ID A0A091TGR3_PHALP Unreviewed; 1347 AA.
AC A0A091TGR3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
DE Flags: Fragment;
GN ORFNames=N335_03894 {ECO:0000313|EMBL:KFQ73460.1};
OS Phaethon lepturus (White-tailed tropicbird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC Phaethontidae; Phaethon.
OX NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ73460.1, ECO:0000313|Proteomes:UP000053638};
RN [1] {ECO:0000313|EMBL:KFQ73460.1, ECO:0000313|Proteomes:UP000053638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ73460.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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; KK450690; KFQ73460.1; -; Genomic_DNA.
DR PhylomeDB; A0A091TGR3; -.
DR Proteomes; UP000053638; 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; 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; 2.
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; 5.
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; 5.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053638};
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 537..556
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 576..598
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 610..636
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 642..663
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 806..830
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 850..873
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1217..1238
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1244..1262
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..41
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 60..126
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 172..238
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 272..338
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 371..437
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 447..513
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ73460.1"
FT NON_TER 1347
FT /evidence="ECO:0000313|EMBL:KFQ73460.1"
SQ SEQUENCE 1347 AA; 145537 MW; C7A2F481EB219FBE CRC64;
KGIVSIKVSL EQNNALIKYL QSEISPEQIC QEIQDMGFDA NIEEERLTTA TLNLSCLREA
VVKLRVEGMT CQSCVTNIEG NIRKLHGVAK IKVSLGNQEA IIAYYPYIIQ PDDLKSHISN
LGYDCTIKSK SAPLKLGVLD LGRLQNANPR ETPVNLESDG VDPPVAKMSG TATVAVRIEG
MHCKSCVRNI EGNISDLHGI QSIKVSLEHK RAVVQYSPIL ITLSAVQQAI ESLPPGNFKV
CLLNGSEANK GASASPAFLC DPFREPLQDT TCTAVVRIDG MTCNSCVQSI EETISQRQGV
QCVAVSLGDR TGTIRYDPAV TNGEELRAAI EDMGFDASVL TEPPHQGCAL DALPDSPHLD
GPNHPSRVTA EKCFLQITGM TCASCVSTIE RNLQKEDGIV SVLVALMAGK AEIKYKPEFI
QPLEIAQLIQ NLGFEATIIE DHAETEGNVE LLVSWMTCAS CVHNIESKLM RTNGIFYASV
ALATCKAHIQ FDPEITGPRD IIKIIEEIGF HASVARRVPN AHNLDHKKEI QQWRKSFLCS
LLFGIPVLIL MIYMLIPDGE HHGSMVLEQN LIPGLSVLNL LFFVLCTFVQ FLGGWYFYLQ
AYKSLKHKAA NMDVLIVLAT TIAYVYSCVI LMVAIIEKAE KSPVTFFDTP PMLFVFIALG
RWLEHIAKSK TSEALAKLIS LQATEATVVT LGPDHSIIRE EQVAVELVQR GDIVKVVPGG
KFPVDGKVIE GSSMADESLI TGEAMPVTKK PGSTVIAGSI NAHGSVLVNA THVGNDTTLA
QIVKLVEEAQ MSKAPIQQLA DKFSGYFVPF IIIISTVTLI VWITIGFINF DVIEKYFPNQ
NKHVSKAELI LRFAFQTSIT VLSIACPCSL GLATPTAVMV GTGVAAQNGI LIKGGKPLEM
AHKIKTVMFD KTGTITCGVP KVMRVLLLGD TAVLSLKKVL AVVGTAEASS EHPLGVAVTK
YCKEELGTQS LGYCTDFQAV PGCGISCKVG GVEAVLGTAE EGLDELDANR SMESRAPLGD
NALITLAESH GPSASHTYSV LIGNREWMRR NGLHIANDVN DAMTDHETKG QTAILVAIDG
LLCGMIAIAD MVKQEAALAV HTLKNMGIDV VLITGDNRKT AKAIATQVGI KKVFAEVLPS
HKVAKVQELQ NGRRKVAMVG DGVNDSPALA RADVGIAIGT GTDVAIEAAD VVLIRNDLLD
VVASIHLSKR TVRRIRINLI LALIYNLLGI PIAAGVFMPV GLVLQPWMGS AAMAASSVSV
MLSSLQLKWY KKPDTESYEA QAQGHMKPLT PSQISVHIGM DDRRRDSSRP APWDQISQVS
LSSLTSDKLP RRSGFVEGEG DKWSLLM
//