ID   FABPH_BOSMU             Reviewed;         133 AA.
AC   Q4TZH2;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 68.
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   Bos mutus grunniens (Wild yak) (Bos grunniens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=30521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RA   Ma Z.-J., Zhong J.-C., Zi X.-D., Chang H.-P., Zhang Q., Zhang X.-Q.;
RT   "Cloning and characterization of the yak heart fatty acid-binding protein
RT   (H-FABP) gene.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; DQ026674; AAY44416.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4TZH2; -.
DR   SMR; Q4TZH2; -.
DR   Ensembl; ENSBGRT00000014436; ENSBGRP00000012517; ENSBGRG00000007849.
DR   GeneTree; ENSGT00940000155104; -.
DR   Proteomes; UP000694520; Chromosome 2.
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   3: Inferred from homology;
KW   Acetylation; Cytoplasm; Lipid-binding; Phosphoprotein; Reference proteome;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P10790"
FT   CHAIN           2..133
FT                   /note="Fatty acid-binding protein, heart"
FT                   /id="PRO_0000253470"
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-acetylvaline"
FT                   /evidence="ECO:0000250|UniProtKB:P10790"
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"
SQ   SEQUENCE   133 AA;  14779 MW;  C620160BFF167BC5 CRC64;
     MVDAFVGTWK LVDSKNFDDY MKSLGVGFAT RQVGNMTKPT TIIEVNGDTV IIKTQSTFKN
     TEISFKLGVE FDETTADDRK VKSIVTLDGG KLVHVQKWNG QETSLVREMV DGKLILTLTH
     GTAVCTRTYE KQA