ABCGI_DICDI
ID ABCGI_DICDI Reviewed; 1476 AA.
AC Q8ST66; Q553B8; Q8MXM5; Q965D3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=ABC transporter G family member 18;
DE AltName: Full=ABC transporter ABCG.18;
DE AltName: Full=ABC transporter mdrA2;
GN Name=abcG18; Synonyms=mdra2; ORFNames=DDB_G0275687;
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], DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11719559; DOI=10.1242/jcs.114.21.3923;
RA Brazill D.T., Meyer L.R., Hatton R.D., Brock D.A., Gomer R.H.;
RT "ABC transporters required for endocytosis and endosomal pH regulation in
RT Dictyostelium.";
RL J. Cell Sci. 114:3923-3932(2001).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [4]
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 -!- FUNCTION: Required for endocytosis and endosomal pH regulation.
CC {ECO:0000269|PubMed:11719559}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells that have a abcG2-abcG18 disruption have an
CC endocytosis rate roughly 70% that of wild-type (or rtoA disrupted
CC cells). Disruption on abcG2-abcG18-rtoA cells have an endocytosis rate
CC roughly 20% that of wild-type. The exocytosis rates of abcG2-abcG18 and
CC abcG2-abcG18-rtoA disrupted cells are roughly that of wild-type; abcG2-
CC abcG18 endosomes have an unusually high pH, whereas abcG2-abcG18-rtoA
CC endosomes have an almost normal pH. {ECO:0000269|PubMed:11719559}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR EMBL; AF246689; AAK69777.1; -; Genomic_DNA.
DR EMBL; AF482381; AAL91487.1; -; Genomic_DNA.
DR EMBL; AAFI02000013; EAL69594.1; -; Genomic_DNA.
DR RefSeq; XP_643502.1; XM_638410.1.
DR AlphaFoldDB; Q8ST66; -.
DR SMR; Q8ST66; -.
DR STRING; 44689.DDB0185012; -.
DR PaxDb; Q8ST66; -.
DR EnsemblProtists; EAL69594; EAL69594; DDB_G0275687.
DR GeneID; 8620083; -.
DR KEGG; ddi:DDB_G0275687; -.
DR dictyBase; DDB_G0275687; abcG18.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; Q8ST66; -.
DR OMA; SIFHWQD; -.
DR PhylomeDB; Q8ST66; -.
DR PRO; PR:Q8ST66; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IGI:dictyBase.
DR GO; GO:0006897; P:endocytosis; IGI:dictyBase.
DR GO; GO:0048388; P:endosomal lumen acidification; IGI:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Endocytosis; Membrane; Nucleotide-binding; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1476
FT /note="ABC transporter G family member 18"
FT /id="PRO_0000330366"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1211..1228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1239..1259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1290..1310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1324..1344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1349..1369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1448..1468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 69..312
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 445..722
FT /note="ABC transmembrane type-2 1"
FT DOMAIN 814..1053
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1201..1471
FT /note="ABC transmembrane type-2 2"
FT REGION 743..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 848..855
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 18
FT /note="R -> G (in Ref. 1; AAK69777)"
FT /evidence="ECO:0000305"
FT CONFLICT 1122
FT /note="S -> R (in Ref. 1; AAK69777)"
FT /evidence="ECO:0000305"
FT CONFLICT 1350
FT /note="A -> G (in Ref. 1; AAK69777)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1476 AA; 166508 MW; D729985CE02821A7 CRC64;
MENEEKREYL AKSRSNSRNF LNDSIESKNI FGVDKKSEPN LKQSIDGGLN FSTTSSYNPS
NLPRTSVFVS ARNLSSTVGH GKNEKKILTD LNFFLKPGSM VLLLGSPGCG KTSLMNTLAL
LTSNEKITGN LLFNGKTGDP NTHHRHVSYV VQDDFHMAPL TVRDTFKFSA DCQSGDKSEK
ERIEIVDNVL DFLDLKHVQN TVVGDEFLRG ISGGQKKRVT IGVELVKESN LLLMDEPTNG
LDSSISLEML TKIKNKVQQE KMSCLISLLQ PGLEITKLFD YLMIMNQGQM SYFGPMNQAI
GYFEGLGFKF PKHHNPAEFF QEIVDEPELY CGIDDGSSDG GSGDSGSSSG GSNYNYNFKN
KASSTMMMMN NNNKIIPPLK GSDEFAMAYR KSIIYKHILE YIDSHIPDEE ERSKFIDYST
TLKPYSTGFG RQLSLNVKRG FKLFLGNKAS IRLRLLKNVI IGFILGTLYW KLDTTQADGS
NRSGLLFFSL LTFVFGGFGS ISVFFDQRQV FYSERAWKYY NTITYFLSMI VTDLPMSIVE
VLIFSNFVYW MTGLNKTWDR FIYFFLTCLV CDVMSLSIIR SVCSFTKTKY AASAISPAVV
SPFILMCGYM KHSNEIPGWW IWLYWISPIH YGFEGLLLNE HSGLDYHCSP DELMPPSFLP
TFNTSYPVGF EGNQVCPITK GEQILDSIGF HTEFYYRWVD LAIISAFTLL FWLITLVCMK
FLVFRVYRKD PVGIKKSKPN KTTTLIKMNR NSTDSTTTNN SMNYFNNKHN KKQNDDSDSG
EEMESVDVDV KSSGKANLRK DIPIGCYMQW KDLVYEVDVK KDGKNQRLRL LNGINGYVKP
GMLVALMGPS GAGKSTLLDV LANRKTGGHT KGQILINGQE RTKYFTRTSA YVEQMDILTP
VSTVREVILF SAKNRLPNSV PIQEKEEFVD NILETLNLLK IQHSLIGDVE SGLSLSQRKR
VNMGIELASD PQLLFLDEPT SGLDSSAALK VMNLIKKIAS SGRSVICTIH QPSTTIFKKF
DHLLLLKRGG ETVYFGPTGT NSKIVLNYFA ERGLICDPFK NPADFILDVT EDIIEIIQPP
QTLPTSTSNE NNNNNNNNNN NNNNNNNNNN NNNNNNNNGN TSDTLNNNNK KNLESSLSSS
SISFDPVESF KESKENQKLL SIVENSIMPV GTPVAVYHGK YSSTIKTQFI ELLKRSWKGG
IRRVDTIRTR VGRSFVLGLV IGTLFLRLDK EQNDVFNRIS FLFFSLMFGG MAGLSIIPTV
STERGVFYRE QASGMYRVWI YYLTFVLSDL PFVIITSYAY VIPVYFLTGL SLSNHGWDFF
YHSFISVMLY LNFGLTSIAF ATSLPVEEMA FLLNGVLLSV TSLFAGFMIP PPSMPAAWKW
AFYLDFISYP LKAFLITEFK DMEFVCTDNK GAIPIPIPSQ NTTKFFCPIT HGTQVLDRID
YKISFQYWDI LIMASFTFAL LVGGYLSLKF IRYQNK
