ID A0A315VKE5_GAMAF Unreviewed; 1312 AA.
AC A0A315VKE5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=CCH79_00005993 {ECO:0000313|EMBL:PWA23561.1};
OS Gambusia affinis (Western mosquitofish) (Heterandria affinis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Gambusia.
OX NCBI_TaxID=33528 {ECO:0000313|EMBL:PWA23561.1, ECO:0000313|Proteomes:UP000250572};
RN [1] {ECO:0000313|EMBL:PWA23561.1, ECO:0000313|Proteomes:UP000250572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NE01/NJP1002.9 {ECO:0000313|EMBL:PWA23561.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PWA23561.1};
RX PubMed=29703783;
RA Hoffberg S.L., Troendle N.J., Glenn T.C., Mahmud O., Louha S., Chalopin D.,
RA Bennetzen J.L., Mauricio R.;
RT "A High-Quality Reference Genome for the Invasive Mosquitofish Gambusia
RT affinis Using a Chicago Library.";
RL G3 (Bethesda) 8:1855-1861(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWA23561.1}.
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DR EMBL; NHOQ01001578; PWA23561.1; -; Genomic_DNA.
DR STRING; 33528.ENSGAFP00000011290; -.
DR Proteomes; UP000250572; 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 CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF79; PHOSPHOLIPID-TRANSPORTING ATPASE VB; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_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:UP000250572};
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 73..91
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 97..115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 293..318
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 345..367
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1035..1059
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1097..1121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1127..1150
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1157..1182
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1202..1221
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 42..97
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 986..1230
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 476..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1312 AA; 148593 MW; 7A062EBE1094D164 CRC64;
MTWRSPLALV RDALEGQRAR ERELRSLVSN LTYEGLEKSK QPNRFFLSNA IKTTKYSLLL
FLPMNLYEQF HRLANLYFVG IAILNFIPVV NAFQPEVALI PICVIMLLTA LKDGWEDFRR
YQSDRKVNNT PCFIYSRRDE QYVERRWKDV RVGDFVRVVS NEIVPADLLL LYSSEPNGVC
HIETANLDGE TNLKQRTVVS GLRAANLGFE PESFNSVVVC ERPNNNLNHF KCFVEKPDKD
KVGANIESLL LRGCTVRNTN HAVGFVVYAG HETKSMLNSS GSRYKRSKLE RKLNVDVFFC
LLLLFTMCLI GALGHYLWLE SLPGVPSFLV PDSSGHLDVP SLESFYMFFT MIILLQILIP
ISLYVSVELV KVGQIFFITN DIDLYDEETD SRVQCRALNI TEDLGQIEYI FSDKTGTLTE
NKMVFRRCSV MGTEYPHKKN AIRLDVIDEP ESEEEVIFNQ HQQLPRTRWS LEAEGISPAD
TQLHGRRRKS KVAANAQSDA AFSSPLETEV IPDQKLLQQI SRAESSGGRR DGNRNFDPHL
DFFLALAICN TVVVSLENAH RHGECTSPHS SQTIDPLETF SNLVKKAGAF FQRNKRNRTR
SEDPVIDSAK TENEADTNRL RTCSLHPPSQ NGSTIVEAEE LCYEAESPDE AALVYAARAY
GFILLARTPD SVTVRLPSGE DLVFEVLDTL TFDSNRKRMS VLVRHPVTKD YVLYTKGADY
SIMELLGTPY AENFSGIEKS IAADTQYHLD CYAKDGLRTL CIAKKVVSES TYQSWLGERK
RAQAAMECRE ELIMRTAVQL ETNLTLLGAT GIEDRLQENV PDSILALREA GIHVWVLTGD
KPETAVNIGY ACRLLEEEDL VINMSCKNKV TCTSILDCTL EEVRRYGDDP RNVGTTQNIS
LVIDGNTLDM AMSPDLQERF MELTKHCRSV LCCRVTPLQK SAVVRLVRDK LKVMTLAVGD
GANDVNMIQA ADVGIGISGQ EGMQAVNASD FAISRFKHLK KLVLVHGHWC YTRLANMIIY
FFYKNVAYVN LLFWYQFFCG FTATTMIDYW LLIFFNLFFT STPPIMFGIF DKDASVEVLQ
GVPELYRTGQ GKGEYNFLTF WISILDAFYQ SLVCFFIPYL AYQDSDIDIF TFGMPLNTAA
LFTILLHLAI EIKSWTLVHW VIMLGSVALY FIVVLAYTAV CVTCNPPSNP YWILQGQMAD
PMFYLIVTLC TVVALLPRYT FHVLKNSVAP SPLLQGRQLD RMDPATRDQW IKEWRGFRGG
APAKRYELPD PPSPTLETPV DIFPDFLPDS DFMGDDLSLN VITESRQRAV HT
//
