ID   FABPH_ICTTR             Reviewed;         133 AA.
AC   Q99P61;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 108.
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   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11779641; DOI=10.1016/s0167-4781(01)00338-4;
RA   Hittel D., Storey K.B.;
RT   "Differential expression of adipose- and heart-type fatty acid binding
RT   proteins in hibernating ground squirrels.";
RL   Biochim. Biophys. Acta 1522:238-243(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. FABPs
CC       are important elements related to the hibernating state in mammals.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Up-regulated during hibernation in brown adipose tissue.
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; AF327854; AAK08083.1; -; mRNA.
DR   RefSeq; NP_001269194.1; NM_001282265.1.
DR   AlphaFoldDB; Q99P61; -.
DR   SMR; Q99P61; -.
DR   STRING; 43179.ENSSTOP00000003437; -.
DR   Ensembl; ENSSTOT00000003834; ENSSTOP00000003437; ENSSTOG00000003842.
DR   GeneID; 101976775; -.
DR   CTD; 2170; -.
DR   eggNOG; KOG4015; Eukaryota.
DR   GeneTree; ENSGT00940000155104; -.
DR   HOGENOM; CLU_113772_0_0_1; -.
DR   InParanoid; Q99P61; -.
DR   OMA; TRQVACM; -.
DR   OrthoDB; 1417203at2759; -.
DR   TreeFam; TF316894; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0042750; P:hibernation; 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; Hibernation; Lipid-binding; Phosphoprotein;
KW   Reference proteome; 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_0000067326"
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;  14853 MW;  9F3D6F6DB78AE721 CRC64;
     MVDAFVGTWK LVDSKNFDDY MKSLGVGFAT RQVASMTKPT TIIEKNGDTI ILKTQSTFKN
     TEISFQLGKE FDETTADDRK VKSTVTLDGG KLVHVQKWDG QETTLVRELN DGKLILTLTH
     GSVVCTRTYE KEA