ABCG3_DICDI
ID ABCG3_DICDI Reviewed; 1393 AA.
AC Q8T690; Q54KC2;
DT 09-FEB-2010, 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 3;
DE AltName: Full=ABC transporter ABCG.3;
GN Name=abcG3; ORFNames=DDB_G0287461;
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:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; AF482382; AAL91488.1; -; Genomic_DNA.
DR EMBL; AAFI02000101; EAL63696.1; -; Genomic_DNA.
DR RefSeq; XP_637199.1; XM_632107.1.
DR AlphaFoldDB; Q8T690; -.
DR SMR; Q8T690; -.
DR STRING; 44689.DDB0191230; -.
DR PaxDb; Q8T690; -.
DR EnsemblProtists; EAL63696; EAL63696; DDB_G0287461.
DR GeneID; 8626136; -.
DR KEGG; ddi:DDB_G0287461; -.
DR dictyBase; DDB_G0287461; abcG3.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_6_1; -.
DR InParanoid; Q8T690; -.
DR OMA; ACGYFVQ; -.
DR PhylomeDB; Q8T690; -.
DR PRO; PR:Q8T690; -.
DR Proteomes; UP000002195; Chromosome 5.
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:0042626; F:ATPase-coupled transmembrane transporter activity; IGC:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IBA:GO_Central.
DR GO; GO:0031288; P:sorocarp morphogenesis; IBA:GO_Central.
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 InterPro; IPR010929; PDR_CDR_ABC.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF06422; PDR_CDR; 1.
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; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1393
FT /note="ABC transporter G family member 3"
FT /id="PRO_0000391392"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..744
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1122..1142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1157..1177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1206..1226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1235..1255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1265..1285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1364..1384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 100..353
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 473..698
FT /note="ABC transmembrane type-2 1"
FT DOMAIN 783..1035
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1121..1388
FT /note="ABC transmembrane type-2 2"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 828..835
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1393 AA; 156729 MW; 690AA2F084E72E3D CRC64;
MEDKNNIELQ EKAPDNYNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNDIN NNDDDNNKII
YQNPTPASSS HIDSIEIDIN YDLSNHIKQR VTQNKTGMFV SANNISYYIP KSIKKGESEE
LSKLYLLNNI SFTMKPGRMI LLMGIPGAGK SLLLKVLGNR LGKGKIEGEL KFNNHEVDET
THQRDTIFVS QDDRHIALLT VRETLEFSAK CNMGENVSQE EQSERVDLVL DQLGLSHTSN
TIIGNQFFRG ISGGQKRRVT IANEFTKRSP NLILMDEPST GLDSATSYNV ISKVKTIAKE
AKASVMVSLL QPSVELTNLF DDILILGEGG NLIYFGELNN LLPYFSSIGL APLPNQPLAE
FMQEVSVEPS KYMITDKIEL SSKDGGDDES KSLLLGGADS GNVEKMDLVK LFKESELNQK
TIQSMQQLIP SDIKVSDHLI KKLETGDNGK SSVRYELKHL LARHIKVMKI MKMQYAVRFF
QAIFMGCVIG SLFVKMGFTQ ADARNRFGLV YFAMVLHIWT TIGSVEEFFT LRGIFDDQKD
SKYYRNFPYF LSLVITKIPI SLIEAILFSS CCYWIAGFQA RVDNFIVFIL GMALTNLIAQ
GIFQVTSAFT SAQLLASLIC PAIVVLFMIM SGYMISRLQI PGWWIWLNAL SPLRYVIDMV
SSNELYGLEF HCSPMEKIPP SNYPLLNVSY ADGGYQGNQI CQYSTGSDFL NQFGFSDNSY
MRWVDIVIIL GFVCTFFFIF FLGVKYIRFE NKKPPRQIKL KKKKEKKDKK DKEVKHKWNG
CYMTFQNLNY VVPSVKDNKE TGKKEKVTLE LLKDVNGFIV PGMCALMGPS GAGKSTLMDV
LAKRKNVGTI TGDIRINGQL VKDMNITRFT GYVEQQDILS ANLTVREAIE FSANCRLPSS
YLQKDRVKLI DEILSVLSLT KMQNTTIGPN PTLGISLANR KKVSIGIELA SDPHLIFLDE
PTSGLDSSAA LKVMNCVKKI AESGRTVVCT IHQPSQEIFE KFDQLLLLDK GKVIYFGDTG
DNSSTVIQHF TSAGYQYEHG RNPADFILEI AEHPPSTGQS ASDYFKSSIH YSNSIQRLES
KTIVPEGVDV PKYKGKYSAP ATAQLHSLVK RGWLNHVRRP QTILLRFLRS FIPAIVIGTL
FLRLDNDQTG ARNRIALVFL GFLFGGMASI GKVPTIVEDR SVYYRESSAG TYPAHLYILA
SVITDLPMMV LTAFSYWIPM FFLTGLTLGD HGWKFFFSLS VYLLVIMCYD SLATLFALTL
PTIPIAILVS GVGLNFLGLF GGFFIPVNNI PRGWIWMHYL VFSKYGLETL SITELKGEPF
FCEEDQYSII PIAGTNFTKK YCAIQSGDTM LLQYGMNDAY DRQFYNLIIL GGYFCAYTFL
GYLALRFINH MKR
