ID A0A3B4AS03_9GOBI Unreviewed; 1457 AA.
AC A0A3B4AS03;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000019379.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000019379.1}
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 STRING; 409849.ENSPMGP00000019379; -.
DR Ensembl; ENSPMGT00000020655.1; ENSPMGP00000019379.1; ENSPMGG00000015732.1.
DR Proteomes; UP000261520; 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; 6.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 6.
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; 5.
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; 6.
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; 6.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 5.
DR PROSITE; PS50846; HMA_2; 6.
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}; 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 617..636
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 667..689
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 710..731
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 737..759
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 904..928
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 948..972
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1322..1343
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1349..1369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..66
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 164..230
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 272..338
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 382..448
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 453..518
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 528..594
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 344..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1457 AA; 157173 MW; A60AA13196CA35C2 CRC64;
SVCVGVEGMT CGSCVQSLEQ RLGSFPGVIH IKVSLELKNA VIVFDQSKQS PVSLSFAIED
MGFESSLADS GNSSPVPTDT QLIPAPGLSP AAQQEALDRL SHIQGVLEVT HSSAQMGFTV
TFVAGLTSTQ QLGEVVSRVA ATVSPKDRGS PGSSLPRSAG AEATLLKLCI EGMTCHSCTT
TIEGKIGKLK GVQKVKVALD AKEATIVYLP YLITIQTILE QISRAGFKAQ VKSKPRPLQL
PTEIESFIDC QKSAVSSPSE NTEETEIFID TTLVTLRVKG MHCRSCVVNI QDNISTLPGV
ASVEVSLQNE KASIVHDPLQ ISVSQIQRAI EALPPGNFRT QLWDSAGALG SPPPPSAPAP
PGLGGNAKYA VPQPCLSQPL SSVANIHIEG MTCNSCVQSI EGVIGQRKGV ASAEVSLSEH
QGVFEYDPLV TTPEELRAAI EDMGFDAFLP AYSKCYIQIG GMTCASCVAN IERNLKNEPI
YSVLVALMAS KAEVRYNADL TDPMKIAECI KELGFTSSVM ENYEGSDGNV EFVIRGMTCA
SCVHKIESSL MKVKGIIYAS VALATNKAHI KYDAEIMGPR DIIKHIENLG FEASLVKKDR
TASHLDHSKE IKWRKSFLIS LFFCVPVMGM MTYMIIMDHQ MNVSHHHNFT NEDRNRYHST
MFLERQLIPG LSIMNLLSFL FCVPVQFIGG RYFYIQAYKA VKHKSANMDV LIVLATTIAF
TYSLIVLIVA IVEKARINPI TFFDTPPMLF VFISLGRWLE QIAKFQSKTS EALSKLMSLQ
ATEATVVTLG SDMSILEEQV DVELVQRGDV VKVVPGGKFP VDGRVLEGHS MADESLITEA
MPVTKKPGST VIAGSINQNG SLLVSATHVG MDTTLSQIVK LVEEAQTSKF QAPIQQYADK
ISGYFVPFIV GISALTLVAW IIVGFLNFSL VEKYFPQGYD KSISMTEAVV RFAFQASITV
LCIACPCSLG LATPTAVMVG TGVGAQNGIL IKGGEPLEMA HKVQSVVFDK TGTITYGAPK
VIQMKMVVEG NRMPRSRLVA IVGTAENNSE HPLGAAITKY CKQELDTEAL GTCTDFQAVP
GCGIRCQVSN TETLLKQADS DGEDNNQRNS VLVQISDART SGSSHPLIMD PQPLPIQTST
YVVLIGNREW MRRNCLQVSP EVDNAMTEHE RRGRTAVLVA VDLLCAMIAI ADTVKPEAEL
AVHTLTNMGL EVILMTGDNS KTARAIAAQV VGIRKVFAEV LPSHKVAKVE QLQRAGKRVA
MVGDGVNDSP ALAMADVGIA IGTGTDVAIE AADVVLIRND LLDVVGSIDL SKKTVKRIRI
NFVFALIYNL VGIPIAAVFL PIGLVLQPWM GSAAMALSSV SVVLSSLLLK YNKPSAEKLE
ARFGKSRRQG SLSDVSVHIG IGELRRSSPK LSLLDRIVNY SRASINSLRS DKHSLNSLAL
EPDKHSLLVG DATEEDL
//
