ABCB2_DICDI
ID ABCB2_DICDI Reviewed; 1397 AA.
AC Q54BT3; Q8T9W5;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=ABC transporter B family member 2;
DE AltName: Full=ABC transporter ABCB.2;
GN Name=abcB2; ORFNames=DDB_G0293438;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NOMENCLATURE.
RC STRAIN=AX4;
RX PubMed=12456012; DOI=10.1128/ec.1.4.643-652.2002;
RA Anjard C., Loomis W.F.;
RT "Evolutionary analyses of ABC transporters of Dictyostelium discoideum.";
RL Eukaryot. Cell 1:643-652(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL74249.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF466305; AAL74249.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AAFI02000210; EAL60721.1; -; Genomic_DNA.
DR RefSeq; XP_629136.1; XM_629134.1.
DR AlphaFoldDB; Q54BT3; -.
DR SMR; Q54BT3; -.
DR STRING; 44689.DDB0201670; -.
DR PaxDb; Q54BT3; -.
DR EnsemblProtists; EAL60721; EAL60721; DDB_G0293438.
DR GeneID; 8629226; -.
DR KEGG; ddi:DDB_G0293438; -.
DR dictyBase; DDB_G0293438; abcB2.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; Q54BT3; -.
DR OMA; LFMLPMT; -.
DR PhylomeDB; Q54BT3; -.
DR Reactome; R-DDI-1369007; Mitochondrial ABC transporters.
DR Reactome; R-DDI-159418; Recycling of bile acids and salts.
DR Reactome; R-DDI-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-DDI-382556; ABC-family proteins mediated transport.
DR Reactome; R-DDI-9754706; Atorvastatin ADME.
DR PRO; PR:Q54BT3; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
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:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 2.
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; 3.
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 3: Inferred from homology;
KW ATP-binding; Coiled coil; Membrane; Nucleotide-binding; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1397
FT /note="ABC transporter B family member 2"
FT /id="PRO_0000391323"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 801..821
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 846..866
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 922..942
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 948..968
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1028..1048
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1101..1121
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 140..438
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 474..710
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 801..1124
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1159..1395
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 37..69
FT /evidence="ECO:0000255"
FT COMPBIAS 7..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 509..516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1194..1201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1397 AA; 153407 MW; C23C6434A3AA2263 CRC64;
MSDKSNDGGE NDSLPMDNIN INSIDDENNN DINNQDDNEN NNNNNNNKNS DDNEENLKDY
KNKKEDFGNI KMDTIDDRPT NNGILSPIDI TSDGGDSVKT LSTTQSKKLD EGEKKEGEVG
PQVPFFSLFR FAKPFDILLM IIGTIGALAN GVSMPAISIV FGRLMNSFSP ENLADPNFDL
VETVTSNAMY FIYIGCGVFV CSYVEVAFWM LAGERQAVRC RKAYLKAILK QEIGWYDVTK
SSELSTRISS DTLLFQEAIG EKIGNFLHHT STFICGFIVG FVNGWQLTLV IFALTPLIAA
AGAFMTKMMA DLTKKGQDAY AKAGGVAEEK IGSIRTVSTF SGEPFEVKRY TERLKEALDI
GTKKGIMNGI GIGLVFLVLF GTYSLSFWYG GKLIVDRKWN PVPDRPWQGG DVLTVFFSVI
MGAMALGQAS PNVASFANGR GAAFKIYEVV DRNSKIDPFS TEGRSIEETV QGNIEYRNIG
FSYPSRPDVK IFNNFNLTIK KGTTVALVGD SGGGKSSVIG LLERFYDPDE GEVYLDGTNI
KEINIHSLRR NIGLVSQEPV LFANSIAENI RYGNENATMD QIIEACKTAN AHDFISALPE
GYDTQVGEKG VQMSGGQKQR IAIARAMIKD PKILLLDEAT SALDSQNELL VQQSIEKLMI
GRTTIVIAHR LSTIQDADQI AVVKGGAIVE IGTHPELYAL NGVYTQLVNR QQKGGDDGDK
KKKKKSKESS KDESNNNIGP SSISIDKSIQ SIGADSLETS TIGLVNDNDN KKKKKKEKKP
QEKSVPIGRI LKLSRGDWPH FLIGLVGATL NGAIMPVFSI IFSEILGIFQ EQDTDELTRR
SRNMALWFIL LAVVAALANF IQIYCFTFIG EKLTFNLRRL SFESIMRQDI GWFDLTENST
GRLTANLATE ATLVQGMTSQ RLGLLIQNIV TIVAGLVIAF VSGWKLTLVV LACVPVIGFA
GKVEMDFFQG FSQKGKEAYA ECGQVASEAI GGIRTVSSFT CENKILEKFR QCLQKPIQMS
FRKSNVSGLS FGFSQCTLFF IYTLTYWYGG KLVDSGEWPA KESTLETYCY NGEYANIGYT
DEATCIKSFT TTEGFSMMMR VFFAIIMSAM GVGQSMAFMP DLGKAKLAAV AIFSLIDRVS
EIDPFENKGQ TLPEFKGDIE FKDIKFSYPS RPNKAVFQGF NLVIPHGKKV ALVGNSGGGK
SSVISLLERF YNPSQGSITI DGVNIKDLNL NWLRGNMGLV GQEPFLFSGT IFENIIYGKP
DATMDEVVEA AKAANAHTFI ESLPDAYHTQ LGDKFTQLSG GQKQRVAIAR AIIRNPKVLL
LDEATSALDT VSEKVVQVAL DNVSKGRTSI VIAHRLSTVI DADLIVVVKE GKVVELGTHE
TLLAENGFYA ELVSRQM
