FABP5_BOVIN
ID FABP5_BOVIN Reviewed; 135 AA.
AC P55052; O62808; Q5E9D9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Fatty acid-binding protein 5 {ECO:0000305};
DE AltName: Full=Differentiation-associated lipid-binding protein LP2;
DE AltName: Full=Epidermal-type fatty acid-binding protein;
DE Short=E-FABP;
DE AltName: Full=Fatty acid-binding protein, epidermal;
GN Name=FABP5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-33 AND 116-129.
RC TISSUE=Lens;
RX PubMed=8947466; DOI=10.1042/bj3200049;
RA Jaworski C., Wistow G.;
RT "LP2, a differentiation-associated lipid-binding protein expressed in
RT bovine lens.";
RL Biochem. J. 320:49-54(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=9521644; DOI=10.1021/bi972520l;
RA Kingma P.B., Bok D., Ong D.E.;
RT "Bovine epidermal fatty acid-binding protein: determination of ligand
RT specificity and cellular localization in retina and testis.";
RL Biochemistry 37:3250-3257(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000250|UniProtKB:Q01469,
CC ECO:0000250|UniProtKB:Q05816}.
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:0000250|UniProtKB:Q05816}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9521644}. 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 -!- TISSUE SPECIFICITY: Most abundant in lens and retina (found in the
CC mueller cells), moderately abundant in heart and testis (found in the
CC Sertoli cells), and present in very low amounts in lung.
CC {ECO:0000269|PubMed:9521644}.
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; U55188; AAB41297.1; -; mRNA.
DR EMBL; AF059507; AAC14711.1; -; mRNA.
DR EMBL; BT020981; AAX08998.1; -; mRNA.
DR EMBL; BC105196; AAI05197.1; -; mRNA.
DR RefSeq; NP_776740.1; NM_174315.3.
DR AlphaFoldDB; P55052; -.
DR SMR; P55052; -.
DR STRING; 9913.ENSBTAP00000055977; -.
DR PeptideAtlas; P55052; -.
DR PRIDE; P55052; -.
DR Ensembl; ENSBTAT00000065769; ENSBTAP00000055977; ENSBTAG00000047330.
DR GeneID; 281760; -.
DR KEGG; bta:281760; -.
DR CTD; 2171; -.
DR VEuPathDB; HostDB:ENSBTAG00000047330; -.
DR GeneTree; ENSGT00940000154530; -.
DR InParanoid; P55052; -.
DR OMA; MGGMAKP; -.
DR OrthoDB; 1417203at2759; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000047330; Expressed in esophagus and 103 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IEA:Ensembl.
DR GO; GO:0001972; F:retinoic acid binding; IEA:Ensembl.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR GO; GO:1990379; P:lipid transport across blood-brain barrier; IEA:Ensembl.
DR GO; GO:0010829; P:negative regulation of glucose transmembrane transport; IEA:Ensembl.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0031392; P:regulation of prostaglandin biosynthetic process; IEA:Ensembl.
DR GO; GO:0099178; P:regulation of retrograde trans-synaptic signaling by endocanabinoid; ISS:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl.
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 Acetylation; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Lipid transport; Lipid-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Secreted; Synapse; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT CHAIN 2..135
FT /note="Fatty acid-binding protein 5"
FT /id="PRO_0000067376"
FT MOTIF 24..34
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT BINDING 43
FT /ligand="N-eicosanoyl ethanolamine"
FT /ligand_id="ChEBI:CHEBI:85253"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
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 131
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT BINDING 131
FT /ligand="N-eicosanoyl ethanolamine"
FT /ligand_id="ChEBI:CHEBI:85253"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT MOD_RES 22
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000305"
FT MOD_RES 131
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT DISULFID 120..127
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT CONFLICT 52
FT /note="L -> P (in Ref. 1; AAB41297)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 135 AA; 15074 MW; 439B86AF88A34E2A CRC64;
MATVQQLVGR WRLVESKGFD EYMKEVGVGM ALRKVGAMAK PDCIITSDGK NLSIKTESTL
KTTQFSCKLG EKFEETTADG RKTQTVCNFT DGALVQHQEW DGKESTITRK LEDGKLVVVC
VMNNVTCTRV YEKVE
