ABCD3_DICDI
ID ABCD3_DICDI Reviewed; 750 AA.
AC Q54W20;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=ABC transporter D family member 3;
DE AltName: Full=ABC transporter ABCD.3;
GN Name=abcD3; ORFNames=DDB_G0279919;
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:0000255|PROSITE-ProRule:PRU00441};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCD family.
CC Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily.
CC {ECO:0000305}.
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DR EMBL; AAFI02000035; EAL67431.1; -; Genomic_DNA.
DR RefSeq; XP_641430.1; XM_636338.1.
DR AlphaFoldDB; Q54W20; -.
DR SMR; Q54W20; -.
DR STRING; 44689.DDB0215374; -.
DR PaxDb; Q54W20; -.
DR EnsemblProtists; EAL67431; EAL67431; DDB_G0279919.
DR GeneID; 8622315; -.
DR KEGG; ddi:DDB_G0279919; -.
DR dictyBase; DDB_G0279919; abcD3.
DR eggNOG; KOG0060; Eukaryota.
DR HOGENOM; CLU_007587_7_0_1; -.
DR InParanoid; Q54W20; -.
DR OMA; WGFGMIV; -.
DR PhylomeDB; Q54W20; -.
DR Reactome; R-DDI-9758881; Uptake of dietary cobalamins into enterocytes.
DR Reactome; R-DDI-9758890; Transport of RCbl within the body.
DR PRO; PR:Q54W20; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IGC:dictyBase.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IGC:dictyBase.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0015910; P:long-chain fatty acid import into peroxisome; IBA:GO_Central.
DR GO; GO:0007031; P:peroxisome organization; IBA:GO_Central.
DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
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; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF06472; ABC_membrane_2; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..750
FT /note="ABC transporter D family member 3"
FT /id="PRO_0000370851"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 74..362
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 507..737
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 334..370
FT /evidence="ECO:0000255"
FT BINDING 540..547
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 750 AA; 86589 MW; EABB7C5ADD2A24E5 CRC64;
MKKNNVNNIT ETLNSSSSSS SSSGSSSDEE VKSKLNFNQT DEMLKKIKEN KFDWALFKRF
IKIVIILYEK PVIPLLLFLL LFGSGVSQTY ISKFTGILLS NIYGSLTSGD KFLFVSSLIK
GCFAIGGSAL FDAIIKFIVS IMAWNWRKTL CLYIQNVYFK KSLFYKILAF DDRIDNPDQR
ITSDIDNFTT LLSSIVSQCI TGPMVVVYYT YLCYTTIDWY APLIVYGYFF LGYFINKLVM
SPMVSINYLQ DKLEGDFRYL HQRIRNFSES IALYNLSKEK QQKKSTTSVD NLDYYDDDHH
YHHHHDDGEE SDEYTDKTKI INRKNKNSKN KRSALLKRSN KNIKNEELLV EEEQAKQQFE
ALLKNKKRVI FWQFGLNTTS DMFTFFSPLI NYFIISIPVF FLSSKAALEP AQVTVQSYNC
IMLASGFSQY INVSQSISDL SGYISRISTM IEVCKKVMGD TSLDIEITKL NEKDKTKSLP
NSLIINNRDT SINTDFRHIS LNEGESITLD DVTYFTPKGT QLYEKISICI KKGNNLLIMG
PSGSGKSSLI RIINGLWPFF KGSINRPENE DMFFLPQQPY LIFGTLEEQI LYPFSKKQKR
IPKSIMRELF QRFDIDYLLD RERFIKKSAQ VNDLTHNWLN QLSPGEQQLI AIIRLIYHKP
KFALMDESTS SIPQSLEERV YSVAKELGIT IISVGHRISL LKYHSTLLRF DKDKNWYLED
IINQNNQSNN INTINIDNNT NKIAEDSVFD
