ID   PRPH2_XENLA             Reviewed;         346 AA.
AC   O42583;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Peripherin-2;
DE   AltName: Full=Retinal degeneration slow protein;
DE            Short=xRDS38;
GN   Name=prph2; Synonyms=rds, rds38;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8923216; DOI=10.1242/jcs.109.10.2551;
RA   Kedzierski W., Moghrabi W.N., Allen A.C., Jablonski-Stiemke M.M.,
RA   Azarian S.M., Bok D., Travis G.H.;
RT   "Three homologs of rds/peripherin in Xenopus laevis photoreceptors that
RT   exhibit covalent and non-covalent interactions.";
RL   J. Cell Sci. 109:2551-2560(1996).
CC   -!- FUNCTION: May be involved in the morphogenesis of retina outer segment
CC       disks and the development and maintenance of the retina ultrastructure.
CC       {ECO:0000250|UniProtKB:P15499}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P17810}; Multi-
CC       pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Found in both rod and cone photoreceptors.
CC       Specifically in the rims and incisures of rod and cone outer segment
CC       disks.
CC   -!- SIMILARITY: Belongs to the PRPH2/ROM1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L79915; AAB64233.1; -; mRNA.
DR   RefSeq; NP_001081695.1; NM_001088226.1.
DR   AlphaFoldDB; O42583; -.
DR   PRIDE; O42583; -.
DR   DNASU; 398002; -.
DR   GeneID; 398002; -.
DR   KEGG; xla:398002; -.
DR   CTD; 398002; -.
DR   Xenbase; XB-GENE-17339014; prph2.S.
DR   OrthoDB; 1470436at2759; -.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 398002; Expressed in camera-type eye and 1 other tissue.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:InterPro.
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; Disulfide bond; Glycoprotein; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..346
FT                   /note="Peripherin-2"
FT                   /id="PRO_0000168109"
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   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   346 AA;  39308 MW;  0A0FE7D2A540EAAE CRC64;
     MALMKTKFNL KRRVKLAQGL WLMNWCCVLA GIALFSMGVF LKIELRKRSE VMDNDESHFV
     PNSLILMGSL ACALNAFPGK ICYDSLDPTK FPRWKPMLKP YLIICLIFNI FIFFTGVVCF
     LTRGSLESTL AHGLKNGMRY YKDTDIPGRC FLKKTIDLLQ IEFKCCGNNG FRDWFELQWV
     SNRYLGGRSK EVKDRIQSNV DGKYLIDGVP FSCCNPSSPR PCIQLQVTNN SAHYSYDHQT
     EELNLWSKGC KEALLNYYTS MMSSMGGMVF LVWIMEMAVM IGLRFLHTCL ETIANPEDPE
     CESEGWILEK SLKDTIKSSW ELVKSMGKLN KVETAGGEEA GVATVS