ATP7A_RAT
ID ATP7A_RAT Reviewed; 1492 AA.
AC P70705;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Copper-transporting ATPase 1;
DE EC=7.2.2.8 {ECO:0000250|UniProtKB:Q04656};
DE AltName: Full=Copper pump 1;
DE AltName: Full=Menkes disease-associated protein homolog;
GN Name=Atp7a {ECO:0000312|RGD:2179}; Synonyms=Mnk;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Astrocyte;
RX PubMed=9562241; DOI=10.1023/a:1006896612272;
RA Qian Y., Tiffany-Castiglioni E., Harris E.D.;
RT "Sequence of a Menkes-type Cu-transporting ATPase from rat C6 glioma cells:
RT comparison of the rat protein with other mammalian Cu-transporting
RT ATPases.";
RL Mol. Cell. Biochem. 181:49-61(1998).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=12488345; DOI=10.1210/en.2002-220716;
RA Steveson T.C., Ciccotosto G.D., Ma X.M., Mueller G.P., Mains R.E.,
RA Eipper B.A.;
RT "Menkes protein contributes to the function of peptidylglycine alpha-
RT amidating monooxygenase.";
RL Endocrinology 144:188-200(2003).
RN [3]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15634787; DOI=10.1523/jneurosci.3699-04.2005;
RA Schlief M.L., Craig A.M., Gitlin J.D.;
RT "NMDA receptor activation mediates copper homeostasis in hippocampal
RT neurons.";
RL J. Neurosci. 25:239-246(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1204, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353 AND SER-1465, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: ATP-driven copper (Cu(+)) ion pump that plays an important
CC role in intracellular copper ion homeostasis (By similarity). Within a
CC catalytic cycle, acquires Cu(+) ion from donor protein on the
CC cytoplasmic side of the membrane and delivers it to acceptor protein on
CC the lumenal side. The transfer of Cu(+) ion across the membrane is
CC coupled to ATP hydrolysis and is associated with a transient
CC phosphorylation that shifts the pump conformation from inward-facing to
CC outward-facing state (By similarity). Under physiological conditions,
CC at low cytosolic copper concentration, it is localized at the trans-
CC Golgi network (TGN) where it transfers Cu(+) ions to cuproenzymes of
CC the secretory pathway (By similarity). Upon elevated cytosolic copper
CC concentrations, it relocalizes to the plasma membrane where it is
CC responsible for the export of excess Cu(+) ions (By similarity). May
CC play a dual role in neuron function and survival by regulating cooper
CC efflux and neuronal transmission at the synapse as well as by supplying
CC Cu(+) ions to enzymes such as PAM, TYR and SOD3 (By similarity). In the
CC melanosomes of pigmented cells, provides copper cofactor to TYR to form
CC an active TYR holoenzyme for melanin biosynthesis (By similarity).
CC {ECO:0000250|UniProtKB:Q04656, ECO:0000250|UniProtKB:Q64430}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:456216; EC=7.2.2.8;
CC Evidence={ECO:0000250|UniProtKB:Q04656};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25793;
CC Evidence={ECO:0000250|UniProtKB:Q04656};
CC -!- SUBUNIT: Monomer. Interacts with PDZD11. Interacts with ATOX1 and
CC COMMD1 (By similarity). Interacts with TYRP1 (By similarity). Directly
CC interacts with SOD3; this interaction is copper-dependent and is
CC required for SOD3 activity (By similarity).
CC {ECO:0000250|UniProtKB:Q04656, ECO:0000250|UniProtKB:Q64430}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q04656, ECO:0000250|UniProtKB:Q64430}; Multi-
CC pass membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:Q04656, ECO:0000250|UniProtKB:Q64430}; Multi-
CC pass membrane protein {ECO:0000255}. Melanosome membrane
CC {ECO:0000250|UniProtKB:Q64430}; Multi-pass membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q64430};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, axon
CC {ECO:0000269|PubMed:15634787}. Cell projection, dendrite
CC {ECO:0000269|PubMed:15634787}. Postsynaptic density
CC {ECO:0000269|PubMed:15634787}. Note=Cycles constitutively between the
CC trans-Golgi network (TGN) and the plasma membrane. Predominantly found
CC in the TGN and relocalized to the plasma membrane in response to
CC elevated copper levels. Targeting into melanosomes is regulated by
CC BLOC-1 complex (By similarity). In response to glutamate translocates
CC to neuron processes with a minor fraction at extrasynaptic sites
CC (PubMed:15634787). {ECO:0000250|UniProtKB:Q04656,
CC ECO:0000250|UniProtKB:Q64430, ECO:0000269|PubMed:15634787}.
CC -!- TISSUE SPECIFICITY: Expressed in hippocampal neuron (at protein level)
CC (PubMed:15634787). Expressed in anterior pituitary gland (at protein
CC level) (PubMed:12488345). {ECO:0000269|PubMed:12488345,
CC ECO:0000269|PubMed:15634787}.
CC -!- DOMAIN: The nucleotide-binding domain consists of a twisted six-
CC stranded antiparallel beta-sheet flanked by two pairs of alpha-helices,
CC forming an hydrophobic pocket that interacts with the adenine ring of
CC ATP. The ATP binding site comprises residues located in alpha-1 and
CC alpha-2 helices and beta-2 and beta-3 strands, which are involved in
CC van der Waal's interactions, and Glu-1073 which forms an hydrogen bond
CC with the adenine ring. {ECO:0000250|UniProtKB:Q04656}.
CC -!- DOMAIN: The heavy-metal-associated domain (HMA) coordinates a Cu(+) ion
CC via the cysteine residues within the CXXC motif. The transfer of Cu(+)
CC ion from ATOX1 to ATP7A involves the formation of a three-coordinate
CC Cu(+)-bridged heterodimer where the metal is shared between the two
CC metal binding sites of ATOX1 and ATP7A. The Cu(+) ion appears to switch
CC between two coordination modes, forming two links with one protein and
CC one with the other. Cisplatin, a chemotherapeutic drug, can bind the
CC CXXC motif and hinder the release of Cu(+) ion.
CC {ECO:0000250|UniProtKB:Q04656}.
CC -!- DOMAIN: Contains three di-leucine motifs in the C-terminus which are
CC required for recycling from the plasma membrane to the TGN. The di-
CC leucine 1479-Leu-Leu-1480 motif mediates endocytosis at the plasma
CC membrane, whereas the di-leucine 1459-Leu-Leu-1460 motif is a sorting
CC signal for retrograde trafficking to TGN via early endosomes.
CC {ECO:0000250|UniProtKB:Q64430}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Heavy metal - Issue 79 of
CC February 2007;
CC URL="https://web.expasy.org/spotlight/back_issues/079";
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DR EMBL; U59245; AAB06393.1; -; mRNA.
DR PIR; S46483; S46483.
DR RefSeq; NP_434690.1; NM_052803.2.
DR RefSeq; XP_006257057.1; XM_006256995.3.
DR RefSeq; XP_008771556.1; XM_008773334.2.
DR AlphaFoldDB; P70705; -.
DR SMR; P70705; -.
DR IntAct; P70705; 1.
DR STRING; 10116.ENSRNOP00000063702; -.
DR GlyGen; P70705; 1 site.
DR iPTMnet; P70705; -.
DR PhosphoSitePlus; P70705; -.
DR jPOST; P70705; -.
DR PaxDb; P70705; -.
DR PRIDE; P70705; -.
DR ABCD; P70705; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000080141; ENSRNOP00000071625; ENSRNOG00000061367.
DR GeneID; 24941; -.
DR KEGG; rno:24941; -.
DR UCSC; RGD:2179; rat.
DR CTD; 538; -.
DR RGD; 2179; Atp7a.
DR eggNOG; KOG0207; Eukaryota.
DR GeneTree; ENSGT00940000159568; -.
DR HOGENOM; CLU_001771_0_1_1; -.
DR InParanoid; P70705; -.
DR OMA; MMVMDSH; -.
DR OrthoDB; 649559at2759; -.
DR PhylomeDB; P70705; -.
DR BRENDA; 7.2.2.8; 5301.
DR BRENDA; 7.2.2.9; 5301.
DR Reactome; R-RNO-6803544; Ion influx/efflux at host-pathogen interface.
DR Reactome; R-RNO-936837; Ion transport by P-type ATPases.
DR PRO; PR:P70705; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000061367; Expressed in duodenum and 18 other tissues.
DR ExpressionAtlas; P70705; baseline and differential.
DR Genevisible; P70705; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0031252; C:cell leading edge; IDA:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005770; C:late endosome; IDA:RGD.
DR GO; GO:0033162; C:melanosome membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0005902; C:microvillus; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IPI:RGD.
DR GO; GO:0005507; F:copper ion binding; ISO:RGD.
DR GO; GO:0005375; F:copper ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0032767; F:copper-dependent protein binding; ISS:UniProtKB.
DR GO; GO:1903136; F:cuprous ion binding; ISS:UniProtKB.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; ISO:RGD.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:RGD.
DR GO; GO:0016532; F:superoxide dismutase copper chaperone activity; ISO:RGD.
DR GO; GO:0046034; P:ATP metabolic process; ISO:RGD.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0001974; P:blood vessel remodeling; ISO:RGD.
DR GO; GO:0051216; P:cartilage development; ISO:RGD.
DR GO; GO:0006584; P:catecholamine metabolic process; ISO:RGD.
DR GO; GO:0006878; P:cellular copper ion homeostasis; ISS:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:RGD.
DR GO; GO:0071236; P:cellular response to antibiotic; IEP:RGD.
DR GO; GO:0071276; P:cellular response to cadmium ion; IEP:RGD.
DR GO; GO:0071279; P:cellular response to cobalt ion; IEP:RGD.
DR GO; GO:0071280; P:cellular response to copper ion; IDA:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0071281; P:cellular response to iron ion; IEP:RGD.
DR GO; GO:0071284; P:cellular response to lead ion; IEP:RGD.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IMP:RGD.
DR GO; GO:0021954; P:central nervous system neuron development; ISO:RGD.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; ISO:RGD.
DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR GO; GO:0060003; P:copper ion export; IMP:RGD.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
DR GO; GO:0015677; P:copper ion import; ISO:RGD.
DR GO; GO:0006825; P:copper ion transport; ISO:RGD.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0010273; P:detoxification of copper ion; ISO:RGD.
DR GO; GO:0042417; P:dopamine metabolic process; ISO:RGD.
DR GO; GO:0048251; P:elastic fiber assembly; ISO:RGD.
DR GO; GO:0051542; P:elastin biosynthetic process; ISO:RGD.
DR GO; GO:0042414; P:epinephrine metabolic process; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0031069; P:hair follicle morphogenesis; ISO:RGD.
DR GO; GO:0035137; P:hindlimb morphogenesis; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; IEP:RGD.
DR GO; GO:0007595; P:lactation; IEP:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0048286; P:lung alveolus development; ISO:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:0045914; P:negative regulation of catecholamine metabolic process; ISO:RGD.
DR GO; GO:0034760; P:negative regulation of iron ion transmembrane transport; IMP:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:RGD.
DR GO; GO:0042421; P:norepinephrine biosynthetic process; ISO:RGD.
DR GO; GO:0042415; P:norepinephrine metabolic process; ISO:RGD.
DR GO; GO:0018205; P:peptidyl-lysine modification; ISO:RGD.
DR GO; GO:0043473; P:pigmentation; ISO:RGD.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISO:RGD.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:RGD.
DR GO; GO:1904960; P:positive regulation of cytochrome-c oxidase activity; ISO:RGD.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:RGD.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:RGD.
DR GO; GO:0048023; P:positive regulation of melanin biosynthetic process; ISS:UniProtKB.
DR GO; GO:1903036; P:positive regulation of response to wounding; IMP:RGD.
DR GO; GO:1901671; P:positive regulation of superoxide dismutase activity; ISO:RGD.
DR GO; GO:0032773; P:positive regulation of tyrosinase activity; ISS:UniProtKB.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IMP:RGD.
DR GO; GO:0021860; P:pyramidal neuron development; ISO:RGD.
DR GO; GO:1904959; P:regulation of cytochrome-c oxidase activity; IMP:RGD.
DR GO; GO:0010468; P:regulation of gene expression; IMP:RGD.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; ISO:RGD.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:RGD.
DR GO; GO:0019430; P:removal of superoxide radicals; ISO:RGD.
DR GO; GO:0046688; P:response to copper ion; IDA:RGD.
DR GO; GO:0010041; P:response to iron(III) ion; IEP:RGD.
DR GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR GO; GO:0010042; P:response to manganese ion; IDA:RGD.
DR GO; GO:0010043; P:response to zinc ion; IEP:RGD.
DR GO; GO:0042428; P:serotonin metabolic process; ISO:RGD.
DR GO; GO:0043588; P:skin development; ISO:RGD.
DR GO; GO:0042093; P:T-helper cell differentiation; ISO:RGD.
DR GO; GO:0006568; P:tryptophan metabolic process; ISO:RGD.
DR GO; GO:0006570; P:tyrosine metabolic process; ISO:RGD.
DR CDD; cd00371; HMA; 6.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006122; HMA_Cu_ion-bd.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00403; HMA; 6.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 6.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR TIGRFAMs; TIGR00003; TIGR00003; 6.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 6.
DR PROSITE; PS50846; HMA_2; 7.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cell projection; Copper; Copper transport;
KW Endosome; Glycoprotein; Golgi apparatus; Ion transport; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1492
FT /note="Copper-transporting ATPase 1"
FT /id="PRO_0000046313"
FT TOPO_DOM 1..645
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..706
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 707..726
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 727..733
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 734..754
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 755..773
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..927
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 928..951
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 952..981
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 982..1003
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1004..1348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1349..1366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1367..1377
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1378..1397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1398..1492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 8..74
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 85..151
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 171..237
FT /note="HMA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 277..343
FT /note="HMA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 377..443
FT /note="HMA 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 480..546
FT /note="HMA 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 556..622
FT /note="HMA 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 1478..1492
FT /note="PDZD11-binding"
FT /evidence="ECO:0000250"
FT MOTIF 1459..1460
FT /note="Endocytosis signal"
FT /evidence="ECO:0000250|UniProtKB:Q64430"
FT MOTIF 1479..1480
FT /note="Endocytosis signal"
FT /evidence="ECO:0000250|UniProtKB:Q64430"
FT ACT_SITE 1036
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT BINDING 19
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 22
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 182
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 185
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 288
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 291
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 388
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 391
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 491
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 494
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 567
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 570
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 1073
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT BINDING 1293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 1297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 327
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64430"
FT MOD_RES 1204
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 1422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 1424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 1452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 1455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 1458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 1461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 1465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64430"
FT MOD_RES 1478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64430"
FT CARBOHYD 678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1492 AA; 162093 MW; 34F75152B105AE9F CRC64;
MEPNMDANSI TITVEGMTCI SCVRTIEQQI GKVNGVHHIK VSLEEKSATV IYNPKLQTPK
TLQEAIDDMG FDALLHNANP LPVLTNTVFL TVTAPLALPW DHIQSTLLKT KGVTGVKISP
QQRSAVVTII PSVVSANQIV ELVPDLSLDM GTQEKKSGTS EEHSTPQAGE VLLKMRVEGM
TCHSCTSTIE GKVGKLQGVQ RIKVSLDNQE ATIVYQPHLI TAEEIKKQIE AVGFPAFIKK
QPKYLKLGAI DVERLKSTPV KSSEGSQQKS PAYPSDSAIT FTIDGMHCKS CVSNIESALS
TLQYVSSIVV SLENRSAIVK YNASLVTPEI LRKAIEAVSP GQYRVSISSE VESPTSSPSS
SSLQKMPLNL VSQPLTQEVV ININGMTCNS CVQSIEGVIS KKPGVKSIHV SLTNSTGTIE
YDPLLTSPEP LREAIEDMGF DAVLPADMKE PLVVIAQPSL ETPLLPSTTE PENVMTPVQN
KCYIQVSGMT CASCVANIER NLRREEGIYS VLVALMAGKA EVRYNPAVIQ PRVIAELIRE
LGFGAVVMEN AGEGNGILEL VVRGMTCASC VHKIESTLTK HKGIFYCSVA LATNKAHIKY
DPEIIGPRDI IHTIGNLGFE ASLVKKDRSA NHLDHKREIK QWRGSFLVSL FFCIPVMGLM
IYMMVMDHHL ATLNHNQNMS NEEMINMHSS MFLERQILPG LSIMNLLSLL LCLPVQFCGG
WYFYIQAYKA LRHKTANMDV LIVLATTIAF AYSLVILLVA MYERAKVNPI TFFDTPPMLF
VFIALGRWLE HIAKGKTSEA LAKLISLQAT EATIVTLNSE NLLLSEEQVD VELVQRGDII
KVVPGGKFPV DGRVIEGHSM VDESLITGEA MPVAKKPGST VIAGSINQNG SLLIRATHVG
ADTTLSQIVK LVEEAQTSKA PIQQFADKLS GYFVPFIVLV SIVTLLVWII IGFQNFEIVE
AYFPGYNRSI SRTETIIRFA FQASITVLCI ACPCSLGLAT PTAVMVGTGV GAQNGILIKG
GEPLEMAHKV KVVVFDKTGT ITHGTPVVNQ VKVLVESNKI SRNKILAIVG TAESNSEHPL
GAAVTKYCKQ ELDTETLGTC TDFQVVPGCG ISCKVTNIEG LLHKSNLKIE ENNIKNASLV
QIDAINEQSS PSSSMIIDAH LSNAVNTQQY KVLIGNREWM IRNGLVISND VDESMIEHER
RGRTAVLVTI DDELCGLIAI ADTVKPEAEL AVHILKSMGL EVVLMTGDNS KTARSIASQV
GITKVFAEVL PSHKVAKVKQ LQEEGKRVAM VGDGINDSPA LAMASVGIAI GTGTDVAIEA
ADVVLIRNDL LDVVASIDLS RKTVKRIRIN FVFALIYNLI GIPIAAGVFL PIGLVLQPWM
GSAAMAASSV SVVLSSLFLK LYRKPTYDNY ELRPRSHTGQ RSPSEISVHV GIDDTSRNSP
RLGLLDRIVN YSRASINSLL SDKRSLNSVV TSEPDKHSLL VGDFREDDDT TL
