ID A0A672J3B2_SALFA Unreviewed; 1151 AA.
AC A0A672J3B2;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:ENSSFAP00005047530.1};
OS Salarias fasciatus (Jewelled blenny) (Blennius fasciatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Blenniimorphae; Blenniiformes; Blennioidei; Blenniidae;
OC Salariinae; Salarias.
OX NCBI_TaxID=181472 {ECO:0000313|Ensembl:ENSSFAP00005047530.1, ECO:0000313|Proteomes:UP000472267};
RN [1] {ECO:0000313|Ensembl:ENSSFAP00005047530.1}
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 AlphaFoldDB; A0A672J3B2; -.
DR Ensembl; ENSSFAT00005049129.1; ENSSFAP00005047530.1; ENSSFAG00005019661.1.
DR InParanoid; A0A672J3B2; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000472267; Unplaced.
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: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; 1.
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:UP000472267};
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 285..308
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 339..358
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 926..946
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 976..998
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1013..1032
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1044..1065
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1085..1107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 37..91
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 862..1109
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1151 AA; 131354 MW; 4A9362E6D3754DCF CRC64;
MLRRRLNRLL GGDERRVDSR TIYVGHRSCP ANEAFIPPKF CDNRIVSSKY TVWNFLPKNL
FEQFRRIANF YFLIIFLVQV IVDTPTSPVT SGLPLFFVIT VTAIKQGYED WLRHKADNEV
NKCPVTVLED GRRMQKESEK IKVGDVLEVE EDETFPCDLI LLQSSRDDDT CFVTTASLDG
ESNHKTHYTV PDTEKDLESL NATIECEQPQ PDLYKFVGRM HIYKSNQEPA VRSLGPENLL
LKGATLKNTQ KICGVAVYTG METKMALNYQ GKSQKRSAVE KSINAFLLVY LCILVSKALV
CTVLKYVWQS KPGQDEPWYN EKTQREKDTN MYLKMFTDFL SFMVLFNFII PVSMYVTVEM
QKFLGSFFIT WDKDFYDPEI EEGALVNTSD LNEELGQVEY VFTDKTGTLT QNNMEFIECC
IDGFQYKYRD ASSELDGFCA TDGPVSKLQQ KAGREREELF LRALCLCHTV QVKESTEQGQ
SQVDGQITQI DGLVGDGDAS HRPQEQRGFI ASSPDEVALV KGAMRYGFTF LGLESKTMKI
LNRSNDVEIY ELLHVLNFDP VRRRMSVIVR TKSGDTLLFC KGADSSIFPR VRQEEVERIR
LHVERNATEG YRTLCVAYKH LSAEEYAQAD EGLKEARLAL QDREEKLMAV YNQVETGMSL
IGATAVEDRL QEEAAETMEA LQGAGINVWV LTGDKMETAK STCYACRLFQ RNTELLELTV
RTLEDGGRRR EERLHELLLE YHKKAVQDAP PAKGGVTRSW SVANQDYGFI IDGATLSMVL
NSSTESNSSR YKNLFLQICQ NCTAVLCCRM APLQKAQIVK MVKNSKGSPI TLSIGDGAND
VSMILEAHVG IGIKGKEGRQ AVRNSDYAIP KLKHLKKLLL AHGHLYYVRI AHLVQYFFYK
NLCFILPQFL YQFFCGYSQQ PLYDAAYLTM YNICFTSMPI LAYSLLEQHI CMEVLLDNAT
LYREIAKNAM LRWGPFLYWT LLGVFHGLLF FFGVRFLFSN SALQDNGQVF GNWSYGTIVF
TVLVFTVTLK LALDTRHWTW INHFVIWGSL AFYVFFSFFW GGIIWPFLRQ QRLYFVFANM
LSSVTAWLVI ILLIVLSLLP EILLVVFRKP RGPHARQKKL VQSSVGGLQS PRSSARPLLM
RTFSDESNTV I
//
