ID A0A3B0K945_DROGU Unreviewed; 1273 AA.
AC A0A3B0K945;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN ORFNames=DGUA_6G020550 {ECO:0000313|EMBL:SPP89873.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP89873.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004166}. Membrane
CC {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|RuleBase:RU362081}.
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DR EMBL; OUUW01000038; SPP89873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0K945; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000268350; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 CDD; cd00371; HMA; 4.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 4.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR NCBIfam; TIGR00003; copper ion binding protein; 4.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 4.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00942; CUATPASEI.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 4.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 3.
DR PROSITE; PS50846; HMA_2; 4.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW Ion transport {ECO:0000256|ARBA:ARBA00022796};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 431..450
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 462..488
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 654..679
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 699..723
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1105..1126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1132..1155
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 28..94
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 98..164
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 222..288
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 298..364
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 167..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1273 AA; 137808 MW; C1D0C564E7E85DEC CRC64;
MNDEENANNV LAIEGQSTDQ LTSHATPSRI RLPIVGMTCQ SCVRNIQDHI GKRSGVLVAR
VVLEEHAGYF DYDASLIDPP QIAEAIDDMG FECSYNTALT NIRVVGMTCQ SCVRNIEGNI
GTKPGIQHIE VQLAAKNARV QYDPSQLTPD QIAELIDDMG FEASVAAAAT SEGSNSRPST
PKTNSAAAPS PRQSPRRETQ PEKKHAQNGT ATAIPVEQEA LTKVFLHIRG MTCASCVAAI
EKHCRKIYGL DSILVALLAA KAEVKFNANV LTAENIAKSI TELGFPTELI NEPNNGEAEV
ELEIGGMTCA SCVNKIESHV LKVRGVTAAS VTLMTKRGKF RYNTEDTGPR SICEAIEGLG
FEAKLMTGRD KMAHNYLEHK EEIRKWRNAF LVSLVFGGPC MVAMVYFMLE MNDKGHANMC
CLVPGLSMEN LVMFLLSTPV QFFGGFHFYV QSYRAIKHGT TNMDVLISMV TTISYVYSVA
VVIVAVLLEQ NSSPLTFFDT PPMLLIFISL GRWLEHIAKG KTSEALSKLL SLKAADALLV
EISPGFDIVS EKVISVDYVQ RGDILKVIPG AKVPVDGKVL YGHSTCDESL ITGESMPVAK
RKGAVVIGGS INQNGVLLVE GTHTGENTTL AQIVRLVEEA QTSKAPIQQL ADRIAGYFVP
FVVVVSSITL ITWIIIGFAN PDLVPVAMEH KMHMDRNTII VSYAFKCALS VLAIACPCAL
GLATPTAVMV ATGTGAINGV LVKGATALEN AHKVKTVVFD KTGTITHGTP MTSKVTLFVP
PQVCSLARAL TIVGAAEQNS EHPIASAIVL FAKDMLSVGP VGTAQQGGNF GKSSHFQAVP
GCGIRVSVSN YEHTLRQACN AERIINYENL YRQHPQSSIN VENGASVEHL MLQRDVRKSM
EVAQQQLLAL EGVVGVEQKL IDGPEIQVLI GNREWMQRNA IEVPLEIGDC MTHEERKGHT
AVLCALNGQL VCMFAVSDMV KPEAHLAVYT LKRMGIDVVL LTGDNKNTAA SIAREVGIRT
VYAEVLPSHK VAKIQRIQQR GIRVAMVGDG VNDSPALAQA DVGITIAAGT DVAAEASDIV
LMRNDLLDVV ACLDLSRCTV RRIRYNFFFA SMYNLLGIPL ASGLFAPYGF TLLPWMASVA
MAASSVSVVC SSLLLKMYRK PTAKTLRTAE YEAHLAAERA RRNGSSSESE LDNLSLHRGL
DDLPEVGGKR LAFKRSNTSL ISRIFMQGNG AIGGHSSTDK HEEGLLDAED QYEGRTKIVK
SRYLNDSTEL QKL
//
