FABPL_PIG
ID FABPL_PIG Reviewed; 127 AA.
AC P49924; Q3LSM5; Q56G54;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Fatty acid-binding protein, liver;
DE AltName: Full=Fatty acid-binding protein 1;
DE AltName: Full=Liver-type fatty acid-binding protein;
DE Short=L-FABP;
GN Name=FABP1;
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 [MRNA].
RC STRAIN=Large white X Landrace; TISSUE=Jejunum;
RX AGRICOLA=IND20415199; DOI=10.1016/0955-2863(93)90110-I;
RA Perozzi G., Baril D., Murgia C., Kelly D., Begbie R., King T.P.;
RT "Expression of differentiated functions in the developing porcine small
RT intestine.";
RL J. Nutr. Biochem. 4:699-705(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Jiang Y.Z., Li X.W.;
RT "Sus scrofa liver fatty acid binding protein (FABP1) gene.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
CC -!- FUNCTION: Plays a role in lipoprotein-mediated cholesterol uptake in
CC hepatocytes. Binds cholesterol. Binds free fatty acids and their
CC coenzyme A derivatives, bilirubin, and some other small molecules in
CC the cytoplasm. May be involved in intracellular lipid transport.
CC {ECO:0000250|UniProtKB:P07148, ECO:0000250|UniProtKB:P82289}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X77640; CAA54730.1; -; mRNA.
DR EMBL; AY960623; AAX62515.1; -; mRNA.
DR EMBL; DQ182323; ABA19231.1; -; Genomic_DNA.
DR EMBL; F14603; CAA23150.1; -; mRNA.
DR PIR; S45379; S45379.
DR RefSeq; NP_001004046.1; NM_001004046.2.
DR AlphaFoldDB; P49924; -.
DR SMR; P49924; -.
DR STRING; 9823.ENSSSCP00000008769; -.
DR PaxDb; P49924; -.
DR PeptideAtlas; P49924; -.
DR GeneID; 445535; -.
DR KEGG; ssc:445535; -.
DR CTD; 2168; -.
DR eggNOG; KOG4015; Eukaryota.
DR HOGENOM; CLU_113772_4_2_1; -.
DR InParanoid; P49924; -.
DR OrthoDB; 1440574at2759; -.
DR TreeFam; TF330348; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P49924; SS.
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:0015908; P: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; IPR031276; Lb-FABP.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PANTHER; PTHR11955:SF96; PTHR11955:SF96; 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 CHAIN 1..127
FT /note="Fatty acid-binding protein, liver"
FT /id="PRO_0000067336"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P80425"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07148"
FT MOD_RES 31
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 36
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02692"
FT MOD_RES 46
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07148"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07148"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 78
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 90
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 121
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT CONFLICT 74
FT /note="L -> M (in Ref. 2; AAX62515 and 3; CAA23150)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 127 AA; 14107 MW; 70FF10B2FCCD812F CRC64;
MNFSGKYQVQ SQENFEAFMK AVGLPDELIQ KGKDIKGTSE IVQNGKHFKL TITTGSKVVQ
NEFTLGEECE METLTGEKVK TVVQLEGDNK LVTTFKGIKS VTELNGDIIT STMTLGDIVF
KRISKRI
