Q9NTI2 (AT8A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
ATPase class I type 8A member 2
ML-1

Gene names

Name:	ATP8A2
Synonyms:	ATPIB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1148 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	ATP + H2O + phospholipid(side 1) = ADP + phosphate + phospholipid(side 2).
Subcellular location	Membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. [View classification]
Sequence caution	The sequence BAC04396.1 differs from that shown. Reason: Erroneous initiation. Isoform 2: The sequence AAF40215.2 differs from that shown. Reason: Frameshift at position 522.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
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	negative regulation of cell proliferation Traceable author statement Ref.3. Source: ProtInc neuron projection development Inferred from electronic annotation. Source: Compara
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cation-transporting ATPase activity 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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NTI2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform 2 (identifier: Q9NTI2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     515-528: MGQEQTFGILNVLE → VSNMRVHISDHLLL
     529-1148: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1148	1148	Probable phospholipid-transporting ATPase IB		PRO_0000046362
Regions
	Topological domain	1 – 44	44	Cytoplasmic Potential
	Transmembrane	45 – 66	22	Helical; Potential
	Topological domain	67 – 71	5	Extracellular Potential
	Transmembrane	72 – 94	23	Helical; Potential
	Topological domain	95 – 276	182	Cytoplasmic Potential
	Transmembrane	277 – 298	22	Helical; Potential
	Topological domain	299 – 323	25	Extracellular Potential
	Transmembrane	324 – 345	22	Helical; Potential
	Topological domain	346 – 837	492	Cytoplasmic Potential
	Transmembrane	838 – 858	21	Helical; Potential
	Topological domain	859 – 870	12	Extracellular Potential
	Transmembrane	871 – 890	20	Helical; Potential
	Topological domain	891 – 920	30	Cytoplasmic Potential
	Transmembrane	921 – 942	22	Helical; Potential
	Topological domain	943 – 956	14	Extracellular Potential
	Transmembrane	957 – 979	23	Helical; Potential
	Topological domain	980 – 985	6	Cytoplasmic Potential
	Transmembrane	986 – 1006	21	Helical; Potential
	Topological domain	1007 – 1024	18	Extracellular Potential
	Transmembrane	1025 – 1049	25	Helical; Potential
	Topological domain	1050 – 1148	99	Cytoplasmic Potential
Sites
	Active site	388	1	4-aspartylphosphate intermediate By similarity
	Metal binding	781	1	Magnesium By similarity
	Metal binding	785	1	Magnesium By similarity
Amino acid modifications
	Modified residue	5	1	Phosphothreonine By similarity
Natural variations
	Alternative sequence	515 – 528	14	MGQEQ…LNVLE → VSNMRVHISDHLLL in isoform 2.		VSP_037646
	Alternative sequence	529 – 1148	620	Missing in isoform 2.		VSP_037647
	Natural variant	1029	1	A → T. Corresponds to variant rs2296242 [ dbSNP | Ensembl ].		VAR_055543

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 30, 2003. Version 2. Checksum: E9F363B568C7EE82	FASTA	1,148	129,242
	10 20 30 40 50 60 MSRATSVGDQ LEAPARTIYL NQPHLNKFRD NQISTAKYSV LTFLPRFLYE QIRRAANAFF 70 80 90 100 110 120 LFIALLQQIP DVSPTGRYTT LVPLIIILTI AGIKEIVEDF KRHKADNAVN KKKTIVLRNG 130 140 150 160 170 180 MWHTIMWKEV AVGDIVKVVN GQYLPADVVL LSSSEPQAMC YVETANLDGE TNLKIRQGLS 190 200 210 220 230 240 HTADMQTREV LMKLSGTIEC EGPNRHLYDF TGNLNLDGKS LVALGPDQIL LRGTQLRNTQ 250 260 270 280 290 300 WVFGIVVYTG HDTKLMQNST KAPLKRSNVE KVTNVQILVL FGILLVMALV SSAGALYWNR 310 320 330 340 350 360 SHGEKNWYIK KMDTTSDNFG YNLLTFIILY NNLIPISLLV TLEVVKYTQA LFINWDTDMY 370 380 390 400 410 420 YIGNDTPAMA RTSNLNEELG QVKYLFSDKT GTLTCNIMNF KKCSIAGVTY GHFPELAREP 430 440 450 460 470 480 SSDDFCRMPP PCSDSCDFDD PRLLKNIEDR HPTAPCIQEF LTLLAVCHTV VPEKDGDNII 490 500 510 520 530 540 YQASSPDEAA LVKGAKKLGF VFTARTPFSV IIEAMGQEQT FGILNVLEFS SDRKRMSVIV 550 560 570 580 590 600 RTPSGRLRLY CKGADNVIFE RLSKDSKYME ETLCHLEYFA TEGLRTLCVA YADLSENEYE 610 620 630 640 650 660 EWLKVYQEAS TILKDRAQRL EECYEIIEKN LLLLGATAIE DRLQAGVPET IATLLKAEIK 670 680 690 700 710 720 IWVLTGDKQE TAINIGYSCR LVSQNMALIL LKEDSLDATR AAITQHCTDL GNLLGKENDV 730 740 750 760 770 780 ALIIDGHTLK YALSFEVRRS FLDLALSCKA VICCRVSPLQ KSEIVDVVKK RVKAITLAIG 790 800 810 820 830 840 DGANDVGMIQ TAHVGVGISG NEGMQATNNS DYAIAQFSYL EKLLLVHGAW SYNRVTKCIL 850 860 870 880 890 900 YCFYKNVVLY IIELWFAFVN GFSGQILFER WCIGLYNVIF TALPPFTLGI FERSCTQESM 910 920 930 940 950 960 LRFPQLYKIT QNGEGFNTKV FWGHCINALV HSLILFWFPM KALEHDTVLT SGHATDYLFV 970 980 990 1000 1010 1020 GNIVYTYVVV TVCLKAGLET TAWTKFSHLA VWGSMLTWLV FFGIYSTIWP TIPIAPDMRG 1030 1040 1050 1060 1070 1080 QATMVLSSAH FWLGLFLVPT ACLIEDVAWR AAKHTCKKTL LEEVQELETK SRVLGKAVLR 1090 1100 1110 1120 1130 1140 DSNGKRLNER DRLIKRLGRK TPPTLFRGSS LQQGVPHGYA FSQEEHGAVS QEEVIRAYDT TKKKSRKK
	Isoform 2 [UniParc]. Checksum: 1CAD4BDC7B38F391	FASTA	528	59,296
	10 20 30 40 50 60 MSRATSVGDQ LEAPARTIYL NQPHLNKFRD NQISTAKYSV LTFLPRFLYE QIRRAANAFF 70 80 90 100 110 120 LFIALLQQIP DVSPTGRYTT LVPLIIILTI AGIKEIVEDF KRHKADNAVN KKKTIVLRNG 130 140 150 160 170 180 MWHTIMWKEV AVGDIVKVVN GQYLPADVVL LSSSEPQAMC YVETANLDGE TNLKIRQGLS 190 200 210 220 230 240 HTADMQTREV LMKLSGTIEC EGPNRHLYDF TGNLNLDGKS LVALGPDQIL LRGTQLRNTQ 250 260 270 280 290 300 WVFGIVVYTG HDTKLMQNST KAPLKRSNVE KVTNVQILVL FGILLVMALV SSAGALYWNR 310 320 330 340 350 360 SHGEKNWYIK KMDTTSDNFG YNLLTFIILY NNLIPISLLV TLEVVKYTQA LFINWDTDMY 370 380 390 400 410 420 YIGNDTPAMA RTSNLNEELG QVKYLFSDKT GTLTCNIMNF KKCSIAGVTY GHFPELAREP 430 440 450 460 470 480 SSDDFCRMPP PCSDSCDFDD PRLLKNIEDR HPTAPCIQEF LTLLAVCHTV VPEKDGDNII 490 500 510 520 YQASSPDEAA LVKGAKKLGF VFTARTPFSV IIEAVSNMRV HISDHLLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Sun X.L., Milo G.E., Li D. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Changes in levels of normal ML-1 gene transcripts associated with the conversion of human nontumorigenic to tumorigenic phenotypes." Sun X.L., Li D., Fang J., Noyes I., Casto B., Theil K., Shuler C., Milo G.E. Gene Expr. 8:129-139(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-1148 (ISOFORM 1). Tissue: Amygdala and Testis.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 319-1148 (ISOFORM 1). Tissue: Amygdala.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF236871 mRNA. Translation: AAF40215.2. Frameshift. AL138815 , AL136438, AL138958, AL157366, AL356316, AL669971 Genomic DNA. Translation: CAH70513.1. AL138958 , AL136438, AL138815, AL157366, AL356316, AL669971 Genomic DNA. Translation: CAH71291.1. AL157366 , AL136438, AL138815, AL138958, AL356316, AL669971 Genomic DNA. Translation: CAH74073.1. AL356316 , AL136438, AL138815, AL138958, AL157366, AL669971 Genomic DNA. Translation: CAH70876.1. AL669971 , AL136438, AL138815, AL138958, AL157366, AL356316 Genomic DNA. Translation: CAH73647.1. AL136438 , AL138815, AL138958, AL157366, AL356316, AL669971 Genomic DNA. Translation: CAH70146.1. AL137256 mRNA. Translation: CAB70658.1. AL390129 mRNA. Translation: CAB99084.1. BX537836 mRNA. Translation: CAD97848.1. AK094653 mRNA. Translation: BAC04396.1. Different initiation.
IPI	IPI00465166. IPI00939691.
PIR	T46328. T51867.
RefSeq	NP_057613.4. NM_016529.4.
UniGene	Hs.444957.
3D structure databases
ProteinModelPortal	Q9NTI2.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000371070.
Polymorphism databases
DMDM	30316390.
Proteomic databases
PaxDb	Q9NTI2.
PRIDE	Q9NTI2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000381655; ENSP00000371070; ENSG00000132932.
GeneID	51761.
KEGG	hsa:51761.
UCSC	uc001uql.1. human.
Organism-specific databases
CTD	51761.
GeneCards	GC13P025946.
HGNC	HGNC:13533. ATP8A2.
HPA	HPA039926.
MIM	605870. gene.
neXtProt	NX_Q9NTI2.
PharmGKB	PA25166.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0474.
HOVERGEN	HBG050601.
InParanoid	Q9NTI2.
KO	K14802.
OrthoDB	EOG4V9TPV.
PhylomeDB	Q9NTI2.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	Q9NTI2.
Bgee	Q9NTI2.
CleanEx	HS_ATP8A2.
Genevestigator	Q9NTI2.
GermOnline	ENSG00000132932. Homo sapiens.
Family and domain databases
Gene3D	2.70.150.10. 2 hits. 3.40.1110.10. 1 hit. 3.40.50.1000. 2 hits.
InterPro	IPR023299. ATPase_P-typ_cyto_domN. IPR018303. ATPase_P-typ_P_site. IPR006539. ATPase_P-typ_Plipid-transp. IPR008250. ATPase_P-typ_transduc_dom_A. IPR001757. Cation_transp_P_typ_ATPase. IPR023214. HAD-like_dom. [Graphical view]
PANTHER	PTHR24092. PTHR24092. 1 hit.
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. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATP8A2. human.
GenomeRNAi	51761.
NextBio	55870.
SOURCE	Search...

Entry information

Entry name

AT8A2_HUMAN

Accession

Primary (citable) accession number: Q9NTI2
Secondary accession number(s): Q9H527 , Q9NPU6, Q9NTL2, Q9NYM3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	April 30, 2003
Last modified:	May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.