PRPH2_MOUSE
ID PRPH2_MOUSE Reviewed; 346 AA.
AC P15499;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Peripherin-2;
DE AltName: Full=Retinal degeneration slow protein;
GN Name=Prph2; Synonyms=Rds;
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].
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=2918924; DOI=10.1038/338070a0;
RA Travis G.H., Brennan M.B., Danielson P.E., Kozak C.A., Sutcliffe J.G.;
RT "Identification of a photoreceptor-specific mRNA encoded by the gene
RT responsible for retinal degeneration slow (rds).";
RL Nature 338:70-73(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=1992463; DOI=10.1073/pnas.88.3.723;
RA Connell G., Bascom R., Molday L., Reid D., McInnes R.R., Molday R.S.;
RT "Photoreceptor peripherin is the normal product of the gene responsible for
RT retinal degeneration in the rds mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:723-726(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-229.
RX PubMed=8530028; DOI=10.1006/geno.1995.1133;
RA Ma J., Norton J.C., Allen A.C., Burns J.B., Hasel K.W., Burns J.L.,
RA Sutcliffe J.G., Travis G.H.;
RT "Retinal degeneration slow (rds) in mouse results from simple insertion of
RT a t haplotype-specific element into protein-coding exon II.";
RL Genomics 28:212-219(1995).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=6715580; DOI=10.1002/cne.902240107;
RA Jansen H.G., Sanyal S.;
RT "Development and degeneration of retina in rds mutant mice: electron
RT microscopy.";
RL J. Comp. Neurol. 224:71-84(1984).
RN [6]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10802659; DOI=10.1038/75621;
RA Clarke G., Goldberg A.F., Vidgen D., Collins L., Ploder L., Schwarz L.,
RA Molday L.L., Rossant J., Szel A., Molday R.S., Birch D.G., McInnes R.R.;
RT "Rom-1 is required for rod photoreceptor viability and the regulation of
RT disk morphogenesis.";
RL Nat. Genet. 25:67-73(2000).
RN [7]
RP INTERACTION WITH MREG, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17260955; DOI=10.1021/bi061466i;
RA Boesze-Battaglia K., Song H., Sokolov M., Lillo C., Pankoski-Walker L.,
RA Gretzula C., Gallagher B., Rachel R.A., Jenkins N.A., Copeland N.G.,
RA Morris F., Jacob J., Yeagle P., Williams D.S., Damek-Poprawa M.;
RT "The tetraspanin protein peripherin-2 forms a complex with melanoregulin, a
RT putative membrane fusion regulator.";
RL Biochemistry 46:1256-1272(2007).
RN [8]
RP INTERACTION WITH ROM1; STX3 AND SNAP25, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=26406599; DOI=10.1371/journal.pone.0138508;
RA Zulliger R., Conley S.M., Mwoyosvi M.L., Stuck M.W., Azadi S., Naash M.I.;
RT "SNAREs Interact with Retinal Degeneration Slow and Rod Outer Segment
RT Membrane Protein-1 during Conventional and Unconventional Outer Segment
RT Targeting.";
RL PLoS ONE 10:E0138508-E0138508(2015).
RN [9]
RP FUNCTION, SUBUNIT, INTERACTION WITH ROM1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, DISUPLHIDE BOND, AND MUTAGENESIS OF
RP TYR-141 AND CYS-150.
RX PubMed=29961824; DOI=10.1093/hmg/ddy240;
RA Zulliger R., Conley S.M., Mwoyosvi M.L., Al-Ubaidi M.R., Naash M.I.;
RT "Oligomerization of Prph2 and Rom1 is essential for photoreceptor outer
RT segment formation.";
RL Hum. Mol. Genet. 27:3507-3518(2018).
CC -!- FUNCTION: Essential for retina photoreceptor outer segment disk
CC morphogenesis, may also play a role with ROM1 in the maintenance of
CC outer segment disk structure (PubMed:6715580). Required for the
CC maintenance of retinal outer nuclear layer thickness (PubMed:6715580,
CC PubMed:29961824). Required for the correct development and organization
CC of the photoreceptor inner segment (PubMed:6715580).
CC {ECO:0000269|PubMed:29961824, ECO:0000269|PubMed:6715580}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:29961824). Forms a
CC homotetramer (PubMed:10802659). Forms a heterotetramer with ROM1
CC (PubMed:26406599, PubMed:29961824). Homotetramer and heterotetramer
CC core complexes go on to form higher order complexes by formation of
CC intermolecular disulfide bonds (By similarity). Interacts with MREG
CC (PubMed:17260955). Interacts with STX3 isoform 3B (PubMed:26406599).
CC Interacts with SNAP25 (PubMed:26406599). {ECO:0000250|UniProtKB:P17810,
CC ECO:0000269|PubMed:10802659, ECO:0000269|PubMed:17260955,
CC ECO:0000269|PubMed:26406599, ECO:0000269|PubMed:29961824}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P17810}; Multi-
CC pass membrane protein {ECO:0000255}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000269|PubMed:10802659,
CC ECO:0000269|PubMed:17260955, ECO:0000269|PubMed:26406599,
CC ECO:0000269|PubMed:29961824}. Photoreceptor inner segment
CC {ECO:0000269|PubMed:17260955, ECO:0000269|PubMed:26406599}.
CC -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level).
CC {ECO:0000269|PubMed:10802659, ECO:0000269|PubMed:17260955,
CC ECO:0000269|PubMed:26406599, ECO:0000269|PubMed:29961824}.
CC -!- DISEASE: Note=Responsible for retinal degeneration slow (Rds)
CC (PubMed:8530028). {ECO:0000269|PubMed:8530028}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice fail to form retinal disk
CC structures, resulting in an absence of the photoreceptor outer segment
CC (PubMed:6715580). At postnatal day 14 the photoreceptor inner segment
CC is stunted and at postnatal day 21 shows disorganization and cell lysis
CC in addition to outer nuclear layer degeneration resulting in a gradual
CC decline in photoreceptors (PubMed:6715580). At postnatal day 21 mice
CC show progressive thinning of the outer plexiform layer and
CC disorganization of the photoreceptor synaptic termini (PubMed:6715580).
CC Adult knockout mice show a reduction in the thickness of the retinal
CC outer nuclear layer, and a decrease in Rom1 protein abundance in the
CC retina (PubMed:29961824). {ECO:0000269|PubMed:29961824,
CC ECO:0000269|PubMed:6715580}.
CC -!- SIMILARITY: Belongs to the PRPH2/ROM1 family. {ECO:0000305}.
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DR EMBL; X14770; CAA32878.1; -; mRNA.
DR EMBL; BC028958; AAH28958.1; -; mRNA.
DR EMBL; BC085266; AAH85266.1; -; mRNA.
DR EMBL; L42167; AAC37674.1; -; Genomic_DNA.
DR CCDS; CCDS28844.1; -.
DR PIR; S03347; S03347.
DR RefSeq; NP_032964.1; NM_008938.1.
DR AlphaFoldDB; P15499; -.
DR BioGRID; 202399; 1.
DR IntAct; P15499; 1.
DR STRING; 10090.ENSMUSP00000024773; -.
DR GlyGen; P15499; 2 sites.
DR PhosphoSitePlus; P15499; -.
DR PaxDb; P15499; -.
DR PRIDE; P15499; -.
DR ProteomicsDB; 291745; -.
DR Antibodypedia; 30169; 68 antibodies from 19 providers.
DR DNASU; 19133; -.
DR Ensembl; ENSMUST00000024773; ENSMUSP00000024773; ENSMUSG00000023978.
DR GeneID; 19133; -.
DR KEGG; mmu:19133; -.
DR UCSC; uc008cun.1; mouse.
DR CTD; 5961; -.
DR MGI; MGI:102791; Prph2.
DR VEuPathDB; HostDB:ENSMUSG00000023978; -.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000157303; -.
DR HOGENOM; CLU_068903_0_0_1; -.
DR InParanoid; P15499; -.
DR OMA; TDIMAKM; -.
DR OrthoDB; 1470436at2759; -.
DR PhylomeDB; P15499; -.
DR TreeFam; TF331684; -.
DR BioGRID-ORCS; 19133; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Prph2; mouse.
DR PRO; PR:P15499; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P15499; protein.
DR Bgee; ENSMUSG00000023978; Expressed in retinal neural layer and 6 other tissues.
DR ExpressionAtlas; P15499; baseline and differential.
DR Genevisible; P15499; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:MGI.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IMP:MGI.
DR GO; GO:0051291; P:protein heterooligomerization; IPI:MGI.
DR GO; GO:0051260; P:protein homooligomerization; IPI:MGI.
DR GO; GO:0009645; P:response to low light intensity stimulus; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR CDD; cd03162; peripherin_like_LEL; 1.
DR Gene3D; 1.10.1450.10; -; 1.
DR InterPro; IPR000830; Peripherin/rom-1.
DR InterPro; IPR018498; Peripherin/rom-1_CS.
DR InterPro; IPR042026; Peripherin_LEL.
DR InterPro; IPR018499; Tetraspanin/Peripherin.
DR InterPro; IPR008952; Tetraspanin_EC2_sf.
DR PANTHER; PTHR19282; PTHR19282; 1.
DR Pfam; PF00335; Tetraspanin; 1.
DR PRINTS; PR00218; PERIPHERNRDS.
DR SUPFAM; SSF48652; SSF48652; 1.
DR PROSITE; PS00930; RDS_ROM1; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell projection; Disulfide bond; Glycoprotein; Membrane;
KW Reference proteome; Sensory transduction; Transmembrane;
KW Transmembrane helix; Vision.
FT CHAIN 1..346
FT /note="Peripherin-2"
FT /id="PRO_0000168106"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..61
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..264
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 341..346
FT /note="Interaction with MREG"
FT /evidence="ECO:0000269|PubMed:17260955"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 150
FT /note="Interchain (with ROM1)"
FT /evidence="ECO:0000269|PubMed:29961824"
FT MUTAGEN 141
FT /note="Y->C: Reduced cone and rod photoreceptor function as
FT a result of outer segment malformation, including
FT disorganization, short outer segments, and elongated disks
FT which affect both rod and cone photoreceptors. Reduced
FT Prph2 protein abundance in the retina."
FT /evidence="ECO:0000269|PubMed:29961824"
FT MUTAGEN 150
FT /note="C->S: Reduced cone and rod photoreceptor function as
FT a result of outer segment malformation, including
FT disorganization, short outer segments, and elongated disks
FT which affect both rod and cone photoreceptors. Reduced
FT Prph2 and Rom1 protein abundance in the retina in addition
FT to disruption of the formation of large disulfide-linked
FT protein complexes."
FT /evidence="ECO:0000269|PubMed:29961824"
SQ SEQUENCE 346 AA; 39260 MW; F9B80C14F2867BDE CRC64;
MALLKVKFDQ KKRVKLAQGL WLMNWLSVLA GIVLFSLGLF LKIELRKRSE VMNNSESHFV
PNSLIGVGVL SCVFNSLAGK ICYDALDPAK YAKWKPWLKP YLAVCIFFNV ILFLVALCCF
LLRGSLESTL AYGLKNGMKY YRDTDTPGRC FMKKTIDMLQ IEFKCCGNNG FRDWFEIQWI
SNRYLDFSSK EVKDRIKSNV DGRYLVDGVP FSCCNPSSPR PCIQYQLTNN SAHYSYDHQT
EELNLWLRGC RAALLNYYSS LMNSMGVVTL LVWLFEVSIT AGLRYLHTAL ESVSNPEDPE
CESEGWLLEK SVPETWKAFL ESFKKLGKSN QVEAEGADAG PAPEAG
