UniProt: M7B5X4

Database: UniProt
Entry: M7B5X4_CHEMY

LinkDB:  M7B5X4_CHEMY 
Original site:  M7B5X4_CHEMY

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (20)   
   InterPro (13)   
   Pfam (4)   
   PROSITE (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (31)   

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ID   M7B5X4_CHEMY            Unreviewed;      1615 AA.
AC   M7B5X4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   ORFNames=UY3_15347 {ECO:0000313|EMBL:EMP27563.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP27563.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
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}. Nucleus
CC       {ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
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; KB568893; EMP27563.1; -; Genomic_DNA.
DR   STRING; 8469.M7B5X4; -.
DR   eggNOG; KOG0206; Eukaryota.
DR   eggNOG; KOG0490; Eukaryota.
DR   Proteomes; UP000031443; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR   CDD; cd00086; homeodomain; 1.
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   Gene3D; 1.10.10.60; Homeodomain-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; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR044822; Myb_DNA-bind_4.
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   NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR24092:SF78; PHOSPHOLIPID-TRANSPORTING ATPASE IK; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   Pfam; PF13837; Myb_DNA-bind_4; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SMART; SM00389; HOX; 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; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362033};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00108,
KW   ECO:0000256|RuleBase:RU000682};
KW   Homeobox {ECO:0000256|PROSITE-ProRule:PRU00108,
KW   ECO:0000256|RuleBase:RU000682}; 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   Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108,
KW   ECO:0000256|RuleBase:RU000682};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031443};
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        500..518
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        701..725
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        745..768
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1298..1318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1330..1351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1380..1403
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1415..1436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1443..1462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1490..1512
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          181..228
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000259|PROSITE:PS50071"
FT   DNA_BIND        183..229
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT   COILED          1030..1057
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1615 AA;  181005 MW;  B1764A1D78A1EEA0 CRC64;
     MAEHTACAHM IGMDVSNTSR RTTVTKERLA SEIKGSSVTE EAIYAKGRRH SCRLGGSGAL
     SHPEGHGPWG KTPGCQLGPS MYYLGEGAQT LGSMNPLSLN YSLNQLPPAP APQPSSLRAV
     SVVDRLAVSS TGDLSLSRDD GVPLCSPVGI NGRASGGFGR WEASKESRWE LLLEARYGIP
     QKQRRSRTAF TGHQLEALET AFEKTHYPDA VTRERLAVLV NLPEARVQRG KLQVTMQSSS
     AEVTMMESQT RKRDPAWTER EVRDLIAVWG EESVLSELRS SFRNAKTFVK ISQGMKDRGH
     NRDPKQCRVK LKELRQAYQK TREANGRSGS EPQTCRFYDE LHAIWGGSAT TTPAVLFDSF
     NGDGGNTEAG GREAALTEDG CHCLLFEARL PSTKMAAPPS PYSGSMTNQE SLESYLNGSK
     KQLDFTWEVK ANDRAYHKQF KKRVAFCLTR KKYEDNAIRT AKYNVLTFLP LNLYEQFHRL
     ANLYFLFVIL LQTVPEISTL PWFTLLLPLS SLLLLRGLRD LIDDIARHRS DWMINSRPCE
     ILVGKSFSSK KWRDICVGDV ICLRKDSFVP ADLLLLSSSE PSSLCYVETA DIDGETNLKF
     RQALLATHQE LVSEASMAAF DGKVTCEEPN SRMHSFIGTL EWKGEKYSLD SEKILLRGCR
     IRNTETCYGL VIYAGLDSKI MKNCGKIKMK KTKLDRLMDR LVIVIFVMLV ITSLCLAFAA
     GFWAVKFHTQ HSYLSALYVG TSPATQAFFT FWGFMILLSI IIPMSMYITF EFIYMVNSCF
     IDWDLEMYYP AKDTPAKARS TSLNDQLGQI EYIFSDKTGT LTQNIMTFKK CCINGITYGS
     AHGENKASKA SVSWNPYVDR TAEFHDPSLL EAVLQNDDPV MREFLRLLAL CHTVMVEEKD
     TGELVYQAAS PDEEALVMAA RNLGYVFLSR TQDTITLSEL GTERTYSLLA MLDFNSVRKR
     MSILDCCRPS RWRAASLPPV KTPEWEWHFS AVTLGGASFA EETLRTLCLA SKEVKEEDYI
     EWSKKHHEAS VLLQNRAQEL DKVYEEMEQD LQLLGATAIE DKLQDGVPET IQLLKKGNIK
     VWVLTGDKQA AQPPPGGPLA RLGFDPTFHP LPAPFLHSEM LEACWVSTNN LGSSEEALCR
     FQQCSGGLHQ GKMALVVTGD FLEKVLGTAE KVKRKEGFWA WLACCKAQTQ PVADSLVEKA
     FVDLATCCQA VICCRVTPKQ KALVVQLVKR HRSAITLAIG DGANDVNMIK TADIGVGISG
     QEGMQAVQCS DYALAQFRYL QRLLLVHGRW SYLRICKFLR YFFYKTFAGM MVQIWFAFYS
     GFTAQPLYEG WFLALYNVFY TAYPVLSMGL MEQDVSAEKS LKFPELYKVG QRDELFNYRV
     FCVTLLHGTV TSLGSFFIAL WAFEDRVGSR VVGDYQSFAI TVATSAFLSV LAEIIMDIKF
     WTILSFLTVA GSLLFFCLFS FLTQNFMVFR EAPTIFRFPD ASQNALTDPY VLSVVLLCVV
     VNTVPSLTVR LLRVITGTGT IQHKIRFRDT RVAESTVELK SHFRRGSLQR RSSYAFSHKE
     GYADLITRGA SLRAKDSRNR GPVNASSYQS ILLPTREGAT PSVASGPSVF LKEYN
//

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