RLBP1_BOVIN
ID RLBP1_BOVIN Reviewed; 317 AA.
AC P10123; Q17QW7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Retinaldehyde-binding protein 1;
DE AltName: Full=Cellular retinaldehyde-binding protein;
GN Name=RLBP1; Synonyms=CRALBP;
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 [MRNA].
RX PubMed=3198595; DOI=10.1016/s0021-9258(18)37339-3;
RA Crabb J.W., Goldflam S., Harris S.E., Saari J.C.;
RT "Cloning of the cDNAs encoding the cellular retinaldehyde-binding protein
RT from bovine and human retina and comparison of the protein structures.";
RL J. Biol. Chem. 263:18688-18692(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-317, AND ACETYLATION AT SER-2.
RX PubMed=3198594; DOI=10.1016/s0021-9258(18)37338-1;
RA Crabb J.W., Johnson C.M., Carr S.A., Armes L.G., Saari J.C.;
RT "The complete primary structure of the cellular retinaldehyde-binding
RT protein from bovine retina.";
RL J. Biol. Chem. 263:18678-18687(1988).
RN [4]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=1715867; DOI=10.1016/s0021-9258(18)55354-0;
RA Crabb J.W., Gaur V.P., Garwin G.G., Marx S.V., Chapline C., Johnson C.M.,
RA Saari J.C.;
RT "Topological and epitope mapping of the cellular retinaldehyde-binding
RT protein from retina.";
RL J. Biol. Chem. 266:16674-16683(1991).
CC -!- FUNCTION: Soluble retinoid carrier essential the proper function of
CC both rod and cone photoreceptors. Participates in the regeneration of
CC active 11-cis-retinol and 11-cis-retinaldehyde, from the inactive 11-
CC trans products of the rhodopsin photocycle and in the de novo synthesis
CC of these retinoids from 11-trans metabolic precursors. The cycling of
CC retinoids between photoreceptor and adjacent pigment epithelium cells
CC is known as the 'visual cycle'.
CC -!- SUBUNIT: Interacts with DEGS1; the interaction increases synthesis of
CC chromophore-precursors by DEGS1. {ECO:0000250|UniProtKB:E1C1U1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Retina and pineal gland.
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DR EMBL; J04214; AAA30751.1; -; mRNA.
DR EMBL; BC118140; AAI18141.1; -; mRNA.
DR PIR; A31955; A31955.
DR RefSeq; NP_776876.2; NM_174451.3.
DR AlphaFoldDB; P10123; -.
DR SMR; P10123; -.
DR STRING; 9913.ENSBTAP00000045055; -.
DR BindingDB; P10123; -.
DR iPTMnet; P10123; -.
DR PaxDb; P10123; -.
DR PRIDE; P10123; -.
DR Ensembl; ENSBTAT00000047900; ENSBTAP00000045055; ENSBTAG00000033721.
DR GeneID; 282038; -.
DR KEGG; bta:282038; -.
DR CTD; 6017; -.
DR VEuPathDB; HostDB:ENSBTAG00000033721; -.
DR VGNC; VGNC:33989; RLBP1.
DR eggNOG; KOG1471; Eukaryota.
DR GeneTree; ENSGT00940000160026; -.
DR HOGENOM; CLU_046597_4_0_1; -.
DR InParanoid; P10123; -.
DR OMA; GPVFGKC; -.
DR OrthoDB; 1133487at2759; -.
DR Reactome; R-BTA-2187335; The retinoid cycle in cones (daylight vision).
DR Reactome; R-BTA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000033721; Expressed in retina and 39 other tissues.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005502; F:11-cis retinal binding; IEA:Ensembl.
DR GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; IBA:GO_Central.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR InterPro; IPR032941; RLBP1.
DR PANTHER; PTHR10174:SF200; PTHR10174:SF200; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Retinol-binding; Sensory transduction; Transport; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3198594"
FT CHAIN 2..317
FT /note="Retinaldehyde-binding protein 1"
FT /id="PRO_0000079329"
FT DOMAIN 136..297
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT BINDING 180
FT /ligand="11-cis-retinal"
FT /ligand_id="ChEBI:CHEBI:16066"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="11-cis-retinal"
FT /ligand_id="ChEBI:CHEBI:16066"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:3198594"
FT CONFLICT 162
FT /note="N -> I (in Ref. 1; AAA30751)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="D -> E (in Ref. 1; AAA30751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 36505 MW; 7CAD389A9FF8CF15 CRC64;
MSEGAGTFRM VPEEEQELRA QLERLTTKDH GPVFGPCSQL PRHTLQKAKD ELNEKEETRE
EAVRELQELV QAEAASGQEL AVAVAERVQG KDSAFFLRFI RARKFHVGRA YELLRGYVNF
RLQYPELFDS LSPEAVRCTV EAGYPGVLST RDKYGRVVML FNIENWDSEE ITFDEILQAY
CVILEKLLEN EETQINGFCI IENFKGFTMQ QAAGLRPSDL RKMVDMLQDS FPARFKAIHF
IYQPWYFTTT YNVVKPFLKS KLLQRVFVHG EDLSSFYQEF DEDILPSDFG GTLPKYDGKA
VAEQLFGPRD QTENTAF
