ID G1SW08_RABIT Unreviewed; 1396 AA.
AC G1SW08;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP10D {ECO:0000313|Ensembl:ENSOCUP00000007640.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000007640.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000007640.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000007640.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000007640.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000007640.3};
RG Ensembl;
RL Submitted (NOV-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 EMBL; AAGW02010879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02010880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9986.ENSOCUP00000007640; -.
DR PaxDb; 9986-ENSOCUP00000007640; -.
DR Ensembl; ENSOCUT00000008849.4; ENSOCUP00000007640.3; ENSOCUG00000008840.4.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000156728; -.
DR HOGENOM; CLU_000846_3_4_1; -.
DR InParanoid; G1SW08; -.
DR TreeFam; TF354252; -.
DR Proteomes; UP000001811; Chromosome 2.
DR Bgee; ENSOCUG00000008840; Expressed in autopod skin and 16 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140351; F:glycosylceramide flippase activity; IEA:Ensembl.
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:SF84; PHOSPHOLIPID-TRANSPORTING ATPASE VD; 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:UP000001811};
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 99..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 124..140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 362..390
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1113..1133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1145..1166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1198..1219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1226..1251
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1271..1290
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 66..123
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1082..1191
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 503..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1396 AA; 156768 MW; 74DBCD089838AFBB CRC64;
MTEALQWARY HWQRLMGGRT RDDDERPYNY SSLLACRGKS SHTPKLAGKH RVVVPHLRPF
KEEYEKVSGT YVNNRIRTTK YTLLNFVPRN LFEQFHRAAN LYFLFLVVLN WVPLVEAFQK
EITMLPLVVV LTIIAIKDGL EDYRKYKIDK QINNLVTKVY SRKEKKYIDH CWKDVTVGDF
IRLSCNEIIP ADMVLLFSTD PDGICHIETS GLDGESNLKQ RQVVRGYADQ ESEVDPEKFS
SRIECESPNN DLSRFRGFLE HSNKERVGLS KENLLLRGCT IRNTEAVVGI VVYAGHETKA
MLNNSGPRYK RSKLERRANT DVLWCVLLLV IMCLTGALGH GIWLSKYEDV LFFNIPEPDG
HIISPVLAGF YMFWTMIILL QVLIPISLYV SIEIVKLGQI YFIQSDVDFY NEKMDSTVQC
RALNITEDLG QIQYLFSDKT GTLTENKMVF RRCSVAGFDY CHEENAKRLE SYQEAISEDE
DFTDNLSNSL SNMVKKRAHS CRTAHNGPLG NKPSNHLAGS SCALGSREGD SEMPHSRQAA
FSSPIETDVV PDTRLLDKFS QITPQLFTPL DETTRNPPLE TLYIMDFFIA LAICNTVVVS
APNQPRQKIR LSSLSGMPSK SLEEIKNLFQ RLSVRRSSSP SLASGKESSS GVPHAFVSRL
SLFSRVKTAS PVQEEISQVS ESTHSPRDSA CGREMEEEDG DTGLTNGKVE SLPGQPLASD
LCYEAESPDE AALVYAARAY RCTLQSRTPE QVMVDFAALG SLTFQLLHIL PFDSVRKRMS
VVVRHPLSNQ VVVYTKGADS VIMELLSRGS PDGATAEEQQ MLIREKTQEH LDDYAKRGLR
TLCIAKKVMS DSEYAEWLRN HFLAETSIDN REELLTESAM RLENKLTLLG ATGIEDRLQE
GVPESIEALH TAGIKIWMLT GDKQETAVNI AYACKLLDAE DKLFILDTQT KDACEMLMNT
ILNELQKKDA VRPEQAALSE RLQQPPGPQH SGPRAALIIT GKTLEFALQE SLQRQFLELT
AWCQAVVCCR ATPLQKSEVV KLVRSRLQVM TLAIGDGAND VSMIQVADIG IGVSGQEGMQ
AVMASDFAVS QFRHLSKLLL VHGHWCYTRL SNMILYFFYK NVAYVNLLFW YQFFCGFSGT
SMTDYWVLIF FNLLFTSAPP VIYGILEKDV SAETLMQLPE LYQTGQKSET YQGSDIDIFT
FGNPLNTAAL LIILLHLVIE SKSLTWIHLL VIVGSVLSYF FFTLAFGAMC VTCNPPSNPY
WIMQKHMLDP VFYLVCVLTT CIALLPRFAY RVLQGSLFPS PILRAKHLDK LTPEERTKAL
KEWRGARRMD QGTPGSADQS AGKSARTPTS ISCTTLTLKT AVSSTVEQGS LPVCETAVDV
GCSGAKPSET DQTSRC
//
