SCP2_YARLI
ID SCP2_YARLI Reviewed; 129 AA.
AC P80547; Q6C7F2; Q8J0I7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Fatty acid-binding protein;
DE AltName: Full=Sterol carrier protein 2;
DE AltName: Full=YLSCP2;
GN Name=SCP2; OrderedLocusNames=YALI0E01298g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, CLEAVAGE OF
RP INITIATOR METHIONINE, FUNCTION, SUBUNIT, AND ACETYLATION AT SER-2.
RC STRAIN=CX-121-1B;
RX PubMed=16890184; DOI=10.1016/j.abb.2006.06.024;
RA Ferreyra R.G., Burgardt N.I., Milikowski D., Melen G., Kornblihtt A.R.,
RA Dell' Angelica E.C., Santome J.A., Ermacora M.R.;
RT "A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding
RT activity.";
RL Arch. Biochem. Biophys. 453:197-206(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [3]
RP PROTEIN SEQUENCE OF 74-81; 101-105 AND 114-129, FUNCTION, AND SUBUNIT.
RC STRAIN=CX-121-1B;
RX PubMed=8828794; DOI=10.1080/15216549600201481;
RA Dell'Angelica E.C., Ermacora M.R., Santome J.A.;
RT "Purification and partial characterization of a fatty acid-binding protein
RT from the yeast, Yarrowia lipolytica.";
RL Biochem. Mol. Biol. Int. 39:439-445(1996).
CC -!- FUNCTION: May play a role in the transport of fatty acids. Binds fatty
CC acids and fatty acyl-CoAs including palmitic acid, oleic acid, cis-
CC parinaric acid and palmitoyl-CoA (in vitro).
CC {ECO:0000269|PubMed:16890184, ECO:0000269|PubMed:8828794}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16890184,
CC ECO:0000269|PubMed:8828794}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC -!- MISCELLANEOUS: Expressed essentially in cells grown on palmitic acid
CC with small amounts found in cells grown on glucose.
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DR EMBL; AJ431362; CAD24067.2; -; mRNA.
DR EMBL; CR382131; CAG78989.1; -; Genomic_DNA.
DR RefSeq; XP_503410.1; XM_503410.1.
DR PDB; 4JGX; X-ray; 2.20 A; A/B=1-129.
DR PDB; 6OVP; X-ray; 1.99 A; A/B=1-129.
DR PDBsum; 4JGX; -.
DR PDBsum; 6OVP; -.
DR AlphaFoldDB; P80547; -.
DR SMR; P80547; -.
DR STRING; 4952.CAG78989; -.
DR iPTMnet; P80547; -.
DR EnsemblFungi; CAG78989; CAG78989; YALI0_E01298g.
DR GeneID; 2911748; -.
DR KEGG; yli:YALI0E01298g; -.
DR VEuPathDB; FungiDB:YALI0_E01298g; -.
DR HOGENOM; CLU_105945_0_2_1; -.
DR InParanoid; P80547; -.
DR OMA; WTIDMKK; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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 3D-structure; Acetylation; Direct protein sequencing; Lipid-binding;
KW Peroxisome; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16890184"
FT CHAIN 2..129
FT /note="Fatty acid-binding protein"
FT /id="PRO_0000097634"
FT DOMAIN 10..129
FT /note="SCP2"
FT MOTIF 127..129
FT /note="Microbody targeting signal"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:16890184"
FT CONFLICT 75
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:6OVP"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:6OVP"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:6OVP"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:6OVP"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:6OVP"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:6OVP"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:6OVP"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6OVP"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:6OVP"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:6OVP"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:6OVP"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:6OVP"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:6OVP"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:6OVP"
SQ SEQUENCE 129 AA; 14034 MW; 7DCAC98D27D31E89 CRC64;
MSLKVDGFTS SIIFDVIRDG LNDPSQAKQK AESIKKANAI IVFNLKNKAG KTESWYLDLK
NDGDVGKGNK SPKGDADIQL TLSDDHFQQL VEGKANAQRL FMTGKLKVKG NVMKAAAIEG
ILKNAQNNL
