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 03-AUG-2022, entry version 126.
DE RecName: Full=Phospholipid-transporting ATPase IF;
DE EC=7.6.2.1 {ECO:0000250|UniProtKB:Q9Y2G3};
DE AltName: Full=ATPase IR;
DE AltName: Full=ATPase class VI type 11B;
DE AltName: Full=P4-ATPase flippase complex alpha subunit ATP11B;
DE AltName: Full=RING finger-binding protein;
DE Flags: Fragment;
GN Name=ATP11B;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), SUBCELLULAR
RP LOCATION (ISOFORM 2), INTERACTION WITH HLTF (ISOFORM 2), TISSUE SPECIFICITY
RP (ISOFORM 2), AND INDUCTION BY HORMONES (ISOFORM 2).
RC TISSUE=Endometrium;
RX 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 that
RT 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 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 FUNCTION (ISOFORM 2), INTERACTION WITH HLTF (ISOFORM 2), AND MUTAGENESIS OF
RP 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., Chilton B.S.;
RT "Conservation of inter-protein binding sites in RUSH and RFBP, an ATP11B
RT isoform.";
RL Mol. Cell. Endocrinol. 292:79-86(2008).
CC -!- FUNCTION: Catalytic component of a P4-ATPase flippase complex which
CC catalyzes the hydrolysis of ATP coupled to the transport of
CC aminophospholipids, phosphatidylserines (PS) and
CC phosphatidylethanolamines (PE), from the outer to the inner leaflet of
CC intracellular membranes. May contribute to the maintenance of membrane
CC lipid asymmetry in endosome compartment.
CC {ECO:0000250|UniProtKB:Q9Y2G3}.
CC -!- FUNCTION: [Isoform 2]: Appears to play a role in the subnuclear
CC trafficking of transcription factors with RING motifs.
CC {ECO:0000269|PubMed:11058586, ECO:0000269|PubMed:18584949}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2G3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O =
CC a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2G3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2G3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2G3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2G3};
CC -!- SUBUNIT: Component of a P4-ATPase flippase complex which consists of a
CC catalytic alpha subunit ATP11B and an accessory beta subunit TMEM30A.
CC {ECO:0000250|UniProtKB:Q9Y2G3}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with HLTF (via the RING-finger).
CC {ECO:0000269|PubMed:11058586, ECO:0000269|PubMed:18584949}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q9Y2G3}; Multi-pass membrane protein
CC {ECO:0000255}. Early endosome {ECO:0000250|UniProtKB:Q9Y2G3}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y2G3}. Golgi apparatus,
CC trans-Golgi network {ECO:0000250|UniProtKB:Q9Y2G3}. Note=Exit from the
CC endoplasmic reticulum requires the presence of TMEM30A, but not
CC TMEM30B. In the presence of TMEM30A, mainly located in recycling
CC endosomes. {ECO:0000250|UniProtKB:Q9Y2G3}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus inner membrane
CC {ECO:0000269|PubMed:11058586}; Multi-pass membrane protein
CC {ECO:0000255}.
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 -!- TISSUE SPECIFICITY: [Isoform 2]: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11058586}.
CC -!- INDUCTION: [Isoform 2]: Up-regulated in endometrium upon stimulation
CC with hormones, progesterone and prolactin.
CC {ECO:0000269|PubMed:11058586}.
CC -!- MISCELLANEOUS: [Isoform 2]: Is missing the sequence which constitutes
CC transmembrane helix 4 and thus has an altered transmembrane
CC architecture compared to isoform 1. The long domain (amino acids 352-
CC 868), which is normally cytoplasmic, extends into the nucleoplasm. This
CC isoform is unique to rabbit. {ECO:0000305}.
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; AF236061; AAF68024.1; -; mRNA.
DR EMBL; AY069938; AAL57758.1; -; mRNA.
DR AlphaFoldDB; Q9N0Z4; -.
DR SMR; Q9N0Z4; -.
DR STRING; 9986.ENSOCUP00000024785; -.
DR PRIDE; Q9N0Z4; -.
DR eggNOG; KOG0206; Eukaryota.
DR InParanoid; Q9N0Z4; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:RHEA.
DR GO; GO:0090556; F:phosphatidylserine floppase activity; IEA:RHEA.
DR GO; GO:0015917; P:aminophospholipid transport; IEA:InterPro.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030362; ATP11B.
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:SF57; PTHR24092:SF57; 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; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; Lipid transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN <1..1169
FT /note="Phospholipid-transporting ATPase IF"
FT /id="PRO_0000046372"
FT TOPO_DOM <1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..74
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..333
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..868
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 869..890
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 891..902
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 903..922
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 923..952
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 953..974
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 975..989
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 990..1012
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1013..1017
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1018..1039
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1040..1057
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1058..1082
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1083..1169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 794..802
FT /note="Required for binding to the RING-finger of HLTF"
FT ACT_SITE 399
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD20"
FT BINDING 813
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT BINDING 817
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT MOD_RES 1146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G3"
FT VAR_SEQ 327..392
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11058586"
FT /id="VSP_007308"
FT MUTAGEN 799
FT /note="I->D: Increased binding to the RING-finger of HLTF."
FT /evidence="ECO:0000269|PubMed:18584949"
FT CONFLICT 133
FT /note="R -> RGMHL (in Ref. 1; AAF68024)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="I -> V (in Ref. 1; AAF68024)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="I -> T (in Ref. 1; AAF68024)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="L -> S (in Ref. 2; AAL57758)"
FT /evidence="ECO:0000305"
FT NON_TER 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
