ATP9B_DANRE
ID ATP9B_DANRE Reviewed; 1125 AA.
AC F1Q4S1;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Probable phospholipid-transporting ATPase IIB;
DE EC=7.6.2.1;
DE AltName: Full=ATPase class II type 9B;
GN Name=atp9b;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
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DR EMBL; BX855612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX890563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_009292513.1; XM_009294238.2.
DR AlphaFoldDB; F1Q4S1; -.
DR SMR; F1Q4S1; -.
DR STRING; 7955.ENSDARP00000114850; -.
DR PaxDb; F1Q4S1; -.
DR GeneID; 568160; -.
DR CTD; 374868; -.
DR ZFIN; ZDB-GENE-060503-583; atp9b.
DR eggNOG; KOG0210; Eukaryota.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; F1Q4S1; -.
DR OMA; IAITTWH; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; F1Q4S1; -.
DR Reactome; R-DRE-936837; Ion transport by P-type ATPases.
DR PRO; PR:F1Q4S1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030355; ATP9B.
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 PANTHER; PTHR24092:SF50; PTHR24092:SF50; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Golgi apparatus; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1125
FT /note="Probable phospholipid-transporting ATPase IIB"
FT /id="PRO_0000416696"
FT TOPO_DOM 1..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..161
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..395
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..928
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 929..949
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 950..951
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 952..972
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 973..1001
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1002..1022
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1023..1030
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1031..1051
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1052..1055
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1056..1076
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1077..1088
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1089..1109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1110..1125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 500..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 455
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 863
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 867
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1125 AA; 127041 MW; DE6DD38F39358DA3 CRC64;
MADGIPLNPV RKNLRKTAYY DASRPARYQI EDESSNLDEM PLMMSEEAFE NDESDYQTLP
RARVSQRRRG LGWFLCGGWK VLCSSCCECL VHTCRRKKEL KARTVWLGHP EKCEEKYPKN
AIKNQKYNIV TFVPGVLYQQ FKFFLNLYFL VVACSQFVPS LKIGYLYTYW APLGFVLAVT
MVREAVDEVR RCRRDKEMNS QLYSKLTVRG KVQVKSSDIQ VGDLIIVEKN QRIPADMIFL
RTSEKTGSCF IRTDQLDGET DWKLRIGVAC TQRLPALGDL FSISAYVYVQ KPQLDIHSFE
GNFTREDCDP PIHESLSIEN TLWASTVVAS GTVIGVVIYT GKEMRSVMNT SQSKNKVGLL
DLELNRLTKA LFLAQVVLSV VMVALQGFLG PWFRNLFRFV VLFSYIIPIS LRVNLDMGKS
AYGWMIMKDE NIPGTVVRTS TIPEELGRLV YLLTDKTGTL TQNEMVFKRL HLGTVSYGTD
TMDEIQSHII QSYAQVSSAQ SNGSSASSTP SRKPQPPAPK VRKSVSSRIH EAVKAIALCH
NVTPVYESRV NGANAEPEST EADQDFSDDN RTYQASSPDE VALVRWTESV GLTLVNRDLT
SLQLKTPAGQ ILTYYILQIF PFTSESKRMG IIVREEATGD ITFYMKGADV AMASIVQYND
WLEEECGNMA REGLRTLVVA KKSLTEEQYQ DFENRYNQAK LSIHDRNLKV AAVVESLERE
MELLCLTGVE DQLQADVRPT LELLRNAGIK IWMLTGDKLE TATCIAKSSH LVSRNQDIHV
FKPVSNRGEA HLELNAFRRK HDCALVISGD SLEVCLRYYE HEFVELACQC PAVVCCRCSP
TQKAQIVRLL QQHTANRTCA IGDGGNDVSM IQAADCGIGI EGKEGKQASL AADFSITQFK
HIGRLLMVHG RNSYKRSAAL GQFVMHRGMI ISTMQAVFSS IFYFASVPLY QGFLMVGYAT
IYTMFPVFSL VLDQDVKPEM ALLYPELYKD LTKGRSLSFK TFLIWVLISI YQGGILMYGA
LVLFDQEFVH VVAISFTALI LTELLMVALT IRTWHWLMVV AQLISLACYL ASLAFLNEYF
DLSFITTRVF LWKVCVITLV SCLPLYIIKY LKRKFSPPSY SKLSS
