PRPH2_RAT
ID PRPH2_RAT Reviewed; 346 AA.
AC P17438;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Peripherin-2;
DE AltName: Full=Retinal degeneration slow protein;
GN Name=Prph2; Synonyms=Rds;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=2349107; DOI=10.1093/nar/18.10.3058;
RA Begy C.R., Bridges C.D.;
RT "Nucleotide and predicted protein sequence of rat retinal degeneration slow
RT (rds).";
RL Nucleic Acids Res. 18:3058-3058(1990).
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; X52376; CAA36603.1; -; mRNA.
DR PIR; S10177; S10177.
DR RefSeq; NP_037153.1; NM_013021.1.
DR AlphaFoldDB; P17438; -.
DR STRING; 10116.ENSRNOP00000058218; -.
DR GlyGen; P17438; 1 site.
DR PaxDb; P17438; -.
DR Ensembl; ENSRNOT00000108165; ENSRNOP00000095739; ENSRNOG00000068377.
DR GeneID; 25534; -.
DR KEGG; rno:25534; -.
DR UCSC; RGD:3549; rat.
DR CTD; 5961; -.
DR RGD; 3549; Prph2.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000157303; -.
DR InParanoid; P17438; -.
DR OrthoDB; 1470436at2759; -.
DR PhylomeDB; P17438; -.
DR PRO; PR:P17438; -.
DR Proteomes; UP000002494; Chromosome 9.
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; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; ISO:RGD.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; ISO:RGD.
DR GO; GO:0051291; P:protein heterooligomerization; ISO:RGD.
DR GO; GO:0051260; P:protein homooligomerization; ISO:RGD.
DR GO; GO:0009645; P:response to low light intensity stimulus; IEP:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
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_0000168107"
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 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"
SQ SEQUENCE 346 AA; 39267 MW; F7EBD542AA1E8737 CRC64;
MALLKVKFDQ KKRVKLAQGL WLMNWLSVLA GIVLFSLGLF LKIELRKRSD VMDNSESHFV
PNSLIGVGVL SCVFNSLAGK ICYDALDPAK YAKWKPWLKL YLAVCVFFNV ILFLVALCCF
LLRGSLESTL AYGLKNGMKY YRDTDTPGRC FMKKTIDMLQ IEFKCCGNNG FRDWFEIQWI
SNRYLDFSSK EVKDRIKSNV DGRYLVDGVP FSCCNPSSPR PCIQYQLTNN SAHYSYDHQT
EELNLWLRGC RAALLNYYSS LMNSMGVVTL LIWLFEVSIT AGLRFLHTAL ESVSNPEDPE
CESEGWLLEN SVSETWKAFL ESFKKLGKSN QVEAEAADAG QAPEAG
