ID ROM1_HUMAN Reviewed; 351 AA. AC Q03395; B2R978; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 2. DT 27-MAR-2024, entry version 192. DE RecName: Full=Rod outer segment membrane protein 1; DE Short=ROSP1; DE AltName: Full=Tetraspanin-23; DE Short=Tspan-23; GN Name=ROM1; Synonyms=TSPAN23; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND VARIANT ALA-118. RC TISSUE=Retina; RX PubMed=1610568; DOI=10.1016/0896-6273(92)90137-3; RA Bascom R.A., Manara S., Collins L., Molday R.S., Kalnins V.I., RA McInnes R.R.; RT "Cloning of the cDNA for a novel photoreceptor membrane protein (rom-1) RT identifies a disk rim protein family implicated in human retinopathies."; RL Neuron 8:1171-1184(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND VARIANT ALA-118. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-118. RC TISSUE=Substantia nigra; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-118. 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). RN [6] RP INVOLVEMENT IN RP7. RX PubMed=8202715; DOI=10.1126/science.8202715; RA Kajiwara K., Berson E.L., Dryja T.P.; RT "Digenic retinitis pigmentosa due to mutations at the unlinked RT peripherin/RDS and ROM1 loci."; RL Science 264:1604-1608(1994). RN [7] RP VARIANTS ALA-118; HIS-229; THR-265 AND THR-271. RX PubMed=7904211; DOI=10.1093/hmg/2.11.1975; RA Bascom R.A., Liu L., Humphries P., Fishman G.A., Murray J.C., McInnes R.R.; RT "Polymorphisms and rare sequence variants at the ROM1 locus."; RL Hum. Mol. Genet. 2:1975-1977(1993). RN [8] RP VARIANTS THR-60; ASP-75; MET-108 AND GLN-242. RX PubMed=8595413; DOI=10.1093/hmg/4.10.1895; RA Bascom R.A., Liu L., Heckenlively J.R., Stone E.M., McInnes R.R.; RT "Mutation analysis of the ROM1 gene in retinitis pigmentosa."; RL Hum. Mol. Genet. 4:1895-1902(1995). RN [9] RP INVOLVEMENT IN RP7, AND VARIANT HIS-16. RX PubMed=9331261; RA Dryja T.P., Hahn L.B., Kajiwara K., Berson E.L.; RT "Dominant and digenic mutations in the peripherin/RDS and ROM1 genes in RT retinitis pigmentosa."; RL Invest. Ophthalmol. Vis. Sci. 38:1972-1982(1997). RN [10] RP VARIANT HIS-229. RX PubMed=20335603; DOI=10.1167/iovs.09-4655; RA Poloschek C.M., Bach M., Lagreze W.A., Glaus E., Lemke J.R., Berger W., RA Neidhardt J.; RT "ABCA4 and ROM1: implications for modification of the PRPH2-associated RT macular dystrophy phenotype."; RL Invest. Ophthalmol. Vis. Sci. 51:4253-4265(2010). 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 (PubMed:1610568). 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, ECO:0000269|PubMed:1610568}. CC -!- INTERACTION: CC Q03395; P78329: CYP4F2; NbExp=3; IntAct=EBI-9395257, EBI-1752413; CC Q03395; Q9HB07: MYG1; NbExp=3; IntAct=EBI-9395257, EBI-709754; CC Q03395; Q8N138: ORMDL3; NbExp=3; IntAct=EBI-9395257, EBI-721750; CC -!- SUBCELLULAR LOCATION: Photoreceptor inner segment membrane CC {ECO:0000250|UniProtKB:P32958, ECO:0000305|PubMed:1610568}; Multi-pass CC membrane protein {ECO:0000255}. Photoreceptor outer segment membrane CC {ECO:0000269|PubMed:1610568}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Retina photoreceptors (at protein level) CC (PubMed:1610568, PubMed:8504299). In rim region of ROS disks CC (PubMed:1610568). {ECO:0000269|PubMed:1610568, CC ECO:0000269|PubMed:8504299}. CC -!- DISEASE: Retinitis pigmentosa 7 (RP7) [MIM:608133]: A retinal dystrophy CC belonging to the group of pigmentary retinopathies. Retinitis CC pigmentosa is characterized by retinal pigment deposits visible on CC fundus examination and primary loss of rod photoreceptor cells followed CC by secondary loss of cone photoreceptors. Patients typically have night CC vision blindness and loss of midperipheral visual field. As their CC condition progresses, they lose their far peripheral visual field and CC eventually central vision as well. {ECO:0000269|PubMed:8202715, CC ECO:0000269|PubMed:9331261}. Note=The disease may be caused by variants CC affecting distinct genetic loci, including the gene represented in this CC entry. A digenic form of retinitis pigmentosa 7 results from a mutation CC in the PRPH2 gene and a null mutation of the ROM1 gene has been CC reported (PubMed:8202715). {ECO:0000269|PubMed:8202715}. CC -!- SIMILARITY: Belongs to the PRPH2/ROM1 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Mutations of the ROM1 gene; Note=Retina CC International's Scientific Newsletter; CC URL="https://www.retina-international.org/files/sci-news/rommut.htm"; 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; L07894; AAA60274.1; -; mRNA. DR EMBL; M96759; AAA60272.1; -; Genomic_DNA. DR EMBL; AK313674; BAG36425.1; -; mRNA. DR EMBL; AP001458; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008100; AAH08100.1; -; mRNA. DR CCDS; CCDS8024.1; -. DR PIR; I54347; I54347. DR RefSeq; NP_000318.1; NM_000327.3. DR PDB; 7ZW1; EM; 3.70 A; B=2-351. DR PDBsum; 7ZW1; -. DR AlphaFoldDB; Q03395; -. DR EMDB; EMD-14991; -. DR SMR; Q03395; -. DR BioGRID; 112021; 4. DR IntAct; Q03395; 5. DR STRING; 9606.ENSP00000278833; -. DR iPTMnet; Q03395; -. DR PhosphoSitePlus; Q03395; -. DR BioMuta; ROM1; -. DR DMDM; 143745282; -. DR jPOST; Q03395; -. DR MassIVE; Q03395; -. DR PaxDb; 9606-ENSP00000278833; -. DR PeptideAtlas; Q03395; -. DR ProteomicsDB; 58206; -. DR Antibodypedia; 28554; 96 antibodies from 21 providers. DR DNASU; 6094; -. DR Ensembl; ENST00000278833.4; ENSP00000278833.3; ENSG00000149489.9. DR GeneID; 6094; -. DR KEGG; hsa:6094; -. DR MANE-Select; ENST00000278833.4; ENSP00000278833.3; NM_000327.4; NP_000318.2. DR UCSC; uc001ntv.5; human. DR AGR; HGNC:10254; -. DR CTD; 6094; -. DR DisGeNET; 6094; -. DR GeneCards; ROM1; -. DR GeneReviews; ROM1; -. DR HGNC; HGNC:10254; ROM1. DR HPA; ENSG00000149489; Tissue enriched (retina). DR MalaCards; ROM1; -. DR MIM; 180721; gene. DR MIM; 608133; phenotype. DR neXtProt; NX_Q03395; -. DR OpenTargets; ENSG00000149489; -. DR Orphanet; 791; Retinitis pigmentosa. DR PharmGKB; PA34626; -. DR VEuPathDB; HostDB:ENSG00000149489; -. DR eggNOG; KOG3882; Eukaryota. DR GeneTree; ENSGT00940000159921; -. DR HOGENOM; CLU_068903_0_0_1; -. DR InParanoid; Q03395; -. DR OMA; AARYPPW; -. DR OrthoDB; 4137027at2759; -. DR PhylomeDB; Q03395; -. DR TreeFam; TF331684; -. DR PathwayCommons; Q03395; -. DR SignaLink; Q03395; -. DR BioGRID-ORCS; 6094; 31 hits in 1155 CRISPR screens. DR GeneWiki; ROM1; -. DR GenomeRNAi; 6094; -. DR Pharos; Q03395; Tbio. DR PRO; PR:Q03395; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q03395; Protein. DR Bgee; ENSG00000149489; Expressed in primordial germ cell in gonad and 129 other cell types or tissues. DR ExpressionAtlas; Q03395; baseline and differential. DR GO; GO:0042622; C:photoreceptor outer segment membrane; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl. DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; 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:1903546; P:protein localization to photoreceptor outer segment; IEA:Ensembl. DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl. DR GO; GO:0061298; P:retina vasculature development in camera-type eye; IEA:Ensembl. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. DR CDD; cd03162; peripherin_like_LEL; 1. DR Gene3D; 1.10.1450.10; Tetraspanin; 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:SF234; ROD OUTER SEGMENT MEMBRANE PROTEIN 1; 1. DR PANTHER; PTHR19282; TETRASPANIN; 1. DR Pfam; PF00335; Tetraspanin; 1. DR PRINTS; PR00218; PERIPHERNRDS. DR SUPFAM; SSF48652; Tetraspanin; 1. DR PROSITE; PS00930; RDS_ROM1; 1. DR Genevisible; Q03395; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell adhesion; Cell projection; Disease variant; KW Disulfide bond; Membrane; Reference proteome; Retinitis pigmentosa; KW Sensory transduction; Transmembrane; Transmembrane helix; Vision. FT CHAIN 1..351 FT /note="Rod outer segment membrane protein 1" FT /id="PRO_0000168111" 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 331..351 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 16 FT /note="R -> H (in dbSNP:rs143166696)" FT /evidence="ECO:0000269|PubMed:9331261" FT /id="VAR_008269" FT VARIANT 60 FT /note="P -> T (in dbSNP:rs199757012)" FT /evidence="ECO:0000269|PubMed:8595413" FT /id="VAR_006896" FT VARIANT 75 FT /note="G -> D (in dbSNP:rs747140028)" FT /evidence="ECO:0000269|PubMed:8595413" FT /id="VAR_008270" FT VARIANT 108 FT /note="T -> M (in dbSNP:rs146358003)" FT /evidence="ECO:0000269|PubMed:8595413" FT /id="VAR_006897" FT VARIANT 118 FT /note="G -> A (in dbSNP:rs1799959)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1610568, FT ECO:0000269|PubMed:7904211, ECO:0000269|PubMed:8504299" FT /id="VAR_008271" FT VARIANT 229 FT /note="R -> H (in patients with macular dysfunction; FT macular dysfunction severity is influenced by the presence FT of a W-172 mutation in PRPH2.; dbSNP:rs150168119)" FT /evidence="ECO:0000269|PubMed:20335603, FT ECO:0000269|PubMed:7904211" FT /id="VAR_006898" FT VARIANT 242 FT /note="R -> Q (in dbSNP:rs767877192)" FT /evidence="ECO:0000269|PubMed:8595413" FT /id="VAR_008272" FT VARIANT 265 FT /note="A -> T (in dbSNP:rs200272942)" FT /evidence="ECO:0000269|PubMed:7904211" FT /id="VAR_006899" FT VARIANT 271 FT /note="M -> T (in dbSNP:rs137950927)" FT /evidence="ECO:0000269|PubMed:7904211" FT /id="VAR_006900" SQ SEQUENCE 351 AA; 37205 MW; 895C33382B681E84 CRC64; MAPVLPLVLP LQPRIRLAQG LWLLSWLLAL AGGVILLCSG HLLVQLRHLG TFLAPSCQFP VLPQAALAAG AVALGTGLVG VGASRASLNA ALYPPWRGVL GPLLVAGTAG GGGLLVVGLG LALALPGSLD EALEEGLVTA LAHYKDTEVP GHCQAKRLVD ELQLRYHCCG RHGYKDWFGV QWVSSRYLDP GDRDVADRIQ SNVEGLYLTD GVPFSCCNPH SPRPCLQNRL SDSYAHPLFD PRQPNQNLWA QGCHEVLLEH LQDLAGTLGS MLAVTFLLQA LVLLGLRYLQ TALEGLGGVI DAGGETQGYL FPSGLKDMLK TAWLQGGVAC RPAPEEAPPG EAPPKEDLSE A //