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Probable phospholipid-transporting ATPase IF (EC 3.6.3.1) (ATPase IR) (ATPase class VI type 11B) (P4-ATPase flippase complex alpha subunit ATP11B) (RING finger-binding protein) (Fragment)

 AT11B_RABIT             Reviewed;        1169 AA.
Q9N0Z4; Q8WMR2;
30-APR-2003, integrated into UniProtKB/Swiss-Prot.
30-APR-2003, sequence version 2.
05-DEC-2018, entry version 112.
RecName: Full=Probable phospholipid-transporting ATPase IF;
EC=7.6.2.1;
AltName: Full=ATPase IR;
AltName: Full=ATPase class VI type 11B;
AltName: Full=P4-ATPase flippase complex alpha subunit ATP11B;
AltName: Full=RING finger-binding protein;
Flags: Fragment;
Name=ATP11B;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION
(ISOFORM 2).
TISSUE=Endometrium;
PubMed=11058586; DOI=10.1074/jbc.M004231200;
Mansharamani M., Hewetson A., Chilton B.S.;
"Cloning and characterization of an atypical type IV P-type ATPase
that binds to the RING motif of RUSH transcription factors.";
J. Biol. Chem. 276:3641-3649(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 97-437 (ISOFORM 1).
STRAIN=New Zealand white; TISSUE=Leukocyte;
PubMed=11790799; DOI=10.1074/jbc.M200240200;
Halleck M.S., Schlegel R.A., Williamson P.L.;
"Reanalysis of ATP11B, a Type IV P-type ATPase.";
J. Biol. Chem. 277:9736-9740(2002).
[3]
INTERACTION WITH HLTF, AND MUTAGENESIS OF ILE-799.
PubMed=18584949; DOI=10.1016/j.mce.2008.05.007;
Hewetson A., Wright-Pastusek A.E., Helmer R.A., Wesley K.A.,
Chilton B.S.;
"Conservation of inter-protein binding sites in RUSH and RFBP, an
ATP11B isoform.";
Mol. Cell. Endocrinol. 292:79-86(2008).
-!- FUNCTION: Catalytic component of a P4-ATPase flippase complex
which catalyzes the hydrolysis of ATP coupled to the transport of
aminophospholipids from the outer to the inner leaflet of various
membranes and ensures the maintenance of asymmetric distribution
of phospholipids. Phospholipid translocation seems also to be
implicated in vesicle formation and in uptake of lipid signaling
molecules (By similarity). Isoform 2/RFBP appears to play a role
in the subnuclear trafficking of transcription factors with RING
motifs. {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=a phospholipid derivative(in) + ATP + H2O = a
phospholipid derivative(out) + ADP + H(+) + phosphate;
Xref=Rhea:RHEA:14989, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16247, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
ChEBI:CHEBI:456216; EC=7.6.2.1;
-!- SUBUNIT: Component of a P4-ATPase flippase complex which consists
of a catalytic alpha subunit and an accessory beta subunit
(Probable). Interacts with TMEM30A. Isoform 2 interacts with HLTF
(via the RING-finger). {ECO:0000269|PubMed:18584949, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Recycling endosome membrane
{ECO:0000250|UniProtKB:Q9Y2G3}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:Q9Y2G3}. Early endosome
{ECO:0000250|UniProtKB:Q9Y2G3}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:Q9Y2G3}. Golgi apparatus, trans-Golgi
network {ECO:0000250|UniProtKB:Q9Y2G3}. Note=Exit from the
endoplasmic reticulum requires the presence of TMEM30A, but not
TMEM30B. In the presence of TMEM30A, mainly located in recycling
endosomes. {ECO:0000250|UniProtKB:Q9Y2G3}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus inner membrane
{ECO:0000269|PubMed:11058586}; Multi-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9N0Z4-1; Sequence=Displayed;
Name=2; Synonyms=RFBP;
IsoId=Q9N0Z4-2; Sequence=VSP_007308;
Note=Is missing the sequence which constitutes transmembrane
helix 4 and thus has an altered transmembrane architecture
compared to isoform 1. The long domain (amino acids 352-868),
which is normally cytoplasmic, extends into the nucleoplasm.
This isoform is unique to rabbit.;
-!- TISSUE SPECIFICITY: Isoform 2 is ubiquitously expressed.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IV subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF236061; AAF68024.1; -; mRNA.
EMBL; AY069938; AAL57758.1; -; mRNA.
UniGene; Ocu.2522; -.
ProteinModelPortal; Q9N0Z4; -.
STRING; 9986.ENSOCUP00000024785; -.
eggNOG; KOG0206; Eukaryota.
eggNOG; ENOG410XPYK; LUCA.
HOGENOM; HOG000202528; -.
HOVERGEN; HBG050601; -.
InParanoid; Q9N0Z4; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004012; F:phospholipid-translocating ATPase activity; IEA:InterPro.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR030362; ATP11B.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006539; P-type_ATPase_IV.
InterPro; IPR032631; P-type_ATPase_N.
InterPro; IPR001757; P_typ_ATPase.
InterPro; IPR032630; P_typ_ATPase_c.
PANTHER; PTHR24092; PTHR24092; 1.
PANTHER; PTHR24092:SF57; PTHR24092:SF57; 1.
Pfam; PF16212; PhoLip_ATPase_C; 1.
Pfam; PF16209; PhoLip_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 1.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 1.
TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 3.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome;
Endoplasmic reticulum; Endosome; Golgi apparatus; Lipid transport;
Magnesium; Membrane; Metal-binding; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Translocase; Transmembrane;
Transmembrane helix; Transport.
CHAIN <1 1169 Probable phospholipid-transporting ATPase
IF.
/FTId=PRO_0000046372.
TOPO_DOM <1 47 Cytoplasmic. {ECO:0000255}.
TRANSMEM 48 69 Helical. {ECO:0000255}.
TOPO_DOM 70 74 Extracellular. {ECO:0000255}.
TRANSMEM 75 96 Helical. {ECO:0000255}.
TOPO_DOM 97 281 Cytoplasmic. {ECO:0000255}.
TRANSMEM 282 303 Helical. {ECO:0000255}.
TOPO_DOM 304 333 Extracellular. {ECO:0000255}.
TRANSMEM 334 351 Helical. {ECO:0000255}.
TOPO_DOM 352 868 Cytoplasmic. {ECO:0000255}.
TRANSMEM 869 890 Helical. {ECO:0000255}.
TOPO_DOM 891 902 Extracellular. {ECO:0000255}.
TRANSMEM 903 922 Helical. {ECO:0000255}.
TOPO_DOM 923 952 Cytoplasmic. {ECO:0000255}.
TRANSMEM 953 974 Helical. {ECO:0000255}.
TOPO_DOM 975 989 Extracellular. {ECO:0000255}.
TRANSMEM 990 1012 Helical. {ECO:0000255}.
TOPO_DOM 1013 1017 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1018 1039 Helical. {ECO:0000255}.
TOPO_DOM 1040 1057 Extracellular. {ECO:0000255}.
TRANSMEM 1058 1082 Helical. {ECO:0000255}.
TOPO_DOM 1083 1169 Cytoplasmic. {ECO:0000255}.
REGION 794 802 Required for binding to the RING-finger
of HLTF.
ACT_SITE 399 399 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 813 813 Magnesium. {ECO:0000250}.
METAL 817 817 Magnesium. {ECO:0000250}.
MOD_RES 1146 1146 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2G3}.
VAR_SEQ 327 392 Missing (in isoform 2).
{ECO:0000303|PubMed:11058586}.
/FTId=VSP_007308.
MUTAGEN 799 799 I->D: Increased binding to the RING-
finger of HLTF.
{ECO:0000269|PubMed:18584949}.
CONFLICT 133 133 R -> RGMHL (in Ref. 1; AAF68024).
{ECO:0000305}.
CONFLICT 217 217 I -> V (in Ref. 1; AAF68024).
{ECO:0000305}.
CONFLICT 283 283 I -> T (in Ref. 1; AAF68024).
{ECO:0000305}.
CONFLICT 299 299 L -> S (in Ref. 2; AAL57758).
{ECO:0000305}.
NON_TER 1 1
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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[ATP8B1 ATPIC FIC1 PFIC] Phospholipid-transporting ATPase IC (EC 7.6.2.1) (ATPase class I type 8B member 1) (Familial intrahepatic cholestasis type 1) (P4-ATPase flippase complex alpha subunit ATP8B1)
[Atp8b1] Phospholipid-transporting ATPase IC (EC 7.6.2.1) (ATPase class I type 8B member 1) (P4-ATPase flippase complex alpha subunit ATP8B1)
[ATP8A2 ATPIB] Phospholipid-transporting ATPase IB (EC 7.6.2.1) (ATPase class I type 8A member 2) (ML-1) (P4-ATPase flippase complex alpha subunit ATP8A2)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
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[ZFP36L1 BERG36 BRF1 ERF1 RNF162B TIS11B] mRNA decay activator protein ZFP36L1 (Butyrate response factor 1) (EGF-response factor 1) (ERF-1) (TPA-induced sequence 11b) (Zinc finger protein 36, C3H1 type-like 1) (ZFP36-like 1)
[gag-pol] Gag-Pol polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; Spacer peptide (SP) (p3); Nucleocapsid protein p12; Protease p15 (EC 3.4.23.-); Reverse transcriptase, beta-subunit (RT-beta); Reverse transcriptase, alpha-subunit (RT-alpha) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-) (pp32); p4]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[HLTF RUSH1 SMARCA3] Helicase-like transcription factor (EC 2.3.2.27) (EC 3.6.4.-) (RING-type E3 ubiquitin transferase HLTF) (RUSH-1) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3) (Sucrose nonfermenting protein 2-like 3)
[ndx-4 Y37H9A.6] Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] (EC 3.6.1.-) (Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase) (Ap4A hydrolase) (Ap4Aase) (Diadenosine tetraphosphatase) (Nudix hydrolase 4)
[Zfp36l1 Brf1 Tis11b] mRNA decay activator protein ZFP36L1 (Butyrate response factor 1) (TPA-induced sequence 11b) (Zinc finger protein 36, C3H1 type-like 1) (ZFP36-like 1)
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[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[gag-pol] Gag-Pol polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; p3; Nucleocapsid protein p12; Protease p15 (EC 3.4.23.-); Reverse transcriptase beta-subunit (RT-beta); Reverse transcriptase alpha-subunit (RT-alpha) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-) (pp32); p4]

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