ID A0A0V0UIF4_9BILA Unreviewed; 1275 AA.
AC A0A0V0UIF4;
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=ATP7B {ECO:0000313|EMBL:KRX51190.1};
GN ORFNames=T05_6030 {ECO:0000313|EMBL:KRX51190.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX51190.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX51190.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX51190.1};
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:KRX51190.1}.
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DR EMBL; JYDJ01000001; KRX51190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0UIF4; -.
DR Proteomes; UP000055048; 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; -; 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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 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; 4.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 3.
DR PROSITE; PS50846; HMA_2; 4.
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:UP000055048};
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 439..460
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 480..499
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 511..536
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 704..729
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1131..1153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1165..1186
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 49..115
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 130..196
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 273..339
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 349..415
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 1275 AA; 139420 MW; D6B390CA7637275C CRC64;
MSTEGIVFVE WTSDRVCEVL HLSDTLCVKD LMSILTKFCS SVVLEDSYLA VKLVISGMTC
QSCASAVKRT LLALQGVYKV KVVVEEKCAY VAYNINHIDV LQMVQSIEEA GFSIVKTNIS
NLEHLSPSVK ECNLNVVGMT CKSCEMNLSK ALLSRLPLLK ATFNAVTNSG IVLYDAQRCT
AHQIIDAIND MGYEASISTE ESSTRKGARE EDSFEVDYLG IGSSRKSLNV KKNKFENNII
SKRKLSSSTA VHIDMQKLQA RMFVGDGQQQ EFERCTLAIE GMTCASCVAN IERNLMNVDG
ISKVLVSLIA GKADVTYDAT VILPSQIVNF VEDMGFACKL MEESTATKRK LELMIVGMTC
TSCVHRIERN VKNLRGVVDA EVTLTNSSGV FIYEPNQCTP RSIMKCIEDL GYSCSLLSKE
NRSAALSHNH DISRWKKSFL ISLLFGLPVM AVMVYYHWIL HTMDKPENQW HVIPGLSFDN
LLLFLLCTPI QFLGGRYFYV KSYKAFKHCT ANMDVLIVLA TTISYIYSVI VLIAAVLSKW
SISPMTFFDV PPMLLMFISL GRWLESIAKA KTSEVLSKLM TLQAKDATIV QLGNNNEILS
EASIDLELVQ IGDYLKVVPG AKIPVDGKVI FGSSSADESY ITGEPLPVTK APGSTVIGGS
VNLNGNLIIE ATHAIQDSTL AQIVKLVEEA QTSKAPIQHL ADKIASYFVP GVILIASLTW
IVWLIIGFID VDIIRNSFGG HCMFLEPVHQ NHSVHSSDAH ADHIQNLELI FKFAFDCAIT
VLAIACPCSL GLATPTAVMV GTGVGAKNGI LIKGGEPLEL AHKITTIIFD KTGTVTQGKP
KLTKICLFVN EIDISLHYLL AIIGTAESNS EHPIAEAITA HVKQFLKTER FGVCKLFQTS
PGHGVRCIVS DVEMMMQKSE KLAEKGNVSF LNDVEVVNYN FDDHSKEEGS NREWEVLIGN
RKWLDKHGIQ ITNEVDGVMS SEEQMGRIAV LVAINGKVVS VFSVADCIKA ESALAVYSLQ
KMGLKTILLT GDNCRTAAAT AKQIGISVVF AEVLPNHKKI KVEQLQRRNE VVAMVGDGIN
DSPALAAADV GIAIAAGADV AIESASIVLI KNNLLDVVAA IDLSQKTTRR IWINFLFASI
YNLLSIPVAA GAFRTIGFGL QPWMAAAAMA LSSVSVVTSS LMLKLYNKPT VESLTTADFA
NHISRLRSAH YGSIEVHRGL EEFKPRKKRS PSASIQSKIL SLIRSVDQNN TSHTCEPTLQ
QGLLSSDSMD DDMQI
//
