ID H2YBK4_CIOSA Unreviewed; 1195 AA.
AC H2YBK4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS Ciona savignyi (Pacific transparent sea squirt).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000002702.1, ECO:0000313|Proteomes:UP000007875};
RN [1] {ECO:0000313|Proteomes:UP000007875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000002702.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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 AlphaFoldDB; H2YBK4; -.
DR Ensembl; ENSCSAVT00000002744.1; ENSCSAVP00000002702.1; ENSCSAVG00000001592.1.
DR GeneTree; ENSGT00940000167226; -.
DR Proteomes; UP000007875; 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; 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; 2.
DR PANTHER; PTHR24092:SF150; 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 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:UP000007875};
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 43..60
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 66..84
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 267..289
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 318..340
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 916..937
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 949..969
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 998..1018
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1038..1056
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1068..1091
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1111..1137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 6..72
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 885..1139
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1195 AA; 135793 MW; 9232B3F845D3451E CRC64;
EKQRDIKAND SEYNGTFNYA VNKIKTSKYT WYNFLLINLW EQFHRVVNVY FVILVVLQFI
PEISSLNPTT SIIPIIVVLG LTAMKDGFYD YKRHKSDSSV NNRSSSVVKD ETLTEEKWMN
IKVGDIIQLK NNENVTADLL LLSSSEEHNL VYIETAELDG ETNLKVRQAL PETGEMKDNL
RTLRQFNGHV KCEAPNNYLH KFTGNLYWNN ETFAIDNENI LLRGCTLRNT EWCFGLVIFA
GPDTKLMQNT GKSVLKRTSI ERLMNKLVWL IFAFLLLLAT VTAVGNTIWE RYVGVHFQVY
MPWASYAPNE YMSGFLMFWS YIIILNTVVP ISLFVSIEFI RVGQSWFINF DRAMYYEKKD
LPALARTTTL NEELGQIEYV FSDKTGTLTQ NIMEFNKCVI GGTCYGEVYN EDGIAIVPDD
VNFKINNKTY LFGLIPSCKL FLIKFLPFLT KSTPNADFSF NKDAENSFRF FDQRLINAIT
SGDTKVHEFF KLIAICHTVM PDFSPEGILT YQAQSPDEGA LVGAARNFGF VFKERTFNTI
TVSELGTDVT YEVLAILDFD NVRKRMSVIV KDPEGNITLF CKGADSVIYE RLGEATDEDI
KNATTVHLDN FAGEGLRTLC LAVKRLNEES YKVWKEAHSK ASMALEDRED RLSAVYEEIE
RDMELLGATA VEDKLQDGVP ETIANLSNAN IKIWVLTGDK QETAVNIGYS CNMLTEEMKN
VFIISGYTFE EQAYEDMQCE DSPRSVLSSR DDLTPVCNTL AGFILQSCFL LKLNVVVHTS
KVANGRSIVF QQDGENKFGL VINGHSLVHA LSEELAIKFL ELATLCTAVI CCRVTPLQKA
KVVELVKQNQ KAVTLAIGDG ANDVSMIKAA HIGVGISGEE GTQAVLSADF AFGQFRFLER
LLLVHGRWSY MRICKFFGYF FYKNFAFTLV HFWYSFFNGL TAQSSFDDWF VTLYNLVYTS
MPVFMLAVFD QDLNDEYCIK FPKLYLPGQT NELFNIKIFF RSIIRGIFTS LALFFIPYGA
FVDGMHSDGT NITDLQTLSI VISTSLIIVV TLQVALDTSY WTPINHFFIW GSIGIYFLVT
FAMYSNGLYQ ILPNNFPFVG VARTAFQFPS LWFTVLLVSA ICFLPVVASR YLTSLLWPTY
TEKVKRKMKA AESLHAMSEK IKSKFQIKRR GSRARSGYAF SHERGFGDLI TTGRM
//
