ID A0A226MGI5_CALSU Unreviewed; 1317 AA.
AC A0A226MGI5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, 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 ORFNames=ASZ78_011119 {ECO:0000313|EMBL:OXB54139.1};
OS Callipepla squamata (Scaled quail).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC Callipepla.
OX NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB54139.1, ECO:0000313|Proteomes:UP000198323};
RN [1] {ECO:0000313|EMBL:OXB54139.1, ECO:0000313|Proteomes:UP000198323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texas {ECO:0000313|EMBL:OXB54139.1,
RC ECO:0000313|Proteomes:UP000198323};
RC TISSUE=Leg muscle {ECO:0000313|EMBL:OXB54139.1};
RA Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA Decker J.E., Seabury C.M.;
RT "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL Submitted (JUL-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXB54139.1}.
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DR EMBL; MCFN01000976; OXB54139.1; -; Genomic_DNA.
DR STRING; 9009.A0A226MGI5; -.
DR Proteomes; UP000198323; 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; -; 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; 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; PR00943; CUATPASE.
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; 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:UP000198323};
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 508..527
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 595..617
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 623..644
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 787..811
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 150..216
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 235..301
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 347..413
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 447..513
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 1317 AA; 142021 MW; 4646DE59C1405E77 CRC64;
MGSEIVGLLV KVAPGSWRKM PAKIMERKLD NKMRRELSCL ATLNNKNITL VSIRKQQAAH
DVPELLIIGE GSKAGSPLEV SSNLQKEEKV LQRSSMGTPE FSATRRQVLS NADSPPSCAL
EPEMKQNFAF DNMGYEESFE AMPSPSSQER TVTVSVVGMT CQSCVQSVEG RISKVKGVVS
IKVSLELNNA LVKYLQSEIS PEQICQEIED MGFDTNIAEE RLTPVSVNLP CSREAVIKLR
IEGMTCQSCV TSIEGKIKKL HGVTKIKVSL SNQEAVIAYH PYIIQPEELR SHIGNLGYDC
TIKSKSAPLK LGVLDVRNLQ STDPKETPAS LENDGLDPLV ANKSSTATVT VHIEGMHCKS
CVRNIEDNIS SLPGIQSIEV SLEHKCAVVQ YSPNLITMPA LQQAIESLPP GNFKVCLPSS
SEAKDQASPS PASVCDLFRE PLKDTMCTAV IGIGGMTCNS CVQSIEGTIS QRQGVQHIAV
SLAGKTGTIH YDPAITNGEE LRDAIEEMGF DASLLTGIVS VLVALMAGKA EIKYKPDIIQ
PLEITQLIQN LGFEATVIED HSETEGSVEL LFLGGWYFYI QAYKSLKHKA ANMDVLIVLA
TTIAYVYSCV ILLVAIIEKA EKSPVTFFDT PPMLFVFIAL GRWLEHIAKS KTSEALAKLI
SLQATEATVV TLGPDHSIIR EEQVPVELVQ RGDIVKVVPG GKFPVDGKVI EGNSMADESL
ITGEAMPVTK KPGSTVIAGS INAHGSVLVN ATHVGNDTTL AQIVKLVEEA QMSKAPIQQL
ADKFSGYFVP FIIIISTVTL IAWITIGFIN FDIIQKYFPN QNKNLSKAEL ILRFAFQTSI
TVLSIACPCS LGLATPTAVM VGTGVAAQNG ILIKGGKPLE MAHKIKTVMF DKTGTITCGV
PKVMRVLLLG DTAVLSLKKV LAVVGTAEAS SEHPLGVAVT KYCKEELGTQ SLGYCTNFQA
VPGCGISCKV GGVEAVLGVA EEGVAKLDTS KSGDNSVPLG DTTLITLSES NGPSSSHIYS
VLIGNREWMR RNGLHIANDV NDAMTDHETK GQTAILVAID GALCGMIAIA DTVKQEAALA
VHTLKNMGID VVLITGDNRK TAKAIATQVG IKKVFAEVLP SHKVAKVQEL QNERRKVAMV
GDGVNDSPAL ARADIGIAIG TGTDVAIEAA DVVLIRNDLL DVVASIHLSK RTVRRIRINL
ILALIYNLLG IPIAADMSCS KFLFKTNFKN YKKPDTESYE AQAQGRMKPL TPSQISVHIG
MDDRRRDSSR SAPWDQISQV SLSSLTSDKP PRHNGFFEEE GDKWSLLMNG GDEEQYI
//
