ABCG2_DICDI
ID ABCG2_DICDI Reviewed; 1328 AA.
AC Q9NGP5; Q553B7; Q8MXM4;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=ABC transporter G family member 2;
DE AltName: Full=ABC transporter ABCG.2;
GN Name=abcG2; Synonyms=mdra1; ORFNames=DDB_G0275689;
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], FUNCTION, DISRUPTION PHENOTYPE,
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
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: Endosome membrane {ECO:0000269|PubMed:11719559};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11719559}.
CC Note=Associated with the endosome/lysosome system.
CC -!- DEVELOPMENTAL STAGE: Present at low levels in vegetative cells, peaks
CC at roughly 5 hours and decrease by 10 hours. There is another peak of
CC production at 12.5 hours, and a slight increase beginning at 20 hours
CC (at protein level). {ECO:0000269|PubMed:11719559}.
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; AAF72517.2; -; Genomic_DNA.
DR EMBL; AF482381; AAL91486.1; -; Genomic_DNA.
DR EMBL; AAFI02000013; EAL69595.1; -; Genomic_DNA.
DR RefSeq; XP_643503.1; XM_638411.1.
DR AlphaFoldDB; Q9NGP5; -.
DR SMR; Q9NGP5; -.
DR STRING; 44689.DDB0191229; -.
DR PaxDb; Q9NGP5; -.
DR PRIDE; Q9NGP5; -.
DR EnsemblProtists; EAL69595; EAL69595; DDB_G0275689.
DR GeneID; 8620084; -.
DR KEGG; ddi:DDB_G0275689; -.
DR dictyBase; DDB_G0275689; abcG2.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_3_1; -.
DR InParanoid; Q9NGP5; -.
DR OMA; GCTDPFE; -.
DR PhylomeDB; Q9NGP5; -.
DR PRO; PR:Q9NGP5; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005768; C:endosome; IDA:dictyBase.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:dictyBase.
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; ISS:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
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; 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; IPR043926; ABCG_dom.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 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 1: Evidence at protein level;
KW ATP-binding; Endocytosis; Endosome; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1328
FT /note="ABC transporter G family member 2"
FT /id="PRO_0000391391"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1059..1076
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1087..1107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1128..1148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1172..1192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1197..1217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1303..1323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 53..299
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 388..665
FT /note="ABC transmembrane type-2 1"
FT DOMAIN 721..960
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1049..1286
FT /note="ABC transmembrane type-2 2"
FT REGION 670..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 755..762
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1328 AA; 149123 MW; F06FF4B462829BA1 CRC64;
MAPPEIGNDE IPLQEFGQKS FAADNTIGGM QSISYDNSGA PMGLYKEKKG MYVTARNLSM
SIGTEKKGDK RNILSDLNFF LKPGSMVLIL GSPGCGKTSV MKALANQLHS ETVSGSLLFN
GKAANKSTHH RDVAYVVQGD HHMAPFTVRE TFKFSADLQM SEGTSEEEKN ARVDYILKTL
DLTRQQDTVV GNEFLRGVSG GQKKRVTIGV EMVKDAGLFL MDEPSTGLDS TTTLELMKHF
RELSNVNQVS SLVALLQPGV EVTKLFDFLM IMNAGHMVYF GPMSDAISYF EGLGFKLPKH
HNPAEFFQEI VDEPELYFEG EGEPPLRGAE EFANAYKNSA MFQSIVNDLD NTQPDLTFCK
DSSHLPKYPT PLSYQIRLAS IRAFKMLISS QVAVRMRIIK SIVMGLILGS LFYGLDLNQT
DGNNRSGLIF FSLLFIVFSG MGAIAILFEQ REVFYIQKDG KYYKTFAFFL SLIFSEIPIA
LLETVVFCVL VYWMCGLQAN AEKFIYFLLM NFVGDLAFQS FFKMVSAFAP NATLASVIAP
AALAPFILFS GFMAPKRSIG GWWIWIYWIS PIKYAFEGLM SNEHHGLIYS CDDSETIPPR
NTPNFELPYP RGSGNSSICQ ITRGDQFLDQ LGMPQNNWFK WIDLLIVFAF GALFSFGMYF
FLKNVHVDHR ASDPKNDKRS KKASKRSKKI KDSKVDIKEN RMVKAQKEIP IGCYMQWKDL
VYEVDVKKDG KNQRLRLLNE INGYVKPGML LALMGPSGAG KSTLLDVLAN RKTGGHTKGQ
ILINGQERTK YFTRLSAYVE QFDVLPPTQT VKEAILFSAK TRLPSDMPNE EKIKFVENII
ETLNLLKIQN KQIGHGEEGL SLSQRKRVNI GVELASDPQL LFLDEPTSGL DSSAALKVMN
LIKKIASSGR SIICTIHQPS TSIFKQFDHL LLLKRGGETV YFGPTGDKSA DLLGYFENHG
LICDPLKNPA DFILDVTDDV IETTLDGKPH QFHPVQQYKE SQLNSDLLAK IDAGVMPVGT
PVPEFHGVYS SSYQTQFVEL GKRSWLAQVR RVQNIRTRLM RSLFLGVVLG TLFVRMEETQ
ENIYNRVSIL FFSLMFGGMS GMSSIPIVNM ERGVFYREQA SGMYSIPIYL FTFIVTDLPW
VFLSAIIYTV PMYFISGLRL DPNGAPFFYH SFISFTTYFN FSMLAMVFAT VLPTDEIAHA
LGGVALSISS LFAGFMIPPA SIAKGWHWFY QLDPTTYPLA IVMINEFQDL EFHCTSSESV
TIPNVLTVNG TYIDVGPICP ITNGNQILQR YEMKPEDKYK FLAVIFGYSV FFFICIFIAL
KFIRHQTK
