ID A0A091DZK7_FUKDA Unreviewed; 135 AA.
AC A0A091DZK7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Fatty acid-binding protein 5 {ECO:0000256|ARBA:ARBA00040120};
DE AltName: Full=Epidermal-type fatty acid-binding protein {ECO:0000256|ARBA:ARBA00041852};
DE AltName: Full=Fatty acid-binding protein, epidermal {ECO:0000256|ARBA:ARBA00042693};
GN ORFNames=H920_10383 {ECO:0000313|EMBL:KFO28226.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO28226.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO28226.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO28226.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in);
CC Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000256|ARBA:ARBA00035938};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate(out) = (9Z,12Z)-
CC octadecadienoate(in); Xref=Rhea:RHEA:45264, ChEBI:CHEBI:30245;
CC Evidence={ECO:0000256|ARBA:ARBA00035842};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256,
CC ChEBI:CHEBI:7896; Evidence={ECO:0000256|ARBA:ARBA00036233};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}. Postsynaptic density
CC {ECO:0000256|ARBA:ARBA00034105}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000256|ARBA:ARBA00008390,
CC ECO:0000256|RuleBase:RU003696}.
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DR EMBL; KN122787; KFO28226.1; -; Genomic_DNA.
DR RefSeq; XP_010634554.1; XM_010636252.2.
DR AlphaFoldDB; A0A091DZK7; -.
DR STRING; 885580.ENSFDAP00000007011; -.
DR Ensembl; ENSFDAT00000020247; ENSFDAP00000007011; ENSFDAG00000015623.
DR GeneID; 104870577; -.
DR CTD; 2171; -.
DR OMA; WCLISSE; -.
DR OrthoDB; 46617at2759; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 CDD; cd19468; FABP5; 1.
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; FATTY ACID BINDING PROTEIN; 1.
DR PANTHER; PTHR11955:SF58; FATTY ACID-BINDING PROTEIN 5; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; Lipocalins; 1.
DR PROSITE; PS00214; FABP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003696}.
FT DOMAIN 9..26
FT /note="Cytosolic fatty-acid binding proteins"
FT /evidence="ECO:0000259|PROSITE:PS00214"
SQ SEQUENCE 135 AA; 15084 MW; FE39CE2D1F403166 CRC64;
MATIQQLVGR WRLVDSKGFE DYMKELGVGV AMRKMGAVAK PDCVITCDGN HLTVKTESTL
KTTQFACNLG EKFEETTADG RKTQTVCNFT DGALVQHQEW DGKESTITRK LKDGKLVVEC
VMNNVTCTRV YEKVE
//
