ID FABP5_HUMAN Reviewed; 135 AA.
AC Q01469; B2R4K0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 239.
DE RecName: Full=Fatty acid-binding protein 5 {ECO:0000305};
DE AltName: Full=Epidermal-type fatty acid-binding protein {ECO:0000303|PubMed:8092987};
DE Short=E-FABP {ECO:0000303|PubMed:8092987};
DE AltName: Full=Fatty acid-binding protein, epidermal;
DE AltName: Full=Psoriasis-associated fatty acid-binding protein homolog;
DE Short=PA-FABP;
GN Name=FABP5 {ECO:0000312|HGNC:HGNC:3560};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Keratinocyte;
RX PubMed=1512466; DOI=10.1111/1523-1747.ep12616641;
RA Madsen P.S., Rasmussen H.H., Leffers H., Honore B., Celis J.E.;
RT "Molecular cloning and expression of a novel keratinocyte protein
RT (psoriasis-associated fatty acid-binding protein [PA-FABP]) that is highly
RT up-regulated in psoriatic skin and that shares similarity to fatty acid-
RT binding proteins.";
RL J. Invest. Dermatol. 99:299-305(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP PROTEIN SEQUENCE OF 18-33; 35-50; 62-103 AND 116-129, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 25-33; 39-50; 62-71; 83-101 AND 120-129.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [9]
RP PROTEIN SEQUENCE OF 67-72 AND 104-110, CHARACTERIZATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=8092987; DOI=10.1042/bj3020363;
RA Siegenthaler G., Hotz R., Chatellard-Gruaz D., Didierjean L., Hellman U.,
RA Saurat J.-H.;
RT "Purification and characterization of the human epidermal fatty acid-
RT binding protein: localization during epidermal cell differentiation in vivo
RT and in vitro.";
RL Biochem. J. 302:363-371(1994).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=21395585; DOI=10.1111/j.1471-4159.2011.07245.x;
RA Mitchell R.W., On N.H., Del Bigio M.R., Miller D.W., Hatch G.M.;
RT "Fatty acid transport protein expression in human brain and potential role
RT in fatty acid transport across human brain microvessel endothelial cells.";
RL J. Neurochem. 117:735-746(2011).
RN [15]
RP FUNCTION.
RX PubMed=22170058; DOI=10.1074/jbc.m111.304907;
RA Kaczocha M., Vivieca S., Sun J., Glaser S.T., Deutsch D.G.;
RT "Fatty acid-binding proteins transport N-acylethanolamines to nuclear
RT receptors and are targets of endocannabinoid transport inhibitors.";
RL J. Biol. Chem. 287:3415-3424(2012).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19] {ECO:0007744|PDB:1B56}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH PALMITATE, AND
RP DISULFIDE BOND.
RX PubMed=10493790; DOI=10.1021/bi990305u;
RA Hohoff C., Borchers T., Rustow B., Spener F., van Tilbeurgh H.;
RT "Expression, purification and crystal structure determination of
RT recombinant human epidermal-type fatty acid-binding protein.";
RL Biochemistry 38:12229-12239(1999).
RN [20] {ECO:0007744|PDB:1JJJ}
RP STRUCTURE BY NMR, AND DISULFIDE BOND.
RX PubMed=12049637; DOI=10.1042/bj20020039;
RA Gutierrez-Gonzalez L.H., Ludwig C., Hohoff C., Rademacher M., Hanhoff T.,
RA Rueterjans H., Spener F., Luecke C.;
RT "Solution structure and backbone dynamics of human epidermal-type fatty
RT acid-binding protein (E-FABP).";
RL Biochem. J. 364:725-737(2002).
RN [21] {ECO:0007744|PDB:4LKP, ECO:0007744|PDB:4LKT}
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH LINOLEATE, DISULFIDE
RP BONDS, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-24; ARG-33 AND LYS-34, AND
RP NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=24692551; DOI=10.1074/jbc.m113.514646;
RA Armstrong E.H., Goswami D., Griffin P.R., Noy N., Ortlund E.A.;
RT "Structural basis for ligand regulation of the fatty acid-binding protein
RT 5, peroxisome proliferator-activated receptor beta/delta (FABP5-
RT PPARbeta/delta) signaling pathway.";
RL J. Biol. Chem. 289:14941-14954(2014).
RN [22] {ECO:0007744|PDB:4AZM, ECO:0007744|PDB:4AZR}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS), SUBUNIT, AND IN COMPLEX WITH
RP N-ARACHIDONOYLETHANOLAMIDE OR SYNTHETIC INHIBITOR BMS-309403.
RX PubMed=24531463; DOI=10.1107/s1399004713026795;
RA Sanson B., Wang T., Sun J., Wang L., Kaczocha M., Ojima I., Deutsch D.,
RA Li H.;
RT "Crystallographic study of FABP5 as an intracellular endocannabinoid
RT transporter.";
RL Acta Crystallogr. D 70:290-298(2014).
CC -!- FUNCTION: Intracellular carrier for long-chain fatty acids and related
CC active lipids, such as endocannabinoids, that regulate the metabolism
CC and actions of the ligands they bind. In addition to the cytosolic
CC transport, selectively delivers specific fatty acids from the cytosol
CC to the nucleus, wherein they activate nuclear receptors
CC (PubMed:22170058, PubMed:21395585). Delivers retinoic acid to the
CC nuclear receptor peroxisome proliferator-activated receptor delta;
CC which promotes proliferation and survival. May also serve as a synaptic
CC carrier of endocannabinoid at central synapses and thus controls
CC retrograde endocannabinoid signaling. Modulates inflammation by
CC regulating PTGES induction via NF-kappa-B activation, and prostaglandin
CC E2 (PGE2) biosynthesis during inflammation (By similarity). May be
CC involved in keratinocyte differentiation (PubMed:8092987).
CC {ECO:0000250|UniProtKB:Q05816, ECO:0000269|PubMed:21395585,
CC ECO:0000269|PubMed:22170058, ECO:0000269|PubMed:8092987}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256,
CC ChEBI:CHEBI:7896; Evidence={ECO:0000269|PubMed:21395585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate(out) = (9Z,12Z)-
CC octadecadienoate(in); Xref=Rhea:RHEA:45264, ChEBI:CHEBI:30245;
CC Evidence={ECO:0000269|PubMed:21395585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in);
CC Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000269|PubMed:21395585};
CC -!- SUBUNIT: Monomer. Homodimer. {ECO:0000269|PubMed:24531463}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24692551,
CC ECO:0000269|PubMed:8092987}. Nucleus {ECO:0000269|PubMed:24692551}.
CC Synapse {ECO:0000250|UniProtKB:Q05816}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q05816}. Secreted
CC {ECO:0000250|UniProtKB:Q05816}. Note=Localizes primarily to the
CC cytoplasm. Upon certain ligand binding, a conformation change exposes a
CC nuclear localization motif and the protein is transported into nucleus
CC (PubMed:24692551). Secreted by astrocytes, but not by neurons (By
CC similarity). {ECO:0000250|UniProtKB:Q05816,
CC ECO:0000269|PubMed:24692551}.
CC -!- TISSUE SPECIFICITY: Keratinocytes; highly expressed in psoriatic skin
CC (PubMed:8092987). Expressed in brain gray matter (PubMed:21395585).
CC {ECO:0000269|PubMed:21395585, ECO:0000269|PubMed:8092987}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic
CC ligand in its interior.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
CC -!- CAUTION: While mouse FABP5 is found only in the monomeric form, human
CC FABP5 can exist as a monomer as well as a domain-swapped dimer.
CC {ECO:0000269|PubMed:24531463}.
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DR EMBL; M94856; AAA58467.1; -; mRNA.
DR EMBL; BT007449; AAP36117.1; -; mRNA.
DR EMBL; AK311856; BAG34797.1; -; mRNA.
DR EMBL; CH471068; EAW87088.1; -; Genomic_DNA.
DR EMBL; BC019385; AAH19385.1; -; mRNA.
DR EMBL; BC070303; AAH70303.1; -; mRNA.
DR CCDS; CCDS6228.1; -.
DR PIR; I56326; I56326.
DR RefSeq; NP_001435.1; NM_001444.2.
DR PDB; 1B56; X-ray; 2.05 A; A=1-135.
DR PDB; 1JJJ; NMR; -; A=1-135.
DR PDB; 4AZM; X-ray; 2.75 A; A/B=1-135.
DR PDB; 4AZR; X-ray; 2.95 A; A/B=1-135.
DR PDB; 4LKP; X-ray; 1.67 A; A=1-135.
DR PDB; 4LKT; X-ray; 2.57 A; A/B/C/D=1-135.
DR PDB; 5HZ5; X-ray; 1.40 A; A=2-135.
DR PDB; 5UR9; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-135.
DR PDB; 7FWI; X-ray; 2.00 A; A/B/C=1-135.
DR PDB; 7FXD; X-ray; 2.44 A; A=1-135.
DR PDB; 7FY0; X-ray; 1.34 A; A=1-135.
DR PDB; 7FYD; X-ray; 1.45 A; A=1-135.
DR PDB; 7G01; X-ray; 1.17 A; A=1-135.
DR PDB; 7G04; X-ray; 1.40 A; A/B=1-135.
DR PDB; 7G0B; X-ray; 1.47 A; A=1-135.
DR PDB; 7G0E; X-ray; 1.11 A; A=1-135.
DR PDB; 7G1Q; X-ray; 1.24 A; A=1-135.
DR PDBsum; 1B56; -.
DR PDBsum; 1JJJ; -.
DR PDBsum; 4AZM; -.
DR PDBsum; 4AZR; -.
DR PDBsum; 4LKP; -.
DR PDBsum; 4LKT; -.
DR PDBsum; 5HZ5; -.
DR PDBsum; 5UR9; -.
DR PDBsum; 7FWI; -.
DR PDBsum; 7FXD; -.
DR PDBsum; 7FY0; -.
DR PDBsum; 7FYD; -.
DR PDBsum; 7G01; -.
DR PDBsum; 7G04; -.
DR PDBsum; 7G0B; -.
DR PDBsum; 7G0E; -.
DR PDBsum; 7G1Q; -.
DR AlphaFoldDB; Q01469; -.
DR SMR; Q01469; -.
DR BioGRID; 108469; 135.
DR IntAct; Q01469; 26.
DR MINT; Q01469; -.
DR STRING; 9606.ENSP00000297258; -.
DR BindingDB; Q01469; -.
DR ChEMBL; CHEMBL3674; -.
DR DrugBank; DB03796; Palmitic Acid.
DR DrugCentral; Q01469; -.
DR GuidetoPHARMACOLOGY; 2535; -.
DR SwissLipids; SLP:000001104; -.
DR TCDB; 8.A.33.1.1; the fatty acid binding protein (fabp) family.
DR GlyGen; Q01469; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q01469; -.
DR MetOSite; Q01469; -.
DR PhosphoSitePlus; Q01469; -.
DR SwissPalm; Q01469; -.
DR BioMuta; FABP5; -.
DR DMDM; 232081; -.
DR SWISS-2DPAGE; Q01469; -.
DR UCD-2DPAGE; Q01469; -.
DR EPD; Q01469; -.
DR jPOST; Q01469; -.
DR MassIVE; Q01469; -.
DR MaxQB; Q01469; -.
DR PaxDb; 9606-ENSP00000297258; -.
DR PeptideAtlas; Q01469; -.
DR PRIDE; Q01469; -.
DR ProteomicsDB; 57957; -.
DR TopDownProteomics; Q01469; -.
DR Antibodypedia; 25313; 474 antibodies from 37 providers.
DR CPTC; Q01469; 3 antibodies.
DR DNASU; 2171; -.
DR Ensembl; ENST00000297258.11; ENSP00000297258.6; ENSG00000164687.11.
DR GeneID; 2171; -.
DR KEGG; hsa:2171; -.
DR MANE-Select; ENST00000297258.11; ENSP00000297258.6; NM_001444.3; NP_001435.1.
DR UCSC; uc003yca.3; human.
DR AGR; HGNC:3560; -.
DR CTD; 2171; -.
DR DisGeNET; 2171; -.
DR GeneCards; FABP5; -.
DR HGNC; HGNC:3560; FABP5.
DR HPA; ENSG00000164687; Tissue enhanced (choroid plexus, esophagus, vagina).
DR MIM; 605168; gene.
DR neXtProt; NX_Q01469; -.
DR OpenTargets; ENSG00000164687; -.
DR PharmGKB; PA27961; -.
DR VEuPathDB; HostDB:ENSG00000164687; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000154530; -.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; Q01469; -.
DR OMA; WCLISSE; -.
DR OrthoDB; 46617at2759; -.
DR PhylomeDB; Q01469; -.
DR TreeFam; TF316894; -.
DR PathwayCommons; Q01469; -.
DR Reactome; R-HSA-163560; Triglyceride catabolism.
DR Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q01469; -.
DR SIGNOR; Q01469; -.
DR BioGRID-ORCS; 2171; 46 hits in 1034 CRISPR screens.
DR ChiTaRS; FABP5; human.
DR EvolutionaryTrace; Q01469; -.
DR GeneWiki; FABP5; -.
DR GenomeRNAi; 2171; -.
DR Pharos; Q01469; Tchem.
DR PRO; PR:Q01469; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q01469; Protein.
DR Bgee; ENSG00000164687; Expressed in lower esophagus mucosa and 99 other cell types or tissues.
DR ExpressionAtlas; Q01469; baseline and differential.
DR Genevisible; Q01469; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; TAS:ProtInc.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IMP:ARUK-UCL.
DR GO; GO:0001972; F:retinoic acid binding; IEA:Ensembl.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:1990379; P:lipid transport across blood-brain barrier; IMP:ARUK-UCL.
DR GO; GO:0015909; P:long-chain fatty acid transport; IMP:ARUK-UCL.
DR GO; GO:0010829; P:negative regulation of glucose transmembrane transport; IEA:Ensembl.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0031392; P:regulation of prostaglandin biosynthetic process; IEA:Ensembl.
DR GO; GO:0099178; P:regulation of retrograde trans-synaptic signaling by endocanabinoid; ISS:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl.
DR CDD; cd19468; FABP5; 1.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; FATTY ACID BINDING PROTEIN; 1.
DR PANTHER; PTHR11955:SF58; FATTY ACID-BINDING PROTEIN 5; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; Lipocalins; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Lipid transport; Lipid-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Secreted; Synapse; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..135
FT /note="Fatty acid-binding protein 5"
FT /id="PRO_0000067377"
FT MOTIF 24..34
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:24692551"
FT BINDING 43
FT /ligand="N-eicosanoyl ethanolamine"
FT /ligand_id="ChEBI:CHEBI:85253"
FT /evidence="ECO:0000269|PubMed:24531463,
FT ECO:0007744|PDB:4AZR"
FT BINDING 109
FT /ligand="N-eicosanoyl ethanolamine"
FT /ligand_id="ChEBI:CHEBI:85253"
FT /evidence="ECO:0000269|PubMed:24531463,
FT ECO:0007744|PDB:4AZR"
FT BINDING 129..131
FT /ligand="(9Z,12Z)-octadecadienoate"
FT /ligand_id="ChEBI:CHEBI:30245"
FT /evidence="ECO:0000269|PubMed:24692551,
FT ECO:0007744|PDB:4LKT"
FT BINDING 131
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:10493790,
FT ECO:0007744|PDB:1B56"
FT BINDING 131
FT /ligand="N-eicosanoyl ethanolamine"
FT /ligand_id="ChEBI:CHEBI:85253"
FT /evidence="ECO:0000269|PubMed:24531463,
FT ECO:0007744|PDB:4AZR"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 131
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT DISULFID 120..127
FT /evidence="ECO:0000269|PubMed:10493790,
FT ECO:0000269|PubMed:12049637, ECO:0000269|PubMed:24692551,
FT ECO:0007744|PDB:1B56, ECO:0007744|PDB:1JJJ,
FT ECO:0007744|PDB:4LKP, ECO:0007744|PDB:5HZ5"
FT MUTAGEN 24
FT /note="K->A: Loss of ligand-induced nuclear import; when
FT associated with A-33 and A-34."
FT /evidence="ECO:0000269|PubMed:24692551"
FT MUTAGEN 33
FT /note="R->A: Loss of ligand-induced nuclear import; when
FT associated with A-24 and A-34."
FT /evidence="ECO:0000269|PubMed:24692551"
FT MUTAGEN 34
FT /note="K->A: Loss of ligand-induced nuclear import; when
FT associated with A-24 and A-33."
FT /evidence="ECO:0000269|PubMed:24692551"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:5HZ5"
FT STRAND 9..18
FT /evidence="ECO:0007829|PDB:5HZ5"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:5HZ5"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:5HZ5"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:5HZ5"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:5HZ5"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:5HZ5"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:5HZ5"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1JJJ"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:5HZ5"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:5HZ5"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:5HZ5"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:5HZ5"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:5HZ5"
SQ SEQUENCE 135 AA; 15164 MW; 77D38F8806143D63 CRC64;
MATVQQLEGR WRLVDSKGFD EYMKELGVGI ALRKMGAMAK PDCIITCDGK NLTIKTESTL
KTTQFSCTLG EKFEETTADG RKTQTVCNFT DGALVQHQEW DGKESTITRK LKDGKLVVEC
VMNNVTCTRI YEKVE
//
