ID A0A452E0K6_CAPHI Unreviewed; 1109 AA.
AC A0A452E0K6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP11C {ECO:0000313|Ensembl:ENSCHIP00000005610.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000005610.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000005610.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_017899694.1; XM_018044205.1.
DR AlphaFoldDB; A0A452E0K6; -.
DR Ensembl; ENSCHIT00000013305.1; ENSCHIP00000005610.1; ENSCHIG00000009648.1.
DR GeneID; 102175374; -.
DR CTD; 286410; -.
DR GeneTree; ENSGT00940000158878; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
DR Bgee; ENSCHIG00000009648; Expressed in liver and 17 other cell types or tissues.
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; 3.
DR PANTHER; PTHR24092:SF38; PHOSPHOLIPID-TRANSPORTING ATPASE IG; 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; 2.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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:UP000291000};
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 64..82
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 290..313
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 344..363
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 885..906
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 936..958
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 970..992
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1004..1028
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1034..1058
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 36..91
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 843..880
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT DOMAIN 881..1069
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1109 AA; 127225 MW; C295FBC2F90E27C6 CRC64;
MFRRSFNRFC AGEEKRVGTR TVFVGNHPVS ETEAYIAQKF CDNRIISSKY TLWNFLPKNL
FEQFRRIANF YFLIIFLIQV TVDTPTSPIT SGLPLFFVIT VTAIKQGYED WLRHRADNEV
NKSTVYIIEN AKRVKKESEK IKVGDIVEVQ ADETFPCDLI LLSSCTVDGT CYVTTASLDG
ESNCKTHYAV RDTIELRTVE SIDNLRAAIE CEQPQSDLYK FVGRINIYSN SLEAVARSLG
PENLLLKGAT LKNTKKIYGV AVYTGMETKM ALNYQGKSQK RSAVEKSINA FLIVYLFILL
TKAAICTTLK YVWQSTPYND EPWYNQKTQK ERETWKVLKM FTDFLSFMVL FNFIIPVSMY
VTVEMQKFLG SFFISWDNDF YDEEINEGAL VNTSDLNEEL GQVDYVFTDK TGTLTENSME
FIECCIDGHK YKGVAQETDG LSQTDGPLPY LDRADKNREE LFLRALCLCH TVEVKPNDTV
DGVTESSELT YMSSSPDEIA LVKGAKKYGF TFVGVQNGYM RVENQRKEIE EYELLHTLNF
DSVRRRMSVI VKTQSGDILL FCKGADSAVF PRVQNHEIDL IKVHVEHNAM EGYRTLCIAF
KEIAPDDYER VNRQLIEAKM ALQDREEKME KVFDEIETDM HLIGATAVED KLQDQAAETI
EALHAAGLKV WVLTGDKMET AKSTCYACRL FQTNTELLEL TTKTIEESER KEDRLHELLT
EYRKKLLREF PKSTRSLKKA WTEHQEYGLI IDGSTLSLIL NSSQDSGSNN YKSIFLQICM
KCTAVLCCRM APLQKAQIVR MVKNLKGSPI TLSIGDGAND VSMILESHVG IGIKGKEGRQ
ASRNSDYAVP KFKHLKKLLL AHGHLYYVRI AHLVQYFFYK PLYDAAYLTM YNICFTSLPI
LAYSLLEQHI NIDTLTSDPR LYMKISGNAM LQLGPFLYWT FLAAFEGTVF FFGTYFLFQT
TSLDENGKVY GNWTFGTIIF TILVFTVTLK LALDTRFWTW INHLVIWGSL AFYVFFSFFW
GGIIWPFLKQ QRMYFIFAQM LSSVSIWLTI ILLIFVSLSP EMLRIVLRSV RRRSTRSNLS
CKKASDSLST RPSVRPLLLR TFSDESNIF
//