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Database: UniProt
Entry: Q6IRQ1_XENLA
LinkDB: Q6IRQ1_XENLA
Original site: Q6IRQ1_XENLA 
ID   Q6IRQ1_XENLA            Unreviewed;       657 AA.
AC   Q6IRQ1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   SubName: Full=70 kDa peroxisomal membrane protein {ECO:0000313|EMBL:ABK62837.1};
DE   SubName: Full=ATP binding cassette subfamily D member 3 S homeolog {ECO:0000313|RefSeq:NP_001084980.1, ECO:0000313|RefSeq:XP_018115053.1};
DE   SubName: Full=ATP binding cassette subfamily D member 3 S homeolog isoform X2 {ECO:0000313|RefSeq:XP_018115052.1};
DE   SubName: Full=MGC82231 protein {ECO:0000313|EMBL:AAH70657.1};
GN   Name=abcd3.S {ECO:0000313|RefSeq:NP_001084980.1,
GN   ECO:0000313|RefSeq:XP_018115052.1, ECO:0000313|RefSeq:XP_018115053.1,
GN   ECO:0000313|Xenbase:XB-GENE-983905};
GN   Synonyms=abcd3 {ECO:0000313|RefSeq:NP_001084980.1,
GN   ECO:0000313|RefSeq:XP_018115052.1, ECO:0000313|RefSeq:XP_018115053.1,
GN   ECO:0000313|Xenbase:XB-GENE-983905}, MGC82231
GN   {ECO:0000313|EMBL:AAH70657.1}, pmp70
GN   {ECO:0000313|RefSeq:NP_001084980.1, ECO:0000313|RefSeq:XP_018115052.1,
GN   ECO:0000313|RefSeq:XP_018115053.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH70657.1};
RN   [1] {ECO:0000313|RefSeq:NP_001084980.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAH70657.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000313|EMBL:AAH70657.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ABK62837.1, ECO:0000313|RefSeq:NP_001084980.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17973332; DOI=10.1002/dvdy.21370;
RA   Cooper C.A., Walsh L.A., Damjanovski S.;
RT   "Peroxisome biogenesis occurs in late dorsal-anterior structures in the
RT   development of Xenopus laevis.";
RL   Dev. Dyn. 236:3554-3561(2007).
RN   [4] {ECO:0000313|RefSeq:XP_018115052.1, ECO:0000313|RefSeq:XP_018115053.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018115052.1,
RC   ECO:0000313|RefSeq:XP_018115053.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018115052.1,
RC   ECO:0000313|RefSeq:XP_018115053.1};
RG   RefSeq;
RL   Submitted (APR-2022) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a very long-chain fatty acid(in) + ATP + H2O = a very long-
CC         chain fatty acid(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:67080,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58950, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00024576};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67081;
CC         Evidence={ECO:0000256|ARBA:ARBA00024576};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a very long-chain fatty acyl-CoA + H2O = a very long-chain
CC         fatty acid + CoA + H(+); Xref=Rhea:RHEA:67072, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:58950,
CC         ChEBI:CHEBI:138261; Evidence={ECO:0000256|ARBA:ARBA00024544};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67073;
CC         Evidence={ECO:0000256|ARBA:ARBA00024544};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Peroxisome
CC       membrane {ECO:0000256|ARBA:ARBA00004585}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004585}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCD family.
CC       Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily.
CC       {ECO:0000256|ARBA:ARBA00008575}.
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DR   EMBL; BC070657; AAH70657.1; -; mRNA.
DR   EMBL; EF070607; ABK62837.1; -; mRNA.
DR   RefSeq; NP_001084980.1; NM_001091511.1.
DR   RefSeq; XP_018115052.1; XM_018259563.2.
DR   RefSeq; XP_018115053.1; XM_018259564.2.
DR   STRING; 8355.Q6IRQ1; -.
DR   PaxDb; 8355-Q6IRQ1; -.
DR   DNASU; 432040; -.
DR   GeneID; 432040; -.
DR   KEGG; xla:432040; -.
DR   AGR; Xenbase:XB-GENE-983905; -.
DR   CTD; 432040; -.
DR   Xenbase; XB-GENE-983905; abcd3.S.
DR   OMA; IHDMYLD; -.
DR   OrthoDB; 7698at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 432040; Expressed in stomach and 19 other cell types or tissues.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005324; F:long-chain fatty acid transporter activity; IEA:InterPro.
DR   GO; GO:0015910; P:long-chain fatty acid import into peroxisome; IEA:InterPro.
DR   CDD; cd03223; ABCD_peroxisomal_ALDP; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR005283; FA_transporter.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00954; 3a01203; 1.
DR   PANTHER; PTHR11384:SF62; ATP-BINDING CASSETTE SUB-FAMILY D MEMBER 3; 1.
DR   PANTHER; PTHR11384; ATP-BINDING CASSETTE, SUB-FAMILY D MEMBER; 1.
DR   Pfam; PF06472; ABC_membrane_2; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        123..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          105..319
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          438..657
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   657 AA;  75039 MW;  DC12D6A1A870D096 CRC64;
     MAPVYSKYLN ARNTSVAGAA LFLLYLISKR RGASGKKNGK SSLQNNEKDG KKEKAVVDRV
     FFGRIGQILK ILVPKTFCKE SGYLLFIAVM LIARTYCDVW MIQNGTFIES AIIGRSRKDF
     KRYLFNFIAA MPAISLVNNF LKFGLNELKL CFRERLTKYL YDEYLKSFTY YKMGNLDNRI
     ANADQLLTQD VERFCNSVVD LYSNLSKPFL DIVLYIFKLT SAIGAQGPAS MMAYLLVSGL
     FLTRLRRPIG KMTVAEQRYE GEYRYVNSRL ITNSEEIAFY NGNKREKLTI YSSFQKLVEH
     LHNFILFRFS MGFVDSIIAK YLATVVGYLV VSRPFLAINH PRHLNSSHAE LLEDYYQSGR
     MLLRMSQALG RIVLAGREMT RLSGFTARIT ELMQVLKDLN QGKYERTMVS QQDKDVEAVP
     SIPLIPGSGK VINADKIIKF DHVPLATPNG DLLIRDLNFE VRSGTNVLVC GPNGCGKSSL
     FRVLGELWPL FGGSLTKPER GKLFYVPQRP YMTLGTLRDQ VIYPDTQEDQ KRKGISDKVL
     KEYLDNVQLG HILDREGGWD SVQDWMDVLS GGEKQRMAMA RLFYHKPQFA ILDECTSAVS
     VDVEGYIYNH CRKVGITLFT VSHRKSLWKH HEYYLHMDGR GNYDFKQITE DTDAFGS
//
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