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Database: UniProt
Entry: A0A0E0HE81_ORYNI
LinkDB: A0A0E0HE81_ORYNI
Original site: A0A0E0HE81_ORYNI 
ID   A0A0E0HE81_ORYNI        Unreviewed;      1158 AA.
AC   A0A0E0HE81;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Cation-transporting ATPase {ECO:0008006|Google:ProtNLM};
OS   Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA05G16410.2};
RN   [1] {ECO:0000313|EnsemblPlants:ONIVA05G16410.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA05G16410.2};
RA   Wing R.A., Hsing Y.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ONIVA05G16410.2}
RP   IDENTIFICATION.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA05G16410.2};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000}.
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DR   AlphaFoldDB; A0A0E0HE81; -.
DR   EnsemblPlants; ONIVA05G16410.2; ONIVA05G16410.2; ONIVA05G16410.
DR   Gramene; ONIVA05G16410.2; ONIVA05G16410.2; ONIVA05G16410.
DR   Proteomes; UP000006591; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd07543; P-type_ATPase_cation; 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; IPR006544; P-type_TPase_V.
DR   InterPro; IPR047820; P5A-type_ATPase.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   NCBIfam; TIGR01657; P-ATPase-V; 1.
DR   PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR   PANTHER; PTHR45630:SF7; ENDOPLASMIC RETICULUM TRANSMEMBRANE HELIX TRANSLOCASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   PRINTS; PR00119; CATATPASE.
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; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01229; COF_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006591};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        28..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        52..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        395..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        943..962
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        974..992
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1004..1028
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1085..1105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1125..1147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          826..881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        834..848
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        849..876
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1158 AA;  129234 MW;  102D1267469408A5 CRC64;
     MARFEVGGKS VEGVDLLRRR HWASRLDFWP FLALYALWLV VVVPALDFTD ALVVLGALSA
     SHVLAFLFTA WSVDFRAFVK DIRAANSCKV TPAKFSGSKE IVPLHIQKTV ASSSAAGETE
     EIYFDFRKQR FIYSSQEDNF FKLRYPTKEP FEHYIKGTGY GTEAKINTAV DKWGRNIFEY
     PQPTFQKLMK EQCMEPFFVF QVFCVGLWCL DEYWYYSLFT LFMLFLFEST MAKNRLKTLT
     ELRRVKVDNQ IVATYRCGKW VRIPGTELLP GDIVSIGRSV SGEDRSVPAD MLLLAGSAIV
     NEAILTGEST PQWKVSVAGR GPEETLSVKR DKNHILFGGT KILQHTPDKS INLRAPDGGC
     IAFVLRTGFE TSQGKLMRTI LFSTERVTAN SKESGLFILF LLFFAVIASG YVLVKGLEDP
     TRSRYKLFLS CSLILTSVIP PELPMELSIA VNTSLIALAR RGIFCTEPFR IPFAGKVDIC
     CFDKTGTLTS DDMEFQGVVS LEDDEELITD ANKLPLRTQE VLSSCHALVF VDNKLVGDPL
     EKAAIKGIDW IYTSDEKAIS KKSGGQPVKI VHRYHFASHL KRMSVVVSIH EKYYAFIKGA
     PETIQERLVD LPAGYVETYK KYTRQGSRVL ALAYKLLPDM PVNDARSLER DQVESDLTFA
     GFAVFNCPIR SDSGAVLQEL EQSSHDLVMI TGDQALTACH VAGQVHICSK PVLILTRTKT
     GGFEWVSPDE TDRAPYSAEE VAAVSGSHDL CISGDCFEML QRTDAVIQVI PYVKVFARVA
     PEQKELVLTT FKTVGRVTLM CGDGTNDVGA LKQAHVGIAL LNAEPVQKSD TKSQASKSEN
     KQGKLKKPKP SQEGSSSQLT QPANSSARAS SSRPLTAAER QRERLQKMMD EMNEESDGRS
     APIVKLGDAS MASPFTAKHA SVAPTLDIIR QGRSTLVTTL QMFKILGLNC LATAYVLSVM
     YLDGVKLGDV QATISGVFTA AFFLFISHAR PLQTLSAERP HPNIFCAYVF LSILGQFAMH
     LFFLISAVNE ATKYMPEECI EPDSEFHPNL VNTVSYMVNM MIQVATFAVN YMGHPFNQSI
     TENKPFKYAL YAAVAFFTVI TSDMFRDLND YMKLEPLPEG MRGKLMLWAI LMFCGCYGWE
     RILRWAFPGK MPAWEKRN
//
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