RP1_MOUSE
ID RP1_MOUSE Reviewed; 2095 AA.
AC P56716; Q548Q8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Oxygen-regulated protein 1;
DE AltName: Full=Retinitis pigmentosa RP1 protein homolog;
GN Name=Rp1; Synonyms=Orp1, Rp1h;
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 [MRNA], AND SEQUENCE REVISION TO 67-76.
RC TISSUE=Retina;
RX PubMed=10391211; DOI=10.1038/10305;
RA Pierce E.A., Quinn T., Meehan T., McGee T.L., Berson E.L., Dryja T.P.;
RT "Mutations in a gene encoding a new oxygen-regulated photoreceptor protein
RT cause dominant retinitis pigmentosa.";
RL Nat. Genet. 22:248-254(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11960024; DOI=10.1073/pnas.042122399;
RA Gao J., Cheon K., Nusinowitz S., Liu Q., Bei D., Atkins K., Azimi A.,
RA Daiger S.P., Farber D.B., Heckenlively J.R., Pierce E.A., Sullivan L.S.,
RA Zuo J.;
RT "Progressive photoreceptor degeneration, outer segment dysplasia, and
RT rhodopsin mislocalization in mice with targeted disruption of the retinitis
RT pigmentosa-1 (Rp1) gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5698-5703(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP PROTEIN SEQUENCE OF 357-367, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11773008;
RA Liu Q., Zhou J., Daiger S.P., Farber D.B., Heckenlively J.R., Smith J.E.,
RA Sullivan L.S., Zuo J., Milam A.H., Pierce E.A.;
RT "Identification and subcellular localization of the RP1 protein in human
RT and mouse photoreceptors.";
RL Invest. Ophthalmol. Vis. Sci. 43:22-32(2002).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14507858; DOI=10.1167/iovs.03-0410;
RA Liu Q., Lyubarsky A., Skalet J.H., Pugh E.N. Jr., Pierce E.A.;
RT "RP1 is required for the correct stacking of outer segment discs.";
RL Invest. Ophthalmol. Vis. Sci. 44:4171-4183(2003).
RN [7]
RP FUNCTION, INTERACTION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
RX PubMed=15269252; DOI=10.1523/jneurosci.1335-04.2004;
RA Liu Q., Zuo J., Pierce E.A.;
RT "The retinitis pigmentosa 1 protein is a photoreceptor microtubule-
RT associated protein.";
RL J. Neurosci. 24:6427-6436(2004).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=16126734; DOI=10.1093/hmg/ddi325;
RA Liu J., Huang Q., Higdon J., Liu W., Xie T., Yamashita T., Cheon K.,
RA Cheng C., Zuo J.;
RT "Distinct gene expression profiles and reduced JNK signaling in retinitis
RT pigmentosa caused by RP1 mutations.";
RL Hum. Mol. Genet. 14:2945-2958(2005).
RN [9]
RP INTERACTION WITH RP1L1, AND DISRUPTION PHENOTYPE.
RX PubMed=19657028; DOI=10.1523/jneurosci.5854-08.2009;
RA Yamashita T., Liu J., Gao J., LeNoue S., Wang C., Kaminoh J., Bowne S.J.,
RA Sullivan L.S., Daiger S.P., Zhang K., Fitzgerald M.E., Kefalov V.J.,
RA Zuo J.;
RT "Essential and synergistic roles of RP1 and RP1L1 in rod photoreceptor
RT axoneme and retinitis pigmentosa.";
RL J. Neurosci. 29:9748-9760(2009).
RN [10]
RP INTERACTION WITH MAK.
RX PubMed=21148103; DOI=10.1073/pnas.1009437108;
RA Omori Y., Chaya T., Katoh K., Kajimura N., Sato S., Muraoka K., Ueno S.,
RA Koyasu T., Kondo M., Furukawa T.;
RT "Negative regulation of ciliary length by ciliary male germ cell-associated
RT kinase (Mak) is required for retinal photoreceptor survival.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:22671-22676(2010).
CC -!- FUNCTION: Microtubule-associated protein regulating the stability and
CC length of the microtubule-based axoneme of photoreceptors. Required for
CC the differentiation of photoreceptor cells, it plays a role in the
CC organization of the outer segment of rod and cone photoreceptors
CC ensuring the correct orientation and higher-order stacking of outer
CC segment disks along the photoreceptor axoneme.
CC {ECO:0000269|PubMed:14507858, ECO:0000269|PubMed:15269252}.
CC -!- SUBUNIT: Interacts (via the doublecortin domains) with microtubules.
CC Interacts with RP1L1. Interacts with MAK. {ECO:0000269|PubMed:15269252,
CC ECO:0000269|PubMed:19657028, ECO:0000269|PubMed:21148103}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme. Cell
CC projection, cilium, photoreceptor outer segment. Note=Specifically
CC localized in the connecting cilia of rod and cone photoreceptors.
CC -!- TISSUE SPECIFICITY: Expressed in the cell bodies and inner segments of
CC photoreceptors. Not found in liver, spleen, kidney, brain, thymus,
CC muscle, heart, lung and testis.
CC -!- INDUCTION: Gene expression is stimulated by retinal hypoxia and
CC suppressed by relative retinal hyperoxia.
CC -!- DOMAIN: The doublecortin domains, which mediate interaction with
CC microtubules, are required for regulation of microtubule polymerization
CC and function in photoreceptor differentiation. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: As early as postnatal day 7, mice have already
CC undergone significant molecular retinal changes. The molecular
CC responses change dramatically during development and were distinct from
CC responses to the disruption of the photoreceptor transcription factors
CC Crx, Pde6b and Nrl. The JNK signaling cascades are specifically
CC compromised in Rp1 defective retinas. Double heterozygotes of Rp1 and
CC Rp1l1 exhibit abnormal outer segment morphology and reduced single rod
CC photosensitivity and dark currents. {ECO:0000269|PubMed:16126734,
CC ECO:0000269|PubMed:19657028}.
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DR EMBL; AF155141; AAD42089.2; -; mRNA.
DR EMBL; AF291754; AAM17919.1; -; Genomic_DNA.
DR EMBL; BC120927; AAI20928.1; -; mRNA.
DR EMBL; BC120928; AAI20929.1; -; mRNA.
DR CCDS; CCDS14804.1; -.
DR RefSeq; NP_035413.1; NM_011283.2.
DR AlphaFoldDB; P56716; -.
DR SMR; P56716; -.
DR BioGRID; 202959; 6.
DR DIP; DIP-59493N; -.
DR IntAct; P56716; 2.
DR STRING; 10090.ENSMUSP00000027032; -.
DR iPTMnet; P56716; -.
DR PhosphoSitePlus; P56716; -.
DR MaxQB; P56716; -.
DR PaxDb; P56716; -.
DR PeptideAtlas; P56716; -.
DR PRIDE; P56716; -.
DR ProteomicsDB; 301595; -.
DR Antibodypedia; 50968; 58 antibodies from 10 providers.
DR DNASU; 19888; -.
DR Ensembl; ENSMUST00000027032; ENSMUSP00000027032; ENSMUSG00000025900.
DR GeneID; 19888; -.
DR KEGG; mmu:19888; -.
DR UCSC; uc007aex.2; mouse.
DR CTD; 6101; -.
DR MGI; MGI:1341105; Rp1.
DR VEuPathDB; HostDB:ENSMUSG00000025900; -.
DR eggNOG; KOG1181; Eukaryota.
DR eggNOG; KOG3757; Eukaryota.
DR GeneTree; ENSGT00940000154242; -.
DR HOGENOM; CLU_232270_0_0_1; -.
DR InParanoid; P56716; -.
DR OrthoDB; 894392at2759; -.
DR PhylomeDB; P56716; -.
DR TreeFam; TF318770; -.
DR BioGRID-ORCS; 19888; 1 hit in 74 CRISPR screens.
DR PRO; PR:P56716; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P56716; protein.
DR Bgee; ENSMUSG00000025900; Expressed in retinal neural layer and 21 other tissues.
DR ExpressionAtlas; P56716; baseline and differential.
DR Genevisible; P56716; MM.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0097542; C:ciliary tip; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005875; C:microtubule associated complex; IDA:UniProtKB.
DR GO; GO:0097733; C:photoreceptor cell cilium; IDA:MGI.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0035082; P:axoneme assembly; IDA:UniProtKB.
DR GO; GO:0071482; P:cellular response to light stimulus; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0046785; P:microtubule polymerization; TAS:BHF-UCL.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; TAS:BHF-UCL.
DR GO; GO:0042461; P:photoreceptor cell development; IMP:UniProtKB.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:UniProtKB.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IDA:UniProtKB.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IDA:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:0046549; P:retinal cone cell development; IDA:UniProtKB.
DR GO; GO:0046548; P:retinal rod cell development; IDA:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 3.10.20.230; -; 2.
DR InterPro; IPR003533; Doublecortin_dom.
DR InterPro; IPR036572; Doublecortin_dom_sf.
DR InterPro; IPR040163; RP1/RP1L1/DCX.
DR PANTHER; PTHR23005; PTHR23005; 1.
DR Pfam; PF03607; DCX; 2.
DR SMART; SM00537; DCX; 2.
DR SUPFAM; SSF89837; SSF89837; 2.
DR PROSITE; PS50309; DC; 2.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Reference proteome; Repeat;
KW Sensory transduction; Vision.
FT CHAIN 1..2095
FT /note="Oxygen-regulated protein 1"
FT /id="PRO_0000097411"
FT DOMAIN 35..117
FT /note="Doublecortin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 157..236
FT /note="Doublecortin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT REGION 358..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1572..1595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2095 AA; 234388 MW; CA5301316633BD62 CRC64;
MSDTPSTSFS MIHLTSEGQV PSPRHSNITH PVVAKRISFY KSGDPQFGGV RVVVNPRSFK
TFDALLDSLS RKVPLPFGVR NISTPRGRHS ITRLEELEDG KSYVCSHNKK VLPVDLDKAR
RRPRPWLSSR SISTHVQLCP ATANMSTMAP GMLRAPRRLV VFRNGDPKNK HVVLLSRRIT
QSFEAFLQYL TQVMQCPVAK LYATDGRKVP SLQAVILSSG AVVAAGREPF KPGNYDIQKY
LLPAKLPGIS HRVHQKGKAK IEKRKMSTHM PSDLRPQTDS LISEKTYDCF SDFSVAPENY
LALETHESQS LSTYPSEDDV EKSIVFNQDG TMTVVMKVRF KIKEEETVKW TTTVNRAGLS
NNDEKNKKSS YPGKTDYGPS SLKLEACSLP EDIVDTTQQG SLTEEENTQM TEQQALSCSS
ASWENASMET DIQESQKQVK HFYRPPTPGP RRMRQKKSVI GTVTVVSETE VQEKQFSYSE
ERKGGEKSEY HMFTHSCSKM SSVSNKLVQI GSDNEMESAL ERTRESGSLK SQAINAGAIE
ITSQKVLKMC HNNALPSTAP ENSVVEEGTD NSAVSGTATI KHFRTCGNAN DSFSSITADS
TPTSVNNYSN DRNISELPSV GSPVLTMRLV NEFAHCGLTE KPENRKKVLS SSASKKKKKK
SQQRMITSND KKKVIETKGP PNIAGKIPRA GTTAQERLLQ ESDCPDKGGR VCEQGLNISP
MAIESNNFFP KSNPTFSKNF YKNKLNTFQN PKTQKLLAKR KSRPRKIVST ERLRKQEIGQ
EDKILLHSDS KLCESHLEKQ SLFHVFNILE EDQKVLHRPP FQVEKVARNL KGMAKKSLVP
KVNDLHIMLR NQKKQMGVKL KSGAEVSEQH VTTRADPLAS LKKPDFPEGI PHHSGKSYVK
RWLQNINSYP DFEHRKSGPL CQNRSDVVNY NRNGFLGNNL HTTSSKGNGF LMESNKSKTK
NDNWSGNTNQ ETGKSLVAKD NGEELNKHHC ESQNGSLYDS YLVSLHDNCT LSQTTINEPS
TKSHLSIEKS RPEVKLVYQE MNFATKRQSI EVAIQVDTMG ENVLKDYLPA LLLRHLEAFV
PNNQKHQNGI SQIPGSLAEV VFPSVIDNSS TNLLLAWLLV LNLKRTMNSF CQSDAHKMTN
RPSETAALLE VLKHVAITEE ADDLKAAVAN LMESTKTCSG SSGREQDMLP VNCTASSLHS
VDECNENGSA QKTLLDEGYS VMGDCTSEMV SKSCNSSCEM HMVSKTNPPK QVDDQSDGLL
TSNSCTVSQR STGACFLTDG VYSHEACAQK EGVYEGACLS DETHIPIRDC HTIHSVHSKE
NKCTDDLEST EELKTVDKVP KGLSILADSM YKNDSNVSTF QNVNKLSSQR TLLSKTYLDS
DKDYSPLEEF QNCPRKKIVN KKKSISSDKE ESRTSEEPRS ITNSMTSSER NAISELESFE
ELESQDTSIF NMNVRAEKKS TKETMQKQSE ARMSSELINV SGRKIIEQER RNTAILETTA
RGQVTPPSLA FCYDSNKNTE KEISEGETKM RVKKMVDSME NESYSESSLN FKKHHRSPGT
LDWSDYGSDS ESGYPCKASS NSHNDDSGQE KEPTRGIVKR AIEKLYGKAE IIKPPFFHGS
IHKSQVCPYN SVEVQCAKKT NFYESECQSL VSSEQVSRSS LIFQEFPQVD ANGMGDSFGD
SSIENVTKSS AHDRVFTEKE NGKLIDNGKW LLRENHLWRV SSDNPGMYGN ADTTSVDTLI
DKNSIEVPYS HFGELAPGPT MAELSSSEIE EMTQPLEVKC NYFNFPHGSD SEPFGEDFPD
AQNKTCPKEK IPNHHTEEKG NYPSERLCTS VTQAFVSAGN KVHPVCSDAI KTQPLPGSNI
THGALQEGDS LDKLYALCGQ HCPILTVIIQ PVNEESRGFA YRKDSDIENS LDFQLWMKIY
PFMPQSKKHV FRSDGRNVSV GEEFAGNVIG DLCDQLYFKS MIDLVDQRAN SLGKEINLKK
FQLYLKKSFS DPLSTSLLVV ENRNSVSLSP SSWTDNFKSI DENNNFLNRL PNSSKNPNQV
VRENTNFQFH LELFGQVYLL DICQVEKPLN IKTRSKLEMY YILEGEVLFI WEEEK
