ID   FABPH_ONCMY             Reviewed;         133 AA.
AC   O13008;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 91.
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;
GN   Name=fabp3;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   PubMed=9530822; DOI=10.1016/s0305-0491(97)00309-x;
RA   Ando S., Xue X.H., Tibbits G.F., Haunerland N.H.;
RT   "Cloning and sequencing of complementary DNA for fatty acid binding protein
RT   from rainbow trout heart.";
RL   Comp. Biochem. Physiol. 119B:213-217(1998).
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic
CC       ligand in its interior. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000305}.
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DR   EMBL; U95296; AAB53643.1; -; mRNA.
DR   RefSeq; NP_001118185.1; NM_001124713.1.
DR   AlphaFoldDB; O13008; -.
DR   SMR; O13008; -.
DR   Ensembl; ENSOMYT00000096936; ENSOMYP00000089002; ENSOMYG00000041099.
DR   GeneID; 100136763; -.
DR   KEGG; omy:100136763; -.
DR   CTD; 2170; -.
DR   GeneTree; ENSGT00940000155104; -.
DR   OrthoDB; 1417203at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Lipid-binding; Phosphoprotein; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..133
FT                   /note="Fatty acid-binding protein, heart"
FT                   /id="PRO_0000067327"
FT   BINDING         127..129
FT                   /ligand="(9Z)-octadecenoate"
FT                   /ligand_id="ChEBI:CHEBI:30823"
FT                   /evidence="ECO:0000250|UniProtKB:P05413"
FT   BINDING         127..129
FT                   /ligand="hexadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:7896"
FT                   /evidence="ECO:0000250|UniProtKB:P05413"
FT   BINDING         127..129
FT                   /ligand="octadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:25629"
FT                   /evidence="ECO:0000250|UniProtKB:P05413"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         20
FT                   /note="Phosphotyrosine; by Tyr-kinases"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   133 AA;  14529 MW;  3ED9E07142574389 CRC64;
     MAEAFAGTWN LKDSKNFDEY MKALGVGFAT RQVGGMTKPT TIIEVAGDTV TLKTQSTFKN
     TEISFKLGAE FDETTADDRK VKSLITIDGG KMVHVQKWDG KETTLVREVS GNALELTLTL
     GDVVSTRSYV KAE