ID A0A5A9P493_9TELE Unreviewed; 1206 AA.
AC A0A5A9P493;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=E1301_Tti008955 {ECO:0000313|EMBL:KAA0716750.1};
OS Triplophysa tibetana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Nemacheilidae; Triplophysa.
OX NCBI_TaxID=1572043 {ECO:0000313|EMBL:KAA0716750.1, ECO:0000313|Proteomes:UP000324632};
RN [1] {ECO:0000313|EMBL:KAA0716750.1, ECO:0000313|Proteomes:UP000324632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTIB1903HZAU {ECO:0000313|EMBL:KAA0716750.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAA0716750.1};
RX PubMed=30977968;
RA Yang X., Liu H., Ma Z., Zou Y., Zou M., Mao Y., Li X., Wang H., Chen T.,
RA Wang W., Yang R.;
RT "Chromosome-level genome assembly of Triplophysa tibetana, a fish adapted
RT to the harsh high-altitude environment of the Tibetan Plateau.";
RL Mol. Ecol. Resour. 19:1027-1036(2019).
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:KAA0716750.1}.
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DR EMBL; SOYY01000009; KAA0716750.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5A9P493; -.
DR Proteomes; UP000324632; Chromosome 9.
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:SF52; PHOSPHOLIPID-TRANSPORTING ATPASE FETA; 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:UP000324632};
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 280..303
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 323..346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 955..978
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 990..1012
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1024..1046
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1067..1089
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 20..86
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 842..1096
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1152..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1206 AA; 137316 MW; E16FA55A8110B474 CRC64;
MSFFGLDWTR KKEKEVERKI RANDREYNSS FKYATNAIQT SKYNIITFLP LNLFEQFQRI
ANAYFLFLLM LQVIPAISSL SWFTTVVPLV LVLCMTAAKD AIDDIHRHRS DRQVNNRKVN
VLINGKLVSE KWMNVQVGDI IKLENNQFVT ADLLLLSSSE PLNLVYIETA ELDGETNLKV
KQSLTLTGDM TDNLEALSAF NGEVCCEPPN NRLDRFTGTL TCGTQKHSLD NERILLRGCT
IRNTDWCFGL VLFAGPETKL MQNCGKSTFK RTSIDRLMNV LVLFIFGLLA LMCIILAVGN
AIWEYKEGSK FTVFLPRDQN KAFSAFLTFW SYIIILNTVV PISLYVSMEV IRLGNSYYIN
WDRNMYHARS DTPAEARTTT LNEELGQIKY IFSDKTGTLT QNIMTFNKCS INGQCYGDVI
DHYSGQRLEI TEEMTPVDFS FNRLADSKFL FYDHSLLEAV KLESPEVHAF FRSLALCHTV
MAEEKKEGDL VYQAQSPDEG ALVTATRSFG FVFRSRSPET VTIEEMGIQR SYELLAILDF
NNVRKRMSVI VRNPEGKLTL YCKGADTLIY ERLDPSCSKL MEATTEHLNE FAGEGLRTLV
LAYKDLDEEY FSEWKQHHHE ASIALEDREE KLDKLYEEIE KDMLLIGATA VEDKLQDGVA
QTIEQLTKAE IKIWVLTGDK QETAENIGYS CNLLREEMNK VFIVAANSPK EVRQELRDAR
LKMCPTTEQD KFLIPETILG NTPKVVEDEH ANGDYGLVIN GHSLAFALES SMELEFLRTA
SMCKSVICCR VTPLQKAQVV ELVKKHKKAV TLAIGDGAND VSMIKAAHIG VGISGQEGMQ
AVLSSDFSFA QFRFLQRLLL VHGRWSYLRM CKFLRYFFYK NFTFTFVHFW YAFFCGFSAQ
TVYDEGFITL YNLVYTALPV LGLSLFDQDV NAGWSLEFPQ LYVPGQLSMY FSKRAFMMCA
LHSCYSSLVI FFVPYVALYD TARSDGRDGV DYQSFALITQ TCLTVTVFFQ LSLDLSYWTV
VNHLFVWGSL GMFFILTFTM YTDGLFRIHP PSFAFIGTAR NCLNQSSVWL TVALTAVLCV
LPVLAYRYLC SQISPTINDK VRYKVHQTKE PAPRPRRTKL IRRSTRRSGY AFSHAQGYGD
LVTSRRFLWR PQPARSTGVT PTGRSPGFKP TGRSAGYSPA GREQNPKQKV EPTSLQMFRA
VKDSSF
//
