FABPH_HUMAN
ID FABPH_HUMAN Reviewed; 133 AA.
AC P05413; B2RAB6; Q5VV93; Q99957;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Fatty acid-binding protein, heart;
DE AltName: Full=Fatty acid-binding protein 3;
DE AltName: Full=Heart-type fatty acid-binding protein;
DE Short=H-FABP;
DE AltName: Full=Mammary-derived growth inhibitor;
DE Short=MDGI;
DE AltName: Full=Muscle fatty acid-binding protein;
DE Short=M-FABP;
GN Name=FABP3; Synonyms=FABP11, MDGI;
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].
RC TISSUE=Skeletal muscle;
RX PubMed=1710107; DOI=10.1042/bj2760203;
RA Peeter R.A., Veerkamp J.H., Kanda T., Ono T., Geurts van Kessel A.;
RT "Cloning of the cDNA encoding human skeletal-muscle fatty-acid-binding
RT protein, its peptide sequence and chromosomal localization.";
RL Biochem. J. 276:203-207(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RA Hu Y.F., Ao X., Russo I.H., Russo J.;
RT "Molecular cloning of human mammary-derived growth inhibitor (MDGI) reveals
RT that its expression is associated with breast differentiation, but not with
RT cancer progression.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wu X., Arlt M., Goodfellow P.J., Rottman J.N.;
RT "Genomic organization and complete nucleotide sequence of the human cardiac
RT fatty acid binding protein gene (FABP3), and identification of a closely
RT related genomic sequence.";
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [9]
RP PROTEIN SEQUENCE OF 2-133.
RX PubMed=3421901; DOI=10.1042/bj2520191;
RA Offner G.D., Brecher P., Sawlivich W.B., Costello C.E., Troxler R.F.;
RT "Characterization and amino acid sequence of a fatty acid-binding protein
RT from human heart.";
RL Biochem. J. 252:191-198(1988).
RN [10]
RP PROTEIN SEQUENCE OF 2-133, AND SEQUENCE REVISION.
RX PubMed=2266954; DOI=10.1007/bf00231376;
RA Boerchers T., Hoejrup P., Nielsen S.U., Roepstorff P., Spener F.,
RA Knudsen J.;
RT "Revision of the amino acid sequence of human heart fatty acid-binding
RT protein.";
RL Mol. Cell. Biochem. 98:127-133(1990).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-133.
RC TISSUE=Heart;
RX PubMed=8262516; DOI=10.1007/bf00420939;
RA Troxler R.F., Offner G.D., Jiang J.W., Wu B.L., Skare J.C., Milunsky A.,
RA Wyandt H.E.;
RT "Localization of the gene for human heart fatty acid binding protein to
RT chromosome 1p32-1p33.";
RL Hum. Genet. 92:563-566(1993).
RN [12]
RP PROTEIN SEQUENCE OF 23-31; 46-53; 67-80; 98-107 AND 114-127, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [13]
RP PROTEIN SEQUENCE OF 32-39.
RC TISSUE=Heart;
RX PubMed=7498159; DOI=10.1002/elps.11501601192;
RA Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A.,
RA Ershova E.S., Egorov T.A., Musalyamov A.K.;
RT "The major protein expression profile and two-dimensional protein database
RT of human heart.";
RL Electrophoresis 16:1160-1169(1995).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-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 [15] {ECO:0007744|PDB:2HMB}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH PALMITATE.
RX PubMed=1526991; DOI=10.2210/pdb2hmb/pdb;
RA Zanotti G., Scapin G., Spadon P., Veerkamp J.H., Sacchettini J.C.;
RT "Three-dimensional structure of recombinant human muscle fatty acid-binding
RT protein.";
RL J. Biol. Chem. 267:18541-18550(1992).
RN [16] {ECO:0007744|PDB:1HMR, ECO:0007744|PDB:1HMS, ECO:0007744|PDB:1HMT}
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEXES WITH C18 FATTY ACIDS.
RX PubMed=7922029; DOI=10.1016/s0969-2126(00)00052-6;
RA Young A.C.M., Scapin G., Kromminga A., Patel S.B., Veerkamp J.H.,
RA Sacchettini J.C.;
RT "Structural studies on human muscle fatty acid binding protein at 1.4-A
RT resolution: binding interactions with three C18 fatty acids.";
RL Structure 2:523-534(1994).
RN [17]
RP STRUCTURE BY NMR.
RX PubMed=11171102; DOI=10.1042/0264-6021:3540259;
RA Luecke C., Rademacher M., Zimmerman A.W., van Moerkerk H.T.B.,
RA Veerkamp J.H., Rueterjans H.;
RT "Spin-system heterogeneities indicate a selected-fit mechanism in fatty
RT acid binding to heart-type fatty acid-binding protein (H-FABP).";
RL Biochem. J. 354:259-266(2001).
CC -!- FUNCTION: FABP are thought to play a role in the intracellular
CC transport of long-chain fatty acids and their acyl-CoA esters.
CC -!- INTERACTION:
CC P05413; P37198: NUP62; NbExp=7; IntAct=EBI-704216, EBI-347978;
CC P05413; A0MZ66: SHTN1; NbExp=3; IntAct=EBI-704216, EBI-308778;
CC P05413; A0MZ66-4: SHTN1; NbExp=3; IntAct=EBI-704216, EBI-12097232;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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}.
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DR EMBL; X56549; CAA39889.1; -; mRNA.
DR EMBL; Y10255; CAA71305.1; -; mRNA.
DR EMBL; U57623; AAB02555.1; -; Genomic_DNA.
DR EMBL; AK314122; BAG36813.1; -; mRNA.
DR EMBL; U17081; AAC99800.1; -; Genomic_DNA.
DR EMBL; S67314; AAB29294.1; -; mRNA.
DR EMBL; BT006727; AAP35373.1; -; mRNA.
DR EMBL; AL451070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07619.1; -; Genomic_DNA.
DR EMBL; BC007021; AAH07021.1; -; mRNA.
DR CCDS; CCDS342.1; -.
DR PIR; S15432; FZHUC.
DR RefSeq; NP_004093.1; NM_004102.4.
DR PDB; 1G5W; NMR; -; A=2-133.
DR PDB; 1HMR; X-ray; 1.40 A; A=2-133.
DR PDB; 1HMS; X-ray; 1.40 A; A=2-133.
DR PDB; 1HMT; X-ray; 1.40 A; A=2-133.
DR PDB; 2HMB; X-ray; 2.10 A; A=2-133.
DR PDB; 3RSW; X-ray; 2.60 A; A/B=1-133.
DR PDB; 3WBG; X-ray; 2.15 A; A/B/C/D=1-133.
DR PDB; 3WVM; X-ray; 0.88 A; A=1-133.
DR PDB; 3WXQ; X-ray; 1.60 A; A=1-133.
DR PDB; 4TJZ; X-ray; 0.87 A; A=1-133.
DR PDB; 4TKB; X-ray; 0.86 A; A=1-133.
DR PDB; 4TKH; X-ray; 0.93 A; A=1-133.
DR PDB; 4TKJ; X-ray; 0.87 A; A=1-133.
DR PDB; 4WBK; X-ray; 1.37 A; A=1-133.
DR PDB; 5B27; X-ray; 1.02 A; A=1-133.
DR PDB; 5B28; X-ray; 0.90 A; A=1-133.
DR PDB; 5B29; X-ray; 1.28 A; A=2-133.
DR PDB; 5CE4; Other; 0.98 A; A=1-132.
DR PDB; 5HZ9; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-133.
DR PDB; 6AQ1; X-ray; 1.40 A; A/B=1-133.
DR PDB; 7EGO; X-ray; 1.21 A; A=1-133.
DR PDBsum; 1G5W; -.
DR PDBsum; 1HMR; -.
DR PDBsum; 1HMS; -.
DR PDBsum; 1HMT; -.
DR PDBsum; 2HMB; -.
DR PDBsum; 3RSW; -.
DR PDBsum; 3WBG; -.
DR PDBsum; 3WVM; -.
DR PDBsum; 3WXQ; -.
DR PDBsum; 4TJZ; -.
DR PDBsum; 4TKB; -.
DR PDBsum; 4TKH; -.
DR PDBsum; 4TKJ; -.
DR PDBsum; 4WBK; -.
DR PDBsum; 5B27; -.
DR PDBsum; 5B28; -.
DR PDBsum; 5B29; -.
DR PDBsum; 5CE4; -.
DR PDBsum; 5HZ9; -.
DR PDBsum; 6AQ1; -.
DR PDBsum; 7EGO; -.
DR AlphaFoldDB; P05413; -.
DR SMR; P05413; -.
DR BioGRID; 108468; 41.
DR IntAct; P05413; 13.
DR MINT; P05413; -.
DR STRING; 9606.ENSP00000362817; -.
DR BindingDB; P05413; -.
DR ChEMBL; CHEMBL3344; -.
DR DrugBank; DB04224; Oleic Acid.
DR DrugBank; DB03796; Palmitic Acid.
DR DrugBank; DB03193; Stearic acid.
DR DrugCentral; P05413; -.
DR GuidetoPHARMACOLOGY; 2533; -.
DR SwissLipids; SLP:000001521; -.
DR CarbonylDB; P05413; -.
DR iPTMnet; P05413; -.
DR PhosphoSitePlus; P05413; -.
DR SwissPalm; P05413; -.
DR BioMuta; FABP3; -.
DR DMDM; 119802; -.
DR REPRODUCTION-2DPAGE; IPI00219684; -.
DR UCD-2DPAGE; P05413; -.
DR EPD; P05413; -.
DR jPOST; P05413; -.
DR MassIVE; P05413; -.
DR MaxQB; P05413; -.
DR PaxDb; P05413; -.
DR PeptideAtlas; P05413; -.
DR PRIDE; P05413; -.
DR ProteomicsDB; 51837; -.
DR Antibodypedia; 4505; 1156 antibodies from 41 providers.
DR DNASU; 2170; -.
DR Ensembl; ENST00000373713.7; ENSP00000362817.2; ENSG00000121769.8.
DR GeneID; 2170; -.
DR KEGG; hsa:2170; -.
DR MANE-Select; ENST00000373713.7; ENSP00000362817.2; NM_004102.5; NP_004093.1.
DR UCSC; uc001bss.2; human.
DR CTD; 2170; -.
DR DisGeNET; 2170; -.
DR GeneCards; FABP3; -.
DR HGNC; HGNC:3557; FABP3.
DR HPA; ENSG00000121769; Group enriched (heart muscle, skeletal muscle, tongue).
DR MIM; 134651; gene.
DR neXtProt; NX_P05413; -.
DR OpenTargets; ENSG00000121769; -.
DR PharmGKB; PA27958; -.
DR VEuPathDB; HostDB:ENSG00000121769; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000155104; -.
DR InParanoid; P05413; -.
DR OMA; TRQVACM; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; P05413; -.
DR TreeFam; TF316894; -.
DR PathwayCommons; P05413; -.
DR Reactome; R-HSA-163560; Triglyceride catabolism.
DR SignaLink; P05413; -.
DR SIGNOR; P05413; -.
DR BioGRID-ORCS; 2170; 15 hits in 1059 CRISPR screens.
DR ChiTaRS; FABP3; human.
DR EvolutionaryTrace; P05413; -.
DR GeneWiki; Heart-type_fatty_acid_binding_protein; -.
DR GenomeRNAi; 2170; -.
DR Pharos; P05413; Tchem.
DR PRO; PR:P05413; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P05413; protein.
DR Bgee; ENSG00000121769; Expressed in apex of heart and 163 other tissues.
DR ExpressionAtlas; P05413; baseline and differential.
DR Genevisible; P05413; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0036041; F:long-chain fatty acid binding; IDA:BHF-UCL.
DR GO; GO:0070538; F:oleic acid binding; IDA:BHF-UCL.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:BHF-UCL.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0032365; P:intracellular lipid transport; ISS:BHF-UCL.
DR GO; GO:0015909; P:long-chain fatty acid transport; ISS:ARUK-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0055091; P:phospholipid homeostasis; ISS:BHF-UCL.
DR GO; GO:0140214; P:positive regulation of long-chain fatty acid import into cell; ISS:ARUK-UCL.
DR GO; GO:0071073; P:positive regulation of phospholipid biosynthetic process; IC:BHF-UCL.
DR GO; GO:0046320; P:regulation of fatty acid oxidation; ISS:BHF-UCL.
DR GO; GO:2001245; P:regulation of phosphatidylcholine biosynthetic process; IEA:Ensembl.
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; PTHR11955; 1.
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; Cytoplasm; Direct protein sequencing;
KW Lipid-binding; Phosphoprotein; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2266954,
FT ECO:0000269|PubMed:3421901, ECO:0007744|PubMed:22223895"
FT CHAIN 2..133
FT /note="Fatty acid-binding protein, heart"
FT /id="PRO_0000067321"
FT BINDING 127..129
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /evidence="ECO:0000269|PubMed:7922029,
FT ECO:0007744|PDB:1HMS"
FT BINDING 127..129
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:1526991,
FT ECO:0007744|PDB:2HMB"
FT BINDING 127..129
FT /ligand="octadecanoate"
FT /ligand_id="ChEBI:CHEBI:25629"
FT /evidence="ECO:0000269|PubMed:7922029,
FT ECO:0007744|PDB:1HMT"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07483"
FT MOD_RES 20
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P07483"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07483"
FT MOD_RES 30
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07483"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07483"
FT VARIANT 53
FT /note="K -> R (in dbSNP:rs2228194)"
FT /id="VAR_061165"
FT CONFLICT 2
FT /note="V -> A (in Ref. 2; CAA71305)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="L -> K (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="C -> S (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="E -> Q (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:4TKB"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:4TKB"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:4TKB"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:4TKB"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:4TKB"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:4TKB"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:4TKB"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:4TKB"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:4TKB"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:4TKB"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:4TKB"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:4TKB"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:4TKB"
SQ SEQUENCE 133 AA; 14858 MW; 5FD396B1BE538A3C CRC64;
MVDAFLGTWK LVDSKNFDDY MKSLGVGFAT RQVASMTKPT TIIEKNGDIL TLKTHSTFKN
TEISFKLGVE FDETTADDRK VKSIVTLDGG KLVHLQKWDG QETTLVRELI DGKLILTLTH
GTAVCTRTYE KEA
