P23942 (PRPH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peripherin-2

Alternative name(s):
Retinal degeneration slow protein
Tetraspanin-22
Short name=Tspan-22

Gene names

Name:	PRPH2
Synonyms:	PRPH, RDS, TSPAN22

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	346 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May function as an adhesion molecule involved in stabilization and compaction of outer segment disks or in the maintenance of the curvature of the rim. It is essential for disk morphogenesis.
Subunit structure	Homodimer; disulfide-linked. Probably forms a complex with a ROM1 homodimer. Other proteins could associate with this complex in rods. Interacts with MREG.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Retina (photoreceptor). In rim region of ROS (rod outer segment) disks.
Involvement in disease	Retinitis pigmentosa 7 (RP7) [MIM:608133]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.7 Ref.8 Ref.13 Ref.16 Ref.20 Ref.24 Retinitis punctata albescens (RPA) [MIM:136880]: Rare form of stationary night blindness characterized by a delay in the regeneration of cone and rod photopigments. Note: The disease is caused by mutations affecting the gene represented in this entry. Adult-onset vitelliform macular dystrophy (AVMD) [MIM:608161]: A rare autosomal dominant disorder with incomplete penetrance and highly variable expression. Patients usually become symptomatic in the fourth or fifth decade of life with a protracted disease of decreased visual acuity. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Patterned dystrophy of retinal pigment epithelium (PDREP) [MIM:169150]: A heterogeneous group of macular disorders. Three main types of PDREP have been described: reticular (fishnet-like) dystrophy, macroreticular (spider-shaped) dystrophy and butterfly-shaped pigment dystrophy. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.18 Ref.22 Choroidal dystrophy, central areolar 2 (CACD2) [MIM:613105]: A disease of the macula leading to a well-demarcated circumscribed area of atrophy of the pigment epithelium and choriocapillaris. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23 Defects in PRPH2 are found in different retinal diseases including cone-rod dystrophy, retinitis pigmentosa, macular degeneration. The mutations underlying autosomal dominant retinitis pigmentosa and severe macular degeneration are largely missense or small in-frame deletions in a large intradiscal loop between the third and fourth transmembrane domains. In contrast, those associated with the milder pattern phenotypes or with digenic RP are scattered more evenly through the gene and are often nonsense mutations. This observation correlates with the hypothesis that the large loop is an important site of interaction between PRPH2 molecules and other protein components in the disk.
Sequence similarities	Belongs to the PRPH2/ROM1 family.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Cone-rod dystrophy Disease mutation Retinitis pigmentosa
Domain	Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW retina development in camera-type eye Inferred from electronic annotation. Source: Compara visual perception Traceable author statement Ref.6. Source: ProtInc
Cellular_component	integral to membrane Traceable author statement Ref.6. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 346	346	Peripherin-2		PRO_0000168105
Regions
	Topological domain	1 – 24	24	Cytoplasmic Potential
	Transmembrane	25 – 43	19	Helical; Potential
	Topological domain	44 – 61	18	Lumenal Potential
	Transmembrane	62 – 80	19	Helical; Potential
	Topological domain	81 – 99	19	Cytoplasmic Potential
	Transmembrane	100 – 123	24	Helical; Potential
	Topological domain	124 – 264	141	Lumenal Potential
	Transmembrane	265 – 290	26	Helical; Potential
	Topological domain	291 – 346	56	Cytoplasmic Potential
	Region	341 – 346	6	Interaction with MREG By similarity
Amino acid modifications
	Glycosylation	53	1	N-linked (GlcNAc...) Potential
	Glycosylation	229	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	13	1	R → W in RP7; in combination with a null mutation of ROM1.		VAR_006853
	Natural variant	32	1	I → V in some patients with macular dystrophy.		VAR_006854
	Natural variant	45	1	L → F in RP7; in combination with a null mutation of ROM1.		VAR_006855
	Natural variant	67	1	Missing in PDREP; also in cone-rod dystrophy.		VAR_006856
	Natural variant	68	1	G → R in PDREP; also in cone-rod dystrophy.		VAR_006857
	Natural variant	118	1	Missing in RP7. Ref.6		VAR_006858
	Natural variant	126	1	L → R in RP7.		VAR_006859
	Natural variant	142	1	R → W in RP7; also found in a patient with central areolar choroidal dystrophy. Ref.24		VAR_006860
	Natural variant	153	1	K → R in RP7.		VAR_006861
	Natural variant	153	1	Missing in RP7.		VAR_006862
	Natural variant	157	1	D → N in PDREP.		VAR_006863
	Natural variant	165	1	C → Y in RP7.		VAR_006864
	Natural variant	167	1	G → D in PDREP; butterfly-shaped. Ref.10		VAR_006865
	Natural variant	167	1	G → S in PDREP; butterfly-shaped. Ref.22		VAR_032052
	Natural variant	169	1	Missing in some patients with macular dystrophy. Ref.21		VAR_032053
	Natural variant	172	1	R → G in PDREP; butterfly-shaped.		VAR_006866
	Natural variant	172	1	R → Q in some patients with macular dystrophy. Ref.11		VAR_006867
	Natural variant	172	1	R → W in some patients with macular dystrophy; also in a family affected by central areolar choroidal dystrophy. Ref.11 Ref.14 Ref.18		VAR_006868
	Natural variant	173	1	D → V in RP7.		VAR_006869
	Natural variant	184	1	Y → S in cone-rod dystrophy.		VAR_006870
	Natural variant	185	1	L → P in RP7; digenic inheritance; results in disease in combination with a null mutation of ROM1. Ref.7		VAR_006871
	Natural variant	193	1	Missing in PDREP; also in cone-rod dystrophy.		VAR_006872
	Natural variant	195	1	R → L in CACD2. Ref.23		VAR_032054
	Natural variant	208	1	G → D in RP7. Ref.20		VAR_006873
	Natural variant	210	1	P → R in PDREP and RP7; also in adult-onset foveomacular dystrophy with choroidal neovascularization. Ref.12 Ref.16 Ref.18		VAR_006874
	Natural variant	210	1	P → S in RP7.		VAR_006875
	Natural variant	211	1	F → L in RP7.		VAR_006876
	Natural variant	212	1	S → G in RP7. Ref.8		VAR_006877
	Natural variant	212	1	S → T in AVMD. Ref.17		VAR_006878
	Natural variant	213	1	C → R in PDREP. Ref.18		VAR_006879
	Natural variant	214	1	C → S in RP7.		VAR_006880
	Natural variant	216	1	P → L in RP7. Ref.7		VAR_006881
	Natural variant	216	1	P → S in RP7.		VAR_006882
	Natural variant	219	1	P → R in some patients with macular dystrophy. Ref.18		VAR_006883
	Natural variant	219	1	Missing in RP7. Ref.7		VAR_006884
	Natural variant	220	1	R → Q in PDREP.		VAR_006885
	Natural variant	220	1	R → W in PDREP. Ref.18		VAR_006886
	Natural variant	244	1	N → H in cone-rod dystrophy.		VAR_006888
	Natural variant	244	1	N → K in RP7; with bulls-eye maculopathy. Ref.13		VAR_006887
	Natural variant	266	1	G → D in RP7.		VAR_006889
	Natural variant	268	1	V → I in AVMD. Ref.17		VAR_006890
	Natural variant	304	1	E → Q Associated with D-338 on the same haplotype. Ref.3 Corresponds to variant rs390659 [ dbSNP | Ensembl ].		VAR_006891
	Natural variant	305	1	G → D in AVMD. Ref.17		VAR_006892
	Natural variant	310	1	K → R. Ref.3 Corresponds to variant rs425876 [ dbSNP | Ensembl ].		VAR_006893
	Natural variant	313	1	P → L. Ref.19		VAR_006894
	Natural variant	338	1	G → D Associated with Q-304 on the same haplotype. Ref.3 Corresponds to variant rs434102 [ dbSNP | Ensembl ].		VAR_006895
Experimental info
	Sequence conflict	44	1	E → G in AAH74720. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P23942 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: 2BB3C5415E194D2A	FASTA	346	39,186
	10 20 30 40 50 60 MALLKVKFDQ KKRVKLAQGL WLMNWFSVLA GIIIFSLGLF LKIELRKRSD VMNNSESHFV 70 80 90 100 110 120 PNSLIGMGVL SCVFNSLAGK ICYDALDPAK YARWKPWLKP YLAICVLFNI ILFLVALCCF 130 140 150 160 170 180 LLRGSLENTL GQGLKNGMKY YRDTDTPGRC FMKKTIDMLQ IEFKCCGNNG FRDWFEIQWI 190 200 210 220 230 240 SNRYLDFSSK EVKDRIKSNV DGRYLVDGVP FSCCNPSSPR PCIQYQITNN SAHYSYDHQT 250 260 270 280 290 300 EELNLWVRGC RAALLSYYSS LMNSMGVVTL LIWLFEVTIT IGLRYLQTSL DGVSNPEESE 310 320 330 340 SESEGWLLEK SVPETWKAFL ESVKKLGKGN QVEAEGAGAG QAPEAG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human retinal degeneration slow (RDS) gene: chromosome assignment and structure of the mRNA." Travis G.H., Christerson L., Danielson P.E., Klisak I., Sparkes R.S., Hahn L.B., Dryja T.P., Sutcliffe G.J. Genomics 10:733-739(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Kajiwara K. Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS GLN-304; ARG-310 AND ASP-338.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"Mutations and polymorphisms in the human peripherin-RDS gene and their involvement in inherited retinal degeneration." Keen T.J., Inglehearn C.F. Hum. Mutat. 8:297-303(1996) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[6]	"A three-base-pair deletion in the peripherin-RDS gene in one form of retinitis pigmentosa." Farrar G.J., Kenna P., Jordan S.A., Kumar-Singh R., Humphries M.M., Sharp E.M., Sheils D.M., Humphries P. Nature 354:478-480(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP7 CYS-118 DEL.
[7]	"Mutations in the human retinal degeneration slow gene in autosomal dominant retinitis pigmentosa." Kajiwara K., Hahn L.B., Mukai S., Travis G.H., Berson E.L., Dryja T.P. Nature 354:480-483(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP7 PRO-185; LEU-216 AND PRO-219 DEL.
[8]	"Autosomal dominant retinitis pigmentosa: a novel mutation at the peripherin/RDS locus in the original 6p-linked pedigree." Farrar G.J., Kenna P., Jordan S.A., Kumar-Singh R., Humphries M.M., Sharp E.M., Sheils D.M., Humphries P. Genomics 14:805-807(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP7 GLY-212.
[9]	Erratum Farrar G.J., Kenna P., Jordan S.A., Kumar-Singh R., Humphries M.M., Sharp E.M., Sheils D.M., Humphries P. Genomics 15:466-466(1993) [PubMed] [Europe PMC] [Abstract]
[10]	"Butterfly-shaped pigment dystrophy of the fovea caused by a point mutation in codon 167 of the RDS gene." Nichols B.E., Sheffield V.C., Vandenburgh K., Drack A.V., Kimura A.E., Stone E.M. Nat. Genet. 3:202-207(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PDREP ASP-167.
[11]	"Mutations in the human retinal degeneration slow (RDS) gene can cause either retinitis pigmentosa or macular dystrophy." Wells J., Wroblewski J., Keen J., Inglehearn C., Jubb C., Eckstein A., Jay M., Arden G., Bhattacharya S., Fitzke F. Nat. Genet. 3:213-218(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLN-172 AND TRP-172.
[12]	"Choroidal neovascularization in a patient with adult foveomacular dystrophy and a mutation in the retinal degeneration slow gene (Pro 210 Arg)." Feist R.M., White M.F. Jr., Skalka H., Stone E.M. Am. J. Ophthalmol. 118:259-260(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FOVEOMACULAR DYSTROPHY ARG-210.
[13]	"A novel mutation (Asn244Lys) in the peripherin/RDS gene causing autosomal dominant retinitis pigmentosa associated with bull's-eye maculopathy detected by nonradioisotopic SSCP." Kikawa E., Nakazawa M., Chida Y., Shiono T., Tamai M. Genomics 20:137-139(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP7 LYS-244.
[14]	"A point mutation in the RDS-peripherin gene in a Spanish family with central areolar choroidal dystrophy." Reig C., Serra A., Gean E., Vidal M., Arumi J., De la Calzada M.D., Antich J., Carballo M. Ophthalmic Genet. 16:39-44(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TRP-172.
[15]	Erratum Reig C., Serra A., Gean E., Vidal M., Arumi J., De la Calzada M.D., Antich J., Carballo M. Ophthalmic Genet. 16:179-179(1995)
[16]	"A peripherin/retinal degeneration slow mutation (Pro-210-Arg) associated with macular and peripheral retinal degeneration." Gorin M.B., Jackson K.E., Ferrell R.E., Sheffield V.C., Jacobson S.G., Gass J.D., Mitchell E., Stone E.M. Ophthalmology 102:246-255(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP7 ARG-210.
[17]	"Adult vitelliform macular dystrophy is frequently associated with mutations in the peripherin/RDS gene." Felbor U., Schilling H., Weber B.H.F. Hum. Mutat. 10:301-309(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AVMD THR-212; ILE-268 AND ASP-305.
[18]	"Founder effect, seen in the British population, of the 172 peripherin/RDS mutation- and further refinement of genetic positioning of the peripherin/RDS gene." Payne A.M., Downes S.M., Bessant D.A.R., Bird A.C., Bhattacharya S.S. Am. J. Hum. Genet. 62:192-195(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PDREP ARG-210; ARG-213 AND TRP-220, VARIANTS MACULAR DYSTROPHY TRP-172 AND ARG-219.
[19]	"P313L: a novel amino acid substitution within the C-terminal domain of the human RDS/peripherin gene." Ruiz A., Borrego S., Sanchez J., Antinolo G. Hum. Mutat. 11:415-416(1998) Cited for: VARIANT LEU-313.
[20]	"Three novel RDS-peripherin mutations (689delT, 857del17, G208D) in Spanish families affected with autosomal dominant retinal degenerations." Trujillo M.J., Bueno J., Osorio A., Sanz R., Garcia-Sandoval B., Ramos C., Ayuso C. Hum. Mutat. 12:70-70(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP7 ASP-208.
[21]	"A peculiar autosomal dominant macular dystrophy caused by an asparagine deletion at codon 169 in the peripherin/RDS gene." van Lith-Verhoeven J.J., van den Helm B., Deutman A.F., Bergen A.A., Cremers F.P., Hoyng C.B., de Jong P.T. Arch. Ophthalmol. 121:1452-1457(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MACULAR DYSTROPHY ASN-169 DEL.
[22]	"A novel mutation in the RDS gene in an Italian family with pattern dystrophy." Testa F., Marini V., Rossi S., Interlandi E., Nesti A., Rinaldi M., Varano M., Garre C., Simonelli F. Br. J. Ophthalmol. 89:1066-1068(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PDREP SER-167.
[23]	"Clinical findings in a multigeneration family with autosomal dominant central areolar choroidal dystrophy associated with an Arg195Leu mutation in the peripherin/RDS gene." Keilhauer C.N., Meigen T., Weber B.H. Arch. Ophthalmol. 124:1020-1027(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CACD2 LEU-195.
[24]	"Next-generation genetic testing for retinitis pigmentosa." Neveling K., Collin R.W., Gilissen C., van Huet R.A., Visser L., Kwint M.P., Gijsen S.J., Zonneveld M.N., Wieskamp N., de Ligt J., Siemiatkowska A.M., Hoefsloot L.H., Buckley M.F., Kellner U., Branham K.E., den Hollander A.I., Hoischen A., Hoyng C. , Klevering B.J., van den Born L.I., Veltman J.A., Cremers F.P., Scheffer H. Hum. Mutat. 33:963-972(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP7 TRP-142.
+	Additional computationally mapped references.

Web resources

Mutations of the RDS gene

Retina International's Scientific Newsletter

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	M73531 mRNA. Translation: AAA60260.1. U07149, U07147, U07148 Genomic DNA. Translation: AAA16958.1. AL049843 Genomic DNA. Translation: CAB75420.1. BC074720 mRNA. Translation: AAH74720.1.
IPI	IPI00013928.
PIR	A40308.
RefSeq	NP_000313.2. NM_000322.4.
UniGene	Hs.654489.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000230381.
PTM databases
PhosphoSite	P23942.
Polymorphism databases
DMDM	132212.
Proteomic databases
PaxDb	P23942.
PRIDE	P23942.
Protocols and materials databases
DNASU	5961.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000230381; ENSP00000230381; ENSG00000112619.
GeneID	5961.
KEGG	hsa:5961.
UCSC	uc003osk.3. human.
Organism-specific databases
CTD	5961.
GeneCards	GC06M042664.
H-InvDB	HIX0025091.
HGNC	HGNC:9942. PRPH2.
HPA	HPA029458.
MIM	136880. phenotype. 169150. phenotype. 179605. gene. 268000. phenotype. 608133. phenotype. 608161. phenotype. 613105. phenotype.
neXtProt	NX_P23942.
Orphanet	99000. Adult-onset foveomacular vitelliform dystrophy. 99001. Butterfly-shaped pigment dystrophy. 75377. Central areolar choroidal dystrophy. 1872. Cone rod dystrophy. 227796. Fundus albipunctatus. 791. Retinitis pigmentosa. 52427. Retinitis punctata albescens.
PharmGKB	PA34310.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG237707.
HOGENOM	HOG000026780.
HOVERGEN	HBG004964.
InParanoid	P23942.
KO	K07607.
OrthoDB	EOG41VK37.
Gene expression databases
Bgee	P23942.
CleanEx	HS_PRPH. HS_PRPH2.
Genevestigator	P23942.
GermOnline	ENSG00000112619. Homo sapiens.
Family and domain databases
InterPro	IPR000830. Peripherin/rom-1. IPR018498. Peripherin/rom-1_CS. IPR018499. Tetraspanin/Peripherin. IPR008952. Tetraspanin_EC2. [Graphical view]
Pfam	PF00335. Tetraspannin. 1 hit. [Graphical view]
PRINTS	PR00218. PERIPHERNRDS.
SUPFAM	SSF48652. Tetraspanin. 1 hit.
PROSITE	PS00930. RDS_ROM1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	5961.
NextBio	23208.
SOURCE	Search...

Entry information

Entry name

PRPH2_HUMAN

Accession

Primary (citable) accession number: P23942
Secondary accession number(s): Q5TFH5, Q6DK65

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	May 1, 2013
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.