ABCB3_DICDI
ID ABCB3_DICDI Reviewed; 1432 AA.
AC Q8T9W4; Q54E96;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=ABC transporter B family member 3;
DE AltName: Full=ABC transporter ABCB.3;
GN Name=abcB3; ORFNames=DDB_G0291714;
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 ---------------------------------------------------------------------------
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; AF466306; AAL74250.1; -; Genomic_DNA.
DR EMBL; AAFI02000182; EAL61553.1; -; Genomic_DNA.
DR RefSeq; XP_629966.1; XM_629964.1.
DR AlphaFoldDB; Q8T9W4; -.
DR SMR; Q8T9W4; -.
DR STRING; 44689.DDB0201629; -.
DR TCDB; 3.A.1.201.23; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q8T9W4; -.
DR EnsemblProtists; EAL61553; EAL61553; DDB_G0291714.
DR GeneID; 8628296; -.
DR KEGG; ddi:DDB_G0291714; -.
DR dictyBase; DDB_G0291714; abcB3.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_8_1; -.
DR InParanoid; Q8T9W4; -.
DR OMA; RSDANFW; -.
DR PhylomeDB; Q8T9W4; -.
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:Q8T9W4; -.
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:0070730; P:cAMP transport; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
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; 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 3: Inferred from homology;
KW ATP-binding; Coiled coil; Membrane; Nucleotide-binding; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1432
FT /note="ABC transporter B family member 3"
FT /id="PRO_0000391324"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 838..858
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 882..902
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 968..988
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 989..1009
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1060..1080
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1134..1154
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 180..479
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 514..750
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 837..1157
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1192..1428
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 117..163
FT /evidence="ECO:0000255"
FT COMPBIAS 48..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 549..556
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1227..1234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1432 AA; 158191 MW; DDBAF872C3DD5AF4 CRC64;
MDDGNENNEN AQHDEYDEEE IEIPIDEIII EEVDDDHLLE GEGEFQIITQ PSNNNNNSNN
NNFGDIYVSN PNTPRNNNNN NNNNNNNNNN NNNNNNNNSN NSFNNNKKNE VSIGISENTN
ENNNKNNNNN NNNNDDYNDG ADERVKTEEE IKKEAENELN QSVPFLSLFR FADNTDKVLM
FLGTIAAVIN GAAMPTVSLV FGLVVDAFKP TQFNDDPNYD IYDTVRSISF YLLMLGGGVF
VLSYLETTLW MIAGERQTSR IRREYLESTL RQEIGWFDTN KANELSSRIN SDTVLFEEAI
GEKVGRFIHF FSTFVAGFVI GFTKGWQLTL VITSVSPLLA IGGFFTAKMM TQMTKLGQEA
YSRAGGVAEE NIGSIRTVAT FSGEKLAIDK YSNNLKDART VGYKRSFFNG LGLGFVQFVI
LGTYALAFWY GSTLISNKVT NSVSDRPWTG GDVVSVFFAV IIGATSIGQA SPCLALFAQG
RGAAYKIFQV IDRQSKANPF STRGIKPETL SGEIEFKDVG FHYPSRPDVP IFNGFNLKIK
PGQTVGLVGD SGGGKSTIIS LLERFYDPCQ GEILLDGEDI RKFNVRGLRQ KIGLVNQEPV
LFATTISENI RYGKEGATQD EIEEAAKLAN AHSFISQLPQ GYNTLVGEKG VQMSGGQRQR
IAIARAVIKN PNILLLDEST SALDAESTKL VQEALDVLMK GRTTIVIAHN LSTIRNADVI
IYIKKGVAVE RGTHDELMAK QGLYFDLVEK QSHQQMYNLL ENGTRSRRSS TFSAEVNPLL
DSFHVSKRSL RKNESESNKK DKEDSNNKKK KKSNKKKVEE VPMSRVVKYN RPELGLWCFG
FLSAVGTGAV YPGFAMVFTE MLTIFQNPDP NYLTDHANFV ALMFVALAVG AGISNFFQGF
LFSVIGEKLT YRLRRDCFAA IMRQDVGWFD LPENSTGKLT SHLATDAALV QGMTSQRLGI
VLQNILTMVG GLVIAFYSGW QLTLVIIACF PLVVITSKVQ MQILAGFSSK DGCGPAGQVA
SEAISGIRTV ASFTTEKQVV ELYKKQQKGP SSEGIKKAHI SGFAFGFTQL ILFCVYCLSF
WYGGKLVGSG VFGATDKEIS DNCTPQTIPY LWKDYDTCER AQNTIYGFNS MTRVFFAIVM
SAIGVGQASS FAPDLAKAKA AAVSVFKLLD TPSKIDPTTE DGDRIDIVGG DIEFKNLHFS
YPTRPDNSVF RGFTLTLQSG TTTALVGDSG GGKSTCLSLL QRFYNPVVGE IFIDGHNIKN
LNVRHLRHLF GLVGQEPTLF SGTIADNIRY GKHDATQEEI EEASKLSNSH SFIIDLPNGY
NTELGEKYTQ LSGGQKQRIA IARAIIRNPK ILLLDESTSA LDADSTKLVQ EALENVMKGR
TTIVIAHNLL TIQNADCIAY VRAGQIIERG THDELLEAEG PYSQLWYNQQ QK
