Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phospholipid-transporting ATPase IC

Gene

Atp8b1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. May play a role in asymmetric distribution of phospholipids in the canicular membrane. Plays a role in bile salt homeostasis. In cooperation with ABCB4 may be involved in establishing integrity of the canalicular membrane thus protecting hepatocytes from bile salts. Involved in the microvillus formation in polarized epithelial cells; the function seems to be independent from its flippase activity. Required for the preservation of cochlear hair cells in the inner ear. Required for the preservation of cochlear hair cells in the inner ear. According PubMed:20852622 is proposed to act as cardiolipin transporter during inflammatory injury; the function is questioned by PubMed:21475228.5 Publications

Catalytic activityi

ATP + H2O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei4544-aspartylphosphate intermediateBy similarity1
Metal bindingi893MagnesiumBy similarity1
Metal bindingi897MagnesiumBy similarity1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cardiolipin binding Source: UniProtKB
  • lipid transporter activity Source: MGI
  • magnesium ion binding Source: InterPro
  • phospholipid-translocating ATPase activity Source: GO_Central

GO - Biological processi

  • bile acid metabolic process Source: MGI
  • drug transmembrane transport Source: MGI
  • Golgi organization Source: GO_Central
  • inner ear receptor cell development Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: MGI
  • phospholipid translocation Source: MGI
  • regulation of microvillus assembly Source: MGI
  • sensory perception of sound Source: UniProtKB
  • vestibulocochlear nerve formation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hearing, Lipid transport, Transport

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.3.1. 3474.
ReactomeiR-MMU-936837. Ion transport by P-type ATPases.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipid-transporting ATPase IC (EC:3.6.3.1)
Alternative name(s):
ATPase class I type 8B member 1
P4-ATPase flippase complex alpha subunit ATP8B1
Gene namesi
Name:Atp8b1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1859665. Atp8b1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 121CytoplasmicSequence analysisAdd BLAST121
Transmembranei122 – 142HelicalSequence analysisAdd BLAST21
Topological domaini143 – 144Exoplasmic loopSequence analysis2
Transmembranei145 – 165HelicalSequence analysisAdd BLAST21
Topological domaini166 – 339CytoplasmicSequence analysisAdd BLAST174
Transmembranei340 – 360HelicalSequence analysisAdd BLAST21
Topological domaini361 – 385Exoplasmic loopSequence analysisAdd BLAST25
Transmembranei386 – 406HelicalSequence analysisAdd BLAST21
Topological domaini407 – 952CytoplasmicSequence analysisAdd BLAST546
Transmembranei953 – 973HelicalSequence analysisAdd BLAST21
Topological domaini974 – 982Exoplasmic loopSequence analysis9
Transmembranei983 – 1003HelicalSequence analysisAdd BLAST21
Topological domaini1004 – 1032CytoplasmicSequence analysisAdd BLAST29
Transmembranei1033 – 1053HelicalSequence analysisAdd BLAST21
Topological domaini1054 – 1071Exoplasmic loopSequence analysisAdd BLAST18
Transmembranei1072 – 1092HelicalSequence analysisAdd BLAST21
Topological domaini1093 – 1094CytoplasmicSequence analysis2
Transmembranei1095 – 1115HelicalSequence analysisAdd BLAST21
Topological domaini1116 – 1142Exoplasmic loopSequence analysisAdd BLAST27
Transmembranei1143 – 1163HelicalSequence analysisAdd BLAST21
Topological domaini1164 – 1251CytoplasmicSequence analysisAdd BLAST88

GO - Cellular componenti

  • apical plasma membrane Source: MGI
  • brush border membrane Source: Ensembl
  • endoplasmic reticulum Source: MGI
  • Golgi apparatus Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: MGI
  • stereocilium Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice have unimpaired bile secretion, and no liver damage, but show mild abnormalities including depressed weight at weaning and elevated serum bile salt levels. Do not suffer from jaundice or diarrhea and have normal serum bilirubin levels and normal liver enzyme activities, except for mildly elevated serum AST (aspartate aminotransferase) activity. Display unimpaired transhepatic bile salt transport and are resistant to bile salt-induced cholestasis. Upon bile salt feeding, demonstrate serum bile salt accumulation, hepatic injury and expansion of the systemic bile salt pool and this failure of bile salt homeostasis occurrs in the absence of any defect in hepatic bile secretion.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi308G → V: Markly decreased expression, hearing loss associated with degeneration of cochlear hair cells and spiral ganglion cells. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003708621 – 1251Phospholipid-transporting ATPase ICAdd BLAST1251

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1223PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ148W0.
PaxDbiQ148W0.
PeptideAtlasiQ148W0.
PRIDEiQ148W0.

PTM databases

iPTMnetiQ148W0.
PhosphoSitePlusiQ148W0.

Expressioni

Tissue specificityi

Hepatocytes, bile duct, intestinal epithelial cells (cholangiocytes and ileocytes), and pancreatic acinar cells.1 Publication

Gene expression databases

BgeeiENSMUSG00000039529.
GenevisibleiQ148W0. MM.

Interactioni

Subunit structurei

Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit. The probable flippase ATP8B1:TMEM30A complex can form an intermediate phosphoenzyme in vitro. Also interacts with beta subunit TMEM30B (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025482.

Structurei

3D structure databases

ProteinModelPortaliQ148W0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410KDRM. Eukaryota.
ENOG410XPYK. LUCA.
GeneTreeiENSGT00860000133706.
HOGENOMiHOG000202528.
InParanoidiQ148W0.
KOiK01530.
OMAiQRTNSKN.
OrthoDBiEOG091G0139.
PhylomeDBiQ148W0.
TreeFamiTF300654.

Family and domain databases

Gene3Di2.70.150.10. 2 hits.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR030346. ATP8B1.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006539. P-type_ATPase_IV.
IPR032631. P-type_ATPase_N.
IPR001757. P_typ_ATPase.
IPR032630. P_typ_ATPase_c.
[Graphical view]
PANTHERiPTHR24092. PTHR24092. 2 hits.
PTHR24092:SF48. PTHR24092:SF48. 2 hits.
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF16212. PhoLip_ATPase_C. 1 hit.
PF16209. PhoLip_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q148W0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTERDSETT FDEESQPNDE VVPYSDDETE DELEDQGSTV EPEQNRVNRE
60 70 80 90 100
AEKKRETFRK DCTWQVKAND RKFHEQPHFM NTKFFCIKES KYASNAIKTY
110 120 130 140 150
KYNGFTFLPM NLFEQFKRAA NFYFLILLIL QAIPQISTLA WYTTLVPLLL
160 170 180 190 200
VLGITAIKDL VDDVARHKMD KEINNRTCEV IKDGRFKIIK WKDIQVGDVI
210 220 230 240 250
RLKKNDFIPA DILLLSSSEP NSLCYVETAE LDGETNLKFK MALEITDQYL
260 270 280 290 300
QIEDNLATFD GFIECEEPNN RLDKFTGTLF WKNQSFPLDA DKILLRGCVI
310 320 330 340 350
RNTDVCHGLV IFAGADTKIM KNSGKTRFKR TKIDYLMNYM VYTIFIVLIL
360 370 380 390 400
VSAGLAIGHA YWEAQVGNYS WYLYDGENAT PSYRGFLNFW GYIIVLNTMV
410 420 430 440 450
PISLYVSVEV IRLGQSHFIN WDLQMYYAEK DTPAKARTTT LNEQLGQIHY
460 470 480 490 500
IFSDKTGTLT QNIMTFKKCC INGTIYGDHR DASQHSHSKI ELVDFSWNTF
510 520 530 540 550
ADGKLAFYDH YLIEQIQSGK EPEVRQFFFL LSICHTVMVD RIDGQINYQA
560 570 580 590 600
ASPDEGALVN AARNFGFAFL ARTQNTITVS ELGSERTYNV LAILDFNSDR
610 620 630 640 650
KRMSIIVRTP EGSIRLYCKG ADTVIYERLH RMNPTKQETQ DALDIFASET
660 670 680 690 700
LRTLCLCYKE IEEKEFTEWN NKFMAASVAS SNRDEALDKV YEEIEKDLIL
710 720 730 740 750
LGATAIEDKL QDGVPETISK LAKADIKIWV LTGDKKETAE NIGFACELLT
760 770 780 790 800
EDTTICYGED INSLLHTRME NQRNRGGVSA KFAPPVYEPF FPPGENRALI
810 820 830 840 850
ITGSWLNEIL LEKKTKRSKI LKLKFPRTEE ERRMRSQSRR RLEEKKEQRQ
860 870 880 890 900
KNFVDLACEC SAVICCRVTP KQKAMVVDLV KRYKKAITLA IGDGANDVNM
910 920 930 940 950
IKTAHIGVGI SGQEGMQAVM SSDYSFAQFR YLQRLLLVHG RWSYIRMCKF
960 970 980 990 1000
LRYFFYKNFA FTLVHFWYSF FNGYSAQTAY EDWFITLYNV LYSSLPVLLM
1010 1020 1030 1040 1050
GLLDQDVSDK LSLRFPGLYV VGQRDLLFNY KRFFVSLLHG VLTSMVLFFI
1060 1070 1080 1090 1100
PLGAYLQTVG QDGEAPSDYQ SFAVTVASAL VITVNFQIGL DTSYWTFVNA
1110 1120 1130 1140 1150
FSIFGSIALY FGIMFDFHSA GIHVLFPSAF QFTGTASNAL RQPYIWLTII
1160 1170 1180 1190 1200
LTVAVCLLPV VAIRFLSMTI WPSESDKIQK HRKRLKAEEQ WKRRQSVFRR
1210 1220 1230 1240 1250
GVSSRRSAYA FSHQRGYADL ISSGRSIRKK RSPLDAIIAD GTAEYRRTVE

S
Length:1,251
Mass (Da):143,798
Last modified:May 5, 2009 - v2
Checksum:i394920189075875D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti104G → A in AAR90342 (PubMed:14976163).Curated1
Sequence conflicti108L → I in AAR90342 (PubMed:14976163).Curated1
Sequence conflicti155T → M in BAE34046 (PubMed:16141072).Curated1
Sequence conflicti174N → S in AAR90342 (PubMed:14976163).Curated1
Sequence conflicti176R → M in AAR90342 (PubMed:14976163).Curated1
Sequence conflicti531L → P in BAE34046 (PubMed:16141072).Curated1
Sequence conflicti575N → Y in BAE34046 (PubMed:16141072).Curated1
Sequence conflicti667T → A in AAI17947 (PubMed:15489334).Curated1
Sequence conflicti671N → K in AAI17947 (PubMed:15489334).Curated1
Sequence conflicti893D → E in BAE34046 (PubMed:16141072).Curated1
Sequence conflicti1226S → C in BAE34046 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY506548 mRNA. Translation: AAR90342.1.
AK157316 mRNA. Translation: BAE34046.1.
BC117946 mRNA. Translation: AAI17947.1.
CCDSiCCDS29304.1.
RefSeqiNP_001001488.2. NM_001001488.3.
UniGeneiMm.270043.
Mm.456199.

Genome annotation databases

EnsembliENSMUST00000025482; ENSMUSP00000025482; ENSMUSG00000039529.
GeneIDi54670.
KEGGimmu:54670.
UCSCiuc008fem.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY506548 mRNA. Translation: AAR90342.1.
AK157316 mRNA. Translation: BAE34046.1.
BC117946 mRNA. Translation: AAI17947.1.
CCDSiCCDS29304.1.
RefSeqiNP_001001488.2. NM_001001488.3.
UniGeneiMm.270043.
Mm.456199.

3D structure databases

ProteinModelPortaliQ148W0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025482.

PTM databases

iPTMnetiQ148W0.
PhosphoSitePlusiQ148W0.

Proteomic databases

MaxQBiQ148W0.
PaxDbiQ148W0.
PeptideAtlasiQ148W0.
PRIDEiQ148W0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025482; ENSMUSP00000025482; ENSMUSG00000039529.
GeneIDi54670.
KEGGimmu:54670.
UCSCiuc008fem.1. mouse.

Organism-specific databases

CTDi5205.
MGIiMGI:1859665. Atp8b1.

Phylogenomic databases

eggNOGiENOG410KDRM. Eukaryota.
ENOG410XPYK. LUCA.
GeneTreeiENSGT00860000133706.
HOGENOMiHOG000202528.
InParanoidiQ148W0.
KOiK01530.
OMAiQRTNSKN.
OrthoDBiEOG091G0139.
PhylomeDBiQ148W0.
TreeFamiTF300654.

Enzyme and pathway databases

BRENDAi3.6.3.1. 3474.
ReactomeiR-MMU-936837. Ion transport by P-type ATPases.

Miscellaneous databases

PROiQ148W0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000039529.
GenevisibleiQ148W0. MM.

Family and domain databases

Gene3Di2.70.150.10. 2 hits.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR030346. ATP8B1.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006539. P-type_ATPase_IV.
IPR032631. P-type_ATPase_N.
IPR001757. P_typ_ATPase.
IPR032630. P_typ_ATPase_c.
[Graphical view]
PANTHERiPTHR24092. PTHR24092. 2 hits.
PTHR24092:SF48. PTHR24092:SF48. 2 hits.
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF16212. PhoLip_ATPase_C. 1 hit.
PF16209. PhoLip_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAT8B1_MOUSE
AccessioniPrimary (citable) accession number: Q148W0
Secondary accession number(s): Q3U010, Q6R964
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 5, 2009
Last modified: November 30, 2016
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.