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Q08201 (MDR2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Multidrug resistance protein 2

EC=3.6.3.44
Alternative name(s):
ATP-binding cassette sub-family B member 4
P-glycoprotein 2
P-glycoprotein 3
Gene names
Name:Abcb4
Synonyms:Mdr2, Pgp3, Pgy2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1278 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 HAX1. Ref.3

Subcellular location

Membrane; Multi-pass membrane protein.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Hax1Q7TSE93EBI-929988,EBI-930005

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12781278Multidrug resistance protein 2
PRO_0000093338

Regions

Topological domain1 – 5454Cytoplasmic Potential
Transmembrane55 – 7521Helical; Potential
Transmembrane119 – 13921Helical; Potential
Transmembrane188 – 20821Helical; Potential
Transmembrane215 – 23521Helical; Potential
Transmembrane296 – 31621Helical; Potential
Transmembrane325 – 34521Helical; Potential
Topological domain346 – 709364Cytoplasmic Potential
Transmembrane710 – 73021Helical; Potential
Transmembrane755 – 77521Helical; Potential
Transmembrane831 – 85121Helical; Potential
Transmembrane852 – 87221Helical; Potential
Transmembrane935 – 95521Helical; Potential
Transmembrane972 – 99221Helical; Potential
Topological domain993 – 1278286Cytoplasmic Potential
Domain54 – 356303ABC transmembrane type-1 1
Domain391 – 627237ABC transporter 1
Domain710 – 998289ABC transmembrane type-1 2
Domain1033 – 1271239ABC transporter 2
Nucleotide binding426 – 4338ATP 1 Potential
Nucleotide binding1068 – 10758ATP 2 Potential
Region622 – 64625Interaction with HAX1

Amino acid modifications

Glycosylation881N-linked (GlcNAc...) Potential
Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation2951N-linked (GlcNAc...) Potential
Glycosylation8071N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q08201 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: D4FB6BE745AF73BF

FASTA1,278140,655
        10         20         30         40         50         60 
MDLEAARNGT ARRLDGDFEL GSISNQSREK KKKVNLIGPL TLFRYSDWQD KLFMLLGTAM 

        70         80         90        100        110        120 
AIAHGSGLPL MMIVFGEMTD KFVDNAGNFS LPVNFSLSML NPGRILEEEM TRYAYYYSGL 

       130        140        150        160        170        180 
GGGVLLAAYI QVSFWTLAAG RQIRKIRQKF FHAILRQEMG WFDIKGTTEL NTRLTDDISK 

       190        200        210        220        230        240 
ISEGIGDKVG MFFQAIATFF AGFIVGFIRG WKLTLVIMAI TAILGLSTAV WAKILSTFSD 

       250        260        270        280        290        300 
KELAAYAKAG AVAEEALGAI RTVIAFGGQN KELERYQKHL ENAKKIGIKK AISANISMGI 

       310        320        330        340        350        360 
AFLLIYASYA LAFWYGSTLV ISKEYTIGNA MTVFFSILIG AFSVGQAAPC IDAFPNARGA 

       370        380        390        400        410        420 
AYVIFDIIDN NPKIDSFSER GHKPDSIKGN LEFSDVHFSY PSRANIKILK GLNLKVKSGQ 

       430        440        450        460        470        480 
TVALVGNSGC GKSTTVQLLQ RLYDPTEGTI SIDGQDIRNF NVRCLREFIG VVSQEPVLFS 

       490        500        510        520        530        540 
TTIAENIRYG RGNVTMDEIK KAVKEANAYD FIMKLPQKFD TLVGDRGAQL SGGQKQRIAI 

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

       610        620        630        640        650        660 
EDGVIVEQGS HSELIKKEGI YFRLVNMQTS GSQILSEEFE VELSDEKAAG GVAPNGWKAR 

       670        680        690        700        710        720 
IFRNSTKKSL KSSRAHQNRL DVETNELDAN VPPVSFLKVL RLNKTEWPYF VVGTLCAIAN 

       730        740        750        760        770        780 
GALQPAFSII LSEMIAIFGP GDDTVKQQKC NMFSLVFLGL GVHSFFTFFL QGFTFGKAGE 

       790        800        810        820        830        840 
ILTTRLRSMA FKAMLRQDMS WFDDHKNSTG ALSTRLATDA AQVQGATGTR LALIAQNTAN 

       850        860        870        880        890        900 
LGTGIIISFI YGWQLTLLLL SVVPFIAVAG IVEMKMLAGN AKRDKKEMEA AGKIATEAIE 

       910        920        930        940        950        960 
NIRTVVSLTQ ERKFESMYVE KLHGPYRNSV RKAHIYGITF SISQAFMYFS YAGCFRFGSY 

       970        980        990       1000       1010       1020 
LIVNGHMRFK DVILVFSAIV LGAVALGHAS SFAPDYAKAK LSAAYLFSLF ERQPLIDSYS 

      1030       1040       1050       1060       1070       1080 
REGMWPDKFE GSVTFNEVVF NYPTRANVPV LQGLSLEVKK GQTLALVGSS GCGKSTVVQL 

      1090       1100       1110       1120       1130       1140 
LERFYDPMAG TVLLDGQEAK KLNVQWLRAQ LGIVSQEPIL FDCSIAKNIA YGDNSRVVSQ 

      1150       1160       1170       1180       1190       1200 
DEIVRAAKEA NIHPFIETLP QKYETRVGDK GTQLSGGQKQ RIAIARALIR QPRVLLLDEA 

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

      1270 
QKGIYFSMVN IQAGTQNL 

« Hide

References

[1]"Cloning and regulation of the rat mdr2 gene."
Brown P.C., Thorgeirsson S.S., Silverman J.A.
Nucleic Acids Res. 21:3885-3891(1993) [PubMed: 8103593] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Fischer.
[2]"Identification of distinct P-glycoprotein gene sequences in rat."
Deuchars K.L., Duthie M., Ling V.
Biochim. Biophys. Acta 1130:157-165(1992) [PubMed: 1348630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1211-1278.
Strain: Sprague-Dawley.
Tissue: Liver.
[3]"Identification of HAX-1 as a protein that binds bile salt export protein and regulates its abundance in the apical membrane of Madin-Darby canine kidney cells."
Ortiz D.F., Moseley J., Calderon G., Swift A.L., Li S., Arias I.M.
J. Biol. Chem. 279:32761-32770(2004) [PubMed: 15159385] [Abstract]
Cited for: INTERACTION WITH HAX1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L15079 mRNA. Translation: AAA02937.1.
X61105 Genomic DNA. Translation: CAA43417.1.
IPIIPI00198519.
PIRS41646.
RefSeqNP_036822.1. NM_012690.1.
UniGeneRn.82691.

3D structure databases

ProteinModelPortalQ08201.
ModBaseSearch...

Protein-protein interaction databases

IntActQ08201. 1 interaction.
STRINGQ08201.

PTM databases

PhosphoSiteQ08201.

Proteomic databases

PRIDEQ08201.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24891.
KEGGrno:24891.
UCSCNM_012690. rat.

Organism-specific databases

CTD5244.
RGD620248. Abcb4.

Phylogenomic databases

eggNOGroNOG07605.
HOVERGENHBG080809.
InParanoidQ08201.
OrthoDBEOG42FSGR.
PhylomeDBQ08201.

Gene expression databases

ArrayExpressQ08201.
GenevestigatorQ08201.
GermOnlineENSRNOG00000029207. Rattus norvegicus.

Family and domain databases

InterProIPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR017940. ABC_transporter_type1.
IPR001140. ABC_transptr_TM_dom.
IPR011527. ABC_transptrTM_dom_typ1.
IPR003593. ATPase_AAA+_core.
[Graphical view]
KOK05659.
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

NextBio604760.

Entry information

Entry nameMDR2_RAT
AccessionPrimary (citable) accession number: Q08201
Secondary accession number(s): Q78E07
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 16, 2011
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families