RET3_MOUSE
ID RET3_MOUSE Reviewed; 1234 AA.
AC P49194; Q6B4R6; Q8VD34; Q9R0H8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Retinol-binding protein 3;
DE AltName: Full=Interphotoreceptor retinoid-binding protein;
DE Short=IRBP;
DE AltName: Full=Interstitial retinol-binding protein;
DE Flags: Precursor;
GN Name=Rbp3;
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].
RC STRAIN=129/Sv;
RX PubMed=12434304; DOI=10.1076/ceyr.24.5.354.8518;
RA Shuler R.K. Jr., Gross E., He W.-Y., Liou G.I., Nickerson J.M.;
RT "Sequence analysis of the mouse IRBP gene and cDNA.";
RL Curr. Eye Res. 24:354-367(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [GENOMIC DNA] OF 1-610.
RC STRAIN=BALB/cJ;
RA Si J.-S., Nickerson J.M.;
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-454, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=1342928; DOI=10.1016/1055-7903(92)90026-d;
RA Stanhope M.J., Czelusniak J., Si J.-S., Nickerson J.M., Goodman M.;
RT "A molecular perspective on mammalian evolution from the gene encoding
RT interphotoreceptor retinoid binding protein, with convincing evidence for
RT bat monophyly.";
RL Mol. Phylogenet. Evol. 1:148-160(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 71-454.
RC STRAIN=MOA;
RA Suzuki H., Serizawa K.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: IRBP shuttles 11-cis and all trans retinoids between the
CC retinol isomerase in the pigment epithelium and the visual pigments in
CC the photoreceptor cells of the retina.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, interphotoreceptor matrix. Note=Interphotoreceptor matrix that
CC permeates the space between the retina and the contiguous layer of
CC pigment epithelium cells.
CC -!- TISSUE SPECIFICITY: Expressed in the photosensitive tissues; retina and
CC pineal gland. {ECO:0000269|PubMed:1342928}.
CC -!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
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DR EMBL; AY682090; AAT81142.1; -; Genomic_DNA.
DR EMBL; BC017610; AAH17610.1; -; mRNA.
DR EMBL; BC042480; AAH42480.1; -; mRNA.
DR EMBL; BC083133; AAH83133.1; -; mRNA.
DR EMBL; AF126968; AAA39331.2; -; Genomic_DNA.
DR EMBL; AB033711; BAA85872.1; -; Genomic_DNA.
DR CCDS; CCDS26929.1; -.
DR RefSeq; NP_056560.1; NM_015745.2.
DR AlphaFoldDB; P49194; -.
DR SMR; P49194; -.
DR STRING; 10090.ENSMUSP00000040249; -.
DR MEROPS; S41.952; -.
DR MEROPS; S41.953; -.
DR GlyGen; P49194; 3 sites.
DR iPTMnet; P49194; -.
DR PhosphoSitePlus; P49194; -.
DR MaxQB; P49194; -.
DR PaxDb; P49194; -.
DR PRIDE; P49194; -.
DR ProteomicsDB; 255288; -.
DR DNASU; 19661; -.
DR GeneID; 19661; -.
DR KEGG; mmu:19661; -.
DR UCSC; uc007tad.1; mouse.
DR CTD; 5949; -.
DR MGI; MGI:97878; Rbp3.
DR eggNOG; ENOG502QW81; Eukaryota.
DR InParanoid; P49194; -.
DR OrthoDB; 116338at2759; -.
DR PhylomeDB; P49194; -.
DR TreeFam; TF332253; -.
DR Reactome; R-MMU-2187335; The retinoid cycle in cones (daylight vision).
DR Reactome; R-MMU-2453902; The canonical retinoid cycle in rods (twilight vision).
DR BioGRID-ORCS; 19661; 4 hits in 77 CRISPR screens.
DR ChiTaRS; Rbp3; mouse.
DR PRO; PR:P49194; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P49194; protein.
DR GO; GO:0090658; C:cone matrix sheath; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0033165; C:interphotoreceptor matrix; ISO:MGI.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0019841; F:retinol binding; ISO:MGI.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR005151; Tail-specific_protease.
DR Pfam; PF03572; Peptidase_S41; 4.
DR SMART; SM00245; TSPc; 4.
DR SUPFAM; SSF52096; SSF52096; 4.
PE 2: Evidence at transcript level;
KW Extracellular matrix; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal; Transport; Vitamin A.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1234
FT /note="Retinol-binding protein 3"
FT /id="PRO_0000021524"
FT REPEAT 18..320
FT /note="1"
FT REPEAT 321..628
FT /note="2"
FT REPEAT 629..929
FT /note="3"
FT REPEAT 930..1228
FT /note="4"
FT REGION 18..1228
FT /note="4 X approximate tandem repeats"
FT REGION 383..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 161
FT /note="G -> S (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 770..773
FT /note="LVDT -> AGGQ (in Ref. 1; AAT81142)"
FT /evidence="ECO:0000305"
FT CONFLICT 930
FT /note="V -> A (in Ref. 1; AAT81142)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1234 AA; 134451 MW; 7884CC3A29D6E7D7 CRC64;
MMREWVLVLS TLLWVPAGPT HLFQPSLVLD MAKILLDNYC FPENLMGMQA AIEQAMKSHE
ILGISDPQTL AQVLTAGVQS SLSDPRLFIS YEPSTLEAPQ QAPVLTNLTR EELLAQIQRN
IRHEVLEGNV GYLRVDDLPG QEVLSELGEF LVSHVWRQLM GTSSLVLDLR HCSGGHFSGI
PYVISYLHPG NTVMHVDTVY DRPSNTTTEI WTLPEVLGER YSADKDVVVL TSGHTGGVAE
DIAYILKQMR RAIVVGERTE GGALDLQKLR IGQSNFFLTV PVSRSLGPLG GGGQTWEGSG
VLPCVGTPAE QALEKALAIL TLRRALPGVV LRLQEALQDY YTLVDRVPGL LHHLASMDYS
AVVSEEDLVT KLNAGLQAVS EDPRLLVRAT GPRDSSSRPE TGPNESPAAT PEVPTEEDAR
RALVDSVFQV SVLPGNVGYL RFDRFADAAV LETLGPYVLK QVWEPLQDTE HLIMDLRHNP
GGPSSAMPLV LSYFQGPEAG PVRLFTTYDR RTNITQEHFS HRELLGQRYG NQRGVYLLTS
HRTATAAEEF AFLMQSLGWA TLVGEITAGS LLHTCTVPLL DSPQGGLALT VPVLTFIDNH
GEAWLGGGVV PDAIVLAEEA LERAQEVLDF HRSLGALVEG TGRLLEAHYA RPEIAQRARA
LLQSKLAQGA YRTAVDLESL ASQLTADLQE VSEDHRLLVF HSPGELVAEE VPLPPPAVPS
PEELSYLIEA LFKTDVLPGQ LGYLRFDAMA ELETVKAIGP QLVQLVWQRL VDTAALIVDL
RYNPGSYSSA VPLLCSYFFE AEPRQHLYSV FDRATSRVTE IWTLPLVAGQ RYGSHKDLYI
LMSHTSGSAA EAFAHTMQDL QRATVIGEPT AGGALSVGIY QVGNSPLYAS MPTQMALSAS
TGEAWDLAGV EPDITVPMSE ALSTAQDIVV LRAKVPTVLQ TAGKLVADNY ASPELGAKMA
AKLSGLQSRY ARVTSEGALA EMLGADLQIL SGDPHLKTAH IPEDAKDRIP GIVPMQIPSP
EVFEDLIKFS FHTNVLEDNI GYLRFDMFGD CELLTQVSEL LVEHIWKKIV HTDALIIDMR
FNLGGPTSSI SALCSYFFDE APPILLDKIY NRPNDSVSEL WTHTQLTGER YGSKKSVAIL
TSGVTAGAAE EFTYIMKRLG RALVIGEVTS GGCQPPQTYH VDDTHLYITI PTARSVGAED
GSSWEGVGVT PNVVVSSELA LTRAKEILQQ ALRG
