ABCB5_MOUSE
ID ABCB5_MOUSE Reviewed; 1255 AA.
AC B5X0E4; W5QLL5;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=ATP-binding cassette sub-family B member 5 {ECO:0000305};
DE AltName: Full=ABCB5 P-gp;
DE AltName: Full=P-glycoprotein ABCB5;
DE EC=7.6.2.2 {ECO:0000250|UniProtKB:Q2M3G0};
GN Name=Abcb5 {ECO:0000312|MGI:MGI:1924956};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, DISRUPTION
RP PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=25030174; DOI=10.1038/nature13426;
RA Ksander B.R., Kolovou P.E., Wilson B.J., Saab K.R., Guo Q., Ma J.,
RA McGuire S.P., Gregory M.S., Vincent W.J., Perez V.L., Cruz-Guilloty F.,
RA Kao W.W., Call M.K., Tucker B.A., Zhan Q., Murphy G.F., Lathrop K.L.,
RA Alt C., Mortensen L.J., Lin C.P., Zieske J.D., Frank M.H., Frank N.Y.;
RT "ABCB5 is a limbal stem cell gene required for corneal development and
RT repair.";
RL Nature 511:353-357(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Energy-dependent efflux transporter responsible for decreased
CC drug accumulation in multidrug-resistant cells (By similarity).
CC Specifically present in limbal stem cells, where it plays a key role in
CC corneal development and repair (PubMed:25030174).
CC {ECO:0000250|UniProtKB:Q2M3G0, ECO:0000269|PubMed:25030174}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + daunorubicin(in) + H2O = ADP + daunorubicin(out) + H(+)
CC + phosphate; Xref=Rhea:RHEA:33147, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64677, ChEBI:CHEBI:456216; EC=7.6.2.2;
CC Evidence={ECO:0000250|UniProtKB:Q2M3G0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33148;
CC Evidence={ECO:0000250|UniProtKB:Q2M3G0};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25030174};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
CC ECO:0000269|PubMed:25030174}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B5X0E4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B5X0E4-2; Sequence=VSP_056757;
CC -!- TISSUE SPECIFICITY: In developing eye, expressed in basal limbal
CC epithelium but not in central cornea. Acts as a marker of limbal stem
CC cells. {ECO:0000269|PubMed:25030174}.
CC -!- DISRUPTION PHENOTYPE: Defects in corneal development. While eyes
CC contain all anterior and posterior segment components, corneas show
CC developmental abnormalities characterized by decreased cellularity of
CC the apical epithelial layer and disorganized basal and wing cell
CC layers. Defects are due to depletion of quiescent limbal stem cells,
CC leading to enhanced proliferation and apoptosis, and resulting in
CC defective corneal differentiation and wound healing.
CC {ECO:0000269|PubMed:25030174}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY766239; AAX11686.1; -; mRNA.
DR EMBL; JQ655148; AFS60113.1; -; mRNA.
DR EMBL; AC126277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49198.1; -. [B5X0E4-1]
DR RefSeq; NP_084237.1; NM_029961.2. [B5X0E4-1]
DR AlphaFoldDB; B5X0E4; -.
DR SMR; B5X0E4; -.
DR BioGRID; 218862; 2.
DR IntAct; B5X0E4; 1.
DR STRING; 10090.ENSMUSP00000046177; -.
DR GlyGen; B5X0E4; 11 sites.
DR iPTMnet; B5X0E4; -.
DR PhosphoSitePlus; B5X0E4; -.
DR jPOST; B5X0E4; -.
DR MaxQB; B5X0E4; -.
DR PaxDb; B5X0E4; -.
DR PRIDE; B5X0E4; -.
DR ProteomicsDB; 286045; -. [B5X0E4-1]
DR ProteomicsDB; 286046; -. [B5X0E4-2]
DR Antibodypedia; 11940; 423 antibodies from 38 providers.
DR Ensembl; ENSMUST00000035515; ENSMUSP00000046177; ENSMUSG00000072791. [B5X0E4-1]
DR GeneID; 77706; -.
DR KEGG; mmu:77706; -.
DR UCSC; uc007pij.2; mouse. [B5X0E4-1]
DR CTD; 340273; -.
DR MGI; MGI:1924956; Abcb5.
DR VEuPathDB; HostDB:ENSMUSG00000072791; -.
DR eggNOG; KOG0055; Eukaryota.
DR GeneTree; ENSGT00940000161340; -.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; B5X0E4; -.
DR OMA; FGYMQIS; -.
DR PhylomeDB; B5X0E4; -.
DR TreeFam; TF105193; -.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR BioGRID-ORCS; 77706; 2 hits in 72 CRISPR screens.
DR PRO; PR:B5X0E4; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; B5X0E4; protein.
DR Bgee; ENSMUSG00000072791; Expressed in morula and 7 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell membrane; Differentiation;
KW Glycoprotein; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1255
FT /note="ATP-binding cassette sub-family B member 5"
FT /id="PRO_0000430433"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 694..714
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 814..836
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 841..863
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 955..975
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 51..351
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 387..623
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 694..981
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1016..1254
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 422..429
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1051..1058
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1036
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..525
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:25030174"
FT /id="VSP_056757"
FT CONFLICT 564
FT /note="V -> I (in Ref. 1; AFS60113)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1255 AA; 137397 MW; 481BA90341116BC6 CRC64;
MANSERTNGL QETNQRYGPL QEQVPKVGNQ AVGPIEIFRF ADNLDIVLMT LGILASMING
ATVPLMSLVL GEISDHLING CLVQTNRTKY QNCSQTQEKL NEDIIVLTLY YIGIGAAALI
FGYVQISFWV ITAARQTTRI RKQFFHSILA QDISWFDGSD ICELNTRMTG DINKLCDGIG
DKIPLMFQNI SGFSIGLVIS LIKSWKLSLV VLSTSPLIMA SSALCSRMII SLTSKELDAY
SKAGAVAEEA LSSIQTVTAF GAQEKEIQRY TQHLKDAKDA GIKRATASKL SLGAVYFFMN
GAYGLAFWYG TSLIFGGEPG YTIGTILAVF FSVIHSSYCI GSVAPHLETF TVARGAAFNI
FQVIDKKPNI DNFSTAGFVP ECIEGNIEFK NVSFSYPSRP SAKVLKGLNL KIKAGETVAL
VGPSGSGKST TVQLLQRLYD PEDGCITVDE NDIRAQNVRH YREQIGVVRQ EPVLFGTTIG
NNIKFGREGV GEKEMEQAAR EANAYDFIMA FPKKFNTLVG EKGAQMSGGQ KQRIAIARAL
VRNPKILILD EATSALDTES ESLVQTALEK ASKGRTTIVV AHRLSTIRGA DLIVTMKDGM
VVEKGTHAEL MAKQGLYYSL AMAQDIKKVD EQMESRTCST AGNASYGSLC DVNSAKAPCT
DQLEEAVHHQ KTSLPEVSLL KIFKLSKSEW PFVVLGTLAS ALNGSVHPVF SIIFGKLVTM
FEDKNKATLK QDAELYSMML VVLGIVALVT YLMQGLFYGR AEENLAMRLR HSAFKAMLYQ
DMAWYDDKEN NTGALTTTLA VDVAQIQGAA TSRLGIVTQD VSNMSLSILI SFIYGWEMTL
LILSFAPVLA VTGMIQTAAM AGFANRDKQA LKRAGKIATE AVENIRTVVS LTRERAFEQM
YEETLQTQHR NALKRAHITG CCYAVSHAFV HFAHAAGFRF GAYLIQAGRM MPEGMFIVFT
AIAYGAMAIG ETLVWAPEYS KAKAGASHLF ALLKNKPTIN SCSQSGEKPD TCEGNLEFRE
VSFVYPCRPE VPVLQNMSLS IEKGKTVAFV GSSGCGKSTC VQLLQRFYDP MKGQVLLDGV
DVKELNVQWL RSQTAIVSQE PVLFNCSIAE NIAYGDNSRM VPLEEIKEVA DAANIHSFIE
GLPRKYNTLV GLRGVQLSGG QKQRLAIARA LLRKPKILLL DEATSALDNE SEKVVQQALD
KARRGKTCLV VAHRLSTIQN ADMIVVLQNG SIKEQGTHQE LLRNGDTYFK LVAAH
