FABPH_PIG
ID FABPH_PIG Reviewed; 133 AA.
AC O02772; A6N7Z0; A6N8I2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 122.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=9107676; DOI=10.1007/s003359900433;
RA Gerbens F.N.A., Rettenberger G., Lenstra J.A., Veerkamp J.H.,
RA te Pas M.F.W.;
RT "Characterization, chromosomal localization, and genetic variation of the
RT porcine heart fatty acid-binding protein gene.";
RL Mamm. Genome 8:328-332(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-51.
RA Gerbens F.N.A.;
RT "Identification of two H-FABP isoforms and various SNPs in the H-FABP
RT encoding gene of the pig.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-51.
RC TISSUE=Longissimus muscle;
RA Huang H., Shuai S.R.;
RT "H-FABP mRNA expression in different tissues of Tibetan pig.";
RL Submitted (MAY-2007) 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 -!- 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; X98558; CAA67168.1; -; Genomic_DNA.
DR EMBL; AJ416019; CAC95165.1; -; mRNA.
DR EMBL; EF619344; ABR12603.1; -; mRNA.
DR EMBL; EF622095; ABR10917.1; -; mRNA.
DR RefSeq; NP_001093401.1; NM_001099931.1.
DR AlphaFoldDB; O02772; -.
DR SMR; O02772; -.
DR PaxDb; O02772; -.
DR PeptideAtlas; O02772; -.
DR PRIDE; O02772; -.
DR Ensembl; ENSSSCT00000044750; ENSSSCP00000040253; ENSSSCG00000036883.
DR Ensembl; ENSSSCT00025078975; ENSSSCP00025034285; ENSSSCG00025057693.
DR Ensembl; ENSSSCT00045065418; ENSSSCP00045046292; ENSSSCG00045037845.
DR Ensembl; ENSSSCT00055001748; ENSSSCP00055001318; ENSSSCG00055000982.
DR Ensembl; ENSSSCT00070055544; ENSSSCP00070047166; ENSSSCG00070027693.
DR GeneID; 399532; -.
DR KEGG; ssc:399532; -.
DR CTD; 2170; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000155104; -.
DR InParanoid; O02772; -.
DR OMA; TRQVACM; -.
DR OrthoDB; 1417203at2759; -.
DR Proteomes; UP000008227; Chromosome 6.
DR Proteomes; UP000314985; Chromosome 6.
DR Bgee; ENSSSCG00000036883; Expressed in psoas major muscle and 41 other tissues.
DR ExpressionAtlas; O02772; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0036041; F:long-chain fatty acid binding; IBA:GO_Central.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0015909; P:long-chain fatty acid transport; IBA:GO_Central.
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; 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_0000067324"
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"
FT VARIANT 51
FT /note="I -> T"
FT /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.3"
SQ SEQUENCE 133 AA; 14749 MW; B543415CD6900A65 CRC64;
MVDAFAGTWK LVDSKNFDDY MKSIGVGFAT RQVANMTKPT TIIEVNGDTI IIKTQSTFKS
TEISFKLGVE FDETTADDRK VKSIVTLDGG KLVHLQKWNG QETTLVRELV DGKLILTLTH
GSAVCTRTYE KEA
