UniProt: A0A6G0YJF7

Database: UniProt
Entry: A0A6G0YJF7_APHCR

LinkDB:  A0A6G0YJF7_APHCR 
Original site:  A0A6G0YJF7_APHCR

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (1)   
All databases (24)   

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ID   A0A6G0YJF7_APHCR        Unreviewed;      1216 AA.
AC   A0A6G0YJF7;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   ORFNames=FWK35_00020531 {ECO:0000313|EMBL:KAF0757190.1};
OS   Aphis craccivora (Cowpea aphid).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aphidomorpha;
OC   Aphidoidea; Aphididae; Aphidini; Aphis; Aphis.
OX   NCBI_TaxID=307492 {ECO:0000313|EMBL:KAF0757190.1, ECO:0000313|Proteomes:UP000478052};
RN   [1] {ECO:0000313|EMBL:KAF0757190.1, ECO:0000313|Proteomes:UP000478052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=180601 {ECO:0000313|EMBL:KAF0757190.1};
RC   TISSUE=Whole Body {ECO:0000313|EMBL:KAF0757190.1};
RA   Voronova N.V., Shulinski R.S., Bandarenka Y.V., Zhorov D.G., Warner D.;
RT   "Whole genome of Aphis craccivora.";
RL   Submitted (AUG-2019) 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}.
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:KAF0757190.1}.
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DR   EMBL; VUJU01003651; KAF0757190.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6G0YJF7; -.
DR   Proteomes; UP000478052; 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   CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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:SF150; 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; 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:UP000478052};
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        274..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        323..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        927..949
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        955..976
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1006..1030
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1042..1063
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1070..1090
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1110..1133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          20..85
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          893..1132
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1216 AA;  138814 MW;  FEE28327FA8C99C9 CRC64;
     MSEARIEEKF LDDLEKERFI KANDSTYNAQ FNYATNYIKT SKYTLLTFLP LNLFEQFQRL
     ANFYFLCLMM LQMISIISSL TPITTSIPLI GVLTISAIKD AYDDYQRHVS DDQVNNRISK
     TVRNGHVVNV KWKDVHVGDV ILMEDGQFVA ADVLLLSTSE PSGLCFIETA ELDGETNLKC
     RQCLAEVADL AHEVTDFDGF IRCEAPNNLL NKFHGILQWN GKELILNNDH IILRGCVLRN
     TEWCYGMVIF AGRDTKLMQN SGKSKFKRTN IDRLLNFLII GIVLFLFLLC LSCMIGSVIW
     EYKTGWHFQT YLPWDSLVPS DRIAGSITIG TLVFFSYAIV LNTLVPISLY VSVEVVRFVQ
     SFFINWDEKM YDKQSGTSAK ARTTSLNEEL GQIQYIFSDK TGTMTKNIMT FKKCSINGIV
     YGDLSEIHYG KSEDVIKTYM DKQTPSAVIR SYNNINYNKI DQGVRRVTIN STLHLVGPPP
     VDFSWNPQYE SDFLWYDQSL VDAARQLNND TENTVVTFFE ILALCHTVMP SWKNGILKYQ
     AQSPDESALV SAARNFGIVF IERTPNSVTI EIMGKIKVYE LLCILDFNNT RRRMSVVFRE
     NNKIRLYCKG ADSVIFNRLE PGNDEYKATT LQNLNEFAGD GLRTLCCAVR DIDDEFFESW
     KHKYMDAAAA RTDREEKLDN VYDEIETHLR LIGITAIEDK LQDAVPKTIS NLLMAGIYIW
     MLTGDKQETA INIGYSCQLL NDEMELWIVD GHTQDQVEHQ LDQCNNSLLG ISEHNRSERN
     SMATSIVRFS EPEDVQTEEN EERMFALVIN GHSLVHALHT ELEYKFVELC TKCKAVICCR
     VTPLQKAMVV QLIKKYKNAV TLAIGDGAND VSMIKEAHIG VGITGQEGNQ ATLASDYSLG
     QFRFLERLLL VHGRWSYYRM CKFLRYFFYK NVAFTLCHIW FGFFCGFSAQ TIFDPFYISV
     YNMFYTALPV LAIGALDQDV NDSKSIMYPK LYTPGLKNMF FNTKEFFKCA ALGTYASLVI
     FFVPYGAYFY GMTSSGLNVL DHMYMAEVVA MILVTAMTVQ VAFDTSYWTV INHIVIWGSL
     TLFFVAEWVY NYLIGGAYVG SLAMAMKQPT FWLVTLLVVV VIVSPVVAWR LYFLETSPVL
     TDKLRLKQLK QMRQVSGTDT RMPSIKHKRR SIRSGYAFAH QEGFGRLITS GKIMRTPRNS
     EGFIDRKNSN ISDTTV
//

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