ID   FBP12_RAT               Reviewed;         132 AA.
AC   B7SUM8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Fatty acid-binding protein 12 {ECO:0000303|PubMed:18786628};
GN   Name=FABP12 {ECO:0000303|PubMed:18786628};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ACI03638.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Sprague-Dawley {ECO:0000312|EMBL:ACI03638.1};
RC   TISSUE=Retina {ECO:0000312|EMBL:ACI03638.1};
RX   PubMed=18786628; DOI=10.1016/j.ygeno.2008.08.003;
RA   Liu R.Z., Li X., Godbout R.;
RT   "A novel fatty acid-binding protein (FABP) gene resulting from tandem gene
RT   duplication in mammals: transcription in rat retina and testis.";
RL   Genomics 92:436-445(2008).
RN   [2] {ECO:0000312|EMBL:EDM00992.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in lipid transport.
CC       {ECO:0000250|UniProtKB:P02690}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in adult retina and testis with
CC       lower levels in cerebral cortex, kidney and epididymis. In the retina,
CC       strongly expressed in the ganglion cell layer and throughout the inner
CC       nuclear layer in amacrine and bipolar cells. Not expressed in the outer
CC       nuclear layer. In the testis, detected in the seminiferous tubules.
CC       {ECO:0000269|PubMed:18786628}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in adult but not at postnatal day 1. In
CC       the seminiferous tubule, expressed in first layer capped spermatids at
CC       stage VII and in spermatids closer to the lumen of the tubule at stage
CC       XII. Not detected in spermatogonia, first layer of spermatocytes or
CC       mature spermatozoa. {ECO:0000269|PubMed:18786628}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000255}.
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DR   EMBL; EU733648; ACI03638.1; -; mRNA.
DR   EMBL; CH473961; EDM00992.1; -; Genomic_DNA.
DR   RefSeq; NP_001128086.1; NM_001134614.1.
DR   RefSeq; XP_006232207.1; XM_006232145.3.
DR   RefSeq; XP_006232208.1; XM_006232146.3.
DR   RefSeq; XP_006232210.1; XM_006232148.3.
DR   RefSeq; XP_017446512.1; XM_017591023.1.
DR   RefSeq; XP_017446513.1; XM_017591024.1.
DR   AlphaFoldDB; B7SUM8; -.
DR   SMR; B7SUM8; -.
DR   STRING; 10116.ENSRNOP00000056087; -.
DR   PaxDb; B7SUM8; -.
DR   Ensembl; ENSRNOT00000059326; ENSRNOP00000056087; ENSRNOG00000038825.
DR   GeneID; 499570; -.
DR   KEGG; rno:499570; -.
DR   UCSC; RGD:1565000; rat.
DR   CTD; 646486; -.
DR   RGD; 1565000; Fabp12.
DR   eggNOG; KOG4015; Eukaryota.
DR   GeneTree; ENSGT00940000162398; -.
DR   HOGENOM; CLU_113772_0_0_1; -.
DR   InParanoid; B7SUM8; -.
DR   OMA; MVVESSV; -.
DR   PhylomeDB; B7SUM8; -.
DR   TreeFam; TF316894; -.
DR   Reactome; R-RNO-163560; Triglyceride catabolism.
DR   PRO; PR:B7SUM8; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Proteomes; UP000234681; Chromosome 2.
DR   Bgee; ENSRNOG00000038825; Expressed in testis and 5 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR   GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR031261; FABP12.
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:SF76; PTHR11955:SF76; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; SSF50814; 1.
PE   2: Evidence at transcript level;
KW   Lipid-binding; Reference proteome; Transport.
FT   CHAIN           1..132
FT                   /note="Fatty acid-binding protein 12"
FT                   /id="PRO_0000394457"
FT   BINDING         107
FT                   /ligand="a fatty acid"
FT                   /ligand_id="ChEBI:CHEBI:28868"
FT                   /evidence="ECO:0000250|UniProtKB:P02690"
FT   BINDING         127..129
FT                   /ligand="a fatty acid"
FT                   /ligand_id="ChEBI:CHEBI:28868"
FT                   /evidence="ECO:0000250|UniProtKB:P02690"
SQ   SEQUENCE   132 AA;  14860 MW;  74F08D017EECAFC5 CRC64;
     MVDQLQGTWK SVSCENFENY MKELGAGRAI RKLGCLARPV VTISTDGDRI TIKTKSIFKN
     KEISFKLGEE FEEITPGGRK SKSTVVLDND SLVQVQDWDG KEATIRRRLV DGKMVVESAV
     NNVTCTRTYQ RV