ID A0A118JV91_CYNCS Unreviewed; 1168 AA.
AC A0A118JV91;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=Ccrd_005797 {ECO:0000313|EMBL:KVH92170.1};
OS Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=59895 {ECO:0000313|EMBL:KVH92170.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVH92170.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVH92170.1};
RX PubMed=26786968; DOI=10.1038/srep19427;
RA Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT "The genome sequence of the outbreeding globe artichoke constructed de novo
RT incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL Sci. Rep. 6:19427-19427(2016).
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:KVH92170.1}.
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DR EMBL; LEKV01004840; KVH92170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A118JV91; -.
DR STRING; 59895.A0A118JV91; -.
DR EnsemblPlants; KVH92170; KVH92170; Ccrd_005797.
DR Gramene; KVH92170; KVH92170; Ccrd_005797.
DR OMA; CDRPDTN; -.
DR Proteomes; UP000243975; 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; 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; 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 NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF91; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
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:UP000243975};
KW Translocase {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 364..386
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 421..442
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 897..917
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 938..959
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 965..982
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1011..1035
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1047..1067
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1079..1102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1108..1128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 104..170
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 898..1137
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1168 AA; 131611 MW; FA82E02195F3EB6A CRC64;
MASNRPLPGP FFRSPISAGP DLSSPTSSKN SDGSQIVNLH PQQRPDTLQN STSQQSISSN
SWRANSVNFG SKGVHYGSRG GAGSEGFSMS MSRREINDED ARLVYVNDPL KTNERFEFAG
NSIRTGKYSV LTFLPRNLFE QFHRVAYMYF LVIAILNQLP QLAVFGRGAS ILPLASVLLV
TAVKDAYEDW RRHRSDRIEN NRMSSVLMND RFQEKKWKDI QVGEVIKILA NETMPCDIVL
LSTSDPTGVA YVQTINLDGE SNLKTRYAKQ ETLPRIPEKD MISGLINCEK PNRNIYGFQA
NMEIDGKRVS LGPSNIVLRG CVLKNTDWAV GVAVYAGRET KAMLNNSGAP SKRSRLETHM
NREIILLSSF LVVLCTIVSA CAGVWLRRHR DELDIMPFYR RKDYSKQEVE NYKYYGWGME
IFFSFLMSVI VFQIMIPISL YISMELVRVG QAYFMIRDDK MFDATSNTRF QCRALNINED
LGQIKYIFSD KTGTLTENKM EFQFASISGV NYSGEKTEFL GEEGGYSIQV EGQVWRPKMK
VQVDRELLQL SQTRNDTKSK EIYDFFLALA ACNTIVPIVV NTSDPTEKLI DYQGESPDEQ
ALVYAAAAYG FMLIERTSGH IVIDIQGERQ RFNVLGMHEF DSDRKRMSVI LGYPDSTVKV
FVKGADTTMF KIIDKSLNLD VVKATETHLH SYSSIGLRTL VVGMRGLSIS EFEQWQSSYE
IASTALMGRA GLLRKVAINL ENNLSLLGAS AIEDRLQKGV PEAIESLRTA SIKVWVLTGD
KQETAISIGY SSKLLTSKMV QIIINNNSKV SCRKSLEDAL ITSRKLINVT RASDDDASSV
ALIIDGTSLV YILDSELEEQ LFELASKCAV VLCANDVSMI QMADVGVGLS GQEGRQAVMA
SDFAMGQFRF LVPLLLVHGH WNYQRMGYMI LYNFYRNALF VLVLFWYVLF TGFTLTTAIT
EWSSVLYSII YTAIPTIVIG ILDKDLSRRS LMTYPQLYGA GQRQESYNAK LFWLTMADML
WQSVVAFFIP LFAYWKSEID SSSIGDLWTL AVVFMVNIHL AMDVIRWTWI SHASIWGSII
ATCICVIVID AVPVLPGYWA IFNLASSGLF WICLLGILVT AMIPRFVIKM FMQHCKPCDI
QIAREAEKFS NRMESTRNGE IEMNPPQR
//
