ABCC3_DICDI
ID ABCC3_DICDI Reviewed; 1412 AA.
AC Q54JR2; Q8T6H6;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=ABC transporter C family member 3;
DE AltName: Full=ABC transporter ABCC.3;
GN Name=abcC3; ORFNames=DDB_G0287691;
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:0000255|PROSITE-ProRule:PRU00441};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; AF474335; AAL85706.1; -; Genomic_DNA.
DR EMBL; AAFI02000104; EAL63492.1; -; Genomic_DNA.
DR RefSeq; XP_637090.1; XM_631998.1.
DR AlphaFoldDB; Q54JR2; -.
DR SMR; Q54JR2; -.
DR STRING; 44689.DDB0216251; -.
DR PaxDb; Q54JR2; -.
DR EnsemblProtists; EAL63492; EAL63492; DDB_G0287691.
DR GeneID; 8626345; -.
DR KEGG; ddi:DDB_G0287691; -.
DR dictyBase; DDB_G0287691; abcC3.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q54JR2; -.
DR OMA; WEPSYQR; -.
DR PhylomeDB; Q54JR2; -.
DR Reactome; R-DDI-189483; Heme degradation.
DR Reactome; R-DDI-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR Reactome; R-DDI-2142850; Hyaluronan biosynthesis and export.
DR Reactome; R-DDI-382556; ABC-family proteins mediated transport.
DR Reactome; R-DDI-9707564; Cytoprotection by HMOX1.
DR Reactome; R-DDI-9748787; Azathioprine ADME.
DR Reactome; R-DDI-9749641; Aspirin ADME.
DR Reactome; R-DDI-9753281; Paracetamol ADME.
DR Reactome; R-DDI-9754706; Atorvastatin ADME.
DR Reactome; R-DDI-9758890; Transport of RCbl within the body.
DR PRO; PR:Q54JR2; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 1.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 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..1412
FT /note="ABC transporter C family member 3"
FT /id="PRO_0000363849"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 724..744
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 854..874
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 875..895
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 967..987
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 119..405
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 439..662
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 735..1025
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1062..1296
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 474..481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1096..1103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 191..212
FT /note="Missing (in Ref. 1; AAL85706)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1412 AA; 158111 MW; 7742BD1171062F36 CRC64;
MELEEVGVEA NQPNNDQGSK KQNKNKDKKV KKEKKIGYGG KKSAEENSNF ISWLTFSWAD
RFVVHCFRHV LQLSHIWDLA SYDKSAYLAE KIAISWDVEI KKPKPSYIRA AFRAFGLYFV
LSWFFYAIYA ASQFVGPEIL KRMVTFVLKS RSGISTEDPN MGYYYALIMF GSAMIGSVCL
YQSNMISART GDRLRSVIVL DVYRKAIKLS NSARANTSPG EIVNLMSNDA QRMVEVFQLV
NNGVFALPQI IVCLALLYRA IGWPTFVGLG LMLAAVPFNG IAAKKLTEIR RHLVGFTDKR
VKTTNEILQA IKIIKLYAWE DSFAKKVIER REAEIKLLFS FSRYRAMLIV IVAALPTAVS
VLVFSSYYGY YKKLDAGEIF AALSYLNILR LPLGFLPIIV ALGIQMKIAA QRVTDFLLLP
EMKEISKIED PSIENGIYIR DATLTWNQEK KEESFTLKNI NFEAKGKTLT MIVGSVGSGK
SSLIQAMLGE MDVLDGSVAM KGNVAYVPQQ AWIINATLKD NILFGSPYDE AKYRKVLEVC
ALERDIELFP QGDLVEIGER GVNLSGGQKQ RVSIARAVYS DSDVYILDDP LSAVDAHVGK
HLFHRCFKGI LKSKTVILAA NQLNYLPFAH NTVVLKAGEI SERGSYQQLI NAQKEFSGLL
QAYGVDESAV NEDVEDDKEI EESDNIVVEE KTKPTEKPKL QNKDGVLTSQ EEREEGAVAM
WVYWKYITVG GGFLFLMAFI FFLMDTGTRT FVDWWLSHWQ NESTKNALAV AQGLEPSGLT
DTQYLGIYIG VGMTSILISA GRNFLFFEYT VRASRALHHQ LFNALLRAPM SFFDTTPLGR
IINRFTRDLD GVDNLMATSI SQFLVFFTTV VATLIIISII TPFLLVPLAP ICIIFYFLQF
FYRYTSRELQ RLEAISRSPI FSHFSETLGG VVSIRAYRKK EENILTNQFR LDNNNKCYLT
LQAMNQWLGL RLDLLANLVT FFACLFITID RDTISAANVG LSLSYALSLT GNLNRATLQA
ADTETKMNSV ERITHYIKGP VEALQIVEDH RPAPDWPPHG AITFDNLVMR YREGLDPVLK
GISCEIKAKE KIGIVGRTGA GKSSIVLALF RLIEASEGAI LIDGENIAKF GLKDLRRNLA
IIPQDPVLFS GTLRENIDPF NEKTDDQLWS VLKDIQLHDV AKSLEGGLDS KVTENGDNWS
VGQRQLLCLA RALLRDPKIL VLDEATASVD GHSDSLIQAT IREKFSNCTI LTIAHRLNTI
MDSDRIIVLD AGKISEFDEP WTLLQNPAGL LNWLVEETGP QNAAYLRRLA QAKKDGVNID
QITPPISPTP EQKPFKNADI DNINSPPQQS LKAEDNPNPK ALDNSGDNNN NNNNNNNNNN
NNNNNNNNNN NNNNNNDNDN DNDNDNSEAG DN
