHKADNAV NKKQTQVLRN GAWEIVHWEK VNVGDIVIIK GKEYIPADTV LLSSSEPQAM 

       190        200        210        220        230        240 
CYIETSNLDG ETNLKIRQGL PATSDIKDID SLMRLSGRIE CESPNRHLYD FVGNIRLDGR 

       250        260        270        280        290        300 
STVPLGADQI LLRGAQLRNT QWVHGIVVYT GHDTKLMQNS TSPPLKLSNV ERITNVQILI 

       310        320        330        340        350        360 
LFCILIAMSL VCSVGSAIWN RRHSGRDWYL NLNYGGANNF GLNFLTFIIL FNNLIPISLL 

       370        380        390        400        410        420 
VTLEVVKFTQ AYFINWDLDM HYEPTDTAAM ARTSNLNVEL GQVKYIFSDK TGTLTCNVMQ 

       430        440        450        460        470        480 
FKKCTIAGVA YGQNSQFGDE KTFSDSSLLE NLQNNHPTAP IICEFLTMMA VCHTAVPERE 

       490        500        510        520        530        540 
GDKIIYQAAS PDEGALVRAA KQLNFVFTGR TPDSVIIDSL GQEERYELLN VLEFTSARKR 

       550        560        570        580        590        600 
MSVIVRTPSG KLRLYCKGAD TVIYDRLAET SKYKEITLKH LEQFATEGLR TLCFAVAEIS 

       610        620        630        640        650        660 
ESDFQEWRAV YHRASTSVQN RLLKLEESYE LIEKNLQLLG ATAIEDKLQD QVPETIETLM 

       670        680        690        700        710        720 
KADIKIWILT GDKQETAINI GHSCKLRRKN MGMIVINEGS LDGTRETLSR HCTTLGDALR 

       730        740        750        760        770        780 
KENDFALIID GKTLKYALTF GVRQYFLDLA LSCKAVICCR VSPLQKSEVV EMVKKQVKVI 

       790        800        810        820        830        840 
TLAIGDGAND VSMIQTAHVG VGISGNEGLQ AANSSDYSIA QFKYLKNLLM VHGAWNYNRG 

       850        860        870        880        890        900 
SKCILYCFYK NIVLYIIEIW FAFVNGFSGQ ILFERWCIGL YNVMFTAMPP LTLGIFERSC 

       910        920        930        940        950        960 
RKEYMLKYPE LYKTSQNALD FNTKVFWVHC LNGLFHSVIL FWFPLKALQY GTVFENGRTS 

       970        980        990       1000       1010       1020 
DYLLLGNFVY TFVVITVCLK AGLETSYWTW FSHIAIWGSI ALWVVFFGIY SSLWPAVPMA 

      1030       1040       1050       1060       1070       1080 
PDMSGEAAML FSSGVFWMGL LFIPVASLLL DVVYKVIKRT AFKTLVDEVQ ELEAKSQDPG 

      1090       1100       1110       1120       1130       1140 
AVVLGKSLTE RAQLLKNVFK KNHVNLYRSE SLQQNLLHGY AFSQDENGIV SQSEVIRAYD 


TTKQRPDEW

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References

[1]"A subfamily of P-type ATPases with aminophospholipid transporting activity."
Tang X., Halleck M.S., Schlegel R.A., Williamson P.L.
Science 272:1495-1497(1996) [PubMed: 8633245] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 502-678 AND 1144-1149.
Tissue: Adrenal medulla.

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Cross-references

Sequence databases

U51100 mRNA. Translation: AAD03352.1.
IPIIPI00696807.
PIRT18515.
RefSeqNP_777263.1.
UniGeneBt.36109

3D structure databases

ModBaseSearch...

Protein family/group databases

TCDB3.A.3.8.1. P-type ATPase (P-ATPase) superfamily.

Genome annotation databases

GeneID317692.
KEGGbta:317692.

Phylogenomic databases

HOVERGENQ29449.

Enzyme and pathway databases

BRENDA3.6.3.1. 251.

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-reg.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_phosphor_site.
IPR006539. ATPase_P-typ_Plipid-transl.
IPR005834. Dehalogen-like_hydro.
[Graphical view]
PANTHERPTHR11939. ATPase_P. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
TIGRFAMsTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 4 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAT8A1_BOVIN
AccessionPrimary (citable) accession number: Q29449
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1999
Last modified: June 16, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents