ID W6U8J4_ECHGR Unreviewed; 1548 AA.
AC W6U8J4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN ORFNames=EGR_08459 {ECO:0000313|EMBL:EUB56731.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB56731.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB56731.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
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|ARBA:ARBA00006024,
CC 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:EUB56731.1}.
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DR EMBL; APAU02000106; EUB56731.1; -; Genomic_DNA.
DR STRING; 6210.W6U8J4; -.
DR EnsemblMetazoa; XM_024497708.1; XP_024347927.1; GeneID_36344174.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000019149; 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; 3.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 3.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 3.
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 NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR NCBIfam; TIGR00003; copper ion binding protein; 1.
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; 3.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00942; CUATPASEI.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 2.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 3.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 3.
DR PROSITE; PS50846; HMA_2; 3.
PE 3: Inferred from homology;
KW ATP-binding {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|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000019149};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 562..583
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 621..643
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 655..680
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 686..704
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 862..883
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 889..907
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1458..1479
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1485..1508
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 3..69
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 391..457
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 474..540
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1088..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1548 AA; 169134 MW; 5FB541AB50D16F3D CRC64;
MFVPCIVHID GMTCQSCVST IQNTLHCVNG IFVVDINLQE KQALIIHSPT QISVDEVTEV
ISGIGFDAHF MTNRIETSSK RGSIVPSVSS AESHPSEIRH QSFRFYSSDV AIISQYLYTL
PGVIYFSIFE KESRIDLWIL SNSLIDQELL CKLNKQGFRV VLADSSVAES TSAEFDPLNS
SLRLPGNKAY LIVDALPSPE IEELRRRLNL ASLSSLAVCR VGQAYCHLVT LSKGLDTRSI
ADILTGNGFP SARIASVGTG FEVYVSIYGV CCKVCEDEVL NVLRHTLPDD AFQVLMDQDE
IILASHSSIP SATDFLAGLH LTQLHNAITH LGYSCHLRDL SGIHCPSKPD DFSTSVTENG
RTTLKSPVLS EEVKVGEMTT IDLEPPIHAL KCCHLRVTGM TCSSCVQTVE NALLKLPGVR
SATVGLLSMK ADIIYDPTLI QPSALTRQIN ELGFSAQILE VRRAAEIHGD EGTQTLEVTI
LGMTCSSCVN SIETAIKKLP GVTSASVALA TKRGKVVFDS RIVGARSILK TIEDMGFDAS
VYKPEFKSTE DFDETKRWRC VFLTNLAFGL PTMFAMMLFM LIWPHSPVGG YCHPRSYNTS
KETSPTHSQP MLLPGLSWEN FILWLLATPV QAISGRNFYI RAYNSLKHGM ANMDVLLVMA
SGVAYTYSVV VVLIAMIQQW PTSPRTVFET TPMLFLFISL GRWLENLAKE RTSEAVSKLL
SLQAKEATLM EPQSGALNEA FSGEQLTIDT LQNYQERCIS VELVQRGDII KILPGEKVPV
DGRVIFGISS CDESLLTGES MPVPKTVDNI VVGGAINLTG LLYIQATHIG SESALAQIIA
LIEDAQSSKA PIQQLADRIS GFFVPCIILL SLASLIFWIV LGFCRSSSIR GYTVSIVFPL
LLPPFAFSPE CSLVGAVLDQ AFRVAVNVLT IACPCSLGLA TPTAVMVGTG VGALHGILIK
GGQPLENLRK VSTILFDKTG TITMGRPQIS RIVMFMPATP SNPESKNQKV DPHALTSPSR
LLYMVGSAES TAQHPIATAI VRMLRSAQSA FSDQPNGSIW KSEFAKVINA ETSPGYGMSC
DVIVSPEDCP SGPELPRPTR LPSDRQSVQQ TQLYADYDAA LRMELNYYSV RWNSDNSPLS
WANVTQGGTY HLLIGNQRWM QKNAVAIPLM DLDSVVRMDE EEGRTVVHVA VDGRLVALIT
IADPIKPEAA LTVAALKVMG IHVALLTGDN TRSATSIARK VGIRDVYSEV IPAHKAMQVR
QIQTRHVKAS GNGLSKLNQT AMKNGKVEGD THCSGERVAF LQSSKHPDTL DQTAETSFLE
YSYSDTDDDS EASLYLYPGD LGVPIERSGR KRFFDDRKGK YTYIGQRNKR QWRNRRCFCA
WCGICPTAPR QRKREFVAMV GDGINDSPAL SQADVGIAIG CGADVAVATA DVVLVRNDLV
DVVAAISLSR ATVRRIRLNF FAALIYNALA IPVAMGFLIP IGIEFAPWMS SAAMATSSVT
VVCLSLLLKR WKKPTEASLV SQKYLRLLTN SGLTIDQVRV KRDNTPNK
//