ID A0A5E4C8Y3_MARMO Unreviewed; 868 AA.
AC A0A5E4C8Y3;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=MONAX_5E019028 {ECO:0000313|EMBL:VTJ78298.1};
OS Marmota monax (Woodchuck).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Marmota.
OX NCBI_TaxID=9995 {ECO:0000313|EMBL:VTJ78298.1, ECO:0000313|Proteomes:UP000335636};
RN [1] {ECO:0000313|EMBL:VTJ78298.1, ECO:0000313|Proteomes:UP000335636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (APR-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 -!- 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; CABDUW010001059; VTJ78298.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5E4C8Y3; -.
DR Proteomes; UP000335636; 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; 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; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
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:SF57; PHOSPHOLIPID-TRANSPORTING ATPASE IF; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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:UP000335636};
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 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 53..74
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 676..698
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 710..734
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 746..769
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 775..801
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 562..815
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 868 AA; 99507 MW; 28CD04559993D0C6 CRC64;
MNTFLIIYLI ILISEAIIST ILKYTWQAEE KWDEPWYNQK TEHQRNSSKI LRFISDFLAF
LVLYNFIIPI SLYVTVEMQK FLGSFFIGWD LDLYHEESDQ KAQVNTSDLN EELGQVEYVF
TDKTGTLTEN EMQFRECSIN GMKYQEINGR LVPEGPTPDS SEGNLTYLNS LSHLNNLSHL
TTSSSFRTSP ENETELIKEH NLFFKAVSLC HTVQISNVHT DGIGDGPWQS NLAPSQLEYY
ASSPDEKALV EAAARIGIVF IGNSEETMEV KILGKLERYK LLHILEFDSD RRRMSVIVQA
PSGEKLLFAK GAESSILPKC IGGEIEKTRI HVDEFALKGL RTLCIAFRQF TSKEYEEIDR
RLFEARTALQ QREEKLANVF QFIEKDLILL GATAVEDRLQ DKVRETIEAL RMAGIKVWVL
TGDKHETAVS VSLSCGHFHR TMNILELINQ KSDNECAEQL RQLARRITED HVIQHGLVVD
GTSLSLALRE HEKLFMEVCR NCSAVLCCRM APLQKAKVIR LIKISPEKPI TLAVGDGAND
VSMIQEAHVG IGIMGKEGRQ AARNSDYAIA RFKFLSKLLF VHGHFYYIRI ATLVQYFFYK
NVCFITPQFL YQFYCLFSQQ TLYDSVYLTL YNICFTSLPI LIYSLLEQHI DPHVLQNKPT
LYRDISKNSL LSIKTFLYWT ILGFTHAFIF FFGSYFLMGK DISLLGNGQM FGNWTFGTLV
FTVMVITVTV KMALETHFWT WINHLVTWGS IIFYFVFSLF YGGILWPFLG SQNMYFVFIQ
LLSSGSAWFA IILMVVTCLF LDVVKKVFDR QLHPTSTEKA QLTETNSSIK CLDSMCCFPE
GETACASVRR MLERVIGRCS PTHISRSW
//
