Full text data of ATP8A1
ATP8A1
(ATPIA)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Probable phospholipid-transporting ATPase IA; 3.6.3.1 (ATPase class I type 8A member 1; Chromaffin granule ATPase II)
Probable phospholipid-transporting ATPase IA; 3.6.3.1 (ATPase class I type 8A member 1; Chromaffin granule ATPase II)
hRBCD
IPI00032402
IPI00032402 Splice Isoform 1 Of Potential phospholipid-transporting ATPase IA translocase PS-PI from outside to inside, preventing coagulation cascade, conteracts the scramblases, also spontaneous flip-flop soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic Isoform 1 or 2 found at its expected molecular weight found at molecular weight
IPI00032402 Splice Isoform 1 Of Potential phospholipid-transporting ATPase IA translocase PS-PI from outside to inside, preventing coagulation cascade, conteracts the scramblases, also spontaneous flip-flop soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic Isoform 1 or 2 found at its expected molecular weight found at molecular weight
UniProt
Q9Y2Q0
ID AT8A1_HUMAN Reviewed; 1164 AA.
AC Q9Y2Q0; Q32M35; Q32M36; Q4W5J7; Q4W5P2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Probable phospholipid-transporting ATPase IA;
DE EC=3.6.3.1;
DE AltName: Full=ATPase class I type 8A member 1;
DE AltName: Full=Chromaffin granule ATPase II;
GN Name=ATP8A1; Synonyms=ATPIA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Skeletal muscle;
RX PubMed=10198212; DOI=10.1006/bbrc.1999.0347;
RA Mouro I., Halleck M.S., Schlegel R.A., Mattei M.-G., Williamson P.L.,
RA Zachowski A., Devaux P., Cartron J.-P., Colin Y.;
RT "Cloning, expression, and chromosomal mapping of a human ATPase II
RT gene, member of the third subfamily of P-type ATPases and orthologous
RT to the presumed bovine and murine aminophospholipid translocase.";
RL Biochem. Biophys. Res. Commun. 257:333-339(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-1164 (ISOFORM 1).
RC TISSUE=Brain;
RA Osada S., Nakanishi Y.;
RT "cDNA cloning of human ATPaseII.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP INTERACTION WITH TMEM30A, AND SUBCELLULAR LOCATION.
RX PubMed=21914794; DOI=10.1074/jbc.M111.281006;
RA Takatsu H., Baba K., Shima T., Umino H., Kato U., Umeda M.,
RA Nakayama K., Shin H.W.;
RT "ATP9B, a P4-ATPase (a putative aminophospholipid translocase),
RT localizes to the trans-Golgi network in a CDC50 protein-independent
RT manner.";
RL J. Biol. Chem. 286:38159-38167(2011).
CC -!- FUNCTION: May play a role in the transport of aminophospholipids
CC from the outer to the inner leaflet of various membranes and the
CC maintenance of asymmetric distribution of phospholipids, mainly in
CC secretory vesicles.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(Side 1) = ADP +
CC phosphate + phospholipid(Side 2).
CC -!- SUBUNIT: Interacts with TMEM30A, but not with TMEM30B.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC chromaffin granule membrane; Multi-pass membrane protein (By
CC similarity). Cytoplasmic granule. Cell membrane. Endoplasmic
CC reticulum. Note=Exit from the endoplasmic reticulum requires the
CC presence of TMEM30A, but not TMEM30B. In the presence of TMEM30A,
CC predominantly located in cytoplasmic punctate structures.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=Q9Y2Q0-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q9Y2Q0-2; Sequence=VSP_000431;
CC Name=3;
CC IsoId=Q9Y2Q0-3; Sequence=VSP_040977, VSP_000431;
CC -!- TISSUE SPECIFICITY: Found in most adult tissues except liver,
CC testis and placenta. Most abundant in heart, brain and skeletal
CC muscle. Also detected in fetal tissues. Isoform 1 is only detected
CC in brain, skeletal muscle and heart and is the most abundant form
CC in skeletal muscle.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC (TC 3.A.3) family. Type IV subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI09318.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAA77248.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF067820; AAD34706.1; -; mRNA.
DR EMBL; AC084010; AAY40980.1; -; Genomic_DNA.
DR EMBL; AC096734; AAY40924.1; -; Genomic_DNA.
DR EMBL; AC110788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471069; EAW93003.1; -; Genomic_DNA.
DR EMBL; BC109317; AAI09318.1; ALT_INIT; mRNA.
DR EMBL; BC109318; AAI09319.1; -; mRNA.
DR EMBL; AB013452; BAA77248.1; ALT_INIT; mRNA.
DR RefSeq; NP_001098999.1; NM_001105529.1.
DR RefSeq; NP_006086.1; NM_006095.2.
DR UniGene; Hs.435052; -.
DR ProteinModelPortal; Q9Y2Q0; -.
DR SMR; Q9Y2Q0; 389-867.
DR STRING; 9606.ENSP00000371084; -.
DR DrugBank; DB00144; Phosphatidylserine.
DR TCDB; 3.A.3.8.13; the p-type atpase (p-atpase) superfamily.
DR PhosphoSite; Q9Y2Q0; -.
DR DMDM; 8134331; -.
DR PaxDb; Q9Y2Q0; -.
DR PRIDE; Q9Y2Q0; -.
DR Ensembl; ENST00000264449; ENSP00000264449; ENSG00000124406.
DR Ensembl; ENST00000381668; ENSP00000371084; ENSG00000124406.
DR GeneID; 10396; -.
DR KEGG; hsa:10396; -.
DR UCSC; uc003gwr.2; human.
DR CTD; 10396; -.
DR GeneCards; GC04M042410; -.
DR HGNC; HGNC:13531; ATP8A1.
DR HPA; HPA049948; -.
DR HPA; HPA052935; -.
DR MIM; 609542; gene.
DR neXtProt; NX_Q9Y2Q0; -.
DR PharmGKB; PA25165; -.
DR eggNOG; COG0474; -.
DR HOGENOM; HOG000202528; -.
DR HOVERGEN; HBG050601; -.
DR InParanoid; Q9Y2Q0; -.
DR KO; K14802; -.
DR OMA; PVEREYK; -.
DR OrthoDB; EOG7RRF68; -.
DR PhylomeDB; Q9Y2Q0; -.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR ChiTaRS; ATP8A1; human.
DR GenomeRNAi; 10396; -.
DR NextBio; 39390; -.
DR PRO; PR:Q9Y2Q0; -.
DR ArrayExpress; Q9Y2Q0; -.
DR Bgee; Q9Y2Q0; -.
DR CleanEx; HS_ATP8A1; -.
DR Genevestigator; Q9Y2Q0; -.
DR GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0015247; F:aminophospholipid transporter activity; NAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0019829; F:cation-transporting ATPase activity; NAS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004012; F:phospholipid-translocating ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0045332; P:phospholipid translocation; NAS:UniProtKB.
DR Gene3D; 2.70.150.10; -; 2.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR006539; ATPase_P-typ_Plipid-transp.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
DR InterPro; IPR001757; Cation_transp_P_typ_ATPase.
DR InterPro; IPR023214; HAD-like_dom.
DR PANTHER; PTHR24092; PTHR24092; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SUPFAM; SSF56784; SSF56784; 3.
DR SUPFAM; SSF81660; SSF81660; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Hydrolase; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Polymorphism; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 1164 Probable phospholipid-transporting ATPase
FT IA.
FT /FTId=PRO_0000046360.
FT TOPO_DOM 1 65 Cytoplasmic (Potential).
FT TRANSMEM 66 86 Helical; (Potential).
FT TOPO_DOM 87 92 Extracellular (Potential).
FT TRANSMEM 93 115 Helical; (Potential).
FT TOPO_DOM 116 297 Cytoplasmic (Potential).
FT TRANSMEM 298 319 Helical; (Potential).
FT TOPO_DOM 320 344 Extracellular (Potential).
FT TRANSMEM 345 366 Helical; (Potential).
FT TOPO_DOM 367 857 Cytoplasmic (Potential).
FT TRANSMEM 858 878 Helical; (Potential).
FT TOPO_DOM 879 890 Extracellular (Potential).
FT TRANSMEM 891 910 Helical; (Potential).
FT TOPO_DOM 911 940 Cytoplasmic (Potential).
FT TRANSMEM 941 962 Helical; (Potential).
FT TOPO_DOM 963 976 Extracellular (Potential).
FT TRANSMEM 977 999 Helical; (Potential).
FT TOPO_DOM 1000 1005 Cytoplasmic (Potential).
FT TRANSMEM 1006 1026 Helical; (Potential).
FT TOPO_DOM 1027 1044 Extracellular (Potential).
FT TRANSMEM 1045 1070 Helical; (Potential).
FT TOPO_DOM 1071 1164 Cytoplasmic (Potential).
FT NP_BIND 741 748 ATP (Potential).
FT NP_BIND 1095 1102 ATP (Potential).
FT ACT_SITE 409 409 4-aspartylphosphate intermediate (By
FT similarity).
FT METAL 801 801 Magnesium (By similarity).
FT METAL 805 805 Magnesium (By similarity).
FT MOD_RES 25 25 Phosphoserine.
FT MOD_RES 28 28 Phosphothreonine (By similarity).
FT MOD_RES 29 29 Phosphoserine (By similarity).
FT VAR_SEQ 152 171 AVGEIVKVTNGEHLPADLIS -> NVGDIVIIKGKEYIPAD
FT TVL (in isoform 3).
FT /FTId=VSP_040977.
FT VAR_SEQ 433 447 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_000431.
FT VARIANT 673 673 T -> M (in dbSNP:rs3792687).
FT /FTId=VAR_022003.
FT CONFLICT 364 364 E -> K (in Ref. 4; BAA77248).
SQ SEQUENCE 1164 AA; 131369 MW; CE1EAF0206CD36F7 CRC64;
MPTMRRTVSE IRSRAEGYEK TDDVSEKTSL ADQEEVRTIF INQPQLTKFC NNHVSTAKYN
IITFLPRFLY SQFRRAANSF FLFIALLQQI PDVSPTGRYT TLVPLLFILA VAAIKEIIED
IKRHKADNAV NKKQTQVLRN GAWEIVHWEK VAVGEIVKVT NGEHLPADLI SLSSSEPQAM
CYIETSNLDG ETNLKIRQGL PATSDIKDVD SLMRISGRIE CESPNRHLYD FVGNIRLDGH
GTVPLGADQI LLRGAQLRNT QWVHGIVVYT GHDTKLMQNS TSPPLKLSNV ERITNVQILI
LFCILIAMSL VCSVGSAIWN RRHSGKDWYL NLNYGGASNF GLNFLTFIIL FNNLIPISLL
VTLEVVKFTQ AYFINWDLDM HYEPTDTAAM ARTSNLNEEL GQVKYIFSDK TGTLTCNVMQ
FKKCTIAGVA YGHVPEPEDY GCSPDEWQNS QFGDEKTFSD SSLLENLQNN HPTAPIICEF
LTMMAVCHTA VPEREGDKII YQAASPDEGA LVRAAKQLNF VFTGRTPDSV IIDSLGQEER
YELLNVLEFT SARKRMSVIV RTPSGKLRLY CKGADTVIYD RLAETSKYKE ITLKHLEQFA
TEGLRTLCFA VAEISESDFQ EWRAVYQRAS TSVQNRLLKL EESYELIEKN LQLLGATAIE
DKLQDQVPET IETLMKADIK IWILTGDKQE TAINIGHSCK LLKKNMGMIV INEGSLDGTR
ETLSRHCTTL GDALRKENDF ALIIDGKTLK YALTFGVRQY FLDLALSCKA VICCRVSPLQ
KSEVVEMVKK QVKVVTLAIG DGANDVSMIQ TAHVGVGISG NEGLQAANSS DYSIAQFKYL
KNLLMIHGAW NYNRVSKCIL YCFYKNIVLY IIEIWFAFVN GFSGQILFER WCIGLYNVMF
TAMPPLTLGI FERSCRKENM LKYPELYKTS QNALDFNTKV FWVHCLNGLF HSVILFWFPL
KALQYGTAFG NGKTSDYLLL GNFVYTFVVI TVCLKAGLET SYWTWFSHIA IWGSIALWVV
FFGIYSSLWP AIPMAPDMSG EAAMLFSSGV FWMGLLFIPV ASLLLDVVYK VIKRTAFKTL
VDEVQELEAK SQDPGAVVLG KSLTERAQLL KNVFKKNHVN LYRSESLQQN LLHGYAFSQD
ENGIVSQSEV IRAYDTTKQR PDEW
//
ID AT8A1_HUMAN Reviewed; 1164 AA.
AC Q9Y2Q0; Q32M35; Q32M36; Q4W5J7; Q4W5P2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Probable phospholipid-transporting ATPase IA;
DE EC=3.6.3.1;
DE AltName: Full=ATPase class I type 8A member 1;
DE AltName: Full=Chromaffin granule ATPase II;
GN Name=ATP8A1; Synonyms=ATPIA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Skeletal muscle;
RX PubMed=10198212; DOI=10.1006/bbrc.1999.0347;
RA Mouro I., Halleck M.S., Schlegel R.A., Mattei M.-G., Williamson P.L.,
RA Zachowski A., Devaux P., Cartron J.-P., Colin Y.;
RT "Cloning, expression, and chromosomal mapping of a human ATPase II
RT gene, member of the third subfamily of P-type ATPases and orthologous
RT to the presumed bovine and murine aminophospholipid translocase.";
RL Biochem. Biophys. Res. Commun. 257:333-339(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-1164 (ISOFORM 1).
RC TISSUE=Brain;
RA Osada S., Nakanishi Y.;
RT "cDNA cloning of human ATPaseII.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP INTERACTION WITH TMEM30A, AND SUBCELLULAR LOCATION.
RX PubMed=21914794; DOI=10.1074/jbc.M111.281006;
RA Takatsu H., Baba K., Shima T., Umino H., Kato U., Umeda M.,
RA Nakayama K., Shin H.W.;
RT "ATP9B, a P4-ATPase (a putative aminophospholipid translocase),
RT localizes to the trans-Golgi network in a CDC50 protein-independent
RT manner.";
RL J. Biol. Chem. 286:38159-38167(2011).
CC -!- FUNCTION: May play a role in the transport of aminophospholipids
CC from the outer to the inner leaflet of various membranes and the
CC maintenance of asymmetric distribution of phospholipids, mainly in
CC secretory vesicles.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(Side 1) = ADP +
CC phosphate + phospholipid(Side 2).
CC -!- SUBUNIT: Interacts with TMEM30A, but not with TMEM30B.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC chromaffin granule membrane; Multi-pass membrane protein (By
CC similarity). Cytoplasmic granule. Cell membrane. Endoplasmic
CC reticulum. Note=Exit from the endoplasmic reticulum requires the
CC presence of TMEM30A, but not TMEM30B. In the presence of TMEM30A,
CC predominantly located in cytoplasmic punctate structures.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=Q9Y2Q0-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q9Y2Q0-2; Sequence=VSP_000431;
CC Name=3;
CC IsoId=Q9Y2Q0-3; Sequence=VSP_040977, VSP_000431;
CC -!- TISSUE SPECIFICITY: Found in most adult tissues except liver,
CC testis and placenta. Most abundant in heart, brain and skeletal
CC muscle. Also detected in fetal tissues. Isoform 1 is only detected
CC in brain, skeletal muscle and heart and is the most abundant form
CC in skeletal muscle.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC (TC 3.A.3) family. Type IV subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI09318.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAA77248.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF067820; AAD34706.1; -; mRNA.
DR EMBL; AC084010; AAY40980.1; -; Genomic_DNA.
DR EMBL; AC096734; AAY40924.1; -; Genomic_DNA.
DR EMBL; AC110788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471069; EAW93003.1; -; Genomic_DNA.
DR EMBL; BC109317; AAI09318.1; ALT_INIT; mRNA.
DR EMBL; BC109318; AAI09319.1; -; mRNA.
DR EMBL; AB013452; BAA77248.1; ALT_INIT; mRNA.
DR RefSeq; NP_001098999.1; NM_001105529.1.
DR RefSeq; NP_006086.1; NM_006095.2.
DR UniGene; Hs.435052; -.
DR ProteinModelPortal; Q9Y2Q0; -.
DR SMR; Q9Y2Q0; 389-867.
DR STRING; 9606.ENSP00000371084; -.
DR DrugBank; DB00144; Phosphatidylserine.
DR TCDB; 3.A.3.8.13; the p-type atpase (p-atpase) superfamily.
DR PhosphoSite; Q9Y2Q0; -.
DR DMDM; 8134331; -.
DR PaxDb; Q9Y2Q0; -.
DR PRIDE; Q9Y2Q0; -.
DR Ensembl; ENST00000264449; ENSP00000264449; ENSG00000124406.
DR Ensembl; ENST00000381668; ENSP00000371084; ENSG00000124406.
DR GeneID; 10396; -.
DR KEGG; hsa:10396; -.
DR UCSC; uc003gwr.2; human.
DR CTD; 10396; -.
DR GeneCards; GC04M042410; -.
DR HGNC; HGNC:13531; ATP8A1.
DR HPA; HPA049948; -.
DR HPA; HPA052935; -.
DR MIM; 609542; gene.
DR neXtProt; NX_Q9Y2Q0; -.
DR PharmGKB; PA25165; -.
DR eggNOG; COG0474; -.
DR HOGENOM; HOG000202528; -.
DR HOVERGEN; HBG050601; -.
DR InParanoid; Q9Y2Q0; -.
DR KO; K14802; -.
DR OMA; PVEREYK; -.
DR OrthoDB; EOG7RRF68; -.
DR PhylomeDB; Q9Y2Q0; -.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR ChiTaRS; ATP8A1; human.
DR GenomeRNAi; 10396; -.
DR NextBio; 39390; -.
DR PRO; PR:Q9Y2Q0; -.
DR ArrayExpress; Q9Y2Q0; -.
DR Bgee; Q9Y2Q0; -.
DR CleanEx; HS_ATP8A1; -.
DR Genevestigator; Q9Y2Q0; -.
DR GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0015247; F:aminophospholipid transporter activity; NAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0019829; F:cation-transporting ATPase activity; NAS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004012; F:phospholipid-translocating ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0045332; P:phospholipid translocation; NAS:UniProtKB.
DR Gene3D; 2.70.150.10; -; 2.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR006539; ATPase_P-typ_Plipid-transp.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
DR InterPro; IPR001757; Cation_transp_P_typ_ATPase.
DR InterPro; IPR023214; HAD-like_dom.
DR PANTHER; PTHR24092; PTHR24092; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SUPFAM; SSF56784; SSF56784; 3.
DR SUPFAM; SSF81660; SSF81660; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Hydrolase; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Polymorphism; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 1164 Probable phospholipid-transporting ATPase
FT IA.
FT /FTId=PRO_0000046360.
FT TOPO_DOM 1 65 Cytoplasmic (Potential).
FT TRANSMEM 66 86 Helical; (Potential).
FT TOPO_DOM 87 92 Extracellular (Potential).
FT TRANSMEM 93 115 Helical; (Potential).
FT TOPO_DOM 116 297 Cytoplasmic (Potential).
FT TRANSMEM 298 319 Helical; (Potential).
FT TOPO_DOM 320 344 Extracellular (Potential).
FT TRANSMEM 345 366 Helical; (Potential).
FT TOPO_DOM 367 857 Cytoplasmic (Potential).
FT TRANSMEM 858 878 Helical; (Potential).
FT TOPO_DOM 879 890 Extracellular (Potential).
FT TRANSMEM 891 910 Helical; (Potential).
FT TOPO_DOM 911 940 Cytoplasmic (Potential).
FT TRANSMEM 941 962 Helical; (Potential).
FT TOPO_DOM 963 976 Extracellular (Potential).
FT TRANSMEM 977 999 Helical; (Potential).
FT TOPO_DOM 1000 1005 Cytoplasmic (Potential).
FT TRANSMEM 1006 1026 Helical; (Potential).
FT TOPO_DOM 1027 1044 Extracellular (Potential).
FT TRANSMEM 1045 1070 Helical; (Potential).
FT TOPO_DOM 1071 1164 Cytoplasmic (Potential).
FT NP_BIND 741 748 ATP (Potential).
FT NP_BIND 1095 1102 ATP (Potential).
FT ACT_SITE 409 409 4-aspartylphosphate intermediate (By
FT similarity).
FT METAL 801 801 Magnesium (By similarity).
FT METAL 805 805 Magnesium (By similarity).
FT MOD_RES 25 25 Phosphoserine.
FT MOD_RES 28 28 Phosphothreonine (By similarity).
FT MOD_RES 29 29 Phosphoserine (By similarity).
FT VAR_SEQ 152 171 AVGEIVKVTNGEHLPADLIS -> NVGDIVIIKGKEYIPAD
FT TVL (in isoform 3).
FT /FTId=VSP_040977.
FT VAR_SEQ 433 447 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_000431.
FT VARIANT 673 673 T -> M (in dbSNP:rs3792687).
FT /FTId=VAR_022003.
FT CONFLICT 364 364 E -> K (in Ref. 4; BAA77248).
SQ SEQUENCE 1164 AA; 131369 MW; CE1EAF0206CD36F7 CRC64;
MPTMRRTVSE IRSRAEGYEK TDDVSEKTSL ADQEEVRTIF INQPQLTKFC NNHVSTAKYN
IITFLPRFLY SQFRRAANSF FLFIALLQQI PDVSPTGRYT TLVPLLFILA VAAIKEIIED
IKRHKADNAV NKKQTQVLRN GAWEIVHWEK VAVGEIVKVT NGEHLPADLI SLSSSEPQAM
CYIETSNLDG ETNLKIRQGL PATSDIKDVD SLMRISGRIE CESPNRHLYD FVGNIRLDGH
GTVPLGADQI LLRGAQLRNT QWVHGIVVYT GHDTKLMQNS TSPPLKLSNV ERITNVQILI
LFCILIAMSL VCSVGSAIWN RRHSGKDWYL NLNYGGASNF GLNFLTFIIL FNNLIPISLL
VTLEVVKFTQ AYFINWDLDM HYEPTDTAAM ARTSNLNEEL GQVKYIFSDK TGTLTCNVMQ
FKKCTIAGVA YGHVPEPEDY GCSPDEWQNS QFGDEKTFSD SSLLENLQNN HPTAPIICEF
LTMMAVCHTA VPEREGDKII YQAASPDEGA LVRAAKQLNF VFTGRTPDSV IIDSLGQEER
YELLNVLEFT SARKRMSVIV RTPSGKLRLY CKGADTVIYD RLAETSKYKE ITLKHLEQFA
TEGLRTLCFA VAEISESDFQ EWRAVYQRAS TSVQNRLLKL EESYELIEKN LQLLGATAIE
DKLQDQVPET IETLMKADIK IWILTGDKQE TAINIGHSCK LLKKNMGMIV INEGSLDGTR
ETLSRHCTTL GDALRKENDF ALIIDGKTLK YALTFGVRQY FLDLALSCKA VICCRVSPLQ
KSEVVEMVKK QVKVVTLAIG DGANDVSMIQ TAHVGVGISG NEGLQAANSS DYSIAQFKYL
KNLLMIHGAW NYNRVSKCIL YCFYKNIVLY IIEIWFAFVN GFSGQILFER WCIGLYNVMF
TAMPPLTLGI FERSCRKENM LKYPELYKTS QNALDFNTKV FWVHCLNGLF HSVILFWFPL
KALQYGTAFG NGKTSDYLLL GNFVYTFVVI TVCLKAGLET SYWTWFSHIA IWGSIALWVV
FFGIYSSLWP AIPMAPDMSG EAAMLFSSGV FWMGLLFIPV ASLLLDVVYK VIKRTAFKTL
VDEVQELEAK SQDPGAVVLG KSLTERAQLL KNVFKKNHVN LYRSESLQQN LLHGYAFSQD
ENGIVSQSEV IRAYDTTKQR PDEW
//
MIM
609542
*RECORD*
*FIELD* NO
609542
*FIELD* TI
*609542 ATPase, CLASS I, TYPE 8A, MEMBER 1; ATP8A1
;;ATPase II
*FIELD* TX
CLONING
read more
By screening a human skeletal muscle cDNA library using bovine ATPase
II, a presumed aminophospholipid translocase, followed by 5-prime RACE,
Mouro et al. (1999) cloned ATP8A1, which they called ATPase II. The
deduced 1,164 amino acid protein contains characteristics of members of
the third subfamily of P-type ATPases. Northern blot analysis detected a
9.5-kb transcript in most adult and fetal tissues examined. Highest
expression was in heart, brain, and skeletal muscle, and no expression
was detected in adult liver, testis, and placenta. RT-PCR revealed an
ATP8A1 splice variant that encodes a protein lacking 15 amino acids in
the predicted second intracytoplasmic loop near a phosphorylation site.
Transcripts encoding proteins with the insert were detected in brain,
skeletal muscle, and heart, and transcripts encoding proteins without
the sequence were detected in all tissues examined.
GENE STRUCTURE
Sobocki et al. (2005) determined that the ATP8A1 gene contains 37 exons
and spans 244 kb. A CpG island covers the entire 5-prime UTR, the entire
first exon, and part of the first intron. The promoter region lacks a
TATA box, but it contains a core promoter region for CPBP (602053)
binding and many other enhancer and repressor elements. The promoter
also has multiple transcription start sites. Sobocki et al. (2005)
identified 2 promoter variants distinguished by the presence or absence
of a 15-bp direct repeat within the GC-rich core promoter region.
Reporter gene assays showed strong promoter activity in human
oligodendroglioma, neuroblastoma, and endothelial cell lines.
MAPPING
By in situ hybridization, Mouro et al. (1999) mapped the ATP8A1 gene to
chromosome 4p14-p12.
*FIELD* RF
1. Mouro, I.; Halleck, M. S.; Schlegel, R. A.; Mattei, M. G.; Williamson,
P.; Zachowski, A.; Devaux, P.; Cartron, J.-P.; Colin, Y.: Cloning,
expression, and chromosomal mapping of a human ATPase II gene, member
of the third subfamily of P-type ATPases and orthologous to the presumed
bovine and murine aminophospholipid translocase. Biochem. Biophys.
Res. Commun. 257: 333-339, 1999.
2. Sobocki, T.; Jayman, F.; Sobocka, M. B.; Duchatellier, R.; Banerjee,
P.: Isolation, sequencing, and functional analysis of the TATA-less
human ATPase II promoter. Biochim. Biophys. Acta 1728: 186-198,
2005.
*FIELD* CD
Patricia A. Hartz: 8/22/2005
*FIELD* ED
mgross: 08/22/2005
*RECORD*
*FIELD* NO
609542
*FIELD* TI
*609542 ATPase, CLASS I, TYPE 8A, MEMBER 1; ATP8A1
;;ATPase II
*FIELD* TX
CLONING
read more
By screening a human skeletal muscle cDNA library using bovine ATPase
II, a presumed aminophospholipid translocase, followed by 5-prime RACE,
Mouro et al. (1999) cloned ATP8A1, which they called ATPase II. The
deduced 1,164 amino acid protein contains characteristics of members of
the third subfamily of P-type ATPases. Northern blot analysis detected a
9.5-kb transcript in most adult and fetal tissues examined. Highest
expression was in heart, brain, and skeletal muscle, and no expression
was detected in adult liver, testis, and placenta. RT-PCR revealed an
ATP8A1 splice variant that encodes a protein lacking 15 amino acids in
the predicted second intracytoplasmic loop near a phosphorylation site.
Transcripts encoding proteins with the insert were detected in brain,
skeletal muscle, and heart, and transcripts encoding proteins without
the sequence were detected in all tissues examined.
GENE STRUCTURE
Sobocki et al. (2005) determined that the ATP8A1 gene contains 37 exons
and spans 244 kb. A CpG island covers the entire 5-prime UTR, the entire
first exon, and part of the first intron. The promoter region lacks a
TATA box, but it contains a core promoter region for CPBP (602053)
binding and many other enhancer and repressor elements. The promoter
also has multiple transcription start sites. Sobocki et al. (2005)
identified 2 promoter variants distinguished by the presence or absence
of a 15-bp direct repeat within the GC-rich core promoter region.
Reporter gene assays showed strong promoter activity in human
oligodendroglioma, neuroblastoma, and endothelial cell lines.
MAPPING
By in situ hybridization, Mouro et al. (1999) mapped the ATP8A1 gene to
chromosome 4p14-p12.
*FIELD* RF
1. Mouro, I.; Halleck, M. S.; Schlegel, R. A.; Mattei, M. G.; Williamson,
P.; Zachowski, A.; Devaux, P.; Cartron, J.-P.; Colin, Y.: Cloning,
expression, and chromosomal mapping of a human ATPase II gene, member
of the third subfamily of P-type ATPases and orthologous to the presumed
bovine and murine aminophospholipid translocase. Biochem. Biophys.
Res. Commun. 257: 333-339, 1999.
2. Sobocki, T.; Jayman, F.; Sobocka, M. B.; Duchatellier, R.; Banerjee,
P.: Isolation, sequencing, and functional analysis of the TATA-less
human ATPase II promoter. Biochim. Biophys. Acta 1728: 186-198,
2005.
*FIELD* CD
Patricia A. Hartz: 8/22/2005
*FIELD* ED
mgross: 08/22/2005