PRPH2_BOVIN
ID PRPH2_BOVIN Reviewed; 346 AA.
AC P17810;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Peripherin-2;
DE AltName: Full=Retinal degeneration slow protein;
GN Name=PRPH2; Synonyms=RDS;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-346, PROTEIN SEQUENCE OF 2-33, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Retina;
RX PubMed=2372552; DOI=10.1021/bi00471a025;
RA Connell G.J., Molday R.S.;
RT "Molecular cloning, primary structure, and orientation of the vertebrate
RT photoreceptor cell protein peripherin in the rod outer segment disk
RT membrane.";
RL Biochemistry 29:4691-4698(1990).
RN [2]
RP SUBUNIT, INTERACTION WITH ROM1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10681511; DOI=10.1074/jbc.275.8.5370;
RA Loewen C.J., Molday R.S.;
RT "Disulfide-mediated oligomerization of Peripherin/Rds and Rom-1 in
RT photoreceptor disk membranes. Implications for photoreceptor outer segment
RT morphogenesis and degeneration.";
RL J. Biol. Chem. 275:5370-5378(2000).
RN [3]
RP INTERACTION WITH MREG, AND MUTAGENESIS OF 315-THR--PHE-319.
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 [4]
RP FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND GLYCOSYLATION AT ASN-229.
RX PubMed=24196967; DOI=10.1074/jbc.m113.520700;
RA Kevany B.M., Tsybovsky Y., Campuzano I.D., Schnier P.D., Engel A.,
RA Palczewski K.;
RT "Structural and functional analysis of the native peripherin-ROM1 complex
RT isolated from photoreceptor cells.";
RL J. Biol. Chem. 288:36272-36284(2013).
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:24196967). 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, ECO:0000269|PubMed:24196967}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:24196967). Forms a
CC homotetramer (PubMed:10681511). Forms a heterotetramer with ROM1
CC (PubMed:10681511, PubMed:24196967). Homotetramer and heterotetramer
CC core complexes go on to form higher order complexes by formation of
CC intermolecular disulfide bonds (PubMed:10681511). Interacts with MREG
CC (PubMed:17260955). Interacts with STX3 (By similarity). Interacts with
CC SNAP25 (By similarity). {ECO:0000250|UniProtKB:P15499,
CC ECO:0000269|PubMed:10681511, ECO:0000269|PubMed:17260955,
CC ECO:0000269|PubMed:24196967}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:2372552}; Multi-pass
CC membrane protein {ECO:0000255}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000269|PubMed:10681511}. Photoreceptor inner
CC segment {ECO:0000250|UniProtKB:P15499}.
CC -!- TISSUE SPECIFICITY: Retina (photoreceptor) (PubMed:2372552,
CC PubMed:10681511, PubMed:24196967). In rim region of ROS (rod outer
CC segment) disks (PubMed:2372552, PubMed:10681511).
CC {ECO:0000269|PubMed:10681511, ECO:0000269|PubMed:2372552,
CC ECO:0000269|PubMed:24196967}.
CC -!- SIMILARITY: Belongs to the PRPH2/ROM1 family. {ECO:0000305}.
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DR EMBL; J02884; AAA30693.1; -; mRNA.
DR PIR; A34608; A34608.
DR RefSeq; NP_001159959.1; NM_001166487.1.
DR AlphaFoldDB; P17810; -.
DR STRING; 9913.ENSBTAP00000007836; -.
DR iPTMnet; P17810; -.
DR PaxDb; P17810; -.
DR PRIDE; P17810; -.
DR Ensembl; ENSBTAT00000007836; ENSBTAP00000007836; ENSBTAG00000005971.
DR GeneID; 280907; -.
DR KEGG; bta:280907; -.
DR CTD; 5961; -.
DR VEuPathDB; HostDB:ENSBTAG00000005971; -.
DR VGNC; VGNC:33385; PRPH2.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000157303; -.
DR HOGENOM; CLU_068903_0_0_1; -.
DR InParanoid; P17810; -.
DR OMA; TDIMAKM; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000005971; Expressed in retina and 24 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
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; IMP:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
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:0051258; P:protein polymerization; IMP:UniProtKB.
DR GO; GO:1903525; P:regulation of membrane tubulation; IMP:UniProtKB.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR CDD; cd03162; peripherin_like_LEL; 1.
DR DisProt; DP00220; -.
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; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Membrane; Reference proteome; Sensory transduction;
KW Transmembrane; Transmembrane helix; Vision.
FT CHAIN 1..346
FT /note="Peripherin-2"
FT /id="PRO_0000168102"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..62
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..264
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..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:0000269|PubMed:24196967"
FT CARBOHYD 263
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 MUTAGEN 315..319
FT /note="TWKAF->AWGAT: Loss of interaction with MREG."
FT /evidence="ECO:0000269|PubMed:17260955"
SQ SEQUENCE 346 AA; 39123 MW; D58BD91222540102 CRC64;
MALLKVKFDQ KKRVKLAQGL WLMNWFSVLA GIIIFGLGLF LKIELRKRSD VMNNSESHFV
PNSLIGVGVL SCVFNSLAGK ICYDALDPAK YAKWKPWLKP YLAVCVLFNV VLFLVALCCF
LLRGSLESTL AHGLKNGMKF YRDTDTPGRC FMKKTIDMLQ IEFKCCGNNG FRDWFEIQWI
SNRYLDFSSK EVKDRIKSNV DGRYLVDGVP FSCCNPNSPR PCIQYQLTNN SAHYSYDHQT
EELNLWLRGC RAALLSYYSN LMNTTGAVTL LVWLFEVTIT VGLRYLHTAL EGMANPEDPE
CESEGWLLEK SVPETWKAFL ESVKKLGKGN QVEAEGEDAG QAPAAG
