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FABPL_CHICK
ID   FABPL_CHICK             Reviewed;         126 AA.
AC   P80226; Q90WB0;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Fatty acid-binding protein, liver;
DE   AltName: Full=Fatty acid-binding protein 1;
DE   AltName: Full=Liver basic FABP;
DE            Short=LB-FABP;
DE   AltName: Full=Liver bile acid-binding protein;
DE            Short=L-BABP;
DE   AltName: Full=Liver-type fatty acid-binding protein;
DE            Short=L-FABP;
GN   Name=FABP1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=White leghorn; TISSUE=Liver;
RA   Murai A., Kusumoto K., Okumura J.;
RT   "Regulation of gene expression of two liver type fatty acid binding
RT   proteins in chicken.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-126, AND ACETYLATION AT ALA-2.
RC   TISSUE=Liver;
RX   PubMed=7553344; DOI=10.1016/0305-0491(94)90010-8;
RA   Ceciliani F., Monaco H.L., Ronchi S., Faotto L., Spadon P.;
RT   "The primary structure of a basic (pI 9.0) fatty acid-binding protein from
RT   liver of Gallus domesticus.";
RL   Comp. Biochem. Physiol. 109B:261-271(1994).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX   PubMed=2266974; DOI=10.1007/bf00231372;
RA   Scapin G., Spadon P., Mammi M., Zanotti G., Monaco H.L.;
RT   "Crystal structure of chicken liver basic fatty acid-binding protein at 2.7
RT   A resolution.";
RL   Mol. Cell. Biochem. 98:95-99(1990).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=12652125; DOI=10.1023/a:1022277727303;
RA   Vasile F., Ragona L., Catalano M., Zetta L., Perduca M., Monaco H.L.,
RA   Molinari H.;
RT   "Solution structure of chicken liver basic fatty acid binding protein.";
RL   J. Biomol. NMR 25:157-160(2003).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CHOLATE.
RX   PubMed=15518556; DOI=10.1021/bi0489661;
RA   Nichesola D., Perduca M., Capaldi S., Carrizo M.E., Righetti P.G.,
RA   Monaco H.L.;
RT   "Crystal structure of chicken liver basic fatty acid-binding protein
RT   complexed with cholic acid.";
RL   Biochemistry 43:14072-14079(2004).
RN   [6]
RP   STRUCTURE BY NMR.
RX   PubMed=16439356; DOI=10.1074/jbc.m513003200;
RA   Ragona L., Catalano M., Luppi M., Cicero D., Eliseo T., Foote J.,
RA   Fogolari F., Zetta L., Molinari H.;
RT   "NMR dynamic studies suggest that allosteric activation regulates ligand
RT   binding in chicken liver bile acid-binding protein.";
RL   J. Biol. Chem. 281:9697-9709(2006).
CC   -!- FUNCTION: Binds free fatty acids and their coenzyme A derivatives,
CC       bilirubin, and some other small molecules in the cytoplasm. May be
CC       involved in intracellular lipid transport. Binds 2 molecules of cholate
CC       per subunit.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC       ligands 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; AF380998; AAK58094.1; -; mRNA.
DR   RefSeq; NP_989965.1; NM_204634.1.
DR   PDB; 1MVG; NMR; -; A=2-126.
DR   PDB; 1TVQ; X-ray; 2.00 A; A=2-126.
DR   PDB; 1TW4; X-ray; 2.00 A; A/B=2-126.
DR   PDB; 1ZRY; NMR; -; A=2-126.
DR   PDB; 2JN3; NMR; -; A=2-126.
DR   PDB; 2K62; NMR; -; A=2-126.
DR   PDB; 2LFO; NMR; -; A=2-126.
DR   PDB; 7O0J; X-ray; 1.40 A; A=1-126.
DR   PDB; 7O0K; X-ray; 1.83 A; A/B=1-126.
DR   PDBsum; 1MVG; -.
DR   PDBsum; 1TVQ; -.
DR   PDBsum; 1TW4; -.
DR   PDBsum; 1ZRY; -.
DR   PDBsum; 2JN3; -.
DR   PDBsum; 2K62; -.
DR   PDBsum; 2LFO; -.
DR   PDBsum; 7O0J; -.
DR   PDBsum; 7O0K; -.
DR   AlphaFoldDB; P80226; -.
DR   BMRB; P80226; -.
DR   SMR; P80226; -.
DR   STRING; 9031.ENSGALP00000006574; -.
DR   iPTMnet; P80226; -.
DR   PaxDb; P80226; -.
DR   GeneID; 395345; -.
DR   KEGG; gga:395345; -.
DR   CTD; 395345; -.
DR   VEuPathDB; HostDB:geneid_395345; -.
DR   eggNOG; KOG4015; Eukaryota.
DR   HOGENOM; CLU_113772_4_1_1; -.
DR   InParanoid; P80226; -.
DR   OrthoDB; 1417203at2759; -.
DR   PhylomeDB; P80226; -.
DR   TreeFam; TF330348; -.
DR   EvolutionaryTrace; P80226; -.
DR   PRO; PR:P80226; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; 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   PANTHER; PTHR11955; PTHR11955; 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; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7553344"
FT   CHAIN           2..126
FT                   /note="Fatty acid-binding protein, liver"
FT                   /id="PRO_0000067338"
FT   BINDING         56
FT                   /ligand="cholate"
FT                   /ligand_id="ChEBI:CHEBI:29747"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:15518556"
FT   BINDING         57
FT                   /ligand="cholate"
FT                   /ligand_id="ChEBI:CHEBI:29747"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:15518556"
FT   BINDING         77
FT                   /ligand="cholate"
FT                   /ligand_id="ChEBI:CHEBI:29747"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:15518556"
FT   BINDING         99
FT                   /ligand="cholate"
FT                   /ligand_id="ChEBI:CHEBI:29747"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:15518556"
FT   BINDING         101
FT                   /ligand="cholate"
FT                   /ligand_id="ChEBI:CHEBI:29747"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:15518556"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:7553344"
FT   CONFLICT        92
FT                   /note="T -> C (in Ref. 1; AAK58094)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..14
FT                   /evidence="ECO:0007829|PDB:7O0J"
FT   HELIX           15..21
FT                   /evidence="ECO:0007829|PDB:7O0J"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:1MVG"
FT   HELIX           26..32
FT                   /evidence="ECO:0007829|PDB:7O0J"
FT   STRAND          38..44
FT                   /evidence="ECO:0007829|PDB:7O0J"
FT   STRAND          47..53
FT                   /evidence="ECO:0007829|PDB:7O0J"
FT   STRAND          58..64
FT                   /evidence="ECO:0007829|PDB:7O0J"
FT   STRAND          69..72
FT                   /evidence="ECO:0007829|PDB:7O0J"
FT   TURN            74..76
FT                   /evidence="ECO:0007829|PDB:1MVG"
FT   STRAND          78..86
FT                   /evidence="ECO:0007829|PDB:7O0J"
FT   STRAND          89..93
FT                   /evidence="ECO:0007829|PDB:7O0J"
FT   STRAND          95..104
FT                   /evidence="ECO:0007829|PDB:7O0J"
FT   STRAND          107..114
FT                   /evidence="ECO:0007829|PDB:7O0J"
FT   STRAND          117..125
FT                   /evidence="ECO:0007829|PDB:7O0J"
SQ   SEQUENCE   126 AA;  14210 MW;  537022389AC431FF CRC64;
     MAFSGTWQVY AQENYEEFLK ALALPEDLIK MARDIKPIVE IQQKGDDFVV TSKTPRQTVT
     NSFTLGKEAD ITTMDGKKLK CTVHLANGKL VTKSEKFSHE QEVKGNEMVE TITFGGVTLI
     RRSKRV
 
 
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