Probable phospholipid-transporting ATPase IA

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P70704 (AT8A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 106. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Probable phospholipid-transporting ATPase IA
EC=3.6.3.1

Alternative name(s):
ATPase class I type 8A member 1
Chromaffin granule ATPase II

Gene names

Name:	Atp8a1
Synonyms:	Atpc1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1149 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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 By similarity.
Tissue specificity	Found in most tissues except liver and testis. Most abundant in brain and lung. Also detected in fetal tissues.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. [View classification]

Ontologies

Keywords
Cellular component	Cytoplasmic vesicle Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cation transport Inferred from electronic annotation. Source: InterPro
Cellular component	chromaffin granule membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: InterPro phospholipid-translocating ATPase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1149

1149

Probable phospholipid-transporting ATPase IA

PRO_0000046361

Regions

Topological domain

1 – 65

Cytoplasmic Potential

Transmembrane

66 – 86

Helical; Potential

Topological domain

87 – 92

Extracellular Potential

Transmembrane

93 – 115

Helical; Potential

Topological domain

116 – 297

182

Cytoplasmic Potential

Transmembrane

298 – 319

Helical; Potential

Topological domain

320 – 344

Extracellular Potential

Transmembrane

345 – 366

Helical; Potential

Topological domain

367 – 842

476

Cytoplasmic Potential

Transmembrane

843 – 863

Helical; Potential

Topological domain

864 – 875

Extracellular Potential

Transmembrane

876 – 895

Helical; Potential

Topological domain

896 – 925

Cytoplasmic Potential

Transmembrane

926 – 947

Helical; Potential

Topological domain

948 – 961

Extracellular Potential

Transmembrane

962 – 984

Helical; Potential

Topological domain

985 – 990

Cytoplasmic Potential

Transmembrane

991 – 1011

Helical; Potential

Topological domain

1012 – 1029

Extracellular Potential

Transmembrane

1030 – 1055

Helical; Potential

Topological domain

1056 – 1149

Cytoplasmic Potential

Nucleotide binding

726 – 733

ATP Potential

Nucleotide binding

1080 – 1087

ATP Potential

Sites

Active site

409

4-aspartylphosphate intermediate By similarity

Metal binding

786

Magnesium By similarity

Metal binding

790

Magnesium By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.6

Modified residue

Phosphoserine Ref.5

Modified residue

Phosphothreonine Ref.3 Ref.4 Ref.5 Ref.6

Modified residue

Phosphoserine Ref.3 Ref.4 Ref.5 Ref.6

Modified residue

269

Phosphotyrosine Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P70704 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 95F70B2B091FD31E
Show »

FASTA

1,149

129,767

        10         20         30         40         50         60 
MPTMRRTVSE IRSRAEGYEK TDDVSEKTSL ADQEEVRTIF INQPQLTKFC NNHVSTAKYN 

        70         80         90        100        110        120 
VITFLPRFLY 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 SLMRISGRIE CESPNRHLYD FVGNIRLDGH 

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

       310        320        330        340        350        360 
LFCILIAMSL VCSVGSAIWN RRHSGKDWYL HLHYGGASNF GLNFLTFIIL FNNLIPISLL 

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

       430        440        450        460        470        480 
FKKCTIAGVA YGQSSQFGDE KTFNDPSLLD NLQNNHPTAP IICEFLTMMA VCHTAVPERE 

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

       550        560        570        580        590        600 
MSVVVRTPSG KLRLYCKGAD TVIYERLAET SKYKEITLKH LEQFATEGLR TLCFAVAEIS 

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

       670        680        690        700        710        720 
KADIKIWILT GDKQETAINI GHSCRLLKRN 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 VHGAWNYNRV 

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

       910        920        930        940        950        960 
RKENMLKYPE LYKTSQNALD FNTKVFWVHC LNGLFHSVIL FWFPLKALQY GTVFGNGKTS 

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

      1030       1040       1050       1060       1070       1080 
PDMSGEAAML FSSGVFWVGL LSIPVASLLL DVLYKVIKRT AFKTLVDEVQ ELEAKSQDPG 

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


TTKQRPDEW

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Multiple members of a third subfamily of P-type ATPases identified by genomic sequences and ESTs." Halleck M.S., Pradhan D., Blackman C.F., Berkes C., Williamson P.L., Schlegel R.A. Genome Res. 8:354-361(1998) [PubMed: 9548971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Teratocarcinoma.
[2]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-269, MASS SPECTROMETRY. Tissue: Brain.
[3]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-28 AND SER-29, MASS SPECTROMETRY. Tissue: Brain cortex.
[4]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-28 AND SER-29, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; THR-28 AND SER-29, MASS SPECTROMETRY. Tissue: Melanoma.
[6]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; THR-28 AND SER-29, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U75321 mRNA. Translation: AAB18627.1.
IPI	IPI00112776.
PIR	T30869.
RefSeq	NP_033857.1. NM_009727.2.
UniGene	Mm.153230.
3D structure databases
ProteinModelPortal	P70704.
SMR	P70704. Positions 764-805.
ModBase	Search...
Protein-protein interaction databases
STRING	P70704.
PTM databases
PhosphoSite	P70704.
Proteomic databases
PRIDE	P70704.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000072971; ENSMUSP00000072738; ENSMUSG00000037685.
GeneID	11980.
KEGG	mmu:11980.
UCSC	uc008xqb.1. mouse.
Organism-specific databases
CTD	10396.
MGI	MGI:1330848. Atp8a1.
Phylogenomic databases
HOVERGEN	HBG050601.
PhylomeDB	P70704.
Gene expression databases
ArrayExpress	P70704.
Bgee	P70704.
Genevestigator	P70704.
GermOnline	ENSMUSG00000037685. Mus musculus.
Family and domain databases
InterPro	IPR023306. ATPase_cation_domN. IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR006539. ATPase_P-typ_Plipid-transl. IPR023214. HAD-like_dom. [Graphical view]
Gene3D	G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 2 hits. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit. G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KO	K14802.
Pfam	PF00122. E1-E2_ATPase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01652. ATPase-Plipid. 1 hit. TIGR01494. ATPase_P-type. 3 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	280119.
SOURCE	Search...

Entry information

Entry name

AT8A1_MOUSE

Accession

Primary (citable) accession number: P70704

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 1, 1997
Last modified:	December 14, 2011
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents