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P06795 (MDR1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Multidrug resistance protein 1B

EC=3.6.3.44
Alternative name(s):
ATP-binding cassette sub-family B member 1B
P-glycoprotein 1
CD_antigen=CD243
Gene names
Name:Abcb1b
Synonyms:Abcb1, Mdr1, Mdr1b, Pgy1, Pgy1-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1276 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells.

Catalytic activity

ATP + H2O + xenobiotic(In) = ADP + phosphate + xenobiotic(Out).

Subunit structure

Interacts with PSMB5 By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Post-translational modification

Several phosphorylated serine residues are present in the linker domain.

Miscellaneous

In mouse the MDR gene family includes three or more related but distinct cellular genes.

Sequence similarities

Belongs to the ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily. [View classification]

Contains 2 ABC transmembrane type-1 domains.

Contains 2 ABC transporter domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12761276Multidrug resistance protein 1B
PRO_0000093334

Regions

Topological domain1 – 4343Cytoplasmic By similarity
Transmembrane44 – 6623Helical; Potential
Topological domain67 – 11549Extracellular By similarity
Transmembrane116 – 13621Helical; Potential
Topological domain137 – 18549Cytoplasmic By similarity
Transmembrane186 – 20722Helical; Potential
Topological domain208 – 2147Extracellular By similarity
Transmembrane215 – 23521Helical; Potential
Topological domain236 – 29358Cytoplasmic By similarity
Transmembrane294 – 31522Helical; Potential
Topological domain316 – 32914Extracellular By similarity
Transmembrane330 – 35122Helical; Potential
Topological domain352 – 709358Cytoplasmic By similarity
Transmembrane710 – 73021Helical; Potential
Topological domain731 – 75424Extracellular By similarity
Transmembrane755 – 77521Helical; Potential
Topological domain776 – 83055Cytoplasmic By similarity
Transmembrane831 – 85121Helical; Potential
Topological domain8521Extracellular By similarity
Transmembrane853 – 87220Helical; Potential
Topological domain873 – 93260Cytoplasmic By similarity
Transmembrane933 – 95523Helical; Potential
Topological domain956 – 97116Extracellular By similarity
Transmembrane972 – 99322Helical; Potential
Topological domain994 – 1276283Cytoplasmic By similarity
Domain50 – 356307ABC transmembrane type-1 1
Domain391 – 627237ABC transporter 1
Domain709 – 998290ABC transmembrane type-1 2
Domain1033 – 1271239ABC transporter 2
Nucleotide binding426 – 4338ATP 1 By similarity
Nucleotide binding1068 – 10758ATP 2 By similarity

Amino acid modifications

Modified residue6411Phosphotyrosine Ref.4
Modified residue6591Phosphoserine Ref.4
Glycosylation731N-linked (GlcNAc...) Potential
Glycosylation911N-linked (GlcNAc...) Potential
Glycosylation961N-linked (GlcNAc...) Potential
Glycosylation1031N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P06795 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 1804D0F011B0FF4E

FASTA1,276140,994
        10         20         30         40         50         60 
MEFEENLKGR ADKNFSKMGK KSKKEKKEKK PAVGVFGMFR YADWLDKLCM ILGTLAAIIH 

        70         80         90        100        110        120 
GTLLPLLMLV FGNMTDSFTK AEASILPSIT NQSGPNSTLI ISNSSLEEEM AIYAYYYTGI 

       130        140        150        160        170        180 
GAGVLIVAYI QVSLWCLAAG RQIHKIRQKF FHAIMNQEIG WFDVHDVGEL NTRLTDDVSK 

       190        200        210        220        230        240 
INDGIGDKIG MFFQSITTFL AGFIIGFISG WKLTLVILAV SPLIGLSSAL WAKVLTSFTN 

       250        260        270        280        290        300 
KELQAYAKAG AVAEEVLAAI RTVIAFGGQQ KELERYNKNL EEAKNVGIKK AITASISIGI 

       310        320        330        340        350        360 
AYLLVYASYA LAFWYGTSLV LSNEYSIGEV LTVFFSILLG TFSIGHLAPN IEAFANARGA 

       370        380        390        400        410        420 
AFEIFKIIDN EPSIDSFSTK GYKPDSIMGN LEFKNVHFNY PSRSEVQILK GLNLKVKSGQ 

       430        440        450        460        470        480 
TVALVGNSGC GKSTTVQLMQ RLYDPLEGVV SIDGQDIRTI NVRYLREIIG VVSQEPVLFA 

       490        500        510        520        530        540 
TTIAENIRYG REDVTMDEIE KAVKEANAYD FIMKLPHQFD TLVGERGAQL SGGQKQRIAI 

       550        560        570        580        590        600 
ARALVRNPKI LLLDEATSAL DTESEAVVQA ALDKAREGRT TIVIAHRLST VRNADVIAGF 

       610        620        630        640        650        660 
DGGVIVEQGN HDELMREKGI YFKLVMTQTR GNEIEPGNNA YGSQSDTDAS ELTSEESKSP 

       670        680        690        700        710        720 
LIRRSIYRSV HRKQDQERRL SMKEAVDEDV PLVSFWRILN LNLSEWPYLL VGVLCAVING 

       730        740        750        760        770        780 
CIQPVFAIVF SRIVGVFSRD DDHETKRQNC NLFSLFFLVM GLISFVTYFF QGFTFGKAGE 

       790        800        810        820        830        840 
ILTKRVRYMV FKSMLRQDIS WFDDHKNSTG SLTTRLASDA SSVKGAMGAR LAVVTQNVAN 

       850        860        870        880        890        900 
LGTGVILSLV YGWQLTLLLV VIIPLIVLGG IIEMKLLSGQ ALKDKKQLEI SGKIATEAIE 

       910        920        930        940        950        960 
NFRTIVSLTR EQKFETMYAQ SLQVPYRNAM KKAHVFGITF SFTQAMMYFS YAACFRFGAY 

       970        980        990       1000       1010       1020 
LVAQQLMTFE NVMLVFSAVV FGAMAAGNTS SFAPDYAKAK VSASHIIRII EKTPEIDSYS 

      1030       1040       1050       1060       1070       1080 
TEGLKPTLLE GNVKFNGVQF NYPTRPNIPV LQGLSLEVKK GQTLALVGSS GCGKSTVVQL 

      1090       1100       1110       1120       1130       1140 
LERFYDPMAG SVFLDGKEIK QLNVQWLRAH LGIVSQEPIL FDCSIAENIA YGDNSRAVSH 

      1150       1160       1170       1180       1190       1200 
EEIVRAAKEA NIHQFIDSLP DKYNTRVGDK GTQLSGGQKQ RIAIARALVR QPHILLLDEA 

      1210       1220       1230       1240       1250       1260 
TSALDTESEK VVQEALDKAR EGRTCIVIAH RLSTIQNADL IVVIENGKVK EHGTHQQLLA 

      1270 
QKGIYFSMVQ AGAKRS 

« Hide

References

« Hide 'large scale' references
[1]"Mammalian multidrug resistance gene: complete cDNA sequence indicates strong homology to bacterial transport proteins."
Gros P., Croop J., Housman D.
Cell 47:371-380(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Mammalian multidrug-resistance gene: correlation of exon organization with structural domains and duplication of an ancestral gene."
Raymond M., Gros P.
Proc. Natl. Acad. Sci. U.S.A. 86:6488-6492(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cell-specific activity of cis-acting regulatory elements in the promoter of the mouse multidrug resistance gene mdr1."
Raymond M., Gros P.
Mol. Cell. Biol. 10:6036-6040(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[4]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-641 AND SER-659, MASS SPECTROMETRY.
Tissue: Macrophage.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14757 mRNA. Translation: AAA79005.1.
M60348 Genomic DNA. Translation: AAA39513.1.
IPIIPI00128152.
PIRDVMS1. A33719.
RefSeqNP_035205.1. NM_011075.2.
UniGeneMm.146649.
Mm.389059.

3D structure databases

ProteinModelPortalP06795.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000009058.

PTM databases

PhosphoSiteP06795.

Proteomic databases

PaxDbP06795.
PRIDEP06795.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000009058; ENSMUSP00000009058; ENSMUSG00000028970.
GeneID18669.
KEGGmmu:18669.

Organism-specific databases

CTD18669.
MGIMGI:97568. Abcb1b.

Phylogenomic databases

eggNOGCOG1132.
GeneTreeENSGT00530000062896.
HOVERGENHBG080809.
InParanoidP06795.
KOK05658.
OMAACIPPSI.
OrthoDBEOG42FSGR.

Enzyme and pathway databases

SABIO-RKP06795.

Gene expression databases

ArrayExpressP06795.
BgeeP06795.
GenevestigatorP06795.
GermOnlineENSMUSG00000028970. Mus musculus.

Family and domain databases

InterProIPR003593. AAA+_ATPase.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR017940. ABC_transporter_type1.
IPR001140. ABC_transptr_TM_dom.
IPR011527. ABC_transptrTM_dom_typ1.
[Graphical view]
PfamPF00664. ABC_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMSSF90123. ABC_TM_1. 2 hits.
PROSITEPS50929. ABC_TM1F. 2 hits.
PS00211. ABC_TRANSPORTER_1. 2 hits.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP06795.
ChEMBLCHEMBL3467.
NextBio294678.
SOURCESearch...

Entry information

Entry nameMDR1B_MOUSE
AccessionPrimary (citable) accession number: P06795
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: April 3, 2013
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families