ITP1_USTMD
ID ITP1_USTMD Reviewed; 491 AA.
AC A0A0U2UXG3;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 25-MAY-2022, entry version 16.
DE RecName: Full=Itaconate transport protein {ECO:0000303|PubMed:26639528};
DE AltName: Full=Itaconic acid/2-hydroxyparaconate biosynthesis cluster protein ITP1 {ECO:0000305};
GN Name=ITP1 {ECO:0000303|PubMed:26639528}; ORFNames=UMAG_11777;
OS Ustilago maydis (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=5270;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=MB215;
RX PubMed=26639528; DOI=10.1111/1751-7915.12329;
RA Geiser E., Przybilla S.K., Friedrich A., Buckel W., Wierckx N., Blank L.M.,
RA Boelker M.;
RT "Ustilago maydis produces itaconic acid via the unusual intermediate trans-
RT aconitate.";
RL Microb. Biotechnol. 9:116-126(2016).
RN [2]
RP FUNCTION.
RX PubMed=27750034; DOI=10.1016/j.ymben.2016.10.006;
RA Geiser E., Przybilla S.K., Engel M., Kleineberg W., Buettner L.,
RA Sarikaya E., Hartog T.D., Klankermayer J., Leitner W., Boelker M.,
RA Blank L.M., Wierckx N.;
RT "Genetic and biochemical insights into the itaconate pathway of Ustilago
RT maydis enable enhanced production.";
RL Metab. Eng. 38:427-435(2016).
CC -!- FUNCTION: MFS transporter; part of the gene cluster that mediates the
CC biosynthesis of itaconic acid and 2-hydroxyparaconate (PubMed:26639528,
CC PubMed:27750034). Cis-aconitate is secreted by the mitochondrial
CC tricarboxylate transporter MTT1. In the cytosol cis-aconitate is
CC converted into trans-aconitate via isomerization by the aconitate-
CC delta-isomerase ADI1 (PubMed:26639528). Decarboxylation of trans-
CC aconitate by the trans-aconitate decarboxylase TAD1 then leads then to
CC the production of itaconic acid (PubMed:26639528). The cytochrome P450
CC monooxygenase CYP3 further converts itaconate to 2-hydroxyparaconate
CC via oxidation of the double bond, leading to a transient epoxide, which
CC can subsequently be lactonized to produce 2-hydroxyparaconate
CC (PubMed:27750034). Secretion of itaconate and possibly 2-
CC hydroxyparaconate into the medium is mediated by the major facilitator
CC ITP1 (PubMed:26639528, PubMed:27750034). The glyoxalase domain-
CC containing protein RDO1 is not involved in the biosynthesis of
CC itaconate and 2-hydroxyparaconate, however, it might play a role in the
CC further conversion of 2-hydroxyparaconate to itatartarate
CC (PubMed:27750034). {ECO:0000269|PubMed:26639528,
CC ECO:0000269|PubMed:27750034}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26639528};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Decreases the production of itaconic acid
CC (PubMed:26639528). {ECO:0000269|PubMed:26639528}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; KT852988; ALS30797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U2UXG3; -.
DR VEuPathDB; FungiDB:UMAG_11777; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..491
FT /note="Itaconate transport protein"
FT /id="PRO_0000438678"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 491 AA; 53364 MW; 5FF756F2A9D67C72 CRC64;
MDQADHSGVP DDAALEEAPN TVPIQEKSAQ PHDTQPYCAF TKRSKLFIVL TVSLAGFFSP
FAINIYIPAL PQIAGMLHTS EAATNVTVTV YMIAQGLSPV IWAPLSDVFG RRPIYILTFF
IFFIANLGLS FTNVYWLLVV LRMVQAAGAC SAIAIGAGTI GDVTERKERG SYMGYYALAQ
YTGPAIGPVV GGALSQRWDY HATFFFLTAI SGPFLLFMLL FLVETLRVIV GNGSAKTSGI
YRPLVEPKLQ RSIANAPRPG IKNPLHGTLD FGFHRPFLVF ARPETSLAIL AFSMVYASYY
LSSGSLPYLF KQVYGLDELL IGVCFVPSGV GCAVGTVLAG KILDWDYRRA LDKSKLGVKV
TRARLQSAWI YLPCYCASLL AYGWCVRAHT HIAAPIVFQF TLGMFSTMYF TNVNTLIVDL
YPGKAASATA AVNVGRCLLG AVAVAVVQPM IDAMGAGWTF TLGALLTLIV GLICQVLIYL
YGEMWAARKH S
