ID I3K2B4_ORENI Unreviewed; 1294 AA.
AC I3K2B4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 78.
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:ENSONIP00000015259.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000015259.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000015259.2}
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 RefSeq; XP_019207565.1; XM_019352020.1.
DR STRING; 8128.ENSONIP00000047349; -.
DR Ensembl; ENSONIT00000015272.2; ENSONIP00000015259.2; ENSONIG00000012121.2.
DR GeneID; 100701459; -.
DR CTD; 540; -.
DR eggNOG; KOG0207; Eukaryota.
DR GeneTree; ENSGT00940000155749; -.
DR HOGENOM; CLU_001771_0_1_1; -.
DR OrthoDB; 5480493at2759; -.
DR TreeFam; TF300460; -.
DR Proteomes; UP000005207; Linkage group LG23.
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; PTHR46594; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR46594:SF8; P-TYPE CU(+) TRANSPORTER; 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; 4.
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:UP000005207};
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 473..492
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 553..575
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 581..602
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 745..769
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 789..812
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1151..1173
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1179..1199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 35..101
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 102..168
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 192..258
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 308..374
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 384..450
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1232..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1294 AA; 139598 MW; C9A5CC0348CBA335 CRC64;
MMQESDPDIE KQGFENLAYE YGSQTELCPP PKAASRAAFK LQRITSEHEV HIIQTRICSL
NGILAVTWSV PNSLAKVDYD ASVIPTKEIA LELQTLGYSV ESVVQIRVDG MHCQSCVQSI
QGQIGELQGV SHIQVSLQDK AALIVFKPLL VTHEELRDKI EDMGFDTALL SEDPSVEDLS
FWQNKEVDAS TQTVTILIGG MTCNSCVRTI EGRISQMTGV RFIAVSLEAE RGTITFDPYL
TEPEQLRAAI EDMGFDASLK EPIKSVQSHE KSQPVSFGLS DMSANRPVVS NGTGSQAPSA
SSPEIKAKRC FICVTGMTCA SCVSNIERNL LKHRGVLSVL VSLMAGKAEV KYDSDVLDAI
AVTELIKDLG FGAKVIEDNA VAHGKLDLTI TGMTCASCVH NIESKLNLTR GILMASVTLA
TNKAQVEFDP EVLGPRDIIK IIQGLGFEAR LEKAGFKNNL DHKEEIRQWK NSFLLSLVFG
LPVMGLMIYM MVMDNLHQEH GGSMPTEQNV LPGLSILNLL FFVLCTPVQI FGGRYFYIQA
YRSLKHRTAN MDVLIVLATS IAYIYSCVVL IVAMAEQASQ SPVTFFDTPP MLFVFIALGR
WLEHIAKSKT SEALAKLMSL QATDATVVTL GSDKSIISEE QVLVELVQRG DIVKVVPGGK
FPVDGKVIEG SSMADESLIT GEPMPVSKKV GSLVIAGSIN AYGALLVEAT HVGAETTLSQ
IVKLVEEAQT SKAPIQQFAD RLSGYFVPFI VIVSLLTLIV WLVIGFVNFD IVKENFPGYN
QSIPKAEVIV RFAFQASITV LSIACPCSLG LATPTAVMVG TGVGAQNGIL IKGGEPLEMA
HKIGVVMFDK TGTITNGVPR VTRVLVLWEV ARMPLRKILA VVGTAEASSE HPLGIAVAKH
CKQELGSDVL GCCQDFQAVP GCGISCRVSS VEHLLLQPSE ERFLLPGAAI EESNMLPAGE
STSAAEGLFY SVLIGNREWM RRNGHHIGAD VDAAMSSHET KGQTAILVAI DGVLCAMLAI
ADTVKAESAL AVHTLNTMGI EVVMMTGDNR RTAKAIAAQV GIRKVFAEVL PSHKVAKVQE
LQKRGLRVAM VGDGVNDSPA LARADVGIAI GTGTDVAIEA ADIVLIRNDL LDVVASIELS
KKTVRRIRIN FVFALFYNLV GIPIAAGVFM PVGLVLQPWM GSAAMAASSV SVVLSSLLLK
MYKKTSVELY EMRARGQMRS LRSSQISTHL GLDGRRRSPA LPNATREQRN PSGMTPPGFS
GRSPSQGASI KVVTEEQGRY SLLEHQTADV LNVL
//
