ID A0A0V1HUM8_9BILA Unreviewed; 1403 AA.
AC A0A0V1HUM8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN Name=ATP7A {ECO:0000313|EMBL:KRZ14198.1};
GN ORFNames=T11_5121 {ECO:0000313|EMBL:KRZ14198.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ14198.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ14198.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ14198.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:KRZ14198.1}.
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DR EMBL; JYDP01000026; KRZ14198.1; -; Genomic_DNA.
DR STRING; 268475.A0A0V1HUM8; -.
DR Proteomes; UP000055024; 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; -; 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; 2.
DR NCBIfam; TIGR00003; copper ion binding protein; 2.
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; PR00943; CUATPASE.
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; 3.
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:UP000055024};
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 560..581
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 601..620
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 632..659
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 825..847
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 894..914
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1263..1285
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1291..1311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 187..253
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 394..460
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 470..536
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 1403 AA; 154274 MW; 5CB6594C95CA1BCE CRC64;
MQFTASSICG RSREISNCCQ VAFIVFLLTT LRRDWIQAGK WHSMRIAHNL LIMNRTKTSE
LALSFHSASE LPNFLNYITR DNFVQNLHSS LIRTLLLGFY MKYNVIMSNV KKHCLLLSIF
RFDELVELSS SSSLNNALIS TEGIIFVEWT SDRVCEVLHL SDTLCVKDLI SILTKFCSSV
VLENSYLAVK LVISGMTCQS CASAVKRTLL ALQGVYKVKV VVEERCAYVA YNINNIDVLP
MVQSIEEAGF SIVKMNISDL EHLSSSVKEC NLHVLLSRLP LLKATFNAVT NSGVVLYDAQ
RCTPHQIIDA INDMGYEASI STEESSTRKA KEDSFEVDYL GVGSSWKSLD VKKNKFKNNI
ISKRKLSSPT AVHIDMQKLQ ARMFVGDGQQ QEFERCTLAI EGMTCASCVA SIERNLMNID
GINKVLVSLI AGKADVTYDA TVILPSQIVN FVEDMGFACK LMEESTSTKR KLELMIVGMT
CTSCVHRIET NVKNLRGVIG AEVTLTNSTG VFIYEANQCT PRSIMKFIED LGYSCSLLSK
ENRSAALSHN HDISRWKKSF LISLLFGLPV MAVMVYYHWI LHTMDKPENQ WHVIPGLSFD
NLLLFLLCTP IQFLGGRYFY VKSYKAFKHC TANMDVLIVL ATTISYIYSV IVLIAAVLLK
WSISPMTFFD VPPMLLMFIS LGRWLESIAK AKTSEVLSKL MTLQAKDATI VQIGNNNEIL
SEASIDLELV QIGDTLKVVP GAKIPVDGKV IFGSSSADES YITGEPLPVT KAPGSMVIGG
SVNLNGNLII EATHAIHDST LAQIVKLVEE AQTSKAPIQH LADKIASYFV PGVILIATLT
WIIWLIIGFV DVDIIRNSFG GHCLFLEPVH QNHSVHSSDV HADRIQNLEL IFKFAFDCAI
TVLAIACPCS LGLATPTAVM VGTGVGAKNG ILIKGGEPLE LAHKITTIIF DKTGTITEGK
PKLTKICLFV NEIDISLHYL LAIIGTAESN SEHPIAEAIT VHVKQFLKTE RFGICKLFQT
SPGHGVRCIV SDVQMMMHES EKLAEKGDMS FLNDVEVVNY NFGLPPSSYN EQILKENSNR
EWEVLIGNRK WLDKHGMQIT NEVDGVMSSE EQMGRIAVLV ALNGKVVSVF SVADCVKAES
ALAVYSLQKM GLKTILLTGD NCRTAAATAK QVGISVVFAE VLPNHKKIKV EQLQKRNEVV
AMVGDGINDS PALAAADVGI AIAAGADVAI ESASIVLIKN NLLDVVAAID LSQKTTRRIR
INFLFASIYN LLSIPVAAGA FRTIGFGLQP WMAAAAMALS SVSVVTSSLM LKLYKKPTVE
SLTTADFANH IARLRSAHYG SIEVHRGLEE LKPRKKRSPS ASIQSKILSI IRSVDQNNAS
HTCEPTLQQG LLSSDSMDDD IQI
//
