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Fatty acid-binding protein, epidermal (Epidermal-type fatty acid-binding protein) (E-FABP) (Fatty acid-binding protein 5) (Psoriasis-associated fatty acid-binding protein homolog) (PA-FABP)

 FABP5_HUMAN             Reviewed;         135 AA.
Q01469; B2R4K0;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 206.
RecName: Full=Fatty acid-binding protein 5;
AltName: Full=Epidermal-type fatty acid-binding protein {ECO:0000303|PubMed:8092987};
Short=E-FABP {ECO:0000303|PubMed:8092987};
AltName: Full=Fatty acid-binding protein, epidermal;
AltName: Full=Psoriasis-associated fatty acid-binding protein homolog;
Short=PA-FABP;
Name=FABP5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Keratinocyte;
PubMed=1512466; DOI=10.1111/1523-1747.ep12616641;
Madsen P.S., Rasmussen H.H., Leffers H., Honore B., Celis J.E.;
"Molecular cloning and expression of a novel keratinocyte protein
(psoriasis-associated fatty acid-binding protein [PA-FABP]) that is
highly up-regulated in psoriatic skin and that shares similarity to
fatty acid-binding proteins.";
J. Invest. Dermatol. 99:299-305(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[7]
PROTEIN SEQUENCE OF 18-33; 35-50; 62-103 AND 116-129, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 25-33; 39-50; 62-71; 83-101 AND 120-129.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[9]
PROTEIN SEQUENCE OF 67-72 AND 104-110, CHARACTERIZATION, AND
SUBCELLULAR LOCATION.
PubMed=8092987; DOI=10.1042/bj3020363;
Siegenthaler G., Hotz R., Chatellard-Gruaz D., Didierjean L.,
Hellman U., Saurat J.-H.;
"Purification and characterization of the human epidermal fatty acid-
binding protein: localization during epidermal cell differentiation in
vivo and in vitro.";
Biochem. J. 302:363-371(1994).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-131, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
FUNCTION.
PubMed=22170058; DOI=10.1074/jbc.M111.304907;
Kaczocha M., Vivieca S., Sun J., Glaser S.T., Deutsch D.G.;
"Fatty acid-binding proteins transport N-acylethanolamines to nuclear
receptors and are targets of endocannabinoid transport inhibitors.";
J. Biol. Chem. 287:3415-3424(2012).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH FATTY ACID, AND
DISULFIDE BOND.
PubMed=10493790; DOI=10.1021/bi990305u;
Hohoff C., Borchers T., Rustow B., Spener F., van Tilbeurgh H.;
"Expression, purification and crystal structure determination of
recombinant human epidermal-type fatty acid-binding protein.";
Biochemistry 38:12229-12239(1999).
[19]
STRUCTURE BY NMR, AND DISULFIDE BOND.
PubMed=12049637; DOI=10.1042/BJ20020039;
Gutierrez-Gonzalez L.H., Ludwig C., Hohoff C., Rademacher M.,
Hanhoff T., Rueterjans H., Spener F., Luecke C.;
"Solution structure and backbone dynamics of human epidermal-type
fatty acid-binding protein (E-FABP).";
Biochem. J. 364:725-737(2002).
[20] {ECO:0000244|PDB:4LKP, ECO:0000244|PDB:4LKT}
X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH LINOLEIC ACID,
DISULFIDE BONDS, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-24; ARG-33
AND LYS-34, AND NUCLEAR LOCALIZATION SIGNAL.
PubMed=24692551; DOI=10.1074/jbc.M113.514646;
Armstrong E.H., Goswami D., Griffin P.R., Noy N., Ortlund E.A.;
"Structural basis for ligand regulation of the fatty acid-binding
protein 5, peroxisome proliferator-activated receptor beta/delta
(FABP5-PPARbeta/delta) signaling pathway.";
J. Biol. Chem. 289:14941-14954(2014).
[21] {ECO:0000244|PDB:4AZM, ECO:0000244|PDB:4AZR}
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS), SUBUNIT, IN COMPLEX WITH
SYNTHETIC INHIBITOR BMS-309403, AND IN COMPLEX WITH
N-ARACHIDONOYLETHANOLAMIDE.
PubMed=24531463; DOI=10.1107/S1399004713026795;
Sanson B., Wang T., Sun J., Wang L., Kaczocha M., Ojima I.,
Deutsch D., Li H.;
"Crystallographic study of FABP5 as an intracellular endocannabinoid
transporter.";
Acta Crystallogr. D 70:290-298(2014).
-!- FUNCTION: Intracellular carrier for long-chain fatty acids and
related active lipids, such as the endocannabinoid, that regulates
the metabolism and actions of the ligands they bind. In addition
to the cytosolic transport, selectively delivers specific fatty
acids from the cytosol to the nucleus, wherein they activate
nuclear receptors (PubMed:22170058). Delivers retinoic acid to the
nuclear receptor peroxisome proliferator-activated receptor delta;
which promotes proliferation and survival. May also serve as a
synaptic carrier of endocannabinoid at central synapses and thus
controls retrograde endocannabinoid signaling. Modulates
inflammation by regulating PTGES induction via NF-kappa-B
activation, and prostaglandin E2 (PGE2) biosynthesis during
inflammation (By similarity). May be involved in keratinocyte
differentiation (PubMed:8092987). {ECO:0000250|UniProtKB:Q05816,
ECO:0000269|PubMed:22170058, ECO:0000269|PubMed:8092987}.
-!- SUBUNIT: Monomer. Homodimer. {ECO:0000269|PubMed:24531463}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24692551,
ECO:0000269|PubMed:8092987}. Nucleus
{ECO:0000269|PubMed:24692551}. Cell junction, synapse
{ECO:0000250|UniProtKB:Q05816}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000250|UniProtKB:Q05816}. Secreted
{ECO:0000250|UniProtKB:Q05816}. Note=Localizes primarily to the
cytoplasm. Upon certain ligand binding, a conformation change
exposes a nuclear localization motif and the protein is
transported into nucleus (PubMed:24692551). Secreted by
astrocytes, but not by neurons (By similarity).
{ECO:0000250|UniProtKB:Q05816, ECO:0000269|PubMed:24692551}.
-!- TISSUE SPECIFICITY: Keratinocytes; highly expressed in psoriatic
skin. {ECO:0000269|PubMed:8092987}.
-!- DOMAIN: Forms a beta-barrel structure that accommodates the
hydrophobic ligand in its interior.
-!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
protein (FABP) family. {ECO:0000305}.
-!- CAUTION: While mouse FABP5 is found only in the monomeric form,
human FABP5 can exist as a monomer as well as a domain-swapped
dimer. {ECO:0000269|PubMed:24531463}.
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EMBL; M94856; AAA58467.1; -; mRNA.
EMBL; BT007449; AAP36117.1; -; mRNA.
EMBL; AK311856; BAG34797.1; -; mRNA.
EMBL; CH471068; EAW87088.1; -; Genomic_DNA.
EMBL; BC019385; AAH19385.1; -; mRNA.
EMBL; BC070303; AAH70303.1; -; mRNA.
CCDS; CCDS6228.1; -.
PIR; I56326; I56326.
RefSeq; NP_001435.1; NM_001444.2.
UniGene; Hs.408061; -.
PDB; 1B56; X-ray; 2.05 A; A=1-135.
PDB; 1JJJ; NMR; -; A=1-135.
PDB; 4AZM; X-ray; 2.75 A; A/B=1-135.
PDB; 4AZR; X-ray; 2.95 A; A/B=1-135.
PDB; 4LKP; X-ray; 1.67 A; A=1-135.
PDB; 4LKT; X-ray; 2.57 A; A/B/C/D=1-135.
PDB; 5HZ5; X-ray; 1.40 A; A=2-135.
PDB; 5UR9; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-135.
PDBsum; 1B56; -.
PDBsum; 1JJJ; -.
PDBsum; 4AZM; -.
PDBsum; 4AZR; -.
PDBsum; 4LKP; -.
PDBsum; 4LKT; -.
PDBsum; 5HZ5; -.
PDBsum; 5UR9; -.
ProteinModelPortal; Q01469; -.
SMR; Q01469; -.
BioGrid; 108469; 40.
IntAct; Q01469; 3.
STRING; 9606.ENSP00000297258; -.
BindingDB; Q01469; -.
ChEMBL; CHEMBL3674; -.
DrugBank; DB03796; Palmitic Acid.
GuidetoPHARMACOLOGY; 2535; -.
SwissLipids; SLP:000001104; -.
TCDB; 8.A.33.1.1; the fatty acid binding protein (fabp) family.
iPTMnet; Q01469; -.
PhosphoSitePlus; Q01469; -.
SwissPalm; Q01469; -.
BioMuta; FABP5; -.
DMDM; 232081; -.
SWISS-2DPAGE; Q01469; -.
UCD-2DPAGE; Q01469; -.
EPD; Q01469; -.
MaxQB; Q01469; -.
PaxDb; Q01469; -.
PeptideAtlas; Q01469; -.
PRIDE; Q01469; -.
ProteomicsDB; 57957; -.
TopDownProteomics; Q01469; -.
DNASU; 2171; -.
Ensembl; ENST00000297258; ENSP00000297258; ENSG00000164687.
GeneID; 2171; -.
KEGG; hsa:2171; -.
UCSC; uc003yca.3; human.
CTD; 2171; -.
DisGeNET; 2171; -.
EuPathDB; HostDB:ENSG00000164687.10; -.
GeneCards; FABP5; -.
HGNC; HGNC:3560; FABP5.
HPA; CAB017831; -.
HPA; CAB040577; -.
HPA; HPA051895; -.
MIM; 605168; gene.
neXtProt; NX_Q01469; -.
OpenTargets; ENSG00000164687; -.
PharmGKB; PA27961; -.
eggNOG; KOG4015; Eukaryota.
eggNOG; ENOG4111US8; LUCA.
GeneTree; ENSGT00760000118898; -.
HOGENOM; HOG000004829; -.
HOVERGEN; HBG005633; -.
InParanoid; Q01469; -.
KO; K08754; -.
OMA; VECDMNG; -.
OrthoDB; EOG091G0QSV; -.
PhylomeDB; Q01469; -.
TreeFam; TF316894; -.
Reactome; R-HSA-163560; Triglyceride catabolism.
Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
Reactome; R-HSA-6798695; Neutrophil degranulation.
EvolutionaryTrace; Q01469; -.
GeneWiki; FABP5; -.
GenomeRNAi; 2171; -.
PRO; PR:Q01469; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000164687; Expressed in 92 organ(s), highest expression level in ectocervix.
CleanEx; HS_FABP5; -.
ExpressionAtlas; Q01469; baseline and differential.
Genevisible; Q01469; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0008289; F:lipid binding; TAS:ProtInc.
GO; GO:0001972; F:retinoic acid binding; IEA:Ensembl.
GO; GO:0008544; P:epidermis development; TAS:ProtInc.
GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
GO; GO:0010829; P:negative regulation of glucose transmembrane transport; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; IEA:Ensembl.
GO; GO:0031392; P:regulation of prostaglandin biosynthetic process; IEA:Ensembl.
GO; GO:0099178; P:regulation of retrograde trans-synaptic signaling by endocanabinoid; ISS:UniProtKB.
GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl.
GO; GO:0019433; P:triglyceride catabolic process; TAS:Reactome.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR000463; Fatty_acid-bd.
InterPro; IPR031259; ILBP.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
PANTHER; PTHR11955; PTHR11955; 1.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR00178; FATTYACIDBP.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00214; FABP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell junction; Cell membrane;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disulfide bond; Lipid-binding; Membrane; Nucleus; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; Secreted; Synapse;
Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801}.
CHAIN 2 135 Fatty acid-binding protein 5.
/FTId=PRO_0000067377.
REGION 129 131 Fatty acid binding.
{ECO:0000244|PDB:1B56,
ECO:0000244|PDB:4AZM,
ECO:0000244|PDB:4LKT,
ECO:0000269|PubMed:10493790,
ECO:0000269|PubMed:24531463,
ECO:0000269|PubMed:24692551}.
MOTIF 24 34 Nuclear localization signal.
{ECO:0000269|PubMed:24692551}.
BINDING 43 43 Fatty acid. {ECO:0000244|PDB:4AZR,
ECO:0000269|PubMed:24531463}.
BINDING 56 56 Fatty acid.
{ECO:0000250|UniProtKB:Q05816}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801}.
MOD_RES 17 17 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 131 131 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
DISULFID 120 127 {ECO:0000244|PDB:1B56,
ECO:0000244|PDB:1JJJ,
ECO:0000244|PDB:4LKP,
ECO:0000244|PDB:5HZ5,
ECO:0000269|PubMed:10493790,
ECO:0000269|PubMed:12049637,
ECO:0000269|PubMed:24692551}.
MUTAGEN 24 24 K->A: Loss of ligand-induced nuclear
import; when associated with A-33 and A-
34. {ECO:0000269|PubMed:24692551}.
MUTAGEN 33 33 R->A: Loss of ligand-induced nuclear
import; when associated with A-24 and A-
34. {ECO:0000269|PubMed:24692551}.
MUTAGEN 34 34 K->A: Loss of ligand-induced nuclear
import; when associated with A-24 and A-
33. {ECO:0000269|PubMed:24692551}.
HELIX 4 7 {ECO:0000244|PDB:5HZ5}.
STRAND 9 18 {ECO:0000244|PDB:5HZ5}.
HELIX 19 25 {ECO:0000244|PDB:5HZ5}.
HELIX 30 38 {ECO:0000244|PDB:5HZ5}.
STRAND 42 48 {ECO:0000244|PDB:5HZ5}.
STRAND 51 57 {ECO:0000244|PDB:5HZ5}.
STRAND 63 68 {ECO:0000244|PDB:5HZ5}.
STRAND 73 76 {ECO:0000244|PDB:5HZ5}.
STRAND 78 80 {ECO:0000244|PDB:1JJJ}.
STRAND 82 90 {ECO:0000244|PDB:5HZ5}.
STRAND 93 100 {ECO:0000244|PDB:5HZ5}.
STRAND 103 112 {ECO:0000244|PDB:5HZ5}.
STRAND 115 122 {ECO:0000244|PDB:5HZ5}.
STRAND 125 134 {ECO:0000244|PDB:5HZ5}.
SEQUENCE 135 AA; 15164 MW; 77D38F8806143D63 CRC64;
MATVQQLEGR WRLVDSKGFD EYMKELGVGI ALRKMGAMAK PDCIITCDGK NLTIKTESTL
KTTQFSCTLG EKFEETTADG RKTQTVCNFT DGALVQHQEW DGKESTITRK LKDGKLVVEC
VMNNVTCTRI YEKVE


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