ID A0A087YAM0_POEFO Unreviewed; 1318 AA.
AC A0A087YAM0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
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:ENSPFOP00000015073.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000015073.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000015073.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 EMBL; AYCK01005438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 48698.ENSPFOP00000015073; -.
DR Ensembl; ENSPFOT00000015095.1; ENSPFOP00000015073.1; ENSPFOG00000014876.1.
DR eggNOG; KOG0207; Eukaryota.
DR GeneTree; ENSGT00940000155749; -.
DR OMA; EHPIANS; -.
DR Proteomes; UP000028760; 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; 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; 4.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 4.
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:UP000028760};
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 520..539
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 600..622
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 628..649
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 792..816
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 836..859
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1197..1219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1225..1245
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 149..215
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 239..305
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 352..418
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 428..497
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1278..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1318 AA; 141964 MW; 66A5002C0788D6B1 CRC64;
MFSPKGSKKQ SGFESGAARD SGEQICMVEC GCKPVCTCGS TCDPTLCAAE LKRNGPDVDP
TAFDNLAYEY GSQSELDLSA KPISRISFKL LGLVSEQQAV ETTLDRLNGV FAIIWSVSDS
LLQVDYNTSI TTTKEIARQL QTLGCRVEAA IRIKVGGMRC QSCVQAIEGQ FGGLPGVSHI
QVSLQDRTAL IVYQPVLVTQ QELRDKIEDM GFDAALLPED SSDGDLSYWQ NDLINAPIQT
VTVWIGGMTC RSCVQSIEGR ICQMIGVKSI MLSLKEGKGT IHWDPSLTDP EQVRAAIEEM
GFDASLEEPL QTQEKQDLAN LSSISRLGMS NGAESQVTPL RSHISSPEMK AEKCFIHVTG
MTCASCVANI EKHILKHKGI VAILVSLMAG KAEVKYDPNL IDPSGVTQLI DDLGFGAKLL
EDNAAAHGKL DLQITGMTCA SCVHKIESKL ITTKGIHSAS VALATQKAHI KFDPEILGAR
DIVRIIQESQ SLGFEASLEK AGFKNNLDHS EEIRQWKNSF LFSLVFGLPV MGLMIYMMIM
DIQHKQHGGS MPEELNVLPG LSLLNLAFFL LCTPVQIFGG RYFYVQAYRS LKHRTANMDV
LIVLATSIAY IYSCVVLVVA IAEQAAQSPV TFFDTPPMLF VFIALGRWLE HIAKSKTSEA
LAKLMSLQAT DATVVTLGPD RCVVSEEQVE VELVQRGDIV KVFPGGKFPI DGKVIEGSSM
ADESLITGEP MPVSKKVGSL VIAGSINAHG ALLVEATHVG AETTLSQIVK LVEEAQTSKA
PIQQFADKIS GYFVPFIIFA SMLTLVAWIS VGFVNFDVVK EHFPGYNQNI SKAEVIIRFA
FQASITVLSI ACPCSLGLAT PTAVMVGTGV GAQNGILIKG GEPLEMAHKI DVVMFDKTGT
ITNGVPKVTR VLVLWEMARM PLRKILALVG TAEVSSEHPL GTAVAKYCKD ELGSDALGYC
QDFQAVPGCG ISCRVSNVEH LLQRSDEAFF LPGVTTDESR LLSAEEATPT AEWASYTVLI
GNREWMRRNG HHIKADVDAA MSSHETKGQT AILVAIDGVL CAMLAIADSV KAESALAVHT
LSSMGIEVAM ITGDNRRTAK AIAAQVGIRK VFAEVLPSHK VAKVQELQGR GRRVAMVGDG
VNDSPALACA DVGIAIGTGT DVAIEAADIV LIRNDLLDVV ASIELSKKTV RRIRINFVFA
LIYNLLGIPV AAGVFMPVGL VLQPWMGSAA MAASSLSVVL SSLLLRTYRK TSFELYESCA
RGHMGSLQSS QISTHLGLDG QRRSPALSNS SRAQKGQRPS GNAAQERQSY RTADNSTI
//
