Potassium-transporting ATPase alpha chain 2 - Oryctolagus cuniculus (Rabbit)

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Protein names

Recommended name:
    Potassium-transporting ATPase alpha chain 2
    EC=3.6.3.10
Alternative name(s):
    Proton pump
    Non-gastric H(+)/K(+) ATPase subunit alpha
    HK alpha 2

Gene names

Name:	ATP12A
Synonyms:	ATP1AL1

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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Sequence length	1094 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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Function	Catalyzes the hydrolysis of ATP coupled with the exchange of H⁺ and K⁺ ions across the plasma membrane. Responsible for potassium absorption in various tissues.
Catalytic activity	ATP + H₂O + H⁺(In) + K⁺(Out) = ADP + phosphate + H⁺(Out) + K⁺(In).
Subunit structure	Composed of two subunits: alpha (catalytic) and beta.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Found in the skin, kidney, distal colon and brain. In the kidney it is found in the connecting tubule, cortical collecting duct and outer medullary collecting duct while in the brain it is specific to choroid plexus and cortex. Ref.3
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IIC subfamily.

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Keywords
Biological process	Hydrogen ion transport Ion transport Potassium transport Transport
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium
Molecular function	Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro potassium ion transport Inferred from electronic annotation. Source: UniProtKB-KW proton transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrogen:potassium-exchanging ATPase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Chain

1 – 1094

1094

Potassium-transporting ATPase alpha chain 2

PRO_0000046262

Topological domain

56 – 157

102

Cytoplasmic Potential

Transmembrane

158 – 178

21

Potential

Topological domain

179 – 201

23

Lumenal Potential

Transmembrane

202 – 222

21

Potential

Topological domain

223 – 358

136

Cytoplasmic Potential

Transmembrane

359 – 378

20

Potential

Topological domain

379 – 390

12

Lumenal Potential

Transmembrane

391 – 408

18

Potential

Topological domain

409 – 842

434

Cytoplasmic Potential

Transmembrane

843 – 862

20

Potential

Topological domain

863 – 872

10

Lumenal Potential

Transmembrane

873 – 893

21

Potential

Topological domain

894 – 913

20

Cytoplasmic Potential

Transmembrane

914 – 936

23

Potential

Topological domain

937 – 988

52

Lumenal Potential

Transmembrane

989 – 1008

20

Potential

Topological domain

1009 – 1022

14

Cytoplasmic Potential

Transmembrane

1023 – 1041

19

Potential

Topological domain

1042 – 1056

15

Lumenal Potential

Transmembrane

1057 – 1077

21

Potential

Topological domain

1078 – 1094

17

Cytoplasmic Potential

Active site

446

1

4-aspartylphosphate intermediate By similarity

Metal binding

787

1

Magnesium By similarity

Metal binding

791

1

Magnesium By similarity

Modified residue

1013

1

Phosphoserine; by PKA By similarity

Alternative sequence

1 – 63

63

MAGGA…TLLLF → MR in isoform Short.

VSP_000413

Sequence conflict

300

1

G → E in AAD11800. Ref.2

Sequence conflict

421

1

V → M in AAD11800. Ref.2

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Sequence		Length	Mass (Da)
Isoform Long (2c) [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 2A8926D8135AE92C Show »	FASTA	1,094	120,966
10 20 30 40 50 60 MAGGAHRADR ATGEERKEGG GRWRAPHSPS PPGPRGCPVP LKAAAQSLCR KPTWGRYCTL 70 80 90 100 110 120 LLFQRKLEIY SVELHAATDI KKKEGRDGKK DNDLELKRNQ QKEELKKELD LDDHKLSNKE 130 140 150 160 170 180 LETKYGTDII RGLSSTRAAE LLAQNGPNAL TPPKQTPEII KFLKQMVGGF SILLWVGAVL 190 200 210 220 230 240 CWIAFGIQYV SNPSASLDRV YLGTVLAVVV ILTGIFAYYQ EAKSTNIMAS FCKMIPQQAV 250 260 270 280 290 300 VIRDSEKKVI PAEQLVVGDI VEIKGGDQIP ADIRLLSAQG CKVDNSSLTG ESEPQSRSSG 310 320 330 340 350 360 FTHENPLETK NITFYSTTCL EGTATGMVIN TGDRTIIGRI ASLASGVGNE KTPIAIEIEH 370 380 390 400 410 420 FVHIVAGVAV SVGILFFIIA VCMKYHVLDA IIFLIAIIVA NVPEGLLATV TVALSLTAKR 430 440 450 460 470 480 VAKKNCLVKN LEAVETLGST SIICSDKTGT LTQNRMTVAH LWFDNQIFVA DTSEDNLNQG 490 500 510 520 530 540 FDQSSGTWTS LSKIIALCNR AEFKPGEESV PIMKRVVVGD ASETALLKFS EVILGDVMEI 550 560 570 580 590 600 RKRNHKVVEI PFNSTNKFQL SIHQTEDPND KRFLLVMKGA PERILEKCST IMINGKEQPL 610 620 630 640 650 660 DKSMAQAFHT AYMELGGLGE RVLGFCHFYL PADEFPETYS FDSESMNFPT SNLCFVGLLS 670 680 690 700 710 720 MIDPPRSTVP DAVTKCRSAG IKVIMVTGDH PITAKAIAKS VGIISANSET VEDIAKRCNI 730 740 750 760 770 780 AVEQVNKRDA KAAVVTGMEL KDMSPEQLDE LLANYPEIVF ARTSPQQKLI IVEGCQRQDA 790 800 810 820 830 840 VVAVTGDGVN DSPALKKADI GVAMGITGSD AAKNAADMIL LDDNFSSIVT GVEEGRLIFD 850 860 870 880 890 900 NLKKTIAYTL TKNIAELCPF LIYIILGLPL PIGTITLLFI DLGTDIIPSI ALAYEKAESD 910 920 930 940 950 960 IMNRKPRHKK KDRLVNQQLA VYSYLHIGLM QALGAFLVYF TVYAQQGFRP TSLFHLRIAW 970 980 990 1000 1010 1020 DSDHLNDLED NYGQEWTSYQ RQYLEWTGYT AFFVGIMVQQ IADLIIRKTR KNSIFKQGLF 1030 1040 1050 1060 1070 1080 RNKVIWVGIA SQIIVALLLS YGLGSITALN FTMLKAQYWF VAVPHAILIW VYDEMRKLFI 1090 RLYPGSWWDK NMYY « Hide
Isoform Short (2a). Checksum: F0E79E4159119DFF Show »	FASTA	1,033	114,503
10 20 30 40 50 60 MRQRKLEIYS VELHAATDIK KKEGRDGKKD NDLELKRNQQ KEELKKELDL DDHKLSNKEL 70 80 90 100 110 120 ETKYGTDIIR GLSSTRAAEL LAQNGPNALT PPKQTPEIIK FLKQMVGGFS ILLWVGAVLC 130 140 150 160 170 180 WIAFGIQYVS NPSASLDRVY LGTVLAVVVI LTGIFAYYQE AKSTNIMASF CKMIPQQAVV 190 200 210 220 230 240 IRDSEKKVIP AEQLVVGDIV EIKGGDQIPA DIRLLSAQGC KVDNSSLTGE SEPQSRSSGF 250 260 270 280 290 300 THENPLETKN ITFYSTTCLE GTATGMVINT GDRTIIGRIA SLASGVGNEK TPIAIEIEHF 310 320 330 340 350 360 VHIVAGVAVS VGILFFIIAV CMKYHVLDAI IFLIAIIVAN VPEGLLATVT VALSLTAKRV 370 380 390 400 410 420 AKKNCLVKNL EAVETLGSTS IICSDKTGTL TQNRMTVAHL WFDNQIFVAD TSEDNLNQGF 430 440 450 460 470 480 DQSSGTWTSL SKIIALCNRA EFKPGEESVP IMKRVVVGDA SETALLKFSE VILGDVMEIR 490 500 510 520 530 540 KRNHKVVEIP FNSTNKFQLS IHQTEDPNDK RFLLVMKGAP ERILEKCSTI MINGKEQPLD 550 560 570 580 590 600 KSMAQAFHTA YMELGGLGER VLGFCHFYLP ADEFPETYSF DSESMNFPTS NLCFVGLLSM 610 620 630 640 650 660 IDPPRSTVPD AVTKCRSAGI KVIMVTGDHP ITAKAIAKSV GIISANSETV EDIAKRCNIA 670 680 690 700 710 720 VEQVNKRDAK AAVVTGMELK DMSPEQLDEL LANYPEIVFA RTSPQQKLII VEGCQRQDAV 730 740 750 760 770 780 VAVTGDGVND SPALKKADIG VAMGITGSDA AKNAADMILL DDNFSSIVTG VEEGRLIFDN 790 800 810 820 830 840 LKKTIAYTLT KNIAELCPFL IYIILGLPLP IGTITLLFID LGTDIIPSIA LAYEKAESDI 850 860 870 880 890 900 MNRKPRHKKK DRLVNQQLAV YSYLHIGLMQ ALGAFLVYFT VYAQQGFRPT SLFHLRIAWD 910 920 930 940 950 960 SDHLNDLEDN YGQEWTSYQR QYLEWTGYTA FFVGIMVQQI ADLIIRKTRK NSIFKQGLFR 970 980 990 1000 1010 1020 NKVIWVGIAS QIIVALLLSY GLGSITALNF TMLKAQYWFV AVPHAILIWV YDEMRKLFIR 1030 LYPGSWWDKN MYY « Hide

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[1]	"H-K-ATPase in the RCCT-28A rabbit cortical collecting duct cell line." Campbell W.G., Weiner I.D., Wingo C.S., Cain B.D. Am. J. Physiol. 276:F237-F245(1999) [PubMed: 9950954] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT). Strain: New Zealand white. Tissue: Kidney cortex.
[2]	"Intrarenal distribution of the colonic H,K-ATPase mRNA in rabbit." Fejes-Toth G., Naray-Fejes-Toth A., Velazquez H. Kidney Int. 56:1029-1036(1999) [PubMed: 10469371] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT). Tissue: Renal collecting duct.
[3]	"Ouabain-sensitive H,K-ATPase: tissue-specific expression of the mammalian genes encoding the catalytic alpha subunit." Pestov N.B., Romanova L.G., Korneenko T.V., Egorov M.V., Kostina M.B., Sverdlov V.E., Askari A., Shakhparonov M.I., Modyanov N.N. FEBS Lett. 440:320-324(1998) [PubMed: 9872395] [Abstract] Cited for: TISSUE SPECIFICITY.

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Sequence databases
	AF023128 mRNA. Translation: AAB80941.1. AF023129 mRNA. Translation: AAC13887.1. AF106063 mRNA. Translation: AAD11800.1.
RefSeq	NP_001075496.1.
UniGene	Ocu.2056
3D structure databases
HSSP	HSSP built from PDB template 1MO7 based on UniProtKB P06685.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9TV52.
Genome annotation databases
GeneID	100008669.
Organism-specific databases
CTD	100008669.
Phylogenomic databases
HOVERGEN	Q9TV52.
Enzyme and pathway databases
BRENDA	3.6.3.10. 255.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-reg. IPR005775. ATPase_P-typ_cation-ex_asu_euk. IPR006069. ATPase_P-typ_cation-exchng_asu. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR005834. Dehalogen-like_hydro. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00121. NAKATPASE.
TIGRFAMs	TIGR01106. ATPase-IIC_X-K. 1 hit. TIGR01494. ATPase_P-type. 4 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry name

AT12A_RABIT

Accession

Primary (citable) accession number: Q9TV52
Secondary accession number(s): Q9TSI2, Q9TV53

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	May 1, 2000
Last modified:	October 13, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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SIMILARITY comments

Index of protein domains and families

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

Isoform Long (identifier: Q9TV52-1)

Also known as: 2c;

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.

Isoform Short (identifier: Q9TV52-2)

Also known as: 2a;

The sequence of this isoform differs from the canonical sequence as follows:
1-63: MAGGAHRADRATGEERKEGGGRWRAPHSPSPPGPRGCPVPLKAAAQSLCRKPTWGRYCTLLLF → MR