RET2_MOUSE
ID RET2_MOUSE Reviewed; 134 AA.
AC Q08652; Q9D1N1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Retinol-binding protein 2;
DE AltName: Full=Cellular retinol-binding protein II;
DE Short=CRBP-II;
GN Name=Rbp2; Synonyms=Crbpii;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Intestine;
RX PubMed=8288643; DOI=10.1016/s0021-9258(17)42196-x;
RA Nakshatri H., Chambon P.;
RT "The directly repeated RG(G/T)TCA motifs of the rat and mouse cellular
RT retinol-binding protein II genes are promiscuous binding sites for RAR,
RT RXR, HNF-4, and ARP-1 homo- and heterodimers.";
RL J. Biol. Chem. 269:890-902(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Intracellular transport of retinol.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in prenatal liver, intestine and lung,
CC and in adult intestine.
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 EMBL; X74154; CAA52268.1; -; mRNA.
DR EMBL; AK003312; BAB22708.1; -; mRNA.
DR CCDS; CCDS23425.1; -.
DR PIR; I48311; S34717.
DR RefSeq; NP_033060.3; NM_009034.4.
DR AlphaFoldDB; Q08652; -.
DR BMRB; Q08652; -.
DR SMR; Q08652; -.
DR BioGRID; 202828; 5.
DR STRING; 10090.ENSMUSP00000140676; -.
DR PhosphoSitePlus; Q08652; -.
DR MaxQB; Q08652; -.
DR PaxDb; Q08652; -.
DR PRIDE; Q08652; -.
DR ProteomicsDB; 253220; -.
DR Antibodypedia; 33461; 252 antibodies from 27 providers.
DR DNASU; 19660; -.
DR Ensembl; ENSMUST00000035029; ENSMUSP00000035029; ENSMUSG00000032454.
DR Ensembl; ENSMUST00000187905; ENSMUSP00000140630; ENSMUSG00000032454.
DR Ensembl; ENSMUST00000189446; ENSMUSP00000140676; ENSMUSG00000032454.
DR GeneID; 19660; -.
DR KEGG; mmu:19660; -.
DR UCSC; uc009rdk.2; mouse.
DR CTD; 5948; -.
DR MGI; MGI:97877; Rbp2.
DR VEuPathDB; HostDB:ENSMUSG00000032454; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000160165; -.
DR HOGENOM; CLU_113772_5_1_1; -.
DR InParanoid; Q08652; -.
DR OMA; HWIEGDI; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; Q08652; -.
DR TreeFam; TF316894; -.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 19660; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q08652; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q08652; protein.
DR Bgee; ENSMUSG00000032454; Expressed in small intestine Peyer's patch and 46 other tissues.
DR ExpressionAtlas; Q08652; baseline and differential.
DR Genevisible; Q08652; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0005501; F:retinoid binding; TAS:MGI.
DR GO; GO:0019841; F:retinol binding; ISO:MGI.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0001523; P:retinoid metabolic process; TAS:MGI.
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 2: Evidence at transcript level;
KW Cytoplasm; Reference proteome; Retinol-binding; Transport; Vitamin A.
FT CHAIN 1..134
FT /note="Retinol-binding protein 2"
FT /id="PRO_0000067396"
FT BINDING 41
FT /ligand="all-trans-retinol"
FT /ligand_id="ChEBI:CHEBI:17336"
FT /evidence="ECO:0000250|UniProtKB:P50120"
FT BINDING 109
FT /ligand="all-trans-retinol"
FT /ligand_id="ChEBI:CHEBI:17336"
FT /evidence="ECO:0000250|UniProtKB:P50120"
FT CONFLICT 98
FT /note="Q -> H (in Ref. 2; BAB22708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 134 AA; 15610 MW; 6B29171BA6A7AB63 CRC64;
MTKDQNGTWE MESNENFEGY MKALDIDFAT RKIAVRLTQT KIITQDGDNF KTKTNSTFRN
YDLDFTVGVE FDEHTKGLDG RHVKTLVTWE GNTLVCVQKG EKENRGWKQW VEGDKLYLEL
TCGDQVCRQV FKKK
