ID   ROM1_RAT                Reviewed;         351 AA.
AC   Q5PPM7;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Rod outer segment membrane protein 1;
DE            Short=ROSP1;
GN   Name=Rom1;
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   STRAIN=Sprague-Dawley; TISSUE=Retina;
RA   Kelln R.M., Patterson M.L., Darrow R.M., Barsalou L., Organisciak D.T.,
RA   Wong P.;
RT   "Defining changes in retinal gene expression after prolonged exposure to
RT   light and light induced oxidative stress.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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).
CC   -!- FUNCTION: Plays a role in rod outer segment (ROS) morphogenesis (By
CC       similarity). May play a role with PRPH2 in the maintenance of the
CC       structure of ROS curved disks (By similarity). Plays a role in the
CC       organization of the ROS and maintenance of ROS disk diameter (By
CC       similarity). Involved in the maintenance of the retina outer nuclear
CC       layer (By similarity). {ECO:0000250|UniProtKB:P32958,
CC       ECO:0000250|UniProtKB:P52205}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Forms a
CC       homotetramer (By similarity). Forms a heterotetramer with PRPH2 (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 STX3 (By similarity). Interacts
CC       with SNAP25 (By similarity). {ECO:0000250|UniProtKB:P32958,
CC       ECO:0000250|UniProtKB:P52205}.
CC   -!- SUBCELLULAR LOCATION: Photoreceptor inner segment membrane
CC       {ECO:0000250|UniProtKB:P32958}; Multi-pass membrane protein
CC       {ECO:0000255}. Photoreceptor outer segment membrane
CC       {ECO:0000250|UniProtKB:P32958}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the PRPH2/ROM1 family. {ECO:0000305}.
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DR   EMBL; AY212508; AAO46095.1; -; mRNA.
DR   EMBL; BC087605; AAH87605.1; -; mRNA.
DR   RefSeq; NP_001009690.1; NM_001009690.1.
DR   AlphaFoldDB; Q5PPM7; -.
DR   STRING; 10116.ENSRNOP00000026897; -.
DR   PaxDb; Q5PPM7; -.
DR   Ensembl; ENSRNOT00000026897; ENSRNOP00000026897; ENSRNOG00000019858.
DR   GeneID; 309201; -.
DR   KEGG; rno:309201; -.
DR   UCSC; RGD:1306070; rat.
DR   CTD; 6094; -.
DR   RGD; 1306070; Rom1.
DR   eggNOG; KOG3882; Eukaryota.
DR   GeneTree; ENSGT00940000159921; -.
DR   HOGENOM; CLU_068903_0_0_1; -.
DR   InParanoid; Q5PPM7; -.
DR   OMA; AARYPPW; -.
DR   OrthoDB; 1125466at2759; -.
DR   PhylomeDB; Q5PPM7; -.
DR   TreeFam; TF331684; -.
DR   PRO; PR:Q5PPM7; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000019858; Expressed in pancreas and 19 other tissues.
DR   Genevisible; Q5PPM7; RN.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0001750; C:photoreceptor outer segment; ISO:RGD.
DR   GO; GO:0042622; C:photoreceptor outer segment membrane; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; 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:1903546; P:protein localization to photoreceptor outer segment; ISO:RGD.
DR   GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR   GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR   GO; GO:0060042; P:retina morphogenesis in camera-type eye; ISO:RGD.
DR   GO; GO:0061298; P:retina vasculature 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; Membrane;
KW   Reference proteome; Sensory transduction; Transmembrane;
KW   Transmembrane helix; Vision.
FT   CHAIN           1..351
FT                   /note="Rod outer segment membrane protein 1"
FT                   /id="PRO_0000168113"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..64
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        85..102
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..263
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        287..351
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          329..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..351
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   351 AA;  37237 MW;  5EAA6FB4F0E14C69 CRC64;
     MAPVLPVVLP LQPRIRLAQG TWLLSWLLAL AGGLTLLCSG HLLVQLWHLG TFLAPSCSFP
     ALPQTALAAG AVALGTGLGG AGASRASLDA AQYPPWRGVL TPLLVVGTAA GGGLLTLGLG
     LALALPVSLH QGLEEGLQAA LAHYKDTEVP GHCQAKRLMD ELQLRYHCCG RHGYKDWFGV
     QWVSSRYLDP NDQDVVDRIQ SNVEGLYLID GVPFSCCNPH SPRPCLQSQL SDPYAHPLFD
     PRQPNLNLWA QGCHEVLVGH LQGLSGTLGS ILAVTLLLQV LVLLGLRYLQ TALEGLGGVI
     DGEGETQGYL LPGGLKDILQ TAWLQGGLAH KPAPEEAPPD EEPPKEVLAE A