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   27-MAR-2024, entry version 147.
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; 10090-ENSMUSP00000027032; -.
DR   PeptideAtlas; P56716; -.
DR   ProteomicsDB; 301595; -.
DR   Antibodypedia; 50968; 73 antibodies from 11 providers.
DR   DNASU; 19888; -.
DR   Ensembl; ENSMUST00000027032.6; ENSMUSP00000027032.5; ENSMUSG00000025900.14.
DR   GeneID; 19888; -.
DR   KEGG; mmu:19888; -.
DR   UCSC; uc007aex.2; mouse.
DR   AGR; MGI:1341105; -.
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; 2879961at2759; -.
DR   PhylomeDB; P56716; -.
DR   TreeFam; TF318770; -.
DR   BioGRID-ORCS; 19888; 1 hit in 79 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 cell types or tissues.
DR   ExpressionAtlas; P56716; baseline and differential.
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   CDD; cd17147; DCX2_RP1; 1.
DR   Gene3D; 3.10.20.230; Doublecortin domain; 2.
DR   InterPro; IPR003533; Doublecortin_dom.
DR   InterPro; IPR036572; Doublecortin_dom_sf.
DR   InterPro; IPR040163; RP1/RP1L1.
DR   PANTHER; PTHR23005:SF4; OXYGEN-REGULATED PROTEIN 1; 1.
DR   PANTHER; PTHR23005; RETINITIS PIGMENTOSA 1 PROTEIN; 1.
DR   Pfam; PF03607; DCX; 2.
DR   SMART; SM00537; DCX; 2.
DR   SUPFAM; SSF89837; Doublecortin (DC); 2.
DR   PROSITE; PS50309; DC; 2.
DR   Genevisible; P56716; MM.
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
//