PXA2_YEAST
ID PXA2_YEAST Reviewed; 853 AA.
AC P34230; D6VX12;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Peroxisomal long-chain fatty acid import protein 1;
DE AltName: Full=Peroxisomal ABC transporter 2;
GN Name=PXA2; Synonyms=PAT1; OrderedLocusNames=YKL188C; ORFNames=YKL741;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8876235; DOI=10.1073/pnas.93.21.11901;
RA Shani N., Valle D.;
RT "A Saccharomyces cerevisiae homolog of the human adrenoleukodystrophy
RT transporter is a heterodimer of two half ATP-binding cassette
RT transporters.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:11901-11906(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8154185; DOI=10.1002/yea.320091208;
RA Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT FAS1 gene.";
RL Yeast 9:1343-1348(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7941751; DOI=10.1002/yea.320100512;
RA Bossier P., Fernandes L., Vilela C., Rodrigues-Pousada C.;
RT "The yeast YKL741 gene situated on the left arm of chromosome XI codes for
RT a homologue of the human ALD protein.";
RL Yeast 10:681-686(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP FUNCTION.
RX PubMed=8670886; DOI=10.1002/j.1460-2075.1996.tb00755.x;
RA Hettema E.H., van Roermund C.W.T., Distel B., van den Berg M., Vilela C.,
RA Rodrigues-Pousada C., Wanders R.J.A., Tabak H.F.;
RT "The ABC transporter proteins Pat1 and Pat2 are required for import of
RT long-chain fatty acids into peroxisomes of Saccharomyces cerevisiae.";
RL EMBO J. 15:3813-3822(1996).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18757502; DOI=10.1096/fj.08-110866;
RA van Roermund C.W., Visser W.F., Ijlst L., van Cruchten A., Boek M.,
RA Kulik W., Waterham H.R., Wanders R.J.;
RT "The human peroxisomal ABC half transporter ALDP functions as a homodimer
RT and accepts acyl-CoA esters.";
RL FASEB J. 22:4201-4208(2008).
CC -!- FUNCTION: Involved in the import of activated long-chain fatty acids
CC from the cytosol to the peroxisomal matrix.
CC {ECO:0000269|PubMed:8670886}.
CC -!- SUBUNIT: Forms a heterodimer with PXA1.
CC -!- INTERACTION:
CC P34230; P00330: ADH1; NbExp=2; IntAct=EBI-2464632, EBI-2218;
CC P34230; P38013: AHP1; NbExp=2; IntAct=EBI-2464632, EBI-2382;
CC P34230; P11076: ARF1; NbExp=2; IntAct=EBI-2464632, EBI-2816;
CC P34230; P25373: GRX1; NbExp=2; IntAct=EBI-2464632, EBI-7903;
CC P34230; P41909: PXA1; NbExp=2; IntAct=EBI-2464632, EBI-14344;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein.
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; U93584; AAB51597.1; -; Genomic_DNA.
DR EMBL; X74151; CAA52250.1; -; Genomic_DNA.
DR EMBL; X76133; CAA53736.1; -; Genomic_DNA.
DR EMBL; Z28188; CAA82031.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08978.1; -; Genomic_DNA.
DR PIR; S34682; S34682.
DR RefSeq; NP_012733.1; NM_001179754.1.
DR AlphaFoldDB; P34230; -.
DR SMR; P34230; -.
DR BioGRID; 33934; 106.
DR ComplexPortal; CPX-1730; Peroxisomal ABC transporter complex PXA1-PXA2.
DR DIP; DIP-741N; -.
DR IntAct; P34230; 47.
DR MINT; P34230; -.
DR STRING; 4932.YKL188C; -.
DR TCDB; 3.A.1.203.6; the atp-binding cassette (abc) superfamily.
DR PaxDb; P34230; -.
DR PRIDE; P34230; -.
DR TopDownProteomics; P34230; -.
DR EnsemblFungi; YKL188C_mRNA; YKL188C; YKL188C.
DR GeneID; 853647; -.
DR KEGG; sce:YKL188C; -.
DR SGD; S000001671; PXA2.
DR VEuPathDB; FungiDB:YKL188C; -.
DR eggNOG; KOG0064; Eukaryota.
DR GeneTree; ENSGT00950000182955; -.
DR HOGENOM; CLU_007587_5_0_1; -.
DR InParanoid; P34230; -.
DR OMA; ASLESWF; -.
DR BioCyc; YEAST:G3O-31951-MON; -.
DR BRENDA; 7.6.2.4; 984.
DR Reactome; R-SCE-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-SCE-9603798; Class I peroxisomal membrane protein import.
DR PRO; PR:P34230; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P34230; protein.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IPI:ComplexPortal.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:SGD.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IGI:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IGI:UniProtKB.
DR GO; GO:1902001; P:fatty acid transmembrane transport; IDA:SGD.
DR GO; GO:0015916; P:fatty-acyl-CoA transport; IGI:UniProtKB.
DR GO; GO:0042758; P:long-chain fatty acid catabolic process; IMP:UniProtKB.
DR GO; GO:0015910; P:long-chain fatty acid import into peroxisome; IDA:ComplexPortal.
DR GO; GO:0007031; P:peroxisome organization; IBA:GO_Central.
DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; IMP:UniProtKB.
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; IPR005283; FA_transporter.
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 TIGRFAMs; TIGR00954; 3a01203; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding; Peroxisome;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..853
FT /note="Peroxisomal long-chain fatty acid import protein 1"
FT /id="PRO_0000093315"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 127..417
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 472..747
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 33..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 505..512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 647
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 836
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 853 AA; 97126 MW; BDD37FB2A6A220DB CRC64;
MISTASAFYQ KHRVNLLRSS YIILLLATLY NSNSSSSNNK TDKKDSESTV LENKKIEEGK
ETAVDREEDE SSKEELTIVS KHSTDSEDGA IIIDKESKTN HKGGERKGKV DFLFKLLLHD
KKCLILFITQ AILLNIRTLL SLRVATLDGQ LVSTLVRAQY ANFTKILLGK WMILGIPASF
INSLISYTTK LCAVTINRKV SDFLLSKYLS NHHTFYSVAS AESVSEIQDN LTKDIYTFSM
NSSLLLNQLL KPMLDLILCS FKLLTSNTSV MGEGTLALGL IVYASNSLLK LIQPNFTRLT
MASASLESWF RSLHSNLHSS NEEIALLRGQ KRELENVDYS FYRLVLFLNR EIKARAIYDV
ATAFVIKYTW GAAGLVLCSI PIFFKNKPSE DTLQLKEPGN DMTADFITNR RLLVTASSSI
GRFVELKRNI QQLRGIRLRL NKFNDLLDAN KGDDEKEPRD ERCIVEYDDS RIKFENIPLI
TPANQVLVPE LSFDLKHGNH LLIIGPNGCG KSSLFRILGG LWPIRATPNK NHQSKLIMPR
RTVDRDCAIF YLPQRPYMGN RSTFREQIIY PDSIEQFKER YHNDYDLGDA DLIKILQLLD
LEDLVTENMS LLLAQRTSKN DSQQLSTEDN QSPCAIKVRD AFSIVRNWSE ELTIGVQQRL
AMARMYYHKP KFAVLDECTS AVAPEMEQRM YENAQNFGIS LISVCHRTSL WHFHNYLLKF
DGKGGYQFGP FNPKERLCNE EKLLELNAIL DQQVPLWERK LKDLTIAKES NIIRKSETNL
NLFEKIEDPK TSKSNALFNA NKGQRITSPT GQETSKRLPL FSQPSSSASS NLLRNNKSLN
KKVKTKKEEG KER
