RET3_BOVIN
ID RET3_BOVIN Reviewed; 1286 AA.
AC P12661;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 AltName: Full=Protein 7S;
DE Flags: Precursor;
GN Name=RBP3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2910846; DOI=10.1016/s0021-9258(19)85061-5;
RA Borst D.E., Redmond T.M., Elser J.E., Gonda M.A., Wiggert B., Chader G.J.,
RA Nickerson J.M.;
RT "Interphotoreceptor retinoid-binding protein. Gene characterization,
RT protein repeat structure, and its evolution.";
RL J. Biol. Chem. 264:1115-1123(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2676730; DOI=10.1016/0378-1119(89)90255-2;
RA Redmond T.M., Si J.S., Barrett D.J., Borst D.E., Rainier S., Kotake S.,
RA Gery I., Nickerson J.M.;
RT "Synthesis of an immunopathogenic fusion protein derived from a bovine
RT interphotoreceptor retinoid-binding protein cDNA clone.";
RL Gene 80:109-118(1989).
RN [3]
RP PROTEIN SEQUENCE OF 23-56.
RC TISSUE=Retina;
RX PubMed=3827838; DOI=10.1042/bj2400019;
RA Redmond T.M., Wiggert B., Robey F.A., Chader G.J.;
RT "Interspecies conservation of structure of interphotoreceptor retinoid-
RT binding protein. Similarities and differences as adjudged by peptide
RT mapping and N-terminal sequencing.";
RL Biochem. J. 240:19-26(1986).
RN [4]
RP PROTEIN SEQUENCE OF 23-46.
RX PubMed=2981203; DOI=10.1016/s0021-9258(18)89715-0;
RA Saari J.C., Teller D.C., Crabb J.W., Bredberg L.;
RT "Properties of an interphotoreceptor retinoid-binding protein from bovine
RT retina.";
RL J. Biol. Chem. 260:195-201(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 1194-1221.
RX PubMed=2413855; DOI=10.1016/0006-291x(85)90202-5;
RA Barrett D.J., Redmond T.M., Wiggert B., Oprian D.D., Chader G.J.,
RA Nickerson J.M.;
RT "cDNA clones encoding bovine interphotoreceptor retinoid binding protein.";
RL Biochem. Biophys. Res. Commun. 131:1086-1093(1985).
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 -!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
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DR EMBL; M20748; AAA30591.1; -; Genomic_DNA.
DR EMBL; M27870; AAA30594.1; -; mRNA.
DR EMBL; M26119; AAA30593.1; -; mRNA.
DR PIR; A32205; RJBOP.
DR RefSeq; NP_776589.1; NM_174164.1.
DR AlphaFoldDB; P12661; -.
DR SMR; P12661; -.
DR IntAct; P12661; 1.
DR MINT; P12661; -.
DR STRING; 9913.ENSBTAP00000006585; -.
DR MEROPS; S41.953; -.
DR MEROPS; S41.954; -.
DR PaxDb; P12661; -.
DR PRIDE; P12661; -.
DR ABCD; P12661; 1 sequenced antibody.
DR GeneID; 281443; -.
DR KEGG; bta:281443; -.
DR CTD; 5949; -.
DR eggNOG; ENOG502QW81; Eukaryota.
DR InParanoid; P12661; -.
DR OrthoDB; 116338at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0090658; C:cone matrix sheath; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0019841; F:retinol binding; IBA:GO_Central.
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 Direct protein sequencing; Extracellular matrix; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Transport; Vitamin A.
FT SIGNAL 1..17
FT PROPEP 18..22
FT /evidence="ECO:0000269|PubMed:2981203,
FT ECO:0000269|PubMed:3827838"
FT /id="PRO_0000021521"
FT CHAIN 23..1286
FT /note="Retinol-binding protein 3"
FT /id="PRO_0000021522"
FT REPEAT 23..323
FT /note="1"
FT REPEAT 324..631
FT /note="2"
FT REPEAT 632..932
FT /note="3"
FT REPEAT 933..1231
FT /note="4"
FT REGION 23..1231
FT /note="4 X approximate tandem repeats"
FT REGION 389..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1252
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
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 CARBOHYD 1114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 40
FT /note="C -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="C -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="N -> V (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1115
FT /note="N -> D (in Ref. 2; AAA30594)"
FT /evidence="ECO:0000305"
FT CONFLICT 1249..1250
FT /note="HR -> QQ (in Ref. 2; AAA30594)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1286 AA; 139698 MW; C7776D698F2C2D55 CRC64;
MVRKWALLLP MLLCGLTGPA HLFQPSLVLE MAQVLLDNYC FPENLMGMQG AIEQAIKSQE
ILSISDPQTL AHVLTAGVQS SLNDPRLVIS YEPSTLEAPP RAPAVTNLTL EEIIAGLQDG
LRHEILEGNV GYLRVDDIPG QEVMSKLRSF LVANVWRKLV NTSALVLDLR HCTGGHVSGI
PYVISYLHPG STVSHVDTVY DRPSNTTTEI WTLPEALGEK YSADKDVVVL TSSRTGGVAE
DIAYILKQMR RAIVVGERTV GGALNLQKLR VGQSDFFLTV PVSRSLGPLG EGSQTWEGSG
VLPCVGTPAE QALEKALAVL MLRRALPGVI QRLQEALREY YTLVDRVPAL LSHLAAMDLS
SVVSEDDLVT KLNAGLQAVS EDPRLQVQVV RPKEASSGPE EEAEEPPEAV PEVPEDEAVR
RALVDSVFQV SVLPGNVGYL RFDSFADASV LEVLGPYILH QVWEPLQDTE HLIMDLRQNP
GGPSSAVPLL LSYFQSPDAS PVRLFSTYDR RTNITREHFS QTELLGRPYG TQRGVYLLTS
HRTATAAEEL AFLMQSLGWA TLVGEITAGS LLHTHTVSLL ETPEGGLALT VPVLTFIDNH
GECWLGGGVV PDAIVLAEEA LDRAQEVLEF HRSLGELVEG TGRLLEAHYA RPEVVGQMGA
LLRAKLAQGA YRTAVDLESL ASQLTADLQE MSGDHRLLVF HSPGEMVAEE APPPPPVVPS
PEELSYLIEA LFKTEVLPGQ LGYLRFDAMA ELETVKAVGP QLVQLVWQKL VDTAALVVDL
RYNPGSYSTA VPLLCSYFFE AEPRRHLYSV FDRATSRVTE VWTLPHVTGQ RYGSHKDLYV
LVSHTSGSAA EAFAHTMQDL QRATIIGEPT AGGALSVGIY QVGSSALYAS MPTQMAMSAS
TGEAWDLAGV EPDITVPMSV ALSTARDIVT LRAKVPTVLQ TAGKLVADNY ASPELGVKMA
AELSGLQSRY ARVTSEAALA ELLQADLQVL SGDPHLKTAH IPEDAKDRIP GIVPMQIPSP
EVFEDLIKFS FHTNVLEGNV GYLRFDMFGD CELLTQVSEL LVEHVWKKIV HTDALIVDMR
FNIGGPTSSI SALCSYFFDE GPPILLDKIY NRPNNSVSEL WTLSQLEGER YGSKKSMVIL
TSTLTAGAAE EFTYIMKRLG RALVIGEVTS GGCQPPQTYH VDDTDLYLTI PTARSVGAAD
GSSWEGVGVV PDVAVPAEAA LTRAQEMLQH TPLRARRSPR LHGRRKGHHR QSQGRAGSLG
RNQGVVRPEV LTEAPSGQKR GLLQCG
