ABCD1_DICDI
ID ABCD1_DICDI Reviewed; 734 AA.
AC Q54W19;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=ABC transporter D family member 1;
DE AltName: Full=ABC transporter ABCD.1;
GN Name=abcD1; ORFNames=DDB_G0279917;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA(in) = (9Z)-octadecenoyl-CoA(out);
CC Xref=Rhea:RHEA:45956, ChEBI:CHEBI:57387;
CC Evidence={ECO:0000250|UniProtKB:P33897};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45958;
CC Evidence={ECO:0000250|UniProtKB:P33897};
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; EAL67430.1; -; Genomic_DNA.
DR RefSeq; XP_641431.1; XM_636339.1.
DR AlphaFoldDB; Q54W19; -.
DR SMR; Q54W19; -.
DR STRING; 44689.DDB0215371; -.
DR PaxDb; Q54W19; -.
DR EnsemblProtists; EAL67430; EAL67430; DDB_G0279917.
DR GeneID; 8622316; -.
DR KEGG; ddi:DDB_G0279917; -.
DR dictyBase; DDB_G0279917; abcD1.
DR eggNOG; KOG0060; Eukaryota.
DR HOGENOM; CLU_007587_7_0_1; -.
DR InParanoid; Q54W19; -.
DR OMA; RESSANH; -.
DR PhylomeDB; Q54W19; -.
DR PRO; PR:Q54W19; -.
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:0005777; C:peroxisome; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0015910; P:long-chain fatty acid import into peroxisome; ISS:UniProtKB.
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; 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..734
FT /note="ABC transporter D family member 1"
FT /id="PRO_0000370849"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 63..351
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 492..729
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 271..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 332..359
FT /evidence="ECO:0000255"
FT COMPBIAS 271..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 525..532
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 734 AA; 84377 MW; DAFAE2F1D3270CD8 CRC64;
MKTTNVKNNN NNINNTDEEI KIKNNYNQND ERLKKIKENK FDWALFKRFI NIIKILYAKP
VIPLTLFLIL FGNGFAQTYV SKFTGILLAD IYASFTSGDK VFFLSSVLKA GFAIGGSALL
AAIINFIVSI MAWNWRKTLC LYIQNVYFKK SLFYKILAFD DRIDNPDQRI TSDIDNFTTL
LASIVSQCIT GPMVVVYYTY LCYTTIDWYA PLIVYGFFFL GYLINKLVMS PMVSINYLQD
KLEGDFRSLH QRIRNFSESI ALYSLSKEKQ HPEKRFDNND YDHGYESDDS DQSCDESTTI
INRKKNKGSQ YYKNKNSTSK KINDFIDKLS GDSNDQKEEL LVEEEQAKIQ FEALLKNKKR
VIFWQLGLNT TSDLFTYLSP IANYFIIAIP VFFLNNKSVL QPGDVTVQSY NCIMLASGFS
QYINVSQSIS DLSGYISRIS SMIEVCKKIM EDVSLDADIT KLNEKVAQTH NNDAIINTGS
SGNISLNNGD SITLDDVTYF TPKGNQLYSK ISINVKRGNN LLIMGPSGSG KSSLIRIING
LWPFFKGSID RPENGDMFFL PQQPYLIFGT LEEQILYPFS KKQKRIPKSI MRELFQRFEI
DYLLDRERFI KKSAQVNDLT HNWLNQLSPG EQQLIAIIRL IYHKPKFALM DESTSSIPQS
LEERVYYVAK ELGITIISVG HRISLLKYHS TLLRFDKDKN WYLEDIINQN NQSNNINNNN
NNNTNKIAED SVFD
