ID H0V6U4_CAVPO Unreviewed; 1220 AA.
AC H0V6U4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000005431.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000005431.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000005431.3};
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 EMBL; AAKN02030427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0V6U4; -.
DR STRING; 10141.ENSCPOP00000005431; -.
DR Ensembl; ENSCPOT00000006081.3; ENSCPOP00000005431.3; ENSCPOG00000006017.4.
DR VEuPathDB; HostDB:ENSCPOG00000006017; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000161917; -.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; H0V6U4; -.
DR OMA; WSYFIVL; -.
DR TreeFam; TF300654; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000006017; Expressed in testis and 8 other cell types or tissues.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140345; F:phosphatidylcholine flippase activity; IEA:Ensembl.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:Ensembl.
DR GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
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; 1.
DR PANTHER; PTHR24092:SF52; PHOSPHOLIPID-TRANSPORTING ATPASE FETA; 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|ARBA:ARBA00022840, 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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
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 44..61
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 67..85
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 264..290
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 317..338
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 857..878
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 890..910
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 943..961
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 976..996
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1008..1025
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1052..1073
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 8..73
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 828..1079
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1165..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1220 AA; 138612 MW; 08987990288BC981 CRC64;
SENERLLQAN NRELTSSFGY PDNAIKTSKY NALNFLPMNL FEQFRKLANA YFLVLVFLQM
IPQISSLASY TTVIPLMVVL SITAVKDAID DLKRHQSDHQ VNNRSVLLLV DGRMEEDKWM
NVQVGDIIKL KNNECVTADI LLLSSSESHG LAYVETAELD GETNLKVKQA LSVTNDLEDN
LELLSTFDGE IKCDLPNNKL DRFTGILTYK GQKYLLDHDK LLLRGCILRN TDWCYGVVVY
TGPDTKLMQN SGKAIFKRTQ MDQLLNVLVL WIFLLLAIMC FIIAVGHGIW QSKIGYYFQI
FLPWENYVSS SVVSATLIYW SYIIILNTMV PISLYISVEI IRLGNSFYIN WDRKMFYAPK
NTPAQARTTT LNEELGQVKY VFSDKTGTLT QNIMTFNRCS INGKVYGMHN CHKRLIKKYK
KVDFSYNKLA NPNFLFYDNT LVEAVKSGDK WVHLFFLSLS LCHTVMSEEK VEGELVYQAQ
SPDEGALVTA ARNFGFVFRA RTSDTITMVE MGETKVYQLL AILDFSNVRK RMSVIVRTPE
DQLLLFCKGA DTIICELLHS SCKDLTNVTM EHLDDFATEG LRTLMVAYRE LDVTFFQAWR
HKHSVAYLSL EDRENKLSIV YEEIEKDLML LGATAIEDKL QDAVPETIIT LSKAKIKIWV
LTGDKQETAV NIAYSCSIFE EDMDGVFMVQ GNNYETICQE LRTARAKMKP ESVLESDPTN
ICLPMKPKIV PDEVPKGRYG LVINGYSLAC ALEENLELEL LQVACMCKGV ICCRMTPLQK
AQVVQLVKRY KKVVTLAIGD GANDVSMIKA AHIGVGISGL EGMQAMLNSD FSFSQFHYLQ
RLLLVHGRWT YNRMCKFLSF FFYKNFVFTL VHFWYAFYNG FSAQTVYDSW FIACYNLIYT
SLPVLGLSLF DQDVNETWSL CFPELYEAGQ HNLSFNKKKF MDCVLHGIYS SFVLFFVPMW
TICSSECSDG KDISDFQTFS LIVQTSLMCV VTMQIALKTT YWTVMSHLLI WGSLGFYFCM
LFLLYSDGLC LMFPNIFQFL GVARNSLSET QLWLSVVLST VLCVIPTVGY IFIKPLLFPV
SVDKVGARQL PRIRHCMKYP VPPPKRARLK RPSFRRSAYA FSHQQGFGAI ITSGKMTKLR
SKKKDKLLRK SHLMLVSHHR FQASSQTSNV EGVERDSVGL PPARGRVSSC PARLPGLSGS
FQGVTCEALV GRGGSRGERA
//
