ROM1_BOVIN
ID ROM1_BOVIN Reviewed; 351 AA.
AC P52205; Q17QV8; Q28926; Q95134;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Rod outer segment membrane protein 1;
DE Short=ROSP1;
GN Name=ROM1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wada H., Murakami A., Ito J., Okisaka S.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=8603840;
RA Moritz O.L., Molday R.S.;
RT "Molecular cloning, membrane topology, and localization of bovine rom-1 in
RT rod and cone photoreceptor cells.";
RL Invest. Ophthalmol. Vis. Sci. 37:352-362(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBUNIT, AND INTERACTION WITH PRPH2.
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 [5]
RP SUBUNIT, INTERACTION WITH PRPH2, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10681511; DOI=10.1074/jbc.275.8.5370;
RA Loewen C.J., Molday R.S.;
RT "Disulfide-mediated oligomerization of Peripherin/Rds and Rom-1 in
RT photoreceptor disk membranes. Implications for photoreceptor outer segment
RT morphogenesis and degeneration.";
RL J. Biol. Chem. 275:5370-5378(2000).
RN [6]
RP FUNCTION, AND INTERACTION WITH PRPH2.
RX PubMed=24196967; DOI=10.1074/jbc.m113.520700;
RA Kevany B.M., Tsybovsky Y., Campuzano I.D., Schnier P.D., Engel A.,
RA Palczewski K.;
RT "Structural and functional analysis of the native peripherin-ROM1 complex
RT isolated from photoreceptor cells.";
RL J. Biol. Chem. 288:36272-36284(2013).
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 (PubMed:24196967). 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:0000269|PubMed:24196967}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:1610568). Forms a
CC homotetramer (PubMed:10681511). Forms a heterotetramer with PRPH2
CC (PubMed:1610568, PubMed:10681511, PubMed:24196967). Homotetramer and
CC heterotetramer core complexes go on to form higher order complexes by
CC formation of intermolecular disulfide bonds (PubMed:10681511).
CC Interacts with STX3 (By similarity). Interacts with SNAP25 (By
CC similarity). {ECO:0000250|UniProtKB:P32958,
CC ECO:0000269|PubMed:10681511, ECO:0000269|PubMed:1610568,
CC ECO:0000269|PubMed:24196967}.
CC -!- INTERACTION:
CC P52205; P43250: GRK6; Xeno; NbExp=9; IntAct=EBI-8176947, EBI-722747;
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:0000269|PubMed:10681511}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Retina photoreceptor (at protein level)
CC (PubMed:8603840, PubMed:10681511). In rim region of ROS disks (at
CC protein level) (PubMed:8603840, PubMed:10681511).
CC {ECO:0000269|PubMed:10681511, ECO:0000269|PubMed:8603840}.
CC -!- DISEASE: Note=May be involved in mammalian retinopathies
CC (PubMed:8603840). {ECO:0000269|PubMed:8603840}.
CC -!- SIMILARITY: Belongs to the PRPH2/ROM1 family. {ECO:0000305}.
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DR EMBL; D83385; BAA11900.1; -; mRNA.
DR EMBL; U72027; AAB17187.1; -; mRNA.
DR EMBL; BC118152; AAI18153.1; -; mRNA.
DR RefSeq; NP_776599.2; NM_174174.3.
DR AlphaFoldDB; P52205; -.
DR IntAct; P52205; 1.
DR MINT; P52205; -.
DR STRING; 9913.ENSBTAP00000001574; -.
DR PaxDb; P52205; -.
DR Ensembl; ENSBTAT00000001574; ENSBTAP00000001574; ENSBTAG00000001188.
DR GeneID; 281465; -.
DR KEGG; bta:281465; -.
DR CTD; 6094; -.
DR VEuPathDB; HostDB:ENSBTAG00000001188; -.
DR VGNC; VGNC:34084; ROM1.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000159921; -.
DR HOGENOM; CLU_068903_0_0_1; -.
DR InParanoid; P52205; -.
DR OMA; AARYPPW; -.
DR OrthoDB; 1125466at2759; -.
DR TreeFam; TF331684; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000001188; Expressed in retina and 102 other tissues.
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 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_0000168110"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 44..64
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 65..84
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 85..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 103..125
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 126..264
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 265..286
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 287..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 325..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 18
FT /note="A -> V (in Ref. 1; BAA11900)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 37418 MW; 7E82B59B7CD0E02D CRC64;
MAPVLPLVLP LQPRIRLAQG LWLLSWLLVL VGGLTLLCSG HLLVQLWHLG TFLAPSCPFS
ALPQVALAAS AVALGTGLVG SGASRASLDA EQYPPWRGVL GPLLVAGTAG GGGLLVLALG
LALALPGTLD TGLEEGLGSA LVHYKDTEVP GRCQAKRLLD ELQLRHHCCG RHGYKDWFGI
QWVSNRYLDP NDPDVVDRIQ SNVEGLYLID GVPFSCCNPH SPRPCLQSQL SDPHAHPLFD
PRQPNLNLWS QGCHEVLLGH LQGLASTLGN MLAVTFLLQT LVLLGLRYLQ TALEGLGGVI
DGEGEAQGYL FPAGLKDMLK TAWLQGAGPH RPAPGETPPE EKPPKECLPE A
