ROM1_HUMAN
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 03-AUG-2022, entry version 183.
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 AlphaFoldDB; 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; Q03395; -.
DR PeptideAtlas; Q03395; -.
DR PRIDE; Q03395; -.
DR ProteomicsDB; 58206; -.
DR Antibodypedia; 28554; 78 antibodies from 20 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 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; 1125466at2759; -.
DR PhylomeDB; Q03395; -.
DR TreeFam; TF331684; -.
DR PathwayCommons; Q03395; -.
DR SignaLink; Q03395; -.
DR BioGRID-ORCS; 6094; 17 hits in 1077 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 C1 segment of cervical spinal cord and 127 other tissues.
DR ExpressionAtlas; Q03395; baseline and differential.
DR Genevisible; Q03395; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IEA:Ensembl.
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; -; 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; Disease variant; Disulfide bond; Membrane;
KW Reference proteome; Retinitis pigmentosa; Sensory transduction;
KW 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
