ID A0A3Q1I072_9TELE Unreviewed; 1240 AA.
AC A0A3Q1I072;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN Name=ATP7B {ECO:0000313|Ensembl:ENSAPOP00000033170.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000033170.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000033170.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 STRING; 80966.ENSAPOP00000033170; -.
DR Ensembl; ENSAPOT00000027768.1; ENSAPOP00000033170.1; ENSAPOG00000021619.1.
DR GeneTree; ENSGT00940000155749; -.
DR InParanoid; A0A3Q1I072; -.
DR Proteomes; UP000257200; Unplaced.
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; -; 5.
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; 2.
DR NCBIfam; TIGR00003; copper ion binding protein; 3.
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; SFLDG00002; C1.7:_P-type_atpase_like; 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; 5.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 3.
DR PROSITE; PS50846; HMA_2; 5.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, 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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
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 512..534
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 540..561
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 704..728
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 748..771
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1110..1132
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1138..1158
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 61..127
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 128..194
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 210..276
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 327..393
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 403..469
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 269..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1240 AA; 133220 MW; A10A575B95514E1C CRC64;
QKEPKKXKTV ERGLTGKATE LMVFPSSLQE DDPDSDKRGF DNLAYESEIQ TELCPPPKPA
SRTTFRLPGL TSEVQIQEVD TRICSLDGVF SVSWSVPDSL AQVDYDSSVV TTKQMVLELQ
ALGYSVESAV QSRVEGMHCQ SCVKTIEEQM LELPGVSYVQ VSLKENSVVV VFQPLLVSQE
KLREKIKDLG FEAALLPEDP AGGFRNLFPQ TTTVWIGGMT CGSCVRSIEG RISDLSGVQS
IVVSLEEEKG TIAFDPSLTD PEQLRAAIEE MGFDASLSEP PKSIQTPDKS RPDTSGPPDL
SDSKSGVNGS QGPSANGLQS SPQVKVQKCF VCVSGMTCAS CVANIERHLR KHKGIVSVLV
SLMAGKAEVK YDPDVLDAAG VARLIQDLGF GAKLIEDEEA TRGKLELTIT GMTCASCVHN
IESKLNTTKG ILGASVTLAT KRAHIQFNPD LLGPRDIIKI IQSLGFEASL VKKGFKNNLD
HSEEIRQQFF GGRYFYIQAY RSLKHRTANM DVLIVLATSI SYVYSCVVLM VAMAEQAAQS
PVTFFDTPPM LFVFIALGRW LEHVAKGKTS EALAKLMSLQ AADATVVTLG SDRSVISEEQ
VEVELVQRGD IVKVVPGGKF PVDGKVVEGS SMADESLITG EPMPVSKKAG SLVIAGSINA
HGSLLVEATH VGAETTLSQI VKLVEEAQTS KAPIQQFADR LSGYFVPFIV FVSLLTLVVW
LVIGFVNFDI VKENFPGYNP NISKAEVIVR FAFQASITVL SIACPCSLGL ATPTAVMVGT
GVGAQNGILI KGGPPLEMAH QIDVVMFDKT GTITNGVPRV TRVLVLWEMA RMPLRKILAL
VGTAEASSEH PLGLAVAKHC KEELGSEVLG YCQDFQAVPG CGISCRVSNV EHLLLQQNEE
QFLLPGATTD ESSLLPDGEV TPAAEAAPYS VLIGNREWMR RNGHHIGADV DAAMSSHETK
GQTAILVAID GVLCAMFAIA DTVKAESALA VHTLSSMGIE VVMITGDNRR TAKAIAAQVG
IRKVFAEVLP SHKVAKVQEL QERGLRVAMV GDGVNDSPAL ARADVGIAIG TGTDVATEAA
HIVLIRNDLL DVVASIELSK KTVRRIRINF VFALVYNLVG IPVAAGVFMP VGLVLQPWMG
SAAMAASSVS VVLSSLLLRM YRKTSVETYE LRVRGQMRSL RSSQISTHLG RDGRRRSPAL
PGSTRDQHPG PGAPQGPSSL RTAVQDQDRY SLLEAGEELQ
//