Reviewed, UniProtKB/Swiss-Prot Q9CTG6 (AT132_MOUSE)

Names and origin

Protein names

Recommended name:
    Probable cation-transporting ATPase 13A2
    EC=3.6.3.-

Gene names

Name:

Atp13a2

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

Protein attributes

Sequence length	1169 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	ATP + H2O = ADP + phosphate.
Subcellular location	Membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type V subfamily.

Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro cation transport Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1169	1169	Probable cation-transporting ATPase 13A2		PRO_0000046424
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 34	22	Potential
	Topological domain	35 – 45	11	Extracellular Potential
	Transmembrane	46 – 66	21	Potential
	Topological domain	67 – 225	159	Cytoplasmic Potential
	Transmembrane	226 – 248	23	Potential
	Topological domain	249 – 251	3	Extracellular Potential
	Transmembrane	252 – 271	20	Potential
	Topological domain	272 – 420	149	Cytoplasmic Potential
	Transmembrane	421 – 440	20	Potential
	Topological domain	441 – 454	14	Extracellular Potential
	Transmembrane	455 – 475	21	Potential
	Topological domain	476 – 921	446	Cytoplasmic Potential
	Transmembrane	922 – 941	20	Potential
	Topological domain	942 – 952	11	Extracellular Potential
	Transmembrane	953 – 970	18	Potential
	Topological domain	971 – 986	16	Cytoplasmic Potential
	Transmembrane	987 – 1007	21	Potential
	Topological domain	1008 – 1035	28	Extracellular Potential
	Transmembrane	1036 – 1055	20	Potential
	Topological domain	1056 – 1068	13	Cytoplasmic Potential
	Transmembrane	1069 – 1086	18	Potential
	Topological domain	1087 – 1102	16	Extracellular Potential
	Transmembrane	1103 – 1123	21	Potential
	Topological domain	1124 – 1169	46	Cytoplasmic Potential
Sites
	Active site	508	1	4-aspartylphosphate intermediate By similarity
	Metal binding	867	1	Magnesium By similarity
	Metal binding	871	1	Magnesium By similarity
Experimental info
	Sequence conflict	695	1	E → A in BAB22896. Ref.2
	Sequence conflict	809	1	F → S in BAB22896. Ref.2
	Sequence conflict	943	1	I → V in BAB22896. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9CTG6-1 [UniParc]. Last modified August 2, 2005. Version 2. Checksum: B20C868D386F5E3E	FASTA	1,169	126,614
	10 20 30 40 50 60 MSADSSLLMG STPPSYGTLT TGTSIDPLSS SASSVRLSGY CGSPWRAIGY HAAVWMLAGI 70 80 90 100 110 120 PWLLFRWKPL WGVRLRLKPC SLAHAETLVI EIKDKEGSSR QLFTVQVQTE ALVQGSLELP 130 140 150 160 170 180 PQAQAEDGRS QAAVGVTPEG TWQDTSELHR QEEAKQVLRY YVLQGQRYVW METQQAFCQV 190 200 210 220 230 240 SLLDHSRTCD DVHCSSSGLS LQDQATRKTI YGPNVISIPV KSYLQLLADE ALNPYYGFQA 250 260 270 280 290 300 FSIALWLADH YYWYALCIFL ISAISICLAL YKTRKQSLTL RDMVKLSVRV QVCRPGGEEE 310 320 330 340 350 360 WVDSSELVPG DCLVLPQEGG VMPCDAALVA GECVVNESSL TGESTPVLKT ALPEGPKPYC 370 380 390 400 410 420 PETHRRHTLF CGTLILQARA YVGPRVLAVV TRTGFCTAKG GLVSSILHPR PISFKFYKHS 430 440 450 460 470 480 MKFVAALSVL ALLGTVYSIV ILYRNRVPVR EIVIRALDLV TVVVPPALPA AMTVCTLYAQ 490 500 510 520 530 540 SRLRAQGIFC IHPLRINLGG KLRLVCFDKT GTLTEDGLDV MGVVPLKGQV LLPLVPEPRH 550 560 570 580 590 600 LPLGPLLRAL ATCHALSQLH DTPVGDPMDL KMVESTGWVL EEGPAAGSAP GSQVLVVMRP 610 620 630 640 650 660 PPGGPRQQEE PPVPVSVLCR FPFSSALQRM DVVVTWPGAT QPEAYVKGSP ELVASLCSPE 670 680 690 700 710 720 TVPSDFSQVL QSYTAAGYRV VALAGKPLPI APSLEAAQQL TRDTVERELS LLGLLVMRNL 730 740 750 760 770 780 LKPQTAPVIQ TLRKTGIRTV MVTGDNLQTA VTVARACGMV GAQEHLAVIH ATHPEQGQPA 790 800 810 820 830 840 ALEFLPTESS AVMNGAKATG YPTVPEPQFC HLALSGSTFA VLRKHFPKLL PKVLVQATVF 850 860 870 880 890 900 ARMAPEQKTE LVCELQRLQY CVGMCGDGAN DCGALKAADV GISLSQAEAS VVSPFTSSMA 910 920 930 940 950 960 SIECVPTVIR EGRCSLDTSF SVFKYMALYS LTQFISVLIL YTINTNLGDL QFLAIDLVIT 970 980 990 1000 1010 1020 TTVAVLMSRT GPALTLVRAR PPGALLSVPV LGSLLLQVAL VAGIQLGGYF LVIAQPWFVP 1030 1040 1050 1060 1070 1080 LNRTVPAPDN LPNYENTVVF SLSGFQYLIL AAAVSKGAPF RQPLYTNVPF LVALALLGSV 1090 1100 1110 1120 1130 1140 LVGLILVPGL LQGPLGLRNI VDSSFKLLLL GLVAFNFVGA FMLESVLDQC LPACLRWLRP 1150 1160 KRASKKQFKR LQQELAEHPW PTLPVGSVR

References

[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Salivary gland.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 582-1169. Strain: C57BL/6J. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC042661 mRNA. Translation: AAH42661.1. AK003623 mRNA. Translation: BAB22896.1.
IPI	IPI00319385.
UniGene	Mm.205625
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q9CTG6.
Genome annotation databases
Ensembl	ENSMUST00000037055; ENSMUSP00000039648; ENSMUSG00000036622; Mus musculus. [Genome view]
KEGG	mmu:74772.
UCSC	uc008vnn.1. mouse.
Organism-specific databases
CTD	74772.
MGI	MGI:1922022. Atp13a2.
Phylogenomic databases
HOGENOM	Q9CTG6.
HOVERGEN	Q9CTG6.
Gene expression databases
ArrayExpress	Q9CTG6.
Bgee	Q9CTG6.
CleanEx	MM_ATP13A2.
Genevestigator	Q9CTG6.
GermOnline	ENSMUSG00000036622. Mus musculus.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-reg. IPR000695. ATPase_P-typ_H-transp. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR006544. ATPase_P-typ_unknown-pump-sp. IPR005834. Dehalogen-like_hydro. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00120. HATPASE.
TIGRFAMs	TIGR01494. ATPase_P-type. 2 hits. TIGR01657. P-ATPase-V. 1 hit.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	341604.
SOURCE	Search...

Entry information

Entry name

AT132_MOUSE

Accession

Primary (citable) accession number: Q9CTG6
Secondary accession number(s): Q8CG98

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	August 2, 2005
Last modified:	October 13, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)