ID   ABCGO_DICDI             Reviewed;        1159 AA.
AC   Q54T02;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=ABC transporter G family member 24;
DE   AltName: Full=ABC transporter ABCG.24;
GN   Name=abcG24; ORFNames=DDB_G0282103;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
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:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC       Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000045; EAL66377.1; -; Genomic_DNA.
DR   RefSeq; XP_640353.1; XM_635261.1.
DR   AlphaFoldDB; Q54T02; -.
DR   SMR; Q54T02; -.
DR   STRING; 44689.DDB0216383; -.
DR   PaxDb; Q54T02; -.
DR   EnsemblProtists; EAL66377; EAL66377; DDB_G0282103.
DR   GeneID; 8623408; -.
DR   KEGG; ddi:DDB_G0282103; -.
DR   dictyBase; DDB_G0282103; abcG24.
DR   eggNOG; KOG0061; Eukaryota.
DR   HOGENOM; CLU_000604_57_1_1; -.
DR   InParanoid; Q54T02; -.
DR   OMA; FGSNNYY; -.
DR   PhylomeDB; Q54T02; -.
DR   Reactome; R-DDI-1369062; ABC transporters in lipid homeostasis.
DR   Reactome; R-DDI-8964058; HDL remodeling.
DR   PRO; PR:Q54T02; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR   GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
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; IPR000742; EGF-like_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01061; ABC2_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS00022; EGF_1; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Membrane; Nucleotide-binding; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1159
FT                   /note="ABC transporter G family member 24"
FT                   /id="PRO_0000391407"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        909..929
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        937..957
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1005..1025
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1047..1067
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1074..1094
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1135..1155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          454..707
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          902..1154
FT                   /note="ABC transmembrane type-2"
FT   REGION          752..846
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..782
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        821..837
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         497..504
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   1159 AA;  129912 MW;  08E543893149191E CRC64;
     MIIFKNNEIR FNSILKSILL LLLLFINGNN CKTAQQFLDE NFNHALFREH QLEKEYKTKQ
     LVKDDPNMYS DWTEVPAATA EAVTIMRGDD YYYDYDKEQK IEMIVFGSEN AISSGSAQNY
     WYGQTCEATN FNNTPTTTCP NDCHSYWGQG QCNETSSTCI CNYFFIGDDC SENVDPQHNW
     DKMNCNGGRY CPPIYNYPTP RSCVCPPGQA GLECTVCLNN EGCQALTGNY SSSFECNSSP
     YTYFEKSYSC VVTSAEVNGD LNNSTASASI DCQFPGGNYN TQTGVCSMNL YYRIHGSPLY
     FNCSFTECDR TILPGQNQSI VCQNSVCNCT TYCGFILDGL ISAVTGEATF ECGAQTNPDG
     TSNCLFSQYT INQMLPAIPL QCMSGECIDV ATGAPTPPPI YPVPVASMSF LYIYVGSGVG
     FIGLTLLIGA IFLIFSLQED RKNFKEDTHL VCELSFHNIS CYVNERSGFF GKDVKRKQIL
     DNVNGVCPPG QLTALMGLSG SGKTSLLDIL SGRKNVGNID GKVLINGAPV GKNFKRISGY
     VTQDDIQIGT LTCREHLMFA ALLKLPENMS LEIKQQRVAS VLEELGLTRV ADNPIGTSEK
     RGISGGERRR LSIATELIVD PSILFIDEPT SGLDSHSASE LITKLKQLAN NSTKGQRTII
     FSIHQPSAEL FEQFDNLILL HQGNPYFSGK REDSVNYFIK QKIAGMTEFE QQNYRMHLKN
     PADFIISMVT DKNCQRFNST YVDSRVASPF YQSTSPALSS NSNNSDINLN HHRIINNPHN
     QNIHHQQHHH HHRHIYGING PSIDNNDSDS DSDERDHLLA SDNINNNNNN NKVKNNDNNN
     KNNDDDVEDI EEASPIIVVG NQGEPLASHI KIGKVEEYAT SFWTQFFVVC RRSLLNYMRN
     PFLLRTTYFV HIFVGLTLGY LFWKLPANLE PGCQNRFGAM FFMTALLSFG SITSLDLFYN
     DRIIFIRERA NGFYRTSAYF LAKVVTDIIP MRVIPPIILG SICYYMIGLR PGILHFIYFL
     ISLVLTSTVA SSMCMAISTI SPTFGTANMV SILLLFVFLL FDGFLLARSS IPKYLIGLVW
     ISFMSYGLEI PVVNEFNGLW IEYNPPNTRP TYADGLEFLS TIGANPNRLF TDMYVLLGMI
     VGYLLLAYVF LRFLVREYR