UniProt: A0A2G5ERK2

Database: UniProt
Entry: A0A2G5ERK2_AQUCA

LinkDB:  A0A2G5ERK2_AQUCA 
Original site:  A0A2G5ERK2_AQUCA

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (17)   
   InterPro (11)   
   Pfam (5)   
   PROSITE (1)   
All databases (25)   

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ID   A0A2G5ERK2_AQUCA        Unreviewed;      1107 AA.
AC   A0A2G5ERK2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   ORFNames=AQUCO_00500355v1 {ECO:0000313|EMBL:PIA58375.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA58375.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA58375.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC         phospholipidSide 2.; EC=7.6.2.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00034036,
CC         ECO:0000256|RuleBase:RU362033};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC       ECO:0000256|RuleBase:RU362033}.
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DR   EMBL; KZ305022; PIA58375.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5ERK2; -.
DR   STRING; 218851.A0A2G5ERK2; -.
DR   InParanoid; A0A2G5ERK2; -.
DR   OrthoDB; 275833at2759; -.
DR   Proteomes; UP000230069; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
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; IPR006539; P-type_ATPase_IV.
DR   InterPro; IPR032631; P-type_ATPase_N.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR032630; P_typ_ATPase_c.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR24092:SF19; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF08282; Hydrolase_3; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   PRINTS; PR00119; CATATPASE.
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; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362033};
KW   Magnesium {ECO:0000256|RuleBase:RU362033};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362033};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362033}.
FT   TRANSMEM        45..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        269..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        819..840
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        895..916
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        923..942
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        948..969
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        990..1011
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          6..71
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          779..1016
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          1034..1053
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1039..1053
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1107 AA;  125236 MW;  0CE7C7C5C8251733 CRC64;
     MKKRYVYIND NDLSEDLYCD NRISNRKYTF LNFLPKNLSE QFSRFMNQYF LLIACLQLWS
     LITPVNPAST WGPLLFIFAV SATKEAWDDY NRYLSDKFAN EKQVWVVKQG VKTHIQAQEV
     HVGNIVWLRE NDEVPCDLVL IGTSDPQGTC YIETAALDGE TDLKMRVIPS ACMGLVPELL
     HKIKGVIECP SPDKDIRRFD ANMRLFPPFI DNDLCPLTIN NTLLQSCYLR NTEWACGVAV
     YTGNETKLGM SRGIPEPKLT AMDAMIDKLT GAIFLFQIVV VIVLGISGNV WKDSEARKQW
     YVLYPNEGPW YELLVIPLRF ELLCSIMIPI SIKVSLDLVK SMYAKFIDWD KEMYDQQTDT
     PALAANTAIS EDLGQVEYIL TDKTGTLTEN RMIFKKCCIN GIFYGNESGD ALTDVELLNA
     VDSHNPDVIR FLTVMAICNT VIPMKRKSGT ILYKAQSQDE DALVNAAAQL HMVFLNKNAN
     VLEVNFNGVI LKYEVLDTLE FTSDRKRMSV VVKDCQNEKI FLLSKGADET ILPCASSGQQ
     IRTLTEAVEQ YAQLGLRTLC MAWRELREDE YHEWSLMFKE ANSTLVDREW KLAEVCQRLE
     HDLVILGVSA IEDRLQDGVP ETIETLRNAG INFWMLTGDK QNTAIQIALL CNFISPEPKG
     QLLLINGKTE DEVSRSLERV LLTMRITSSE PKDVAFVVDG WALEIALKHY RRAFTELAIL
     SRTAICCRVT PSQKAQLVEL LKSCDYRTLA IGDGGNDVRM IQTADIGVGI SGREGMQAAR
     AADYSIGKFR FLKRLILVHG RYSYNRTAFL SQYSFYKSLL ICFIQILFSF ISGISGTSLF
     NSVSLMAYNV FYTSIPVLAS VLDKDLSEKT VMQNPQILFY CQAGRLLNPS TFAGWFGRSL
     FHAVVVFLIS IHVYAYEKSE MEELAMVALS GCIWLQAFVV TMETNSFTVL QHLAIWGNLA
     GFYILNLIVS TLPSSGMYTI MFRLCRQPSY WITMFLIVAV GMGPVLALKY FRYTYRSSAI
     NILQQAERSG GPILSLETME PQSRPTDKDV ASLSITQPRN RNSVYEPLLS ESPTATRRSL
     GSATQFDFFQ STQSRLSTSY SRNYKNN
//

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