ROM1_MOUSE
ID ROM1_MOUSE Reviewed; 351 AA.
AC P32958;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Rod outer segment membrane protein 1;
DE Short=ROSP1;
GN Name=Rom1; Synonyms=Rom-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8504299; DOI=10.1093/hmg/2.4.385;
RA Bascom R.A., Schappert K.T., McInnes R.R.;
RT "Cloning of the human and murine ROM1 genes: genomic organization and
RT sequence conservation.";
RL Hum. Mol. Genet. 2:385-391(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10802659; DOI=10.1038/75621;
RA Clarke G., Goldberg A.F., Vidgen D., Collins L., Ploder L., Schwarz L.,
RA Molday L.L., Rossant J., Szel A., Molday R.S., Birch D.G., McInnes R.R.;
RT "Rom-1 is required for rod photoreceptor viability and the regulation of
RT disk morphogenesis.";
RL Nat. Genet. 25:67-73(2000).
RN [4]
RP INTERACTION WITH PRPH2; STX3 AND SNAP25, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=26406599; DOI=10.1371/journal.pone.0138508;
RA Zulliger R., Conley S.M., Mwoyosvi M.L., Stuck M.W., Azadi S., Naash M.I.;
RT "SNAREs Interact with Retinal Degeneration Slow and Rod Outer Segment
RT Membrane Protein-1 during Conventional and Unconventional Outer Segment
RT Targeting.";
RL PLoS ONE 10:E0138508-E0138508(2015).
RN [5]
RP INTERACTION WITH PRPH2, AND SUBCELLULAR LOCATION.
RX PubMed=29961824; DOI=10.1093/hmg/ddy240;
RA Zulliger R., Conley S.M., Mwoyosvi M.L., Al-Ubaidi M.R., Naash M.I.;
RT "Oligomerization of Prph2 and Rom1 is essential for photoreceptor outer
RT segment formation.";
RL Hum. Mol. Genet. 27:3507-3518(2018).
CC -!- FUNCTION: Plays a role in rod outer segment (ROS) morphogenesis
CC (PubMed:10802659). 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
CC (PubMed:10802659). Involved in the maintenance of the retina outer
CC nuclear layer (PubMed:10802659). {ECO:0000250|UniProtKB:P52205,
CC ECO:0000269|PubMed:10802659}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Forms a
CC homotetramer (By similarity). Forms a heterotetramer with PRPH2
CC (PubMed:26406599, PubMed:29961824). Homotetramer and heterotetramer
CC core complexes go on to form higher order complexes by formation of
CC intermolecular disulfide bonds (By similarity). Interacts with STX3
CC isoform 3B (PubMed:26406599). Interacts with SNAP25 (PubMed:26406599).
CC {ECO:0000250|UniProtKB:P52205, ECO:0000269|PubMed:26406599,
CC ECO:0000269|PubMed:29961824}.
CC -!- SUBCELLULAR LOCATION: Photoreceptor inner segment membrane
CC {ECO:0000305|PubMed:26406599}; Multi-pass membrane protein
CC {ECO:0000255}. Photoreceptor outer segment membrane
CC {ECO:0000305|PubMed:26406599, ECO:0000305|PubMed:29961824}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level).
CC {ECO:0000269|PubMed:26406599}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice are viable, fertile and grossly
CC phenotypically normal (PubMed:10802659). 50% reduction in maximal rod
CC photoreceptor response at 9 months of age (PubMed:10802659).
CC Progressive thinning of the retinal outer nuclear layer becomes evident
CC at 1 month of age (PubMed:10802659). Evidence of rod photoreceptor
CC degeneration, shortened rod outer segment (ROS) length, increased ROS
CC disk diameter, and progressive disorganization of the ROS at 1 month of
CC age, leading to near-complete loss of organization by 2 months of age,
CC however organization returns to near normal levels by 4 months of age
CC (PubMed:10802659). Rod photoreceptors progressively die by apoptosis
CC (PubMed:10802659). Knockout does not affect localization of Prph2 or
CC Abca4 to ROS disk rims (PubMed:10802659).
CC {ECO:0000269|PubMed:10802659}.
CC -!- SIMILARITY: Belongs to the PRPH2/ROM1 family. {ECO:0000305}.
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DR EMBL; M96760; AAA40063.1; -; Genomic_DNA.
DR EMBL; BC014827; AAH14827.1; -; mRNA.
DR CCDS; CCDS29559.1; -.
DR PIR; I68620; I68620.
DR RefSeq; NP_033099.3; NM_009073.4.
DR AlphaFoldDB; P32958; -.
DR BioGRID; 202954; 1.
DR STRING; 10090.ENSMUSP00000093961; -.
DR iPTMnet; P32958; -.
DR PhosphoSitePlus; P32958; -.
DR PaxDb; P32958; -.
DR PRIDE; P32958; -.
DR ProteomicsDB; 301643; -.
DR Antibodypedia; 28554; 78 antibodies from 20 providers.
DR DNASU; 19881; -.
DR Ensembl; ENSMUST00000096242; ENSMUSP00000093961; ENSMUSG00000071648.
DR GeneID; 19881; -.
DR KEGG; mmu:19881; -.
DR UCSC; uc008goc.2; mouse.
DR CTD; 6094; -.
DR MGI; MGI:97998; Rom1.
DR VEuPathDB; HostDB:ENSMUSG00000071648; -.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000159921; -.
DR HOGENOM; CLU_068903_0_0_1; -.
DR InParanoid; P32958; -.
DR OMA; AARYPPW; -.
DR OrthoDB; 1125466at2759; -.
DR PhylomeDB; P32958; -.
DR TreeFam; TF331684; -.
DR BioGRID-ORCS; 19881; 3 hits in 72 CRISPR screens.
DR PRO; PR:P32958; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P32958; protein.
DR Bgee; ENSMUSG00000071648; Expressed in retinal neural layer and 127 other tissues.
DR Genevisible; P32958; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IGI:MGI.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IMP:MGI.
DR GO; GO:0051291; P:protein heterooligomerization; IPI:MGI.
DR GO; GO:0051260; P:protein homooligomerization; IPI:MGI.
DR GO; GO:1903546; P:protein localization to photoreceptor outer segment; IDA:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:0061298; P:retina vasculature development in camera-type eye; IMP:MGI.
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 1: Evidence at protein 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_0000168112"
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; 37265 MW; 64CB47F552886394 CRC64;
MAPVLPVVLP LQPRIRLAQG IWLLSWLLAL VGGLTLLCSG HLLVQLGHLG TFLAPSCSFP
ALPQTALAAG TVALGTGLGG AGASRASLDA AQYPPWRGVL TPLLAVGTAA GGGLLTLALG
LALALPVSLN QGLEEGLEAA LAHYKDTEVP GRCQAKRLMD ELQLRYHCCG RHGYKDWFGV
QWVSNRYLDP SDQDVVDRIQ SNVEGLYLID GVPFSCCNPH SPRPCLQSQL SDPYAHPLFD
PRQPNLNLWA QGCHEVLLEH LQGLSGTLGS ILAVTLLLQI LVLLGLRYLQ TALEGLGGVI
DGEGEAQGYL FPGGLKDILK TAWLQGGLAH KPAPEEAPPD EEPPKEVLAE A
