RET7_MOUSE
ID RET7_MOUSE Reviewed; 134 AA.
AC Q9EPC5; Q9CTK0;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Retinoid-binding protein 7;
DE AltName: Full=Cellular retinoic acid-binding protein 4;
DE Short=CRABP4;
DE Short=CRBP4;
DE AltName: Full=Cellular retinoic acid-binding protein IV;
DE Short=CRABP-IV;
GN Name=Rbp7;
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 [GENOMIC DNA / MRNA].
RC STRAIN=129, C57BL/6J, and C57BL/Wlds;
RX PubMed=11027338; DOI=10.1073/pnas.97.21.11377;
RA Conforti L., Tarlton A., Mack T.G.A., Mi W., Buckmaster E.A., Wagner D.,
RA Perry V.H., Coleman M.P.;
RT "A Ufd2/D4Cole1e chimeric protein and overexpression of Rbp7 in the slow
RT Wallerian degeneration (WldS) mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:11377-11382(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-134.
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Intracellular transport of retinol. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in white adipose tissue and
CC mammary gland.
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; AF260927; AAG38491.1; -; Genomic_DNA.
DR EMBL; AF260923; AAG17284.1; -; mRNA.
DR EMBL; BC028432; AAH28432.1; -; mRNA.
DR EMBL; AK003307; BAB22705.1; -; mRNA.
DR CCDS; CCDS18959.1; -.
DR RefSeq; NP_071303.1; NM_022020.2.
DR AlphaFoldDB; Q9EPC5; -.
DR SMR; Q9EPC5; -.
DR STRING; 10090.ENSMUSP00000030848; -.
DR MaxQB; Q9EPC5; -.
DR PaxDb; Q9EPC5; -.
DR PRIDE; Q9EPC5; -.
DR ProteomicsDB; 254917; -.
DR Antibodypedia; 27796; 127 antibodies from 20 providers.
DR DNASU; 63954; -.
DR Ensembl; ENSMUST00000030848; ENSMUSP00000030848; ENSMUSG00000028996.
DR GeneID; 63954; -.
DR KEGG; mmu:63954; -.
DR UCSC; uc008vwh.1; mouse.
DR CTD; 116362; -.
DR MGI; MGI:1890409; Rbp7.
DR VEuPathDB; HostDB:ENSMUSG00000028996; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000162218; -.
DR HOGENOM; CLU_113772_5_1_1; -.
DR InParanoid; Q9EPC5; -.
DR OMA; FYIHTTS; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; Q9EPC5; -.
DR TreeFam; TF316894; -.
DR BioGRID-ORCS; 63954; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Rbp7; mouse.
DR PRO; PR:Q9EPC5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9EPC5; protein.
DR Bgee; ENSMUSG00000028996; Expressed in interventricular septum and 112 other tissues.
DR ExpressionAtlas; Q9EPC5; baseline and differential.
DR Genevisible; Q9EPC5; MM.
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:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0005501; F:retinoid binding; IDA:MGI.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
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 Cytoplasm; Reference proteome; Retinol-binding; Transport; Vitamin A.
FT CHAIN 1..134
FT /note="Retinoid-binding protein 7"
FT /id="PRO_0000067404"
SQ SEQUENCE 134 AA; 15428 MW; 04D1A591AD7263E6 CRC64;
MPADLSGTWN LLSSDNFEGY MLALGIDFAT RKIAKLLKPQ KVIEQNGDSF TIQTCSSLRN
YLVKFKVGEE FEEDNKGLDN RKCTSLVTWE NDKLTCVQRG EKKNRGWSHW IEGDQLHLEM
FCEGQVCKQT FQRA
