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Protein

Manganese-transporting ATPase 13A1

Gene

Atp13a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Mediates manganese transport into the endoplasmic reticulum. The ATPase activity is required for cellular manganese homeostasis (By similarity).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei530 – 53014-aspartylphosphate intermediateBy similarity
Metal bindingi861 – 8611MagnesiumBy similarity
Metal bindingi865 – 8651MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Transport

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-936837. Ion transport by P-type ATPases.

Names & Taxonomyi

Protein namesi
Recommended name:
Manganese-transporting ATPase 13A1 (EC:3.6.3.-)
Short name:
CATP
Gene namesi
Name:Atp13a1
Synonyms:Atp13a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2180801. Atp13a1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6363CytoplasmicSequence analysisAdd
BLAST
Transmembranei64 – 8421HelicalSequence analysisAdd
BLAST
Topological domaini85 – 928ExtracellularSequence analysis
Transmembranei93 – 11321HelicalSequence analysisAdd
BLAST
Topological domaini114 – 240127CytoplasmicSequence analysisAdd
BLAST
Transmembranei241 – 26121HelicalSequence analysisAdd
BLAST
Topological domaini262 – 440179ExtracellularSequence analysisAdd
BLAST
Transmembranei441 – 46121HelicalSequence analysisAdd
BLAST
Topological domaini462 – 985524CytoplasmicSequence analysisAdd
BLAST
Transmembranei986 – 100621HelicalSequence analysisAdd
BLAST
Topological domaini1007 – 10071ExtracellularSequence analysis
Transmembranei1008 – 102821HelicalSequence analysisAdd
BLAST
Topological domaini1029 – 104719CytoplasmicSequence analysisAdd
BLAST
Transmembranei1048 – 106821HelicalSequence analysisAdd
BLAST
Topological domaini1069 – 109224ExtracellularSequence analysisAdd
BLAST
Transmembranei1093 – 111321HelicalSequence analysisAdd
BLAST
Topological domaini1114 – 112815CytoplasmicSequence analysisAdd
BLAST
Transmembranei1129 – 114921HelicalSequence analysisAdd
BLAST
Topological domaini1150 – 116213ExtracellularSequence analysisAdd
BLAST
Transmembranei1163 – 118321HelicalSequence analysisAdd
BLAST
Topological domaini1184 – 120017CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12001200Manganese-transporting ATPase 13A1PRO_0000046422Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi284 – 2841N-linked (GlcNAc...)Sequence analysis
Glycosylationi417 – 4171N-linked (GlcNAc...)Sequence analysis
Modified residuei896 – 8961PhosphoserineCombined sources

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9EPE9.
MaxQBiQ9EPE9.
PaxDbiQ9EPE9.
PRIDEiQ9EPE9.

PTM databases

iPTMnetiQ9EPE9.
PhosphoSiteiQ9EPE9.

Expressioni

Gene expression databases

BgeeiQ9EPE9.
CleanExiMM_ATP13A1.
GenevisibleiQ9EPE9. MM.

Interactioni

Protein-protein interaction databases

IntActiQ9EPE9. 3 interactions.
MINTiMINT-1850391.
STRINGi10090.ENSMUSP00000034326.

Structurei

3D structure databases

ProteinModelPortaliQ9EPE9.
SMRiQ9EPE9. Positions 309-878.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0209. Eukaryota.
COG0474. LUCA.
GeneTreeiENSGT00550000075064.
HOGENOMiHOG000199432.
HOVERGENiHBG050602.
InParanoidiQ9EPE9.
KOiK14950.
OMAiYLYSEAQ.
OrthoDBiEOG7T1R9G.
TreeFamiTF300725.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006544. P-type_TPase_V.
IPR001757. P_typ_ATPase.
[Graphical view]
PANTHERiPTHR24093:SF82. PTHR24093:SF82. 3 hits.
PfamiPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01494. ATPase_P-type. 2 hits.
TIGR01657. P-ATPase-V. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9EPE9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVVGNAVPC GARPGGARDN GSPQPGSRLR PGLAAGPALI ANGDELVAAV
60 70 80 90 100
WPYRRLALLR RLTVLPFAGL LYPAWLGAAA SGCWGWGSSW TQIPEAALLA
110 120 130 140 150
LATICLAHAL TVLSGHWSVH AHCALTCTPE YDPNKVTFVK VVPTPNNGST
160 170 180 190 200
ELVALHRDKG EDGLEVLSFE FQKIKYSYDA LEKKQFLPVA FPVGNAFSYY
210 220 230 240 250
QSNRGFQEDS EIRAAEKKFG SNKAEMVVPD FSELFKERAT APFFVFQVFC
260 270 280 290 300
VGLWCLDEYW YYSVFTLSML VAFEASLVQQ QMRNMSEIRK MGNKPHMIQV
310 320 330 340 350
YRSRKWRPVA SDDIVPGDIV SIGRSPQENL VPCDVLLLRG RCIVDEAMLT
360 370 380 390 400
GESVPQMKEP IEDLSPDRVL DLQADARLHV IFGGTKVVQH IPPQKATSGL
410 420 430 440 450
KPVDNGCVAF VLRTGFNTSQ GRLLRTILFG VKRVTANNLE TFIFILFLLV
460 470 480 490 500
FAIAAAAYVW VEGTKDPSRN RYKLFLECTL ILTSVVPPEL PIELSLAVNT
510 520 530 540 550
SLIALAKLYM YCTEPFRIPF AGKVEVCCFD KTGTLTSDSL VVRGVAGLRD
560 570 580 590 600
GKEVTPVSSI PIETHRALAS CHSLMQLDDG TLVGDPLEKA MLTAVDWTLT
610 620 630 640 650
KDEKVFPRSI KTQGLKIHQR FHFASALKRM SVLASYEKLG STDLCYIAAV
660 670 680 690 700
KGAPETLHSM FSQCPPDYHH IHTEISREGA RVLALGYKEL GHLTHQQARE
710 720 730 740 750
IKREALECSL KFVGFIVVSC PLKADSKAVI REIQNASHRV VMITGDNPLT
760 770 780 790 800
ACHVAQELHF IDKAHTLILH PPSEKGQPCE WRSIDSSIVL PLTLGSPKAL
810 820 830 840 850
ALEHALCLTG DGLAHLQAVD PQQLLCLIPH VQVFARVAPK QKEFVITSLK
860 870 880 890 900
ELGYVTLMCG DGTNDVGALK HADVGVALLA NAPERVVERR RRPRDSPVLS
910 920 930 940 950
NSGPRVSRST KQKSALLSPE EPPASHRDRL SQVLRDLEEE STPIVKLGDA
960 970 980 990 1000
SIAAPFTSKL SSIQCICHVI KQGRCTLVTT LQMFKILALN ALILAYSQSV
1010 1020 1030 1040 1050
LYLEGVKFSD FQATLQGLLL AGCFLFISRS KPLKTLSRER PLPNIFNLYT
1060 1070 1080 1090 1100
ILTVMLQFSV HFLSLVYLYR EAQARSPEKQ EQFVDLYKEF EPSLVNSTVY
1110 1120 1130 1140 1150
IMAMAMQMAT FAINYKGPPF MESLPENKPL VWSLAVSLLA IIGLLLGSSP
1160 1170 1180 1190 1200
DFNSQFGLVD IPVEFKLVIG QVLALDFCLA LLADRVLQFF LGTPKLRVPS
Length:1,200
Mass (Da):132,388
Last modified:July 27, 2011 - v2
Checksum:i059C366D63030B82
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881P → S in BAB20095 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035381 mRNA. Translation: BAB20095.1.
CH466569 Genomic DNA. Translation: EDL28752.1.
BC138721 mRNA. Translation: AAI38722.1.
BC138722 mRNA. Translation: AAI38723.1.
CCDSiCCDS22349.1.
RefSeqiNP_573487.2. NM_133224.2.
UniGeneiMm.186066.

Genome annotation databases

EnsembliENSMUST00000034326; ENSMUSP00000034326; ENSMUSG00000031862.
GeneIDi170759.
KEGGimmu:170759.
UCSCiuc009lxr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035381 mRNA. Translation: BAB20095.1.
CH466569 Genomic DNA. Translation: EDL28752.1.
BC138721 mRNA. Translation: AAI38722.1.
BC138722 mRNA. Translation: AAI38723.1.
CCDSiCCDS22349.1.
RefSeqiNP_573487.2. NM_133224.2.
UniGeneiMm.186066.

3D structure databases

ProteinModelPortaliQ9EPE9.
SMRiQ9EPE9. Positions 309-878.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9EPE9. 3 interactions.
MINTiMINT-1850391.
STRINGi10090.ENSMUSP00000034326.

PTM databases

iPTMnetiQ9EPE9.
PhosphoSiteiQ9EPE9.

Proteomic databases

EPDiQ9EPE9.
MaxQBiQ9EPE9.
PaxDbiQ9EPE9.
PRIDEiQ9EPE9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034326; ENSMUSP00000034326; ENSMUSG00000031862.
GeneIDi170759.
KEGGimmu:170759.
UCSCiuc009lxr.2. mouse.

Organism-specific databases

CTDi57130.
MGIiMGI:2180801. Atp13a1.

Phylogenomic databases

eggNOGiKOG0209. Eukaryota.
COG0474. LUCA.
GeneTreeiENSGT00550000075064.
HOGENOMiHOG000199432.
HOVERGENiHBG050602.
InParanoidiQ9EPE9.
KOiK14950.
OMAiYLYSEAQ.
OrthoDBiEOG7T1R9G.
TreeFamiTF300725.

Enzyme and pathway databases

ReactomeiR-MMU-936837. Ion transport by P-type ATPases.

Miscellaneous databases

NextBioi370358.
PROiQ9EPE9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EPE9.
CleanExiMM_ATP13A1.
GenevisibleiQ9EPE9. MM.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006544. P-type_TPase_V.
IPR001757. P_typ_ATPase.
[Graphical view]
PANTHERiPTHR24093:SF82. PTHR24093:SF82. 3 hits.
PfamiPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01494. ATPase_P-type. 2 hits.
TIGR01657. P-ATPase-V. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Inoue S., Ohta M.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Testis.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-896, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiAT131_MOUSE
AccessioniPrimary (citable) accession number: Q9EPE9
Secondary accession number(s): B2RS54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.