ATP7A_CRIGR
ID ATP7A_CRIGR Reviewed; 1476 AA.
AC P49015;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Copper-transporting ATPase 1;
DE EC=7.2.2.8;
DE AltName: Full=Copper pump 1;
DE Flags: Fragment;
GN Name=ATP7A;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Ovary;
RX PubMed=8589689; DOI=10.1093/hmg/4.11.2117;
RA Camakaris J., Petris M.J., Bailey L., Shen P., Lockhart P., Glover T.W.,
RA Barcroft C., Patton J., Mercer J.F.B.;
RT "Gene amplification of the Menkes (MNK; ATP7A) P-type ATPase gene of CHO
RT cells is associated with copper resistance and enhanced copper efflux.";
RL Hum. Mol. Genet. 4:2117-2123(1995).
CC -!- FUNCTION: May function in the export of copper from the cytoplasm to an
CC intracellular organelle. It may serve as well for the export of other
CC metals.
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 -!- SUBUNIT: Monomer. Interacts with PDZD11 (By similarity). Interacts with
CC ATOX1 and COMMD1 (By similarity). Interacts with TYRP1 (By similarity).
CC Directly interacts with SOD3; this interaction is copper-dependent and
CC is 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}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q04656}; Multi-pass
CC membrane protein {ECO:0000255}. 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. {ECO:0000250|UniProtKB:Q04656}.
CC -!- TISSUE SPECIFICITY: Expressed in most tissues except liver.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {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; U29946; AAB39918.1; -; mRNA.
DR AlphaFoldDB; P49015; -.
DR BMRB; P49015; -.
DR SMR; P49015; -.
DR STRING; 10029.XP_007614755.1; -.
DR iPTMnet; P49015; -.
DR eggNOG; KOG0207; Eukaryota.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
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; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR TIGRFAMs; TIGR00003; TIGR00003; 5.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 5.
DR PROSITE; PS50846; HMA_2; 7.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Copper; Copper transport; Glycoprotein;
KW Golgi apparatus; Ion transport; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..>1476
FT /note="Copper-transporting ATPase 1"
FT /id="PRO_0000046310"
FT TOPO_DOM 1..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..665
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 695..717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 736..760
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 770..788
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 930..952
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 978..998
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1347..1373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1379..1397
FT /note="Helical"
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 276..342
FT /note="HMA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 376..442
FT /note="HMA 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 478..544
FT /note="HMA 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 554..620
FT /note="HMA 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 1034
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305"
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 287
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 290
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 387
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 390
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 489
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 492
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 565
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 568
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70705"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64430"
FT MOD_RES 1420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 1422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 1450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 1453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 1456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 1459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 1463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04656"
FT MOD_RES 1466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64430"
FT MOD_RES 1476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64430"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 887
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 953
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1476
SQ SEQUENCE 1476 AA; 160336 MW; 6B36F5A2AC358C0B CRC64;
MEPSMDVNSV TISVEGMTCI SCVRTIEQKI GKENGIHHIK VSLEEKSATI IYDPKLQTPK
TLQEAIDDMG FDALLHNANP LPVLTDTLFL TVTASLTLPW DHIQSTLLKT KGVTDIKIFP
QKRTLAVTII PSIVNANQIK ELVPELSLET GTLEKRSGAC EDHSMAQAGE VVLKIKVEGM
TCHSCTSTTE GKIGKLQGVQ RIKVSLDNQE ATIVYQPHLI SVEEIKKQIE AMGFPAFVKK
QPKYLKLGAI DVERLKNTPV KSLEGSQQRP SYPSDSTATF IIEGMHCKSC VSNIESALPT
LQYVSSIAVS LENRSAIVKY NASSVTPEML IKAIEAVSPG QYRVSIANEV ESTSSSPSSS
SLQKMPLNVV SQPLTQETVI NISGMTCNSC VQSIEGVVSK KPGVKSIHVS LANSFGTVEY
DPLLTAPETL REVIVDMGFD AVLPDMSEPL VVIAQPSLET PLLPSTNDQD NMMTAVHSKC
YIQVSGMTCA SCVANIERNL RREEGIYSVL VALMAGKAEV RYNPAVIQPP VIAEFIRELG
FGATVMENAD EGDGILKLVV RGMTCASCVH KIESTLTKHK GIFYCSVALA TNKAHIKYDP
EIIGPRDIIH TIGSLGFEAS LVKKDRSASH LDHKREIKQW RSSFLVSLFF CTPVMGLMMY
MMAMEHHFAT IHHNQSMSNE EMIKNHSSMF LERQILPGLS IMNLLSLLLC LPVQFFGGWY
FYIQAYKALK HKTANMDVLI VLATTIAFAY SLIILLVAMY ERAKVNPITS FDTPPMLFVF
IALGRWLEHI AKGKTSEALA KLISLQATEA TIVTLDSDNI LLSEEQVDVE LVQRGDIIKV
VPGGKFPVDG RVIEGHSMVD ESLITGEAMP VAKKPGSTVI AGSINQNGSL LICATHVGAD
TTLSQIVKLV EEAQTSKAPI QQFADKLGGY FVPFIVLVSI ATLLVWIIIG FQNFTIVETY
FPGYSRSISR TETIIRFAFQ ASITVLCIAC PCSLGLATPT AVMVGTGVGA QNGILIKGGE
PLEMAHKVKV VVFDKTGTIT HGTPVVNQVK VLVESNKIPR SKILAIVGTA ESNSEHPLGA
AVTKYCKQEL DTETLGTCTD FQVVPGCGIS CKVTNIEGLL HKSNLKIEEN NTKNASLVQI
DAINEQSSTS SSMIIDAPLS NAVDTQQYKV LIGNREWMIR NGLVISNDVD DSMIDHGRKG
RPAVLVTIDD ELCGLIAIAD TVKPEAELAV HILKSMGLEV VLMTGDNSKT ARSIASQVGI
TKVFAEVLPS HKVAKVKQLQ EEGKRVAMVG DGINDSPALA MANVGIAIGT GTDVTIEAAD
VVFIRNDLLD VVASIDLSRK TVKRIRINFL FPLIYNLVGI PIAAGVFLPI GLVFQPWMGS
AAMAASSVSV VLSSLFLKLY RKPTYDNYEL RTRSHTGQRS PSEISVHVGI DDASRNSPRL
GLLDRIVNYS RASINSLLSD KRSLNSVVNS EPDKHS
