(data stored in ACNUC6163 zone)

HOVERGEN: AT11B_RABIT

ID   AT11B_RABIT             Reviewed;        1169 AA.
AC   Q9N0Z4; Q8WMR2;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 2.
DT   13-OCT-2009, entry version 63.
DE   RecName: Full=Probable phospholipid-transporting ATPase IF;
DE            EC=3.6.3.1;
DE   AltName: Full=ATPase class VI type 11B;
DE   AltName: Full=ATPase IR;
DE   AltName: Full=RING finger-binding protein;
DE   Flags: Fragment;
GN   Name=ATP11B;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Endometrium;
RX   MEDLINE=21264844; PubMed=11058586; DOI=10.1074/jbc.M004231200;
RA   Mansharamani M., Hewetson A., Chilton B.S.;
RT   "Cloning and characterization of an atypical type IV P-type ATPase
RT   that binds to the RING motif of RUSH transcription factors.";
RL   J. Biol. Chem. 276:3641-3649(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 97-437 (ISOFORM 1).
RC   STRAIN=New Zealand white; TISSUE=Leukocyte;
RX   MEDLINE=21895878; PubMed=11790799; DOI=10.1074/jbc.M200240200;
RA   Halleck M.S., Schlegel R.A., Williamson P.L.;
RT   "Reanalysis of ATP11B, a Type IV P-type ATPase.";
RL   J. Biol. Chem. 277:9736-9740(2002).
RN   [3]
RP   INTERACTION WITH HLTF, AND MUTAGENESIS OF ILE-799.
RX   PubMed=18584949; DOI=10.1016/j.mce.2008.05.007;
RA   Hewetson A., Wright-Pastusek A.E., Helmer R.A., Wesley K.A.,
RA   Chilton B.S.;
RT   "Conservation of inter-protein binding sites in RUSH and RFBP, an
RT   ATP11B isoform.";
RL   Mol. Cell. Endocrinol. 292:79-86(2008).
CC   -!- FUNCTION: Isoform 2/RFBP appears to play a role in the subnuclear
CC       trafficking of transcription factors with RING motifs.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(In) = ADP +
CC       phosphate + phospholipid(Out).
CC   -!- SUBUNIT: Isoform 2 interacts with HLTF (via the RING-finger).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Nucleus inner membrane; Multi-
CC       pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9N0Z4-1; Sequence=Displayed;
CC       Name=2; Synonyms=RFBP;
CC         IsoId=Q9N0Z4-2; Sequence=VSP_007308;
CC         Note=Is missing the sequence which constitutes transmembrane
CC         helix 4 and thus has an altered transmembrane architecture
CC         compared to isoform 1. The long domain (amino acids 352-868),
CC         which is normally cytoplasmic, extends into the nucleoplasm.
CC         This isoform is unique to rabbit;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is ubiquitously expressed.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       family. Type IV subfamily.
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CC   -!- GENE_FAMILY: HBG050601 [ FAMILY / ALN / TREE ]
DR   EMBL; AF236061; AAF68024.1; -; mRNA.
DR   EMBL; AY069938; AAL57758.1; -; mRNA.
DR   UniGene; Ocu.2522; -.
DR   HOVERGEN; Q9N0Z4; -.
DR   BRENDA; 3.6.3.1; 255.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015662; F:ATPase activity, coupled to transmembrane m...; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004012; F:phospholipid-translocating ATPase activity; IEA:EC.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-reg.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR006539; ATPase_P-typ_Plipid-transl.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   PANTHER; PTHR11939; ATPase_P; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q9N0Z4.
DR   SWISS-2DPAGE; Q9N0Z4.
KW   Alternative splicing; ATP-binding; Hydrolase; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Transmembrane.
FT   CHAIN        <1   1169       Probable phospholipid-transporting ATPase
FT                                IF.
FT                                /FTId=PRO_0000046372.
FT   TOPO_DOM     <1     47       Cytoplasmic (Potential).
FT   TRANSMEM     48     69       Potential.
FT   TOPO_DOM     70     74       Extracellular (Potential).
FT   TRANSMEM     75     96       Potential.
FT   TOPO_DOM     97    281       Cytoplasmic (Potential).
FT   TRANSMEM    282    303       Potential.
FT   TOPO_DOM    304    333       Extracellular (Potential).
FT   TRANSMEM    334    351       Potential.
FT   TOPO_DOM    352    868       Cytoplasmic (Potential).
FT   TRANSMEM    869    890       Potential.
FT   TOPO_DOM    891    902       Extracellular (Potential).
FT   TRANSMEM    903    922       Potential.
FT   TOPO_DOM    923    952       Cytoplasmic (Potential).
FT   TRANSMEM    953    974       Potential.
FT   TOPO_DOM    975    989       Extracellular (Potential).
FT   TRANSMEM    990   1012       Potential.
FT   TOPO_DOM   1013   1017       Cytoplasmic (Potential).
FT   TRANSMEM   1018   1039       Potential.
FT   TOPO_DOM   1040   1057       Extracellular (Potential).
FT   TRANSMEM   1058   1082       Potential.
FT   TOPO_DOM   1083   1169       Cytoplasmic (Potential).
FT   REGION      794    802       Required for binding to the RING-finger
FT                                of HLTF.
FT   ACT_SITE    399    399       4-aspartylphosphate intermediate (By
FT                                similarity).
FT   METAL       813    813       Magnesium (By similarity).
FT   METAL       817    817       Magnesium (By similarity).
FT   VAR_SEQ     327    392       Missing (in isoform 2).
FT                                /FTId=VSP_007308.
FT   MUTAGEN     799    799       I->D: Increased binding to the RING-
FT                                finger of HLTF.
FT   CONFLICT    133    133       R -> RGMHL (in Ref. 1; AAF68024).
FT   CONFLICT    217    217       I -> V (in Ref. 1; AAF68024).
FT   CONFLICT    283    283       I -> T (in Ref. 1; AAF68024).
FT   CONFLICT    299    299       L -> S (in Ref. 2; AAL57758).
FT   NON_TER       1      1
SQ   SEQUENCE   1169 AA;  133449 MW;  D9A4CAE466A6528E CRC64;
     LGFDPPHQSD TRTIYIANRF PQNGLYTPQK FIDNRIISSK YTVWNFVPKN LFEQFRRVAN
     FYFLIIFLVQ LMIDTPTSPI TSGLPLFFVI TVTAIKQGYE DWLRHNSDNE VNGAPVYVVR
     SGGLVKTRSK NIRVGDIVRI AKDEIFPADL VLLSSDRLDG SCHVTTASLD GETNLKTHVA
     VPETAVLQTV ANLDTLVAVI ECQQPEADLY RFMGRMIITQ QMEEIVRPLG PESLLLRGAR
     LKNTKEIFGV AVYTGMETKM ALNYKSKSQK RSAVEKSMNT FLIIYLIILI SEAIISTILK
     YTWQAEEKWD EPWYNQKTEH QRNSSKILRF ISDFLAFLVL YNFIIPISLY VTVEMQKFLG
     SFFIGWDLDL YHEESDQKAQ VNTSDLNEEL GQVEYVFTDK TGTLTENEMQ FRECSIHGMK
     YQEINGRLVP EGPTPDSSEG NLSYLSSLSH VNSLSHLTSS SSFRTSPEND TELIKEHDLF
     FKAVSLCHTV QISSVQTDGI GDGPWQSSLA PSQLEYYASS PDEKALVEAA ARIGIVFVGN
     TEETMEVKIL GKLERYKLLH VLEFDSDRRR MSVIVQAPSG ERFLFAKGAE SSILPKCIGG
     EIEKTRIHVD EFALKGLRTL CVAYRQFTSK EYEVIDRRLF EARTALQQRE EKLADVFHYI
     EKDLILLGAT AVEDRLQDKV RETIEALRMA GIKVWVLTGD KHETAVSVSL SCGHFHRTMN
     ILELTNQKSD SECAEQLRQL ARRITEDHVI QHGLVVDGTS LSLALREHEK LFMEVCRNCS
     AVLCCRMAPL QKAKVIRLIK ISPEKPITIG CWDGANDVSM IQEAHVGIGI MGKERRQAAR
     NSDYAIARFK FLSKLLFVHG HFYYIRIATL VQYFFYKNVC FITPQFLYQF YCLFSQQTLY
     DSVYLTLYNI CFTSLPILIY SLLEQHIDPH ILQNKPTLYR DISKNRLLSI KTFLYWTILG
     FSRSFIFLFG SYFLIGKDAS LLGNGQMFGN WTFGTLVFTV MVITVTVKMA LETHFWTWIN
     HLVTWGSIIF YFVFSLFYGG ILWPFLGSQN MYFVFIQLVS SGSAWFAIIL MVVTCLFLDV
     MKKVFDRQLH PTSTEKAQLT ETNSSIKCVD SLCCFPEGET TCTSVRRMLE RVIGRCSPTH
     ISRSWSASDP FYTNDRSILT LSTMDSSTC
//

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