RET3_XENLA
ID RET3_XENLA Reviewed; 1219 AA.
AC Q7SZI7; A0JMY0; B2GTX9; Q08107; Q3B8C0; Q56A62;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Retinol-binding protein 3;
DE AltName: Full=Interphotoreceptor retinoid-binding protein;
DE Short=IRBP;
DE Short=xIRBP;
DE AltName: Full=Interstitial retinol-binding protein;
DE Flags: Precursor;
GN Name=rbp3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Tadpole;
RX PubMed=17683573; DOI=10.1186/1471-2091-8-15;
RA Gonzalez-Fernandez F., Baer C.A., Ghosh D.;
RT "Module structure of interphotoreceptor retinoid-binding protein (IRBP) may
RT provide bases for its complex role in the visual cycle -structure/function
RT study of Xenopus IRBP.";
RL BMC Biochem. 8:15-15(2007).
RN [2]
RP PROTEIN SEQUENCE OF 23-27, CRYSTALLIZATION, AND INTERACTION WITH RETINOL.
RX PubMed=18079675;
RA Ghosh D., Griswold J.B., Bevilacqua T., Gonzalez-Fernandez F.;
RT "Purification of the full-length Xenopus interphotoreceptor retinoid
RT binding protein and growth of diffraction-quality crystals.";
RL Mol. Vis. 13:2275-2281(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 897-1219.
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 923-1219, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, GLYCOSYLATION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Tadpole;
RX PubMed=8360278; DOI=10.1242/jcs.105.1.7;
RA Gonzalez-Fernandez F., Kittredge K.L., Rayborn M.E., Hollyfield J.G.,
RA Landers R.A., Saha M., Grainger R.M.;
RT "Interphotoreceptor retinoid-binding protein (IRBP), a major 124 kDa
RT glycoprotein in the interphotoreceptor matrix of Xenopus laevis.
RT Characterization, molecular cloning and biosynthesis.";
RL J. Cell Sci. 105:7-21(1993).
RN [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=8698895;
RX DOI=10.1002/(sici)1096-9861(19960408)367:3<329::aid-cne1>3.0.co;2-7;
RA Hessler R.B., Baer C.A., Bukelman A., Kittredge K.L.,
RA Gonzalez-Fernandez F.;
RT "Interphotoreceptor retinoid-binding protein (IRBP): expression in the
RT adult and developing Xenopus retina.";
RL J. Comp. Neurol. 367:329-341(1996).
RN [6]
RP CRYSTALLIZATION.
RX PubMed=11446776; DOI=10.1006/exer.2001.1031;
RA Loew A., Baer C., Gonzalez-Fernandez F.;
RT "The functional unit of interphotoreceptor retinoid-binding protein (IRBP)
RT -- purification, characterization and preliminary crystallographic
RT analysis.";
RL Exp. Eye Res. 73:257-264(2001).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=14556291; DOI=10.1002/cne.10861;
RA Cunningham L.L., Gonzalez-Fernandez F.;
RT "Internalization of interphotoreceptor retinoid-binding protein by the
RT Xenopus retinal pigment epithelium.";
RL J. Comp. Neurol. 466:331-342(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 319-615, AND SUBUNIT.
RX PubMed=11796109; DOI=10.1016/s0969-2126(01)00698-0;
RA Loew A., Gonzalez-Fernandez F.;
RT "Crystal structure of the functional unit of interphotoreceptor retinoid
RT binding protein.";
RL Structure 10:43-49(2002).
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. Also involved in the transport
CC of fatty acids and retinal development.
CC -!- SUBUNIT: Monomer. Interacts with retinol. Predominantly found as a
CC monomer, but to a really lower extent also found as a homodimer.
CC {ECO:0000269|PubMed:11796109, ECO:0000269|PubMed:18079675}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, interphotoreceptor matrix. Cytoplasm. Note=Interphotoreceptor
CC matrix that permeates the space between the retina and the contiguous
CC layer of pigment epithelium cells. Lesser amounts found in the pigment
CC epithelial cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in retina; at similar levels by both
CC cones and rods. Weakly expressed in brain. In embryos, expression is
CC restricted to the central retina. {ECO:0000269|PubMed:8360278,
CC ECO:0000269|PubMed:8698895}.
CC -!- DEVELOPMENTAL STAGE: Expressed in retina at stage 42. In swimming
CC tadpole, expression begins from stage 40, is clearly visible at stage
CC 43 and increased markedly by stage 45/46. Expression appears to be
CC restricted to the head. {ECO:0000269|PubMed:8360278,
CC ECO:0000269|PubMed:8698895}.
CC -!- PTM: Glycosylated. {ECO:0000305|PubMed:8360278}.
CC -!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
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DR EMBL; X95473; CAA64745.1; -; mRNA.
DR EMBL; BC092153; AAH92153.1; -; mRNA.
DR EMBL; BC106609; AAI06610.1; -; mRNA.
DR EMBL; BC126046; AAI26047.1; -; mRNA.
DR EMBL; BC166054; AAI66054.1; -; mRNA.
DR EMBL; X69469; CAA49228.1; -; Genomic_DNA.
DR PIR; S33927; S33927.
DR RefSeq; NP_001082637.1; NM_001089168.2.
DR PDB; 1J7X; X-ray; 1.80 A; A=319-615.
DR PDBsum; 1J7X; -.
DR AlphaFoldDB; Q7SZI7; -.
DR SMR; Q7SZI7; -.
DR MEROPS; S41.951; -.
DR PRIDE; Q7SZI7; -.
DR GeneID; 398616; -.
DR KEGG; xla:398616; -.
DR CTD; 398616; -.
DR Xenbase; XB-GENE-1008802; rbp3.L.
DR OrthoDB; 116338at2759; -.
DR EvolutionaryTrace; Q7SZI7; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 398616; Expressed in camera-type eye and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0033165; C:interphotoreceptor matrix; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Extracellular matrix;
KW Glycoprotein; Receptor; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:18079675"
FT CHAIN 23..1219
FT /note="Retinol-binding protein 3"
FT /id="PRO_5000146732"
FT REPEAT 127..301
FT /note="1"
FT REPEAT 423..598
FT /note="2"
FT REPEAT 721..897
FT /note="3"
FT REPEAT 1022..1198
FT /note="4"
FT REGION 127..1198
FT /note="4 X approximate tandem repeats"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 319..334
FT /evidence="ECO:0007829|PDB:1J7X"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:1J7X"
FT HELIX 341..347
FT /evidence="ECO:0007829|PDB:1J7X"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:1J7X"
FT HELIX 359..374
FT /evidence="ECO:0007829|PDB:1J7X"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:1J7X"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:1J7X"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:1J7X"
FT HELIX 404..414
FT /evidence="ECO:0007829|PDB:1J7X"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:1J7X"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:1J7X"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:1J7X"
FT HELIX 435..448
FT /evidence="ECO:0007829|PDB:1J7X"
FT HELIX 450..453
FT /evidence="ECO:0007829|PDB:1J7X"
FT STRAND 457..462
FT /evidence="ECO:0007829|PDB:1J7X"
FT HELIX 474..479
FT /evidence="ECO:0007829|PDB:1J7X"
FT STRAND 489..495
FT /evidence="ECO:0007829|PDB:1J7X"
FT TURN 496..499
FT /evidence="ECO:0007829|PDB:1J7X"
FT STRAND 502..505
FT /evidence="ECO:0007829|PDB:1J7X"
FT STRAND 517..525
FT /evidence="ECO:0007829|PDB:1J7X"
FT HELIX 532..542
FT /evidence="ECO:0007829|PDB:1J7X"
FT STRAND 547..551
FT /evidence="ECO:0007829|PDB:1J7X"
FT STRAND 560..564
FT /evidence="ECO:0007829|PDB:1J7X"
FT STRAND 568..575
FT /evidence="ECO:0007829|PDB:1J7X"
FT STRAND 577..581
FT /evidence="ECO:0007829|PDB:1J7X"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:1J7X"
FT HELIX 600..602
FT /evidence="ECO:0007829|PDB:1J7X"
FT HELIX 603..612
FT /evidence="ECO:0007829|PDB:1J7X"
SQ SEQUENCE 1219 AA; 135022 MW; F39A96DEE053F1C8 CRC64;
MPPLFQALTT ALFFCGIASN PLFQPSLVMD MAKVLLDNYC FPENLVGMQE TIEQAVKGGE
ILHISDPDTL ANVFTSGVQG YLNDPRLVVS YEPNYSGPQT EQSLELTPEQ LKFLINHSVK
YDILPGNIGY LRIDFIIGQD VVQKVGPHLV NNIWKKLMPT SALILDLRYS TQGEVSGIPF
VVSYLCDSEI HIDSIYNRPS NTTTDLWTLP ELMGERYGKV KDVVVLTSKY TKGVAEDASY
ILKHMNRAIV VGEKTAGGSL DTQKIKIGQS DFYITVPVSR SLSPLTGQSW EVSGVSPCVV
VNAKDALDKA QAILAVRSSV THVLHQLCDI LANNYAFSER IPTLLQHLPN LDYSTVISEE
DIAAKLNYEL QSLTEDPRLV LKSKTDTLVM PGDSIQAENI PEDEAMLQAL VNTVFKVSIL
PGNIGYLRFD QFADVSVIAK LAPFIVNTVW EPITITENLI IDLRYNVGGS STAVPLLLSY
FLDPETKIHL FTLHNRQQNS TDEVYSHPKV LGKPYGSKKG VYVLTSHQTA TAAEEFAYLM
QSLSRATIIG EITSGNLMHS KVFPFDGTQL SVTVPIINFI DSNGDYWLGG GVVPDAIVLA
DEALDKAKEI IAFHPSIFPL VKGTGHLLEV HYAIPEVAYK VSSVLQNKWS EGGYRSVVDL
ESLASLLTSE MQENSGDHRL HVFYSDTEPE ILEDQPPKIP SPEELNYIID ALFKIEVLPG
NVGYLRFDMM ADTEIIKAIG PQLVSLVWNK LVETNSLIID MRYNTGGYST AIPIFCSYFF
DPEPLQHLYT VYDRSTSTGK DIWTLPEVFG ERYGSTKDIY ILTSHMTGSA AEVFTRSLKD
LNRATLIGEP TSGVSLSVGM YKVGDSNLYV TIPNQVVISS VTGKVWSVSG VEPHVIIQAN
EAMNIAHRII KLRTKIPTVI QTAAKLVADN YAFADTGANV ASKFIALVDK IDYKMIKSEV
ELAEKINDDL QSLSKDFHLK AVYIPENSKD RIPGVVPMQI PSPELFEELI KFSFHTDVFE
KNIGYIRFDM FADSDLLNQV SDLLVEHVWK KVVDQDALII DMRFNIGGPT SSIPIFCSYF
FDEGTPVLLD KIYSRTSNAM TDIWTLPDLV GKTFGSKKPL IILTSSLTEG AAEEFVYIMK
RLGRAYVVGE VTSGGCHPPQ TYHVDDTHLY LTIPTSRSAS AEPGESWEGK GVLPDLEISS
ETALLKAKEI LESQLEGRR
