UniProt: A0A0N5AGX9

Database: UniProt
Entry: A0A0N5AGX9_9BILA

LinkDB:  A0A0N5AGX9_9BILA 
Original site:  A0A0N5AGX9_9BILA

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein domain (19)   
   InterPro (13)   
   Pfam (3)   
   PROSITE (3)   
All databases (26)   

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ID   A0A0N5AGX9_9BILA        Unreviewed;      1139 AA.
AC   A0A0N5AGX9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE            EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
OS   Syphacia muris.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX   NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000360901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMUV_0000360901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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   AlphaFoldDB; A0A0N5AGX9; -.
DR   STRING; 451379.A0A0N5AGX9; -.
DR   WBParaSite; SMUV_0000360901-mRNA-1; SMUV_0000360901-mRNA-1; SMUV_0000360901.
DR   Proteomes; UP000046393; Unplaced.
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; 2.
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; 4.
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; 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   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        457..478
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        548..573
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        579..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        737..764
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          36..124
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          150..216
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          284..350
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          360..426
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   1139 AA;  125108 MW;  8ABD54B5A420BAA3 CRC64;
     MWGLLISWNF RMKDTEADVN VLNEHLCTQV PEAHCSKTVI SVEGMTCHSC VNNIQNFIGS
     KNGIYSISVS LSDRQGMRSF YVSSFAYFLF LKVVISYSIV EYDESIWNAD SVAEAIDDMG
     FDAKVIGNFK SKDFEMDSLP LPLPSSTSYR NAYIDVKGMT CNSCVKHIQE QVKLLEGVKD
     IEVSLDSGEA FITFNSNILS NDAVVQAIED LGYDAKLKRF TDGPQVTKAS AKQNSDESGN
     LKLSTTSLQS REMLNCNNDR KLLDLSNTSL KRSKDCVNME ESLKKCIITI KGMTCASCVA
     NIEKNVMKLK GVQSVVVALM ASKAEVVFDA NRIDADQIVN RIRRLGYNSL LLECGVSLFQ
     KINLQLSGIS NSMDEKRIES RLLERKGIES CTILSLNATA SIEFSPTLIG PRDVIKIIDA
     SFYYLFDLGY SAVLVENDEK FKQFDCSKEI AKWKNSLLLS LFFGLPVMGI MVYFHWFLHT
     PMVPENQTPV FIRAISLDNL LLFALCTPIQ KYLNSDKINH LYKQIIGGRY FYIKSWKALK
     HRTSNMDVLI VLATSIAYLY SIIALLIAVV LGWSSSPMTF FDVPPMLIVF ISLGRWLEHK
     AKGRTSEALS KLMSLQAKEA ILVTRDESGY TIAEEKIDID LVQRNDLIKI LPGGKIPMDG
     IVVDGKSSVD ESFITGEFMP VVKDIGSPVI SGSVNQNGTL LVKVTHVSQE STLAQIVHLV
     EQAQTSKAPI QQVADRVAGY FVPVVVCLAC LTLFGWIIFG FFFMHVNYVN KSEQLEFVLK
     RAFESAITVL AVACPCSLGL ATPTAVMVGT GIGASNGILI KGSDALETAH KLTTVVFDKT
     GTITEGVPTV VGVQLLVAEH FLPLRKMFAL IGSAESNSEH PIASSIISFV KKYMDITEWG
     VIERFHASPG NGLSCVVTKL PNCVTEITDK DKEFSQKLSS IGGVFNIKPA DIEIRQSAQL
     YGGKTEDYDT SKPFSVIIGN ERWLLKNSVF LDENILSILN DEQSKGHISV LCAINGRCAA
     IISITDRIKQ ESRLAVWGLK KMGIHVVLLT GDNARTAEVT GQQVGITDVF AEVLPNQKEL
     LIEKLQNTGQ VVAMVGDGVN DSPALASADV GIAIAAGSDV AIESAGIVLV KVSITLLQF
//

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