ID A0A672J2S1_SALFA Unreviewed; 1102 AA.
AC A0A672J2S1;
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:ENSSFAP00005047604.1};
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:ENSSFAP00005047604.1, ECO:0000313|Proteomes:UP000472267};
RN [1] {ECO:0000313|Ensembl:ENSSFAP00005047604.1}
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; A0A672J2S1; -.
DR Ensembl; ENSSFAT00005049203.1; ENSSFAP00005047604.1; ENSSFAG00005019661.1.
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; 1.
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; 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: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 68..87
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 93..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 287..310
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 341..360
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 866..884
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 896..916
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 946..968
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 983..1002
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1014..1035
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1055..1077
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 37..88
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 832..1079
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1102 AA; 126492 MW; 02E0803C7DA33F53 CRC64;
MLRRRLNRLL GGDERRVDSR TIYVGHRSCP ANEAFIPPKF CDNRIVSSKY TVWNFLPKNL
FEQFRRIANF YFLIIFLVQV RTTLYPTNSP DSIFVFFLLI SVCLALLQGY EDWLRHKADN
EVNKCPVTVL EDGRRMQKES EKIKVGDVLE VEEDETFPCD LILLQSSRDD DTCFVTTASL
DGESNHKTHY TVPDTEKDLE SLNATIECEQ PQPDLYKFVG RMHIYKSNQE PAVRSLGPEN
LLLKGATLKN TQKICGVAVY TGMETKMALN YQGKSQKRSA VEKSINAFLL VYLCILVSKA
LVCTVLKYVW QSKPGQDEPW YNEKTQREKD TNMYLKMFTD FLSFMVLFNF IIPVSMYVTV
EMQKFLGSFF ITWDKDFYDP EIEEGALVNT SDLNEELGQV EYVFTDKTGT LTQNNMEFIE
CCIDGFQYKY RDASSELDGF CATDGPVSKL QQKAGREREE LFLRALCLCH TVQVKESTEQ
GQSQQRGFIA SSPDEVALVK GAMRYGFTFL GLESKTMKIL NRSNDVEIYE LLHVLNFDPV
RRRMSVIVRT KSGDTLLFCK GADSSIFPRV RQEEVERIRL HVERNATGYR TLCVAYKHLS
AEEYAQADEG LKEARLALQD REEKLMAVYN QVETGMSLIG ATAVEDRLQE EAAETMEALQ
GAGINVWVLT GDKMETAKST CYACRLFQRN TELLELTVRT LEDGGRRREE RLHELLLEYH
KKAVQDAPSW 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
RGPHARQVGP RLYSHSFSVH SL
//
