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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
 
 
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