ABCCC_DICDI
ID ABCCC_DICDI Reviewed; 1323 AA.
AC Q54U44; Q8T6G8;
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 12;
DE AltName: Full=ABC transporter ABCC.12;
GN Name=abcC12; ORFNames=DDB_G0280973;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1265, 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).
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; AAFI02000040; EAL66783.1; -; Genomic_DNA.
DR EMBL; AF474344; AAL85715.1; -; Genomic_DNA.
DR RefSeq; XP_640932.1; XM_635840.1.
DR AlphaFoldDB; Q54U44; -.
DR SMR; Q54U44; -.
DR STRING; 44689.DDB0214809; -.
DR PaxDb; Q54U44; -.
DR EnsemblProtists; EAL66783; EAL66783; DDB_G0280973.
DR GeneID; 8622995; -.
DR KEGG; ddi:DDB_G0280973; -.
DR dictyBase; DDB_G0280973; abcC12.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q54U44; -.
DR OMA; MDLMTFL; -.
DR PhylomeDB; Q54U44; -.
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:Q54U44; -.
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: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: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; 2.
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..1323
FT /note="ABC transporter C family member 12"
FT /id="PRO_0000363856"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 712..732
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 772..792
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 840..860
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 862..882
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 952..972
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 110..396
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 428..652
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 720..1010
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1047..1281
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 657..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 464..471
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1081..1088
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 10..19
FT /note="DNLETKGGKE -> EIWKLREER (in Ref. 2; AAL85715)"
FT /evidence="ECO:0000305"
FT CONFLICT 829
FT /note="R -> C (in Ref. 2; AAL85715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1323 AA; 148126 MW; 338966DE25C8F404 CRC64;
MEDIELNSVD NLETKGGKEI KKKEKKIGYG GKKSPEENSN FLSNLTFSWA DGFVIHCFRN
VLQLSHLWDL ASYDKSEYLA KKIAKSWEIE IQKPKPSYLR AGFRAFGKLH CISLFFYSIY
VGSQFVGPEI LSRMVTFVVE SKLGTSTEDP NMGYYYALIM FGTAMIGSFC NYQANRVTVR
TGDRLRSIIV LDVYKKAIKL SNSARSNTSP GQIVNLISND AQRMIEVFGI LNNGLFALPQ
IIICLALLYE KIGWPTFVGL GLMLAAIPFN GLAAKKLTET RRILIGHTDG RVKVTSEILQ
AMKIIKLYAW EDSFAKKVLD RRNNEIKLLF SFTRYRTILI AMIGAIPTAA SILVFSTYYG
YNGSLDAGKI FSALSYLNLL KIPLGFLPIL IALGIQMQIA SKRVTDFLLL PEMKEVQQID
NPSLPNGVYM KNSTTTWNKE KEDSFGLKNI NFEAKGQSLT MVVGSVGSGK STLVQAMLGE
LETIDGEIGI KGSIAYVPQQ AWIINATLKE NIIFGKELDE ERYQKVLEVC ALKRDIELFP
QGDSVEIGER GINLSGGQKQ RVSIARAVYS DADVYILDDP LSAVDSHVGK HLFHKCFKGI
LSSKTVILVA NQINYLPFAD NTVVLKSGEI VERGTYYELI NAKLEFASLL QEYGVDENTK
GDDSDDDDDK KDDDKKEEKV EKPKQSDKDG TLISEEEAEQ GAVAGKVYWK YVTAGGGLLF
LFAMILFLLE TGSKTFTDWW LSHWQTESSE RMESILLGEE PTGLTDDQNL GIYIGVGMAS
IIVTVVRTFS FFEYAVRAAH SIHHELFNAL LKKPMSFFDQ TPLGRIINRF TRDLDIIDNL
IATSIAQFFT LMLSVLATLI LISIIVPWLL IPLAPICILF FILQYFYRYT SRGLQRIEAI
TRSPIFNHFS ETLNGVVSIR AYKKQQENIL KNQKRLDDNN NCYLTLQAMN RWLGLRLDFL
GNLIVFFSCI FITLKKDTIS PSDVGLVLSY ALSITSNLNQ GVLQAADTET KMNSVERISQ
YIRGAVEAPQ IIDDCRPSPD WPINGSIKFD NLVMRYREGL DPVLKGITCE IKAKEKIGIV
GRTGAGKSSI VLALFRLIEA SEGSISIDGE NIAKFGLKDL RRNLAIIPQD PVLFSGTLRE
NLDPFNECPD HELWSILDDI QLSKVFKSTE EGLNSKVTEN GENFSVGQRQ LIVLARALLR
KPKILVLDEA TASVDGQSDS LIQATIRNKF SNCTILTIAH RLNTIMDSDK IMVLDAGKIS
EFDEPWTLLQ NQNGLLTWLV NETGPQNAIY LRKLAEAKKS GLNINEITQI DQQNDNLNTP
PRL
