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   27-MAR-2024, entry version 214.
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: FABPs 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   PDB; 7EUV; X-ray; 1.28 A; A=1-133.
DR   PDB; 7EUW; X-ray; 1.55 A; A=1-133.
DR   PDB; 7FBF; X-ray; 0.86 A; A=1-133.
DR   PDB; 7FBM; X-ray; 1.00 A; A=1-133.
DR   PDB; 7FBN; X-ray; 1.44 A; A=1-133.
DR   PDB; 7FC4; X-ray; 1.50 A; A=1-133.
DR   PDB; 7FCG; X-ray; 1.19 A; A=1-133.
DR   PDB; 7FCX; X-ray; 1.15 A; A=1-133.
DR   PDB; 7FD7; X-ray; 1.00 A; A=1-133.
DR   PDB; 7FDT; X-ray; 0.86 A; A=1-133.
DR   PDB; 7FDU; X-ray; 0.86 A; A=1-133.
DR   PDB; 7FDX; X-ray; 0.95 A; A=1-133.
DR   PDB; 7FEK; X-ray; 1.05 A; A=1-133.
DR   PDB; 7FEU; X-ray; 0.95 A; A=1-133.
DR   PDB; 7FEZ; X-ray; 0.76 A; A=1-133.
DR   PDB; 7FF6; X-ray; 0.83 A; A=1-133.
DR   PDB; 7FFK; X-ray; 0.84 A; A=1-133.
DR   PDB; 7FFX; X-ray; 0.88 A; A=1-133.
DR   PDB; 7FG1; X-ray; 0.93 A; A=1-133.
DR   PDB; 7FG5; X-ray; 1.30 A; A=1-133.
DR   PDB; 7FZQ; X-ray; 1.60 A; A/B=1-133.
DR   PDB; 7V2G; X-ray; 0.98 A; A=1-133.
DR   PDB; 7V5U; X-ray; 0.92 A; A=1-133.
DR   PDB; 7VB1; X-ray; 0.90 A; A=1-133.
DR   PDB; 7WCI; X-ray; 0.85 A; A=1-133.
DR   PDB; 7WD6; X-ray; 0.95 A; A=1-133.
DR   PDB; 7WDJ; X-ray; 0.90 A; A=1-133.
DR   PDB; 7WE5; X-ray; 0.87 A; A=1-133.
DR   PDB; 7WF0; X-ray; 0.83 A; A=1-133.
DR   PDB; 7WJ1; X-ray; 0.86 A; A=1-133.
DR   PDB; 7WKB; X-ray; 0.81 A; A=1-133.
DR   PDB; 7WKG; X-ray; 0.84 A; A=1-133.
DR   PDB; 7WOM; X-ray; 0.90 A; A=1-133.
DR   PDB; 7WPG; X-ray; 0.90 A; A=1-133.
DR   PDB; 7WPU; X-ray; 0.95 A; A=1-133.
DR   PDB; 7WPW; X-ray; 0.97 A; A=1-133.
DR   PDB; 7WQ7; X-ray; 0.87 A; A=1-133.
DR   PDB; 7X48; X-ray; 0.86 A; A=1-133.
DR   PDB; 7X4J; X-ray; 0.96 A; A=1-133.
DR   PDB; 7X50; X-ray; 0.93 A; A=1-133.
DR   PDB; 7XBC; X-ray; 0.92 A; A=1-133.
DR   PDB; 7XHM; X-ray; 0.88 A; A=1-133.
DR   PDB; 7XHU; X-ray; 0.88 A; A=1-133.
DR   PDB; 8GEW; X-ray; 0.97 A; A=1-132.
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   PDBsum; 7EUV; -.
DR   PDBsum; 7EUW; -.
DR   PDBsum; 7FBF; -.
DR   PDBsum; 7FBM; -.
DR   PDBsum; 7FBN; -.
DR   PDBsum; 7FC4; -.
DR   PDBsum; 7FCG; -.
DR   PDBsum; 7FCX; -.
DR   PDBsum; 7FD7; -.
DR   PDBsum; 7FDT; -.
DR   PDBsum; 7FDU; -.
DR   PDBsum; 7FDX; -.
DR   PDBsum; 7FEK; -.
DR   PDBsum; 7FEU; -.
DR   PDBsum; 7FEZ; -.
DR   PDBsum; 7FF6; -.
DR   PDBsum; 7FFK; -.
DR   PDBsum; 7FFX; -.
DR   PDBsum; 7FG1; -.
DR   PDBsum; 7FG5; -.
DR   PDBsum; 7FZQ; -.
DR   PDBsum; 7V2G; -.
DR   PDBsum; 7V5U; -.
DR   PDBsum; 7VB1; -.
DR   PDBsum; 7WCI; -.
DR   PDBsum; 7WD6; -.
DR   PDBsum; 7WDJ; -.
DR   PDBsum; 7WE5; -.
DR   PDBsum; 7WF0; -.
DR   PDBsum; 7WJ1; -.
DR   PDBsum; 7WKB; -.
DR   PDBsum; 7WKG; -.
DR   PDBsum; 7WOM; -.
DR   PDBsum; 7WPG; -.
DR   PDBsum; 7WPU; -.
DR   PDBsum; 7WPW; -.
DR   PDBsum; 7WQ7; -.
DR   PDBsum; 7X48; -.
DR   PDBsum; 7X4J; -.
DR   PDBsum; 7X50; -.
DR   PDBsum; 7XBC; -.
DR   PDBsum; 7XHM; -.
DR   PDBsum; 7XHU; -.
DR   PDBsum; 8GEW; -.
DR   AlphaFoldDB; P05413; -.
DR   SMR; P05413; -.
DR   BioGRID; 108468; 42.
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   EPD; P05413; -.
DR   jPOST; P05413; -.
DR   MassIVE; P05413; -.
DR   MaxQB; P05413; -.
DR   PaxDb; 9606-ENSP00000362817; -.
DR   PeptideAtlas; P05413; -.
DR   ProteomicsDB; 51837; -.
DR   Pumba; P05413; -.
DR   Antibodypedia; 4505; 1335 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   AGR; HGNC:3557; -.
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; KWDGQES; -.
DR   OrthoDB; 46617at2759; -.
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; 16 hits in 1139 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 165 other cell types or tissues.
DR   ExpressionAtlas; P05413; baseline and differential.
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: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: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   CDD; cd19466; FABP3; 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:SF61; FATTY ACID-BINDING PROTEIN, HEART; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; Lipocalins; 1.
DR   PROSITE; PS00214; FABP; 1.
DR   UCD-2DPAGE; P05413; -.
DR   Genevisible; P05413; HS.
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:7FEZ"
FT   STRAND          7..16
FT                   /evidence="ECO:0007829|PDB:7FEZ"
FT   HELIX           17..23
FT                   /evidence="ECO:0007829|PDB:7FEZ"
FT   HELIX           28..34
FT                   /evidence="ECO:0007829|PDB:7FEZ"
FT   STRAND          40..46
FT                   /evidence="ECO:0007829|PDB:7FEZ"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:7FEZ"
FT   STRAND          61..66
FT                   /evidence="ECO:0007829|PDB:7FEZ"
FT   STRAND          71..74
FT                   /evidence="ECO:0007829|PDB:7FEZ"
FT   STRAND          80..88
FT                   /evidence="ECO:0007829|PDB:7FEZ"
FT   STRAND          91..98
FT                   /evidence="ECO:0007829|PDB:7FEZ"
FT   STRAND          101..110
FT                   /evidence="ECO:0007829|PDB:7FEZ"
FT   STRAND          113..120
FT                   /evidence="ECO:0007829|PDB:7FEZ"
FT   STRAND          123..131
FT                   /evidence="ECO:0007829|PDB:7FEZ"
SQ   SEQUENCE   133 AA;  14858 MW;  5FD396B1BE538A3C CRC64;
     MVDAFLGTWK LVDSKNFDDY MKSLGVGFAT RQVASMTKPT TIIEKNGDIL TLKTHSTFKN
     TEISFKLGVE FDETTADDRK VKSIVTLDGG KLVHLQKWDG QETTLVRELI DGKLILTLTH
     GTAVCTRTYE KEA
//