FABP5_PYGPA
ID FABP5_PYGPA Reviewed; 134 AA.
AC A0A0K0MJ13;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Fatty acid-binding protein 5 {ECO:0000303|PubMed:26206084};
DE AltName: Full=Epidermal-type fatty acid-binding protein {ECO:0000305};
DE Short=E-FABP {ECO:0000305};
DE AltName: Full=Fatty acid-binding protein, epidermal {ECO:0000305};
GN Name=FABP5 {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:5BVT}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF
RP APOPROTEIN AND IN COMPLEX WITH PALMITATE, 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: Intracellular carrier for long-chain fatty acids and related
CC active lipids, such as endocannabinoids, that regulate the metabolism
CC and actions of the ligands they bind. In addition to the cytosolic
CC transport, selectively delivers specific fatty acids from the cytosol
CC to the nucleus, wherein they activate nuclear receptors (By
CC similarity). Delivers retinoic acid to the nuclear receptor peroxisome
CC proliferator-activated receptor delta; which promotes proliferation and
CC survival. May also serve as a synaptic carrier of endocannabinoid at
CC central synapses and thus controls retrograde endocannabinoid
CC signaling. Modulates inflammation by regulating PTGES induction via NF-
CC kappa-B activation, and prostaglandin E2 (PGE2) biosynthesis during
CC inflammation (By similarity). Has the highest binding affinity for
CC docosahexaenoic acid (DHA) and decreasing relative affinity for
CC eicosapentaenoic acid (EPA), alpha-linolenic acid (ALA), oleic acid,
CC palmitic acid, linoleic acid and stearic acid, respectively
CC (PubMed:26206084). {ECO:0000250|UniProtKB:Q01469,
CC ECO:0000250|UniProtKB:Q05816, ECO:0000269|PubMed:26206084}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256,
CC ChEBI:CHEBI:7896; Evidence={ECO:0000250|UniProtKB:Q01469};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate(out) = (9Z,12Z)-
CC octadecadienoate(in); Xref=Rhea:RHEA:45264, ChEBI:CHEBI:30245;
CC Evidence={ECO:0000250|UniProtKB:Q01469};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in);
CC Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000250|UniProtKB:Q01469};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:26206084}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q01469}. Nucleus
CC {ECO:0000250|UniProtKB:Q01469}. Synapse {ECO:0000250|UniProtKB:Q05816}.
CC Postsynaptic density {ECO:0000250|UniProtKB:Q05816}. Secreted
CC {ECO:0000250|UniProtKB:Q05816}. Note=Localizes primarily to the
CC cytoplasm. Upon certain ligand binding, a conformation change exposes a
CC nuclear localization motif and the protein is transported into nucleus
CC (By similarity). Secreted by astrocytes, but not by neurons (By
CC similarity). {ECO:0000250|UniProtKB:Q01469,
CC ECO:0000250|UniProtKB:Q05816}.
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; KR054394; AKE37139.1; -; mRNA.
DR PDB; 5BVT; X-ray; 2.31 A; A=1-134.
DR PDBsum; 5BVT; -.
DR AlphaFoldDB; A0A0K0MJ13; -.
DR SMR; A0A0K0MJ13; -.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; 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 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; Cytoplasm; Lipid transport; Lipid-binding; Nucleus; Secreted;
KW Synapse; Transport.
FT CHAIN 1..134
FT /note="Fatty acid-binding protein 5"
FT /id="PRO_0000444561"
FT MOTIF 23..33
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT BINDING 109
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:26206084"
FT BINDING 109
FT /ligand="N-eicosanoyl ethanolamine"
FT /ligand_id="ChEBI:CHEBI:85253"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT BINDING 129..131
FT /ligand="(9Z,12Z)-octadecadienoate"
FT /ligand_id="ChEBI:CHEBI:30245"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT BINDING 129..131
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:26206084"
FT BINDING 131
FT /ligand="N-eicosanoyl ethanolamine"
FT /ligand_id="ChEBI:CHEBI:85253"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT HELIX 2..6
FT /evidence="ECO:0007829|PDB:5BVT"
FT STRAND 8..17
FT /evidence="ECO:0007829|PDB:5BVT"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:5BVT"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:5BVT"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:5BVT"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:5BVT"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:5BVT"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:5BVT"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:5BVT"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:5BVT"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:5BVT"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:5BVT"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:5BVT"
SQ SEQUENCE 134 AA; 15107 MW; 08503ED1EDBB161E CRC64;
MAIDAFLGKW CLISSEGFDE YMKELGVGMA MRKMGSMAKP DVYIIKDGDT ITVKTESTFK
TSQFSFKLGE KFEENTLDGR KTQTLVSLKD DGSLIQEQEW DGKKTIITRK LVDGQLVVEC
DMNGIKCVRV YQKA
