RLBP1_CHICK
ID RLBP1_CHICK Reviewed; 316 AA.
AC E1C1U1;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Retinaldehyde-binding protein 1 {ECO:0000305};
DE AltName: Full=Cellular retinaldehyde-binding protein;
GN Name=RLBP1; Synonyms=CRALBP;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP INTERACTION WITH DEGS1.
RX PubMed=23143414; DOI=10.1038/nchembio.1114;
RA Kaylor J.J., Yuan Q., Cook J., Sarfare S., Makshanoff J., Miu A., Kim A.,
RA Kim P., Habib S., Roybal C.N., Xu T., Nusinowitz S., Travis G.H.;
RT "Identification of DES1 as a vitamin A isomerase in Mueller glial cells of
RT the retina.";
RL Nat. Chem. Biol. 9:30-36(2013).
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'. {ECO:0000250|UniProtKB:P12271}.
CC -!- SUBUNIT: Interacts with DEGS1; the interaction increases synthesis of
CC chromophore-precursors by DEGS1. {ECO:0000269|PubMed:23143414}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P12271}.
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DR EMBL; AADN05000047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001019865.1; NM_001024694.1.
DR AlphaFoldDB; E1C1U1; -.
DR SMR; E1C1U1; -.
DR DIP; DIP-61752N; -.
DR IntAct; E1C1U1; 1.
DR PaxDb; E1C1U1; -.
DR Ensembl; ENSGALT00000010796; ENSGALP00000010782; ENSGALG00000006676.
DR GeneID; 415492; -.
DR KEGG; gga:415492; -.
DR CTD; 6017; -.
DR VEuPathDB; HostDB:geneid_415492; -.
DR eggNOG; KOG1471; Eukaryota.
DR GeneTree; ENSGT00940000160026; -.
DR HOGENOM; CLU_046597_4_0_1; -.
DR InParanoid; E1C1U1; -.
DR OMA; GPVFGKC; -.
DR OrthoDB; 1133487at2759; -.
DR PhylomeDB; E1C1U1; -.
DR Reactome; R-GGA-2187335; The retinoid cycle in cones (daylight vision).
DR Reactome; R-GGA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR PRO; PR:E1C1U1; -.
DR Proteomes; UP000000539; Chromosome 10.
DR Bgee; ENSGALG00000006676; Expressed in brain and 4 other tissues.
DR ExpressionAtlas; E1C1U1; baseline.
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: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 Pfam; PF03765; CRAL_TRIO_N; 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; Coiled coil; Cytoplasm; Reference proteome; Retinol-binding;
KW Sensory transduction; Transport; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P10123"
FT CHAIN 2..316
FT /note="Retinaldehyde-binding protein 1"
FT /id="PRO_0000450322"
FT DOMAIN 135..296
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT COILED 45..72
FT /evidence="ECO:0000255"
FT BINDING 179
FT /ligand="11-cis-retinal"
FT /ligand_id="ChEBI:CHEBI:16066"
FT /evidence="ECO:0000250|UniProtKB:P12271"
FT BINDING 201
FT /ligand="11-cis-retinal"
FT /ligand_id="ChEBI:CHEBI:16066"
FT /evidence="ECO:0000250|UniProtKB:P12271"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P10123"
SQ SEQUENCE 316 AA; 36476 MW; 8BFD0B8175A1B5CE CRC64;
MSAVTGTFRI VSEEEQALRT KLERLTTKDH GPVFGRCQQI PPHTLQKAKD ELNETEEQRE
AAVKALRELV QERAGSEDVC KAVAEKMQGK DDSFFLRFIR ARKFDVHRAY DLLKGYVNFR
QQYPELFDNL TPEAVRSTIE AGYPGILASR DKYGRVVMLF NIENWDYEEI TFDEILRAYC
VILEKLLENE ETQINGFCII ENFKGFTMQQ ASGIKPSELK KMVDMLQDSF PARFKAVHFI
HQPWYFTTTY NVVKPFLKSK LLERVFVHGE ELESFYQEID ADILPADFGG NLPKYDGKAT
AEQLFGPRIE AEDTAL