UniProt: A0A199UCE9

Database: UniProt
Entry: A0A199UCE9_MANES

LinkDB:  A0A199UCE9_MANES 
Original site:  A0A199UCE9_MANES

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (2)   
   PROSITE (3)   
All databases (25)   

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ID   A0A199UCE9_MANES        Unreviewed;       997 AA.
AC   A0A199UCE9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=P-type Zn(2+) transporter {ECO:0000256|ARBA:ARBA00039097};
DE            EC=7.2.2.12 {ECO:0000256|ARBA:ARBA00039097};
GN   ORFNames=MANES_S011100 {ECO:0000313|EMBL:OAY22317.1};
OS   Manihot esculenta (Cassava) (Jatropha manihot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC   Manihot.
OX   NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY22317.1};
RN   [1] {ECO:0000313|EMBL:OAY22317.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaf {ECO:0000313|EMBL:OAY22317.1};
RA   Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA   Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA   Stites J., Rounsley S., Rokhsar D.S.;
RT   "WGS assembly of Manihot esculenta.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + Zn(2+)(in) = ADP + H(+) + phosphate + Zn(2+)(out);
CC         Xref=Rhea:RHEA:20621, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29105, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00035906};
CC   -!- SUBCELLULAR LOCATION: Membrane {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   EMBL; KV450447; OAY22317.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A199UCE9; -.
DR   STRING; 3983.A0A199UCE9; -.
DR   EnsemblPlants; OAY22317; OAY22317; MANES_S011100.
DR   Gramene; OAY22317; OAY22317; MANES_S011100.
DR   OrthoDB; 7279at2759; -.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   CDD; cd02079; P-type_ATPase_HM; 1.
DR   Gene3D; 3.30.70.100; -; 1.
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; 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; TIGR01512; ATPase-IB2_Cd; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR   PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00943; CUATPASE.
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; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01229; COF_2; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
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}.
FT   TRANSMEM        124..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        316..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        346..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        658..677
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        683..705
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          18..84
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          865..885
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   997 AA;  108031 MW;  1E9C651729B09724 CRC64;
     MAAQEKGLAG NISKKKFQKS YFDVLGICCS SEVPLIENIL KSLDGVKEFS VIVPTRTVVV
     VHDNLIISQI QIVKALNQAR LEANVRVNGD TSYQKKWPSP FAVAGGVLLL LSLLKFVYHP
     LHWLALGSVA IGIPPIILKA IASIRNFRLD TNILVLIAVV GTIALKDYLE AGTIVFLFTI
     AEWLESRASH KANAVMSSLM NIAPQKAIIA ETGEEVDADE VKLNTILAVK AGEIIPIDGI
     VVDGNCEVDE KTLTGESFPV AKQKDSTVWA STINLNGYIS VKTTALAEDC VVAKMVKLVE
     EAQNNKSRTQ RLIDKIAQYY TPVVIIISVS LVVVPLTLRV HNRNHWFHLA LVVLVSACPC
     ALILSTPVAT FCTLTKAATS GVLIKGGDYL ETLAKIKVMA FDKTGTITRG EFVVVDFQPL
     CEDVSLDALV YWVSCIESKS SHPMAAALVD YGRSHSVEPN PENVVDFQNF PGEGIHGKID
     GKEIYIGNRK IALRAGCGTV PMPEEGDMKG GKTIGYVFSG GNPIGIFSLS DACRTGVAEA
     ISELKSFGIR TAMLTGDSQA AAMHAQEQLG NALEVVHAEL LPEDKARIIE TFKKEGSTAM
     IGDGINDAPA LAMADIGISM GISGSALATE TGHVILMSND IRKVPKTIQL ARKAHRKVIE
     NIILSISTKS AILALGFAGH PLVWAAVLAD VGTCLLVIFN SMLLLRGTHE KGRKCCKSSS
     AAEHTKKCDS TYSSHHHKPC CSNKKVTKSC EPQELQTCTS RCESDDVNKN RSCGKKCTNP
     ANKEQNEVKH CSHGSCNTVD LEANNPHKHA CSKSSAEENT KKCKNKSSSH HHKPCCSSKQ
     KVAKVCEHQE LQTCASGFES DDLDKSTSCG KTCQNSPNKE KNEVKHCGHN HSDQMNHHCI
     SNHSNHSSDI DHCDDSSKST WESGFNHRPL HLEHAVKNCC SSHNNLHCST MDIHHACMNL
     EKRESGSCCK SYMKECCGKH GRFSNGFGGG LSEITIE
//

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