Reviewed, UniProtKB/Swiss-Prot Q9N0Z4 (AT11B_RABIT)

Names and origin

Protein names

Recommended name:
    Probable phospholipid-transporting ATPase IF
    EC=3.6.3.1
Alternative name(s):
    ATPase class VI type 11B
    ATPase IR
    RING finger-binding protein

Gene names

Name:

ATP11B

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	1169 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Isoform 2/RFBP appears to play a role in the subnuclear trafficking of transcription factors with RING motifs.
Catalytic activity	ATP + H2O + phospholipid(In) = ADP + phosphate + phospholipid(Out).
Subunit structure	Isoform 2 interacts with HLTF (via the RING-finger). Ref.3
Subcellular location	Membrane; Multi-pass membrane protein. Isoform 2: Nucleus inner membrane; Multi-pass membrane protein.
Tissue specificity	Isoform 2 is ubiquitously expressed.
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IV subfamily.

Ontologies

Keywords
Cellular component	Membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	Transmembrane
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro phospholipid transport Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipid-translocating ATPase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9N0Z4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9N0Z4-2)

Also known as: RFBP;

The sequence of this isoform differs from the canonical sequence as follows:
     327-392: Missing.

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 1169	›1169	Probable phospholipid-transporting ATPase IF		PRO_0000046372
Regions
	Topological domain	‹1 – 47	›47	Cytoplasmic Potential
	Transmembrane	48 – 69	22	Potential
	Topological domain	70 – 74	5	Extracellular Potential
	Transmembrane	75 – 96	22	Potential
	Topological domain	97 – 281	185	Cytoplasmic Potential
	Transmembrane	282 – 303	22	Potential
	Topological domain	304 – 333	30	Extracellular Potential
	Transmembrane	334 – 351	18	Potential
	Topological domain	352 – 868	517	Cytoplasmic Potential
	Transmembrane	869 – 890	22	Potential
	Topological domain	891 – 902	12	Extracellular Potential
	Transmembrane	903 – 922	20	Potential
	Topological domain	923 – 952	30	Cytoplasmic Potential
	Transmembrane	953 – 974	22	Potential
	Topological domain	975 – 989	15	Extracellular Potential
	Transmembrane	990 – 1012	23	Potential
	Topological domain	1013 – 1017	5	Cytoplasmic Potential
	Transmembrane	1018 – 1039	22	Potential
	Topological domain	1040 – 1057	18	Extracellular Potential
	Transmembrane	1058 – 1082	25	Potential
	Topological domain	1083 – 1169	87	Cytoplasmic Potential
	Region	794 – 802	9	Required for binding to the RING-finger of HLTF
Sites
	Active site	399	1	4-aspartylphosphate intermediate By similarity
	Metal binding	813	1	Magnesium By similarity
	Metal binding	817	1	Magnesium By similarity
Amino acid modifications
	Modified residue	1146	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	327 – 392	66	Missing in isoform 2.		VSP_007308
Experimental info
	Mutagenesis	799	1	I → D: Increased binding to the RING-finger of HLTF. Ref.3
	Sequence conflict	133	1	R → RGMHL in AAF68024. Ref.1
	Sequence conflict	217	1	I → V in AAF68024. Ref.1
	Sequence conflict	283	1	I → T in AAF68024. Ref.1
	Sequence conflict	299	1	L → S in AAL57758. Ref.2
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 30, 2003. Version 2. Checksum: D9A4CAE466A6528E	FASTA	1,169	133,449
	10 20 30 40 50 60 LGFDPPHQSD TRTIYIANRF PQNGLYTPQK FIDNRIISSK YTVWNFVPKN LFEQFRRVAN 70 80 90 100 110 120 FYFLIIFLVQ LMIDTPTSPI TSGLPLFFVI TVTAIKQGYE DWLRHNSDNE VNGAPVYVVR 130 140 150 160 170 180 SGGLVKTRSK NIRVGDIVRI AKDEIFPADL VLLSSDRLDG SCHVTTASLD GETNLKTHVA 190 200 210 220 230 240 VPETAVLQTV ANLDTLVAVI ECQQPEADLY RFMGRMIITQ QMEEIVRPLG PESLLLRGAR 250 260 270 280 290 300 LKNTKEIFGV AVYTGMETKM ALNYKSKSQK RSAVEKSMNT FLIIYLIILI SEAIISTILK 310 320 330 340 350 360 YTWQAEEKWD EPWYNQKTEH QRNSSKILRF ISDFLAFLVL YNFIIPISLY VTVEMQKFLG 370 380 390 400 410 420 SFFIGWDLDL YHEESDQKAQ VNTSDLNEEL GQVEYVFTDK TGTLTENEMQ FRECSIHGMK 430 440 450 460 470 480 YQEINGRLVP EGPTPDSSEG NLSYLSSLSH VNSLSHLTSS SSFRTSPEND TELIKEHDLF 490 500 510 520 530 540 FKAVSLCHTV QISSVQTDGI GDGPWQSSLA PSQLEYYASS PDEKALVEAA ARIGIVFVGN 550 560 570 580 590 600 TEETMEVKIL GKLERYKLLH VLEFDSDRRR MSVIVQAPSG ERFLFAKGAE SSILPKCIGG 610 620 630 640 650 660 EIEKTRIHVD EFALKGLRTL CVAYRQFTSK EYEVIDRRLF EARTALQQRE EKLADVFHYI 670 680 690 700 710 720 EKDLILLGAT AVEDRLQDKV RETIEALRMA GIKVWVLTGD KHETAVSVSL SCGHFHRTMN 730 740 750 760 770 780 ILELTNQKSD SECAEQLRQL ARRITEDHVI QHGLVVDGTS LSLALREHEK LFMEVCRNCS 790 800 810 820 830 840 AVLCCRMAPL QKAKVIRLIK ISPEKPITIG CWDGANDVSM IQEAHVGIGI MGKERRQAAR 850 860 870 880 890 900 NSDYAIARFK FLSKLLFVHG HFYYIRIATL VQYFFYKNVC FITPQFLYQF YCLFSQQTLY 910 920 930 940 950 960 DSVYLTLYNI CFTSLPILIY SLLEQHIDPH ILQNKPTLYR DISKNRLLSI KTFLYWTILG 970 980 990 1000 1010 1020 FSRSFIFLFG SYFLIGKDAS LLGNGQMFGN WTFGTLVFTV MVITVTVKMA LETHFWTWIN 1030 1040 1050 1060 1070 1080 HLVTWGSIIF YFVFSLFYGG ILWPFLGSQN MYFVFIQLVS SGSAWFAIIL MVVTCLFLDV 1090 1100 1110 1120 1130 1140 MKKVFDRQLH PTSTEKAQLT ETNSSIKCVD SLCCFPEGET TCTSVRRMLE RVIGRCSPTH 1150 1160 ISRSWSASDP FYTNDRSILT LSTMDSSTC
	Isoform 2 (RFBP). Checksum: AF2E74ADA7251A5A	FASTA	1,103	125,731
	10 20 30 40 50 60 LGFDPPHQSD TRTIYIANRF PQNGLYTPQK FIDNRIISSK YTVWNFVPKN LFEQFRRVAN 70 80 90 100 110 120 FYFLIIFLVQ LMIDTPTSPI TSGLPLFFVI TVTAIKQGYE DWLRHNSDNE VNGAPVYVVR 130 140 150 160 170 180 SGGLVKTRSK NIRVGDIVRI AKDEIFPADL VLLSSDRLDG SCHVTTASLD GETNLKTHVA 190 200 210 220 230 240 VPETAVLQTV ANLDTLVAVI ECQQPEADLY RFMGRMIITQ QMEEIVRPLG PESLLLRGAR 250 260 270 280 290 300 LKNTKEIFGV AVYTGMETKM ALNYKSKSQK RSAVEKSMNT FLIIYLIILI SEAIISTILK 310 320 330 340 350 360 YTWQAEEKWD EPWYNQKTEH QRNSSKVEYV FTDKTGTLTE NEMQFRECSI HGMKYQEING 370 380 390 400 410 420 RLVPEGPTPD SSEGNLSYLS SLSHVNSLSH LTSSSSFRTS PENDTELIKE HDLFFKAVSL 430 440 450 460 470 480 CHTVQISSVQ TDGIGDGPWQ SSLAPSQLEY YASSPDEKAL VEAAARIGIV FVGNTEETME 490 500 510 520 530 540 VKILGKLERY KLLHVLEFDS DRRRMSVIVQ APSGERFLFA KGAESSILPK CIGGEIEKTR 550 560 570 580 590 600 IHVDEFALKG LRTLCVAYRQ FTSKEYEVID RRLFEARTAL QQREEKLADV FHYIEKDLIL 610 620 630 640 650 660 LGATAVEDRL QDKVRETIEA LRMAGIKVWV LTGDKHETAV SVSLSCGHFH RTMNILELTN 670 680 690 700 710 720 QKSDSECAEQ LRQLARRITE DHVIQHGLVV DGTSLSLALR EHEKLFMEVC RNCSAVLCCR 730 740 750 760 770 780 MAPLQKAKVI RLIKISPEKP ITIGCWDGAN DVSMIQEAHV GIGIMGKERR QAARNSDYAI 790 800 810 820 830 840 ARFKFLSKLL FVHGHFYYIR IATLVQYFFY KNVCFITPQF LYQFYCLFSQ QTLYDSVYLT 850 860 870 880 890 900 LYNICFTSLP ILIYSLLEQH IDPHILQNKP TLYRDISKNR LLSIKTFLYW TILGFSRSFI 910 920 930 940 950 960 FLFGSYFLIG KDASLLGNGQ MFGNWTFGTL VFTVMVITVT VKMALETHFW TWINHLVTWG 970 980 990 1000 1010 1020 SIIFYFVFSL FYGGILWPFL GSQNMYFVFI QLVSSGSAWF AIILMVVTCL FLDVMKKVFD 1030 1040 1050 1060 1070 1080 RQLHPTSTEK AQLTETNSSI KCVDSLCCFP EGETTCTSVR RMLERVIGRC SPTHISRSWS 1090 1100 ASDPFYTNDR SILTLSTMDS STC

References

[1]	"Cloning and characterization of an atypical type IV P-type ATPase that binds to the RING motif of RUSH transcription factors." Mansharamani M., Hewetson A., Chilton B.S. J. Biol. Chem. 276:3641-3649(2001) [PubMed: 11058586] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Endometrium.
[2]	"Reanalysis of ATP11B, a Type IV P-type ATPase." Halleck M.S., Schlegel R.A., Williamson P.L. J. Biol. Chem. 277:9736-9740(2002) [PubMed: 11790799] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 97-437 (ISOFORM 1). Strain: New Zealand white. Tissue: Leukocyte.
[3]	"Conservation of inter-protein binding sites in RUSH and RFBP, an ATP11B isoform." Hewetson A., Wright-Pastusek A.E., Helmer R.A., Wesley K.A., Chilton B.S. Mol. Cell. Endocrinol. 292:79-86(2008) [PubMed: 18584949] [Abstract] Cited for: INTERACTION WITH HLTF, MUTAGENESIS OF ILE-799.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF236061 mRNA. Translation: AAF68024.1. AY069938 mRNA. Translation: AAL57758.1.
UniGene	Ocu.2522
3D structure databases
ModBase	Search...
Phylogenomic databases
eggNOG	maNOG09977.
HOVERGEN	Q9N0Z4.
Enzyme and pathway databases
BRENDA	3.6.3.1. 255.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR006539. ATPase_P-typ_Plipid-transl. IPR005834. Dehalogen-like_hydro. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
TIGRFAMs	TIGR01652. ATPase-Plipid. 1 hit. TIGR01494. ATPase_P-type. 4 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AT11B_RABIT

Accession

Primary (citable) accession number: Q9N0Z4
Secondary accession number(s): Q8WMR2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	April 30, 2003
Last modified:	February 9, 2010
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)