PRPH2_CANLF
ID PRPH2_CANLF Reviewed; 346 AA.
AC P52204; Q95NE3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Peripherin-2;
DE AltName: Full=Retinal degeneration slow protein;
GN Name=PRPH2; Synonyms=RDS;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=8654508; DOI=10.1016/s0014-4835(05)80059-4;
RA Moghrabi W.N., Kedzierski W., Travis G.H.;
RT "Canine homolog and exclusion of retinal degeneration slow (rds) as the
RT gene for early retinal degeneration (erd) in the dog.";
RL Exp. Eye Res. 61:641-643(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=8603863;
RA Ray K., Acland G.M., Aguirre G.D.;
RT "Nonallelism of erd and prcd and exclusion of the canine RDS/peripherin
RT gene as a candidate for both retinal degeneration loci.";
RL Invest. Ophthalmol. Vis. Sci. 37:783-794(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RA Petersen-Jones S.M., Sargan D.R.;
RT "Canine peripherin/RDS complete cDNA sequence, polymorphisms and exclusion
RT as a candidate gene for progressive retinal atrophy in nn breeds.";
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-339.
RX PubMed=10895316; DOI=10.1046/j.1365-2052.2000.00633.x;
RA Runte M., Dekomien G., Epplen J.T.;
RT "Evaluation of RDS/Peripherin and ROM1 as candidate genes in generalised
RT progressive retinal atrophy and exclusion of digenic inheritance.";
RL Anim. Genet. 31:223-227(2000).
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 (By similarity). Required for the
CC maintenance of retinal outer nuclear layer thickness (By similarity).
CC Required for the correct development and organization of the
CC photoreceptor inner segment (By similarity).
CC {ECO:0000250|UniProtKB:P15499}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Forms a
CC homotetramer (By similarity). Forms a heterotetramer with ROM1 (By
CC similarity). Homotetramer and heterotetramer core complexes go on to
CC form higher order complexes by formation of intermolecular disulfide
CC bonds (By similarity). Interacts with MREG (By similarity). Interacts
CC with STX3 (By similarity). Interacts with SNAP25 (By similarity).
CC {ECO:0000250|UniProtKB:P15499, ECO:0000250|UniProtKB:P17810}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P17810}; Multi-
CC pass membrane protein {ECO:0000255}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000250|UniProtKB:P15499}.
CC Photoreceptor inner segment {ECO:0000250|UniProtKB:P15499}.
CC -!- TISSUE SPECIFICITY: Retina (photoreceptor). In rim region of ROS (rod
CC outer segment) disks.
CC -!- SIMILARITY: Belongs to the PRPH2/ROM1 family. {ECO:0000305}.
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DR EMBL; U36577; AAB08751.1; -; mRNA.
DR EMBL; U27349; AAB01510.1; -; mRNA.
DR EMBL; X94122; CAA63842.1; -; mRNA.
DR EMBL; AJ249964; CAB57832.1; -; Genomic_DNA.
DR EMBL; AJ249965; CAB57832.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001003289.1; NM_001003289.1.
DR AlphaFoldDB; P52204; -.
DR STRING; 9612.ENSCAFP00000002506; -.
DR PaxDb; P52204; -.
DR Ensembl; ENSCAFT00030027156; ENSCAFP00030023702; ENSCAFG00030014715.
DR Ensembl; ENSCAFT00040012417; ENSCAFP00040010764; ENSCAFG00040006679.
DR Ensembl; ENSCAFT00845011657; ENSCAFP00845009098; ENSCAFG00845006562.
DR GeneID; 403972; -.
DR KEGG; cfa:403972; -.
DR CTD; 5961; -.
DR VEuPathDB; HostDB:ENSCAFG00845006562; -.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000157303; -.
DR HOGENOM; CLU_068903_0_0_1; -.
DR InParanoid; P52204; -.
DR OMA; TDIMAKM; -.
DR OrthoDB; 1470436at2759; -.
DR TreeFam; TF331684; -.
DR Proteomes; UP000002254; Chromosome 12.
DR Bgee; ENSCAFG00000001722; Expressed in bone marrow and 8 other tissues.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IEA:Ensembl.
DR GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
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 2: Evidence at transcript 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_0000168103"
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:0000250"
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:0000250|UniProtKB:P15499"
FT VARIANT 339
FT /note="A -> T"
FT /evidence="ECO:0000269|PubMed:10895316"
FT CONFLICT 319
FT /note="F -> L (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 39195 MW; 8C5E416F2D2087BB CRC64;
MALLKVKFDQ KKRVKLAQGL WLMNWLSVLA GIVIFSLGLF LKIELRKRSD VMNNSESHFV
PNSLIVMGVL SCVFNSLAGK ICYDALDPAK YAKWKPWLKP YLAVCVLFNI ALFLVTLCCF
LMRGSLESTL AHGLKNGMKY YRDTDTPGRC FMKKTIDMLQ IEFRCCGNNG FRDWFEIQWI
SNRYLDFSSK EVKDRIKSNV DGRYLVDGVP FSCCNPSSPR PCIQYQLTNN SAHYSYDHQT
EELNLWVNGC RAALLSYYSS LMNSMGAVTL LVWLFEVTIT IGLRYLHTAL EGVSNPEDPE
CESEGWLLEK SVSETWKAFL ESLKKLGKSN QVEAEGADAG QAPEAG
