ID A0A452GK59_9SAUR Unreviewed; 1490 AA.
AC A0A452GK59;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000002108.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000002108.1}
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 Ensembl; ENSGAGT00000002398.1; ENSGAGP00000002108.1; ENSGAGG00000000613.1.
DR Proteomes; UP000291020; 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; 2.
DR PANTHER; PTHR24092:SF81; PHOSPHOLIPID-TRANSPORTING ATPASE VA; 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:UP000291020};
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 72..90
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 96..114
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 294..317
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 337..359
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1071..1091
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1103..1123
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1153..1176
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1182..1203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1210..1230
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1250..1269
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 42..95
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1039..1281
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1490 AA; 168566 MW; 86696D6C9FC82C5F CRC64;
RVRESEGKKK LSPPKHRRRR KRTRTVRSNL LLPGPEAEKP QRSPMANNRL KTTKYTALSF
LPKNLFEQFH RLANVYFVFI ALLNFVPAVN AFQPELALAP VLFILAVTAI KDLWEDYSRY
RSDNEINHTE CLVYCRNEKK YMNRYWKEVE VGDFVQLRCN EIIPADILLL SSSDPDGLCH
IETANLDGET NLKQRQVVRR FLELDSEFDP LKFTSVIECE KPNNDLSRFR GYIVHTSGKR
DGLYKENLLL RGCTVRNTEE VAGIVIYAGH ETKALLNNSG PRYKRSKLER QMNIDVLWCV
LILIVMCLFS TIGHGLWVWQ YGEKKPVFDV PGLDGNYLSP VLAAVYIFLT MIIVFQVLIP
ISLYVSIEIV KACQVFFIHQ DKDLYDEETD SQLQCRALNI TEDLGQMQYI FSDKTGTLTE
NKMVFRRCTV SGIEYSHDAN ARRLAMYQEA DSEEEETAAK GGTLSQRNSV SSHQSIKVVH
RSLSMKSHRR TGSRAEAKRA SILSKHTAFS SPMEKDITPD PNLLEKVNEC ARSLEVTRSH
EQPLSKLTPE LSDIFDFFIA LTICNTVVVT SPDQPRQKVR VRFELKSPVK TIEDFIRRFT
PSRLTSGSNS SSSSSLTTSK SMPRLGSSIL SSVSSESTLL KLEEKLAHSP QMNNNDYRSQ
QDRRAIGCRP EEGELRYEAE SPDEAALVYA ARAYNCALVG RLSDQVSVEL PHLGRLTFEL
LHTLGFDSIR KRMSVVVRHP LTDEISVYTK GADSVIMDLL LPCSSDDPRG NHQKKIQSKT
QNYLNLYAVD GLRTLCIAKR VLSKEEYASW LKSHLEAESS IENREELLFQ SALRIETNLH
LLGATGVEDR LQDGVPETIA NLRKAGLQIW ILTGDKQETA INIAYACKLL GHDEEIITLN
AESLETSATL LDHCLQYIES KFSNNTIDKT AGNTTVGFCP LSPPSSSVHS SLGLVIDGKT
LAYALDKTLE DKFLSLARRC RSVLCCRSTP LQKSMVVKLV RDKLKAMTLA IGDGANDVSM
IQVADVGVGI SGPEGMQAVM ASDFAVPRFR HLEKLLLVHG HWCYSRLANM VLYFFYKNAM
FVALLFWYQF YCGFSGSSMI DQWYLIFFNV LFSSLPQLVT GVLDKDIPAE VLIGVPHLYK
SGQKMEEYQP HMFWMNMIDA LYQSLVCFYI PFFTYYDSEV DLFSWGTPIT VIALFTIILH
LAIETKTWTL FHWSSCIFSI LLFFIVALVY NVSCPICYPP SNPYWTMEKL MGEPVFYLIC
IISPVVALLP RYSILFLYRT LQGTIFPTQL QLGRQLNRLP PETHSQILNR LNIKKETIPQ
KPPCAEHSPQ NPLSNDSDCF KACNHTPSLQ SSQYGNDPAF PSNTKAEHTT GLSVTASPPE
SLLCGGNKQM ESMSVEETFP WNTTVDQSGF SLLNWITSTP LFSRFGRVLQ LSPHRLQNEA
QDNMCVLGSI SSLHRDFKGL TGKNSNDFQE QLKGTPTNCC KSETLETTFL
//
