Full text data of FABP5
FABP5
[Confidence: low (only semi-automatic identification from reviews)]
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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q01469
ID FABP5_HUMAN Reviewed; 135 AA.
AC Q01469; B2R4K0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 157.
DE RecName: Full=Fatty acid-binding protein, epidermal;
DE AltName: Full=Epidermal-type fatty acid-binding protein;
DE Short=E-FABP;
DE AltName: Full=Fatty acid-binding protein 5;
DE AltName: Full=Psoriasis-associated fatty acid-binding protein homolog;
DE Short=PA-FABP;
GN Name=FABP5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT highly up-regulated in psoriatic skin and that shares similarity to
RT fatty acid-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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric 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 MASS
RP 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
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [9]
RP PROTEIN SEQUENCE OF 67-72 AND 104-110, AND CHARACTERIZATION.
RX PubMed=8092987;
RA Siegenthaler G., Hotz R., Chatellard-Gruaz D., Didierjean L.,
RA Hellman U., Saurat J.-H.;
RT "Purification and characterization of the human epidermal fatty acid-
RT binding protein: localization during epidermal cell differentiation in
RT vivo and in vitro.";
RL Biochem. J. 302:363-371(1994).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-131, AND MASS
RP SPECTROMETRY.
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
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH FATTY ACID, 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 [16]
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.,
RA Hanhoff T., Rueterjans H., Spener F., Luecke C.;
RT "Solution structure and backbone dynamics of human epidermal-type
RT fatty acid-binding protein (E-FABP).";
RL Biochem. J. 364:725-737(2002).
CC -!- FUNCTION: High specificity for fatty acids. Highest affinity for
CC C18 chain length. Decreasing the chain length or introducing
CC double bonds reduces the affinity. May be involved in keratinocyte
CC differentiation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Keratinocytes; highly expressed in psoriatic
CC skin.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates the
CC hydrophobic ligand in its interior.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family.
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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 PIR; I56326; I56326.
DR RefSeq; NP_001435.1; NM_001444.2.
DR UniGene; Hs.408061; -.
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 PDBsum; 1B56; -.
DR PDBsum; 1JJJ; -.
DR PDBsum; 4AZM; -.
DR PDBsum; 4AZR; -.
DR ProteinModelPortal; Q01469; -.
DR SMR; Q01469; 3-135.
DR IntAct; Q01469; 2.
DR MINT; MINT-3024261; -.
DR STRING; 9606.ENSP00000297258; -.
DR BindingDB; Q01469; -.
DR ChEMBL; CHEMBL3674; -.
DR TCDB; 8.A.33.1.1; the fatty acid binding protein (fabp) family.
DR PhosphoSite; Q01469; -.
DR DMDM; 232081; -.
DR SWISS-2DPAGE; Q01469; -.
DR UCD-2DPAGE; Q01469; -.
DR PaxDb; Q01469; -.
DR PRIDE; Q01469; -.
DR DNASU; 2171; -.
DR Ensembl; ENST00000297258; ENSP00000297258; ENSG00000164687.
DR GeneID; 2171; -.
DR KEGG; hsa:2171; -.
DR UCSC; uc003yca.2; human.
DR CTD; 2171; -.
DR GeneCards; GC08P082242; -.
DR HGNC; HGNC:3560; FABP5.
DR HPA; CAB017831; -.
DR HPA; CAB040577; -.
DR MIM; 605168; gene.
DR neXtProt; NX_Q01469; -.
DR PharmGKB; PA27961; -.
DR eggNOG; NOG309791; -.
DR HOGENOM; HOG000004829; -.
DR HOVERGEN; HBG005633; -.
DR InParanoid; Q01469; -.
DR KO; K08754; -.
DR OMA; TCHRVYE; -.
DR OrthoDB; EOG7NW6BZ; -.
DR PhylomeDB; Q01469; -.
DR EvolutionaryTrace; Q01469; -.
DR GeneWiki; FABP5; -.
DR GenomeRNAi; 2171; -.
DR NextBio; 8767; -.
DR PRO; PR:Q01469; -.
DR ArrayExpress; Q01469; -.
DR Bgee; Q01469; -.
DR CleanEx; HS_FABP5; -.
DR Genevestigator; Q01469; -.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; TAS:ProtInc.
DR GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR GO; GO:0015758; P:glucose transport; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR011038; Calycin-like.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Lipid-binding;
KW Phosphoprotein; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 135 Fatty acid-binding protein, epidermal.
FT /FTId=PRO_0000067377.
FT REGION 129 131 Fatty acid binding (By similarity).
FT BINDING 109 109 Fatty acid (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 17 17 N6-acetyllysine.
FT MOD_RES 131 131 Phosphotyrosine.
FT DISULFID 120 127
FT HELIX 4 7
FT STRAND 9 15
FT HELIX 19 26
FT HELIX 30 38
FT STRAND 42 48
FT STRAND 51 57
FT STRAND 62 68
FT STRAND 73 76
FT STRAND 78 80
FT STRAND 82 90
FT STRAND 93 100
FT STRAND 103 112
FT STRAND 115 122
FT STRAND 125 133
SQ SEQUENCE 135 AA; 15164 MW; 77D38F8806143D63 CRC64;
MATVQQLEGR WRLVDSKGFD EYMKELGVGI ALRKMGAMAK PDCIITCDGK NLTIKTESTL
KTTQFSCTLG EKFEETTADG RKTQTVCNFT DGALVQHQEW DGKESTITRK LKDGKLVVEC
VMNNVTCTRI YEKVE
//
ID FABP5_HUMAN Reviewed; 135 AA.
AC Q01469; B2R4K0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 157.
DE RecName: Full=Fatty acid-binding protein, epidermal;
DE AltName: Full=Epidermal-type fatty acid-binding protein;
DE Short=E-FABP;
DE AltName: Full=Fatty acid-binding protein 5;
DE AltName: Full=Psoriasis-associated fatty acid-binding protein homolog;
DE Short=PA-FABP;
GN Name=FABP5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT highly up-regulated in psoriatic skin and that shares similarity to
RT fatty acid-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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric 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 MASS
RP 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
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [9]
RP PROTEIN SEQUENCE OF 67-72 AND 104-110, AND CHARACTERIZATION.
RX PubMed=8092987;
RA Siegenthaler G., Hotz R., Chatellard-Gruaz D., Didierjean L.,
RA Hellman U., Saurat J.-H.;
RT "Purification and characterization of the human epidermal fatty acid-
RT binding protein: localization during epidermal cell differentiation in
RT vivo and in vitro.";
RL Biochem. J. 302:363-371(1994).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-131, AND MASS
RP SPECTROMETRY.
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
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH FATTY ACID, 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 [16]
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.,
RA Hanhoff T., Rueterjans H., Spener F., Luecke C.;
RT "Solution structure and backbone dynamics of human epidermal-type
RT fatty acid-binding protein (E-FABP).";
RL Biochem. J. 364:725-737(2002).
CC -!- FUNCTION: High specificity for fatty acids. Highest affinity for
CC C18 chain length. Decreasing the chain length or introducing
CC double bonds reduces the affinity. May be involved in keratinocyte
CC differentiation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Keratinocytes; highly expressed in psoriatic
CC skin.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates the
CC hydrophobic ligand in its interior.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family.
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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 PIR; I56326; I56326.
DR RefSeq; NP_001435.1; NM_001444.2.
DR UniGene; Hs.408061; -.
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 PDBsum; 1B56; -.
DR PDBsum; 1JJJ; -.
DR PDBsum; 4AZM; -.
DR PDBsum; 4AZR; -.
DR ProteinModelPortal; Q01469; -.
DR SMR; Q01469; 3-135.
DR IntAct; Q01469; 2.
DR MINT; MINT-3024261; -.
DR STRING; 9606.ENSP00000297258; -.
DR BindingDB; Q01469; -.
DR ChEMBL; CHEMBL3674; -.
DR TCDB; 8.A.33.1.1; the fatty acid binding protein (fabp) family.
DR PhosphoSite; Q01469; -.
DR DMDM; 232081; -.
DR SWISS-2DPAGE; Q01469; -.
DR UCD-2DPAGE; Q01469; -.
DR PaxDb; Q01469; -.
DR PRIDE; Q01469; -.
DR DNASU; 2171; -.
DR Ensembl; ENST00000297258; ENSP00000297258; ENSG00000164687.
DR GeneID; 2171; -.
DR KEGG; hsa:2171; -.
DR UCSC; uc003yca.2; human.
DR CTD; 2171; -.
DR GeneCards; GC08P082242; -.
DR HGNC; HGNC:3560; FABP5.
DR HPA; CAB017831; -.
DR HPA; CAB040577; -.
DR MIM; 605168; gene.
DR neXtProt; NX_Q01469; -.
DR PharmGKB; PA27961; -.
DR eggNOG; NOG309791; -.
DR HOGENOM; HOG000004829; -.
DR HOVERGEN; HBG005633; -.
DR InParanoid; Q01469; -.
DR KO; K08754; -.
DR OMA; TCHRVYE; -.
DR OrthoDB; EOG7NW6BZ; -.
DR PhylomeDB; Q01469; -.
DR EvolutionaryTrace; Q01469; -.
DR GeneWiki; FABP5; -.
DR GenomeRNAi; 2171; -.
DR NextBio; 8767; -.
DR PRO; PR:Q01469; -.
DR ArrayExpress; Q01469; -.
DR Bgee; Q01469; -.
DR CleanEx; HS_FABP5; -.
DR Genevestigator; Q01469; -.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; TAS:ProtInc.
DR GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR GO; GO:0015758; P:glucose transport; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR011038; Calycin-like.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Lipid-binding;
KW Phosphoprotein; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 135 Fatty acid-binding protein, epidermal.
FT /FTId=PRO_0000067377.
FT REGION 129 131 Fatty acid binding (By similarity).
FT BINDING 109 109 Fatty acid (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 17 17 N6-acetyllysine.
FT MOD_RES 131 131 Phosphotyrosine.
FT DISULFID 120 127
FT HELIX 4 7
FT STRAND 9 15
FT HELIX 19 26
FT HELIX 30 38
FT STRAND 42 48
FT STRAND 51 57
FT STRAND 62 68
FT STRAND 73 76
FT STRAND 78 80
FT STRAND 82 90
FT STRAND 93 100
FT STRAND 103 112
FT STRAND 115 122
FT STRAND 125 133
SQ SEQUENCE 135 AA; 15164 MW; 77D38F8806143D63 CRC64;
MATVQQLEGR WRLVDSKGFD EYMKELGVGI ALRKMGAMAK PDCIITCDGK NLTIKTESTL
KTTQFSCTLG EKFEETTADG RKTQTVCNFT DGALVQHQEW DGKESTITRK LKDGKLVVEC
VMNNVTCTRI YEKVE
//
MIM
605168
*RECORD*
*FIELD* NO
605168
*FIELD* TI
*605168 FATTY ACID-BINDING PROTEIN 5; FABP5
;;FATTY ACID-BINDING PROTEIN, PSORIASIS-ASSOCIATED; PAFABP;;
read moreFATTY ACID-BINDING PROTEIN, EPIDERMAL; EFABP
*FIELD* TX
DESCRIPTION
Fatty acid-binding proteins (FABPs) bind free fatty acids and regulate
lipid metabolism and transport. See also FABP3 (134651).
CLONING
Using 2D gel electrophoresis, Madsen et al. (1992) isolated a fatty
acid-binding protein, designated PAFABP for 'psoriasis-associated fatty
acid-binding protein,' upregulated in noncultured psoriatic skin
keratinocytes. The protein was microsequenced, and degenerate
oligonucleotides based on the amino acid sequence were used to screen a
lambda-gt11 cDNA library prepared from noncultured psoriatic
keratinocytes. The PAFABP cDNA encodes a 135-amino acid protein with
molecular weight 15,164. By Northern blot analysis, the authors detected
elevated levels of PAFABP message in noncultured psoriatic keratinocytes
as compared to normal keratinocytes. PAFABP mRNA was also observed in
transformed human epithelial cell lines, A431 epidermoid carcinoma
cells, transformed human amnion (AMA) cells, and lymphoid Molt 4 cells.
PAFABP protein was increased in primary normal keratinocytes induced to
differentiate, as determined by 2D gel electrophoresis.
Hertzel and Bernlohr (1998) cloned mouse keratinocyte lipid-binding
protein (KLBP), the murine ortholog of human EFABP.
MAPPING
Hertzel and Bernlohr (1998) mapped the mouse Klbp gene to chromosome
3A3, within a region sharing homology of synteny with human chromosomes
3, 4, and 8.
GENE FUNCTION
Siegenthaler et al. (1994) characterized EFABP, which they determined to
be identical to PAFABP by peptide sequencing. EFABP is abundant in
psoriatic skin lesions. Purified EFABP specifically and reversibly binds
oleic, linoleic, and stearic acids, but not cholesterol or retinoids.
Use of antibodies specific for EFABP detected the protein in psoriatic
lesions, heart, intestine, and adipose tissue. High levels of EFABP were
also observed in abnormally differentiated epidermis.
Immunohistochemistry localized EFABP to the stratum granulosum of normal
skin.
The endocannabinoid anandamide, arachidonoyl ethanolamide (AEA), is a
neuromodulatory lipid expected to have limited diffusion through the
aqueous cytosol because of its hydrophobic character. In COS-7 cells,
Kaczocha et al. (2009) identified FABP5 and FABP7 (602965) as cytosolic
proteins that transport AEA from the plasma membrane to subcellular
fatty acid amide hydrolase (FAAH; 602935), where it is hydrolyzed and
inactivated. FABP3 did not show this specific transport function.
*FIELD* RF
1. Hertzel, A. V.; Bernlohr, D. A.: Cloning and chromosomal location
of the murine keratinocyte lipid-binding protein gene. Gene 221:
235-243, 1998.
2. Kaczocha, M.; Glaser, S. T.; Deutsch, D. G.: Identification of
intracellular carriers for the endocannabinoid anandamide. Proc.
Nat. Acad. Sci. 106: 6375-6380, 2009.
3. Madsen, P.; 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. Derm. 99: 299-305, 1992.
4. 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.
*FIELD* CN
Cassandra L. Kniffin - updated: 11/20/2009
*FIELD* CD
Stefanie A. Nelson: 7/24/2000
*FIELD* ED
wwang: 12/10/2009
ckniffin: 11/20/2009
alopez: 8/1/2000
alopez: 7/26/2000
alopez: 7/25/2000
*RECORD*
*FIELD* NO
605168
*FIELD* TI
*605168 FATTY ACID-BINDING PROTEIN 5; FABP5
;;FATTY ACID-BINDING PROTEIN, PSORIASIS-ASSOCIATED; PAFABP;;
read moreFATTY ACID-BINDING PROTEIN, EPIDERMAL; EFABP
*FIELD* TX
DESCRIPTION
Fatty acid-binding proteins (FABPs) bind free fatty acids and regulate
lipid metabolism and transport. See also FABP3 (134651).
CLONING
Using 2D gel electrophoresis, Madsen et al. (1992) isolated a fatty
acid-binding protein, designated PAFABP for 'psoriasis-associated fatty
acid-binding protein,' upregulated in noncultured psoriatic skin
keratinocytes. The protein was microsequenced, and degenerate
oligonucleotides based on the amino acid sequence were used to screen a
lambda-gt11 cDNA library prepared from noncultured psoriatic
keratinocytes. The PAFABP cDNA encodes a 135-amino acid protein with
molecular weight 15,164. By Northern blot analysis, the authors detected
elevated levels of PAFABP message in noncultured psoriatic keratinocytes
as compared to normal keratinocytes. PAFABP mRNA was also observed in
transformed human epithelial cell lines, A431 epidermoid carcinoma
cells, transformed human amnion (AMA) cells, and lymphoid Molt 4 cells.
PAFABP protein was increased in primary normal keratinocytes induced to
differentiate, as determined by 2D gel electrophoresis.
Hertzel and Bernlohr (1998) cloned mouse keratinocyte lipid-binding
protein (KLBP), the murine ortholog of human EFABP.
MAPPING
Hertzel and Bernlohr (1998) mapped the mouse Klbp gene to chromosome
3A3, within a region sharing homology of synteny with human chromosomes
3, 4, and 8.
GENE FUNCTION
Siegenthaler et al. (1994) characterized EFABP, which they determined to
be identical to PAFABP by peptide sequencing. EFABP is abundant in
psoriatic skin lesions. Purified EFABP specifically and reversibly binds
oleic, linoleic, and stearic acids, but not cholesterol or retinoids.
Use of antibodies specific for EFABP detected the protein in psoriatic
lesions, heart, intestine, and adipose tissue. High levels of EFABP were
also observed in abnormally differentiated epidermis.
Immunohistochemistry localized EFABP to the stratum granulosum of normal
skin.
The endocannabinoid anandamide, arachidonoyl ethanolamide (AEA), is a
neuromodulatory lipid expected to have limited diffusion through the
aqueous cytosol because of its hydrophobic character. In COS-7 cells,
Kaczocha et al. (2009) identified FABP5 and FABP7 (602965) as cytosolic
proteins that transport AEA from the plasma membrane to subcellular
fatty acid amide hydrolase (FAAH; 602935), where it is hydrolyzed and
inactivated. FABP3 did not show this specific transport function.
*FIELD* RF
1. Hertzel, A. V.; Bernlohr, D. A.: Cloning and chromosomal location
of the murine keratinocyte lipid-binding protein gene. Gene 221:
235-243, 1998.
2. Kaczocha, M.; Glaser, S. T.; Deutsch, D. G.: Identification of
intracellular carriers for the endocannabinoid anandamide. Proc.
Nat. Acad. Sci. 106: 6375-6380, 2009.
3. Madsen, P.; 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. Derm. 99: 299-305, 1992.
4. 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.
*FIELD* CN
Cassandra L. Kniffin - updated: 11/20/2009
*FIELD* CD
Stefanie A. Nelson: 7/24/2000
*FIELD* ED
wwang: 12/10/2009
ckniffin: 11/20/2009
alopez: 8/1/2000
alopez: 7/26/2000
alopez: 7/25/2000