FABP4_PYGPA
ID FABP4_PYGPA Reviewed; 132 AA.
AC A0A0K0MJN3;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Fatty acid-binding protein, adipocyte {ECO:0000305};
DE AltName: Full=Adipocyte lipid-binding protein {ECO:0000305};
DE Short=ALBP {ECO:0000305};
DE AltName: Full=Adipocyte-type fatty acid-binding protein {ECO:0000305};
DE Short=AFABP {ECO:0000305};
DE AltName: Full=Fatty acid-binding protein 4 {ECO:0000303|PubMed:26206084};
GN Name=FABP4 {ECO:0000303|PubMed:26206084};
OS Pygoscelis papua (Gentoo penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=30457;
RN [1] {ECO:0007744|PDB:5BVQ, ECO:0007744|PDB:5BVS}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF
RP APOPROTEIN AND IN COMPLEX WITH LINOLEATE, FUNCTION, SUBSTRATE SPECIFICITY,
RP SUBUNIT, AND DOMAIN.
RX PubMed=26206084; DOI=10.1016/j.bbrc.2015.07.087;
RA Lee C.W., Kim J.E., Do H., Kim R.O., Lee S.G., Park H.H., Chang J.H.,
RA Yim J.H., Park H., Kim I.C., Lee J.H.;
RT "Structural basis for the ligand-binding specificity of fatty acid-binding
RT proteins (pFABP4 and pFABP5) in gentoo penguin.";
RL Biochem. Biophys. Res. Commun. 465:12-18(2015).
CC -!- FUNCTION: Lipid transport protein in adipocytes. Binds both long chain
CC fatty acids and retinoic acid. Delivers long-chain fatty acids and
CC retinoic acid to their cognate receptors in the nucleus (By
CC similarity). Has the highest binding affinity for linoleic acid and
CC decreasing relative affinity for eicosapentaenoic acid (EPA), alpha-
CC linolenic acid (ALA), docosahexaenoic acid (DHA), oleic acid, palmitic
CC acid and stearic acid, respectively (PubMed:26206084).
CC {ECO:0000250|UniProtKB:P04117, ECO:0000269|PubMed:26206084}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:26206084}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04117}. Nucleus
CC {ECO:0000250|UniProtKB:P04117}. Note=Depending on the nature of the
CC ligand, a conformation change exposes a nuclear localization motif and
CC the protein is transported into the nucleus. Subject to constitutive
CC nuclear export. {ECO:0000250|UniProtKB:P04117}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic
CC ligand in its interior. {ECO:0000269|PubMed:26206084}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000255|RuleBase:RU003696}.
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DR EMBL; KR054393; AKE37138.1; -; mRNA.
DR PDB; 5BVQ; X-ray; 2.10 A; A/B=1-132.
DR PDB; 5BVS; X-ray; 2.20 A; A/B=1-132.
DR PDBsum; 5BVQ; -.
DR PDBsum; 5BVS; -.
DR AlphaFoldDB; A0A0K0MJN3; -.
DR SMR; A0A0K0MJN3; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0070539; F:linoleic acid binding; IDA:UniProtKB.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISS:UniProtKB.
DR GO; GO:0070538; F:oleic acid binding; IDA:UniProtKB.
DR GO; GO:0070540; F:stearic acid binding; IDA:UniProtKB.
DR GO; GO:0071399; P:cellular response to linoleic acid; IDA:UniProtKB.
DR GO; GO:0015909; P:long-chain fatty acid transport; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IEA:InterPro.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR033073; FABP4.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PANTHER; PTHR11955:SF83; PTHR11955:SF83; 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; Cytoplasm; Lipid-binding; Nucleus; Transport.
FT CHAIN 1..132
FT /note="Fatty acid-binding protein, adipocyte"
FT /evidence="ECO:0000250|UniProtKB:P04117"
FT /id="PRO_0000444560"
FT MOTIF 22..32
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P04117"
FT BINDING 107
FT /ligand="(9Z,12Z)-octadecadienoate"
FT /ligand_id="ChEBI:CHEBI:30245"
FT /evidence="ECO:0000269|PubMed:26206084,
FT ECO:0007744|PDB:5BVS"
FT BINDING 127
FT /ligand="(9Z,12Z)-octadecadienoate"
FT /ligand_id="ChEBI:CHEBI:30245"
FT /evidence="ECO:0000269|PubMed:26206084,
FT ECO:0007744|PDB:5BVS"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:5BVQ"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:5BVQ"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:5BVQ"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:5BVQ"
FT STRAND 49..59
FT /evidence="ECO:0007829|PDB:5BVQ"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:5BVQ"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:5BVQ"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:5BVQ"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:5BVQ"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:5BVQ"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:5BVQ"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:5BVQ"
SQ SEQUENCE 132 AA; 14944 MW; C9055B98161C8C5F CRC64;
MCDQFVGTWK FLSSENFEDY MKELGVGFAT RKMAGVAKPN VTISINGDVI TIKTESTFKN
TEVSFRLGEE FDETTADDRK TKNVITLDNG ILNQVQKWDG KETVIKRKVM DGNLVVECTM
NTVTSKRVYE RA
