ABCC8_DICDI
ID ABCC8_DICDI Reviewed; 1593 AA.
AC Q54P13; Q8T6H1;
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 8;
DE AltName: Full=ABC transporter ABCC.8;
GN Name=abcC8; ORFNames=DDB_G0284867;
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; AF474340; AAL85711.1; -; Genomic_DNA.
DR EMBL; AAFI02000073; EAL64897.1; -; Genomic_DNA.
DR RefSeq; XP_639904.1; XM_634812.1.
DR AlphaFoldDB; Q54P13; -.
DR SMR; Q54P13; -.
DR STRING; 44689.DDB0191225; -.
DR PaxDb; Q54P13; -.
DR EnsemblProtists; EAL64897; EAL64897; DDB_G0284867.
DR GeneID; 8624816; -.
DR KEGG; ddi:DDB_G0284867; -.
DR dictyBase; DDB_G0284867; abcC8.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q54P13; -.
DR OMA; IRYDFTP; -.
DR PhylomeDB; Q54P13; -.
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:Q54P13; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
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:0008514; F:organic anion transmembrane transporter activity; IEA:InterPro.
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; 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; IPR030247; ABCC2.
DR InterPro; IPR032410; MTABC_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF176; PTHR24223:SF176; 3.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF16185; MTABC_N; 1.
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; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Membrane; Nucleotide-binding; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1593
FT /note="ABC transporter C family member 8"
FT /id="PRO_0000363853"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1005..1025
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1064..1084
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1157..1177
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1251..1271
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1280..1300
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 280..561
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 594..818
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1010..1308
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1344..1578
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 816..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 844..875
FT /evidence="ECO:0000255"
FT COMPBIAS 816..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 627..634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1378..1385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 61
FT /note="S -> F (in Ref. 1; AAL85711)"
FT /evidence="ECO:0000305"
FT CONFLICT 1325
FT /note="E -> K (in Ref. 1; AAL85711)"
FT /evidence="ECO:0000305"
FT CONFLICT 1587
FT /note="D -> N (in Ref. 1; AAL85711)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1593 AA; 178339 MW; C1BC5D9F4A480A35 CRC64;
MGFCGDEPFT VWHNDSGDFS KCFEDSVVMT LPAIYLLIFG MKRLYYLENK KPDLFTLKQL
SQDFQTWRKT LQLEVIVSIL LVAWKILFFI VIVSIYNKPF EILYSVVTVV QWTVSLGLVY
LEMKKGQSRS WEIRLYWVFA FFVATVKLRT LTLAIAGKSI YNVGFLEYFS YFVGYCLILI
LSITSVLFFD NLESYQNLEE NEISKEVNAN LFSRLTFWWI NSVLVKGHKK ALEISDVPTL
GEIDQSILLS EKFEKAWEEQ LKKPNPSLPW ALAKAFGPHF YIAALFKIIQ DLLIFVGPTL
LKRVLGFVES RDGSQDTYDG LIYALLYFLA PVVQSLLLHQ YFHRCYRVGM WLRSAVVTAV
YKKALKTSLR EGTTIGEIVN LMSVDAQKFM DLCPYLHMIW SAPLQLAISL VLLYRILNAS
VFAGLGIMLV MIPINLAISN LAKKRQTISM KLKDRRTKAV NEVLNGIKVI KLYSWEQSFM
DHVNEIRNKE LDVMKAIKYI QGFSLLLWSM SPVFVSVSTF TVYILTGQVL SATQAFPALS
LFNVMQFPIN MLPSVVSSII EASVSVARLQ KFLLKKDLDP NVVEHHINEP GIAVKIDNAT
LEWEPNKPIL HDINLTIKKG ELVAIVGQVG SGKSSIVSSL VGDLDKTKGT VAVNGSVALV
SQQAWIQNAT LKNNILFAKE LNQDKYQSVV QACCLEPDIK ILPGGDQTEI GEKGINLSGG
QKQRVSIARA VYNNADIYIF DDPLSAVDAH VGKAIFKNVL SNQDGILCNK TRILVTHAVH
YLPYVDRIIL MKDGRIVEEG DFNTLIEAGS HFTELMSHDE QQQQLQQQQA PDKSSDSNEQ
IGGGDNKESE NNEEQNEEEE GENENLLEKV LRKSRSRSPS PSSNRNIDGD DIASGSILQT
TRTPEEDEQD ERELMEDIDI DGGENIQTPL QKGEKSSVLK QPLRLLKKLP TSINKKLNNS
GSGVSLKPIT TVNAKPQDKN KIISVETKQE GKVSFKIYLS YFKAIGVLLA TCIIGFYVLT
QLLSILANWW ISIWTNSYGG NGNGSGSGSI SLSSSSTVED NEKAKYYLSI YVAFSCGTIA
ATFLRSFSMV FGSIKGSKLF HEKMFKAVIL SPMSFFDTTP IGRILNRFSK DQLTIDESIA
RTLGMFLNTF CQVVGSIIVI AWVSPFIILA MVPVGALFYF IQKYYLNSSR ELTRLEGVSR
SPIYAHFSET LAGVTTIRAF KDVARFVTEN ERLLDENQKC YYINISSNRW LAIRLEFLGA
CLVSCAVLYT VLARSRIEAG TAGLVITYAL AITGNMNWMV RMSCDLENSV VSIERIQEYC
LLPSEAPLFN DKSVPMSWPS HGKIVFKNLW LTYREGLDPV LRGINCTIEP KTKVGIVGRT
GAGKSSLTQA LFRLVEPLRG TIEIDGIDIT ELGLNPLRSR MAIIPQDPVL FAGSVRYNLD
PFDQYDDHEI WEAIENAHLL KAIKDLDGGL DAMVQDGGDN FSVGQRQLLV IGRALLKKAN
IIVLDEASSS IDIASDALIQ ETIRTKFADC TVLTIAHRLG TIADSDKIMV LDKGELIEYD
SPSELLKNQD SIYYSLVKAS ESKQNIDNDD ESN
