FABPH_BOVIN
ID FABPH_BOVIN Reviewed; 133 AA.
AC P10790; P12103; Q3T125;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 170.
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;
GN Name=FABP3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3409882; DOI=10.1111/j.1432-1033.1988.tb14227.x;
RA Billich S., Wissel T., Kratzin H., Hahn U., Hagenhoff B., Lezius A.G.,
RA Spener F.;
RT "Cloning of a full-length complementary DNA for fatty-acid-binding protein
RT from bovine heart.";
RL Eur. J. Biochem. 175:549-556(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=2335570; DOI=10.1083/jcb.110.5.1779;
RA Kurtz A., Vogel F., Funa K., Heldin C.-H., Grosse R.;
RT "Developmental regulation of mammary-derived growth inhibitor expression in
RT bovine mammary tissue.";
RL J. Cell Biol. 110:1779-1789(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Korean;
RA Chung E.R., Shin S.C., Kim W.T.;
RT "Sequencing of heart fatty acid-binding protein (FABP) gene in Korean
RT cattle (Hanwoo).";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 2-133, AND ACETYLATION AT VAL-2.
RX PubMed=2398054; DOI=10.1016/s0021-9258(17)46216-8;
RA Unterberg C., Boerchers T., Hoejrup P., Roepstorff P., Knudsen J.,
RA Spener F.;
RT "Cardiac fatty acid-binding proteins. Isolation and characterization of the
RT mitochondrial fatty acid-binding protein and its structural relationship
RT with the cytosolic isoforms.";
RL J. Biol. Chem. 265:16255-16261(1990).
RN [6]
RP PROTEIN SEQUENCE OF 2-132.
RX PubMed=3667628; DOI=10.1016/s0021-9258(18)48149-5;
RA Boehmer F.-D., Kraft R., Otto A., Wernstedt C., Hellman U., Kurtz A.,
RA Mueller T., Rohde K., Etzold G., Lehmann W., Langen P., Heldin C.-H.,
RA Grosse R.;
RT "Identification of a polypeptide growth inhibitor from bovine mammary
RT gland. Sequence homology to fatty acid- and retinoid-binding proteins.";
RL J. Biol. Chem. 262:15137-15143(1987).
RN [7]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Skeletal muscle;
RX PubMed=8312397; DOI=10.1016/0300-9084(93)90052-t;
RA Zabari M., Berri M., Rouchon P., Zamora F., Tassy C., Ribadeau-Dumas B.,
RA Ouali A.;
RT "Purification and characterisation of a polymorphic low M(r) bovine muscle
RT cysteine proteinase inhibitor: structural identity with fatty-acid-binding
RT proteins.";
RL Biochimie 75:937-945(1993).
RN [8]
RP CRYSTALLIZATION.
RX PubMed=2070787; DOI=10.1111/j.1432-1033.1991.tb16120.x;
RA Mueller-Fahrnow A., Egner U., Jones T.A., Ruedel H., Spener F., Saenger W.;
RT "Three-dimensional structure of fatty-acid-binding protein from bovine
RT heart.";
RL Eur. J. Biochem. 199:271-276(1991).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=1483473; DOI=10.1111/j.1432-1033.1992.tb17494.x;
RA Luecke C., Lassen D., Kreienkamp H.-J., Spener F., Rueterjans H.;
RT "Sequence-specific 1H-NMR assignment and determination of the secondary
RT structure of bovine heart fatty-acid-binding protein.";
RL Eur. J. Biochem. 210:901-910(1992).
RN [10]
RP STRUCTURE BY NMR IN COMPLEX WITH PALMITATE.
RX PubMed=7601110; DOI=10.1111/j.1432-1033.1995.tb20560.x;
RA Lassen D., Luecke C., Kveder M., Mesgarzadeh A., Schmidt J.M., Specht B.,
RA Lezius A., Spener F., Rueterjans H.;
RT "Three-dimensional structure of bovine heart fatty-acid-binding protein
RT with bound palmitic acid, determined by multidimensional NMR
RT spectroscopy.";
RL Eur. J. Biochem. 230:266-280(1995).
RN [11]
RP STRUCTURE BY NMR.
RX PubMed=9490052; DOI=10.1046/j.1432-1327.1998.2510781.x;
RA Mesgarzadeh A., Pfeiffer S., Engelke J., Lassen D., Rueterjans H.;
RT "Bound water in apo and holo bovine heart fatty-acid-binding protein
RT determined by heteronuclear NMR spectroscopy.";
RL Eur. J. Biochem. 251:781-786(1998).
RN [12]
RP VARIANT ASP-99.
RX PubMed=8354262; DOI=10.1111/j.1432-1033.1993.tb18065.x;
RA Bartetzko N., Lezius A.G., Spener F.;
RT "Isoforms of fatty-acid-binding protein in bovine heart are coded by
RT distinct mRNA.";
RL Eur. J. Biochem. 215:555-559(1993).
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 -!- FUNCTION: MDGI reversibly inhibits proliferation of mammary carcinoma
CC cells.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion matrix.
CC -!- TISSUE SPECIFICITY: Mammary epithelial cells of developing
CC lobuloalveolar structures and heart.
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; X12710; CAA31212.1; -; mRNA.
DR EMBL; X51933; CAA36199.1; -; mRNA.
DR EMBL; DQ174319; AAZ99892.1; -; Genomic_DNA.
DR EMBL; BC102153; AAI02154.1; -; mRNA.
DR PIR; A34676; A34676.
DR RefSeq; NP_776738.1; NM_174313.2.
DR PDB; 1BWY; NMR; -; A=2-133.
DR PDBsum; 1BWY; -.
DR AlphaFoldDB; P10790; -.
DR SMR; P10790; -.
DR STRING; 9913.ENSBTAP00000022375; -.
DR iPTMnet; P10790; -.
DR PaxDb; P10790; -.
DR PeptideAtlas; P10790; -.
DR PRIDE; P10790; -.
DR Ensembl; ENSBTAT00000022375; ENSBTAP00000022375; ENSBTAG00000016819.
DR GeneID; 281758; -.
DR KEGG; bta:281758; -.
DR CTD; 2170; -.
DR VEuPathDB; HostDB:ENSBTAG00000016819; -.
DR VGNC; VGNC:28697; FABP3.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000155104; -.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; P10790; -.
DR OMA; TRQVACM; -.
DR OrthoDB; 1417203at2759; -.
DR TreeFam; TF316894; -.
DR Reactome; R-BTA-163560; Triglyceride catabolism.
DR EvolutionaryTrace; P10790; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000016819; Expressed in gluteus medius and 107 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Lipid-binding; Mitochondrion; Phosphoprotein; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2398054,
FT ECO:0000269|PubMed:3667628"
FT CHAIN 2..133
FT /note="Fatty acid-binding protein, heart"
FT /id="PRO_0000067320"
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:0000269|PubMed:2398054"
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 99
FT /note="N -> D"
FT /evidence="ECO:0000269|PubMed:8354262"
FT CONFLICT 13..15
FT /note="DSK -> SSE (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="T -> L (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="E -> S (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="H -> Q (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="T -> V (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:1BWY"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:1BWY"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:1BWY"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:1BWY"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:1BWY"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1BWY"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1BWY"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1BWY"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:1BWY"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1BWY"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:1BWY"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:1BWY"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:1BWY"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:1BWY"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:1BWY"
SQ SEQUENCE 133 AA; 14779 MW; C620160BFF167BC5 CRC64;
MVDAFVGTWK LVDSKNFDDY MKSLGVGFAT RQVGNMTKPT TIIEVNGDTV IIKTQSTFKN
TEISFKLGVE FDETTADDRK VKSIVTLDGG KLVHVQKWNG QETSLVREMV DGKLILTLTH
GTAVCTRTYE KQA
