ID   RABP2_CHICK             Reviewed;          37 AA.
AC   P30370;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Cellular retinoic acid-binding protein 2;
DE   AltName: Full=Cellular retinoic acid-binding protein II;
DE            Short=CRABP-II;
DE   Flags: Fragment;
GN   Name=CRABP2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-37.
RX   PubMed=2849937; DOI=10.1016/s0006-291x(88)81016-7;
RA   Kitamoto T., Momoi T., Momoi M.;
RT   "The presence of a novel cellular retinoic acid-binding protein in chick
RT   embryos: purification and partial characterization.";
RL   Biochem. Biophys. Res. Commun. 157:1302-1308(1988).
RN   [2]
RP   ERRATUM OF PUBMED:2849937.
RA   Kitamoto T., Momoi T., Momoi M.;
RL   Biochem. Biophys. Res. Commun. 159:371-371(1989).
CC   -!- FUNCTION: Transports retinoic acid to the nucleus. Regulates the access
CC       of retinoic acid to the nuclear retinoic acid receptors (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum {ECO:0000250}.
CC       Nucleus {ECO:0000250}. Note=Upon ligand binding, a conformation change
CC       exposes a nuclear localization motif and the protein is transported
CC       into the nucleus. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Embryo.
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}.
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DR   PIR; B31872; B31872.
DR   AlphaFoldDB; P30370; -.
DR   SMR; P30370; -.
DR   STRING; 9031.ENSGALP00000042960; -.
DR   eggNOG; KOG4015; Eukaryota.
DR   HOGENOM; CLU_113772_9_0_1; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR   GO; GO:0001972; F:retinoic acid binding; IEA:InterPro.
DR   GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR   GO; GO:0048385; P:regulation of retinoic acid receptor signaling pathway; IEA:InterPro.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR031281; CRABP2.
DR   InterPro; IPR000463; Fatty_acid-bd.
DR   InterPro; IPR031259; ILBP.
DR   PANTHER; PTHR11955; PTHR11955; 1.
DR   PANTHER; PTHR11955:SF60; PTHR11955:SF60; 1.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00214; FABP; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Nucleus;
KW   Reference proteome; Retinol-binding; Transport; Vitamin A.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2849937"
FT   CHAIN           2..>37
FT                   /note="Cellular retinoic acid-binding protein 2"
FT                   /id="PRO_0000067418"
FT   MOTIF           21..31
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   NON_TER         37
SQ   SEQUENCE   37 AA;  4128 MW;  2BC1C154D26490F4 CRC64;
     MPNFSGNWKM KSSENFEELL KALGVNMMLR KIAVAAA