POX18_CANTR
ID POX18_CANTR Reviewed; 127 AA.
AC P22009;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Oleate-induced peroxisomal protein POX18;
DE Short=PXP-18;
DE AltName: Full=Lipid-transfer protein;
GN Name=POX18;
OS Candida tropicalis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5482;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-17.
RC STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX PubMed=2470648; DOI=10.1016/0378-1119(89)90388-0;
RA Szabo L.J., Small G.M., Lazarow P.B.;
RT "The nucleotide sequence of POX18, a gene encoding a small oleate-inducible
RT peroxisomal protein from Candida tropicalis.";
RL Gene 75:119-126(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX PubMed=2364939; DOI=10.1111/j.1432-1033.1990.tb15552.x;
RA Tan H., Okazaki K., Kubota I., Kamiryo T., Utiyama H.;
RT "A novel peroxisomal nonspecific lipid-transfer protein from Candida
RT tropicalis. Gene structure, purification and possible role in beta-
RT oxidation.";
RL Eur. J. Biochem. 190:107-112(1990).
CC -!- FUNCTION: Is involved in beta-oxidation of long-chain fatty acids. Its
CC exact function is unknown, but possesses a nonspecific lipid-transfer
CC activity, despite the absence of a cysteine residue thought to be
CC essential for the activity of its mammalian counterparts.
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- INDUCTION: By alkanes or fatty acids; repressed by glucose.
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DR EMBL; X53633; CAA37682.1; -; Genomic_DNA.
DR EMBL; M24440; AAA56863.1; -; Genomic_DNA.
DR PIR; JS0155; JS0155.
DR AlphaFoldDB; P22009; -.
DR SMR; P22009; -.
DR VEuPathDB; FungiDB:CTMYA2_051240; -.
DR VEuPathDB; FungiDB:CTRG_02171; -.
DR UniPathway; UPA00199; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.1050.10; -; 1.
DR InterPro; IPR039543; POX18/UbiT/NSL-TP1.
DR InterPro; IPR003033; SCP2_sterol-bd_dom.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR PANTHER; PTHR10094; PTHR10094; 1.
DR Pfam; PF02036; SCP2; 1.
DR SUPFAM; SSF55718; SSF55718; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lipid-binding; Peroxisome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2470648"
FT CHAIN 2..127
FT /note="Oleate-induced peroxisomal protein POX18"
FT /id="PRO_0000058528"
FT DOMAIN 14..119
FT /note="SCP2"
FT /evidence="ECO:0000255"
FT REGION 33..41
FT /note="Hydrophobic"
FT REGION 43..52
FT /note="Hydrophilic"
SQ SEQUENCE 127 AA; 13806 MW; 942D99F56A4FAC00 CRC64;
MSVEVDGFNA SPLFKELNDG LADKAKAQEA VKAVNAIIVI TLKNKEGKEQ SWVLDLKKDG
TLAKVDGAAP KGDVQLILKD VDFVKLANNK VNGQKLFMNG KLKVKGNMMK ATAIEAVFKK
LDPRPKL