FABPL_CHAVI
ID FABPL_CHAVI Reviewed; 95 AA.
AC P82145;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 11-DEC-2019, entry version 81.
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;
DE Flags: Fragments;
GN Name=FABP1;
OS Chaetophractus villosus (South American armadillo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Xenarthra; Cingulata; Chlamyphoridae; Chaetophractus.
OX NCBI_TaxID=29080;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=9418007; DOI=10.1016/s0305-0491(97)00052-7;
RA Cavagnari B.M., Cordoba O.L., Affanni J.M., Santome J.A.;
RT "Purification and partial structural characterization of a fatty acid-
RT binding protein from the liver of the South American armadillo
RT Chaetophractus villosus.";
RL Comp. Biochem. Physiol. 118B:173-180(1997).
CC -!- FUNCTION: This protein binds free fatty acids and their coenzyme A
CC derivatives, bilirubin, and some other small molecules in the
CC cytoplasm; it may be involved in intracellular lipid transport.
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005504; F:fatty acid binding; IEA:InterPro.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR031276; Lb-FABP.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PANTHER; PTHR11955:SF96; PTHR11955:SF96; 1.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Lipid-binding; Phosphoprotein;
KW Transport.
FT CHAIN 1..95
FT /note="Fatty acid-binding protein, liver"
FT /id="PRO_0000067339"
FT MOD_RES 13
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 18
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02692"
FT MOD_RES 28
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07148"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07148"
FT MOD_RES 39
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 47
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 59
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT MOD_RES 90
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12710"
FT NON_CONS 39..40
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 95 AA; 10466 MW; E1F538457825F84D CRC64;
MKAIGLPDDL IQKGKDIKGV SEVVQEGKHF KVTITTGSKM ETMTGEKVKT VVRMEGDNKL
VTTFKGIKSV TEFNGDTVXN XMTLGXIVFK RVSKR