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Q9BZV3 (IMPG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interphotoreceptor matrix proteoglycan 2
Alternative name(s):
Interphotoreceptor matrix proteoglycan of 200 kDa
Short name=IPM 200
Sialoprotein associated with cones and rods proteoglycan
Short name=Spacrcan
Gene names
Name:IMPG2
Synonyms:IPM200
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1241 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Chondroitin sulfate- and hyaluronan-binding proteoglycan involved in the organization of interphotoreceptor matrix; may participate in the maturation and maintenance of the light-sensitive photoreceptor outer segment. Binds heparin. Ref.2

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Expressed in the retina. Expressed by photoreceptors of the interphotoreceptor matrix (IPM) surrounding both rods and cones. IPM occupies the subretinal space between the apices of the retinal pigment epithelium and the neural retina. Detected in the pineal gland. Ref.1 Ref.2

Post-translational modification

Highly glycosylated (N- and O-linked carbohydrates). Ref.2

Involvement in disease

Retinitis pigmentosa 56 (RP56) [MIM:613581]: 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.5

Maculopathy, IMPG2-related (MACLP-IMPG2) [MIM:613581]: A mild maculopathy characterized by full-field electroretinogram responses within normal limits, normal color vision, elevation of the photoreceptor layer in the foveal region and mild nuclear sclerosis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5

Sequence similarities

Contains 2 EGF-like domains.

Contains 2 SEA domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 12411219Interphotoreceptor matrix proteoglycan 2
PRO_0000320149

Regions

Topological domain23 – 10991077Extracellular Potential
Transmembrane1100 – 112021Helical; Potential
Topological domain1121 – 1241121Cytoplasmic Potential
Domain239 – 353115SEA 1
Domain897 – 1010114SEA 2
Domain1010 – 105142EGF-like 1
Domain1052 – 109342EGF-like 2
Region259 – 2679Hyaluronan-binding motif involved in chondroitin sulfate A-binding By similarity
Region1080 – 10889Hyaluronan-binding motif involved in chondroitin sulfate C-binding By similarity
Region1125 – 11339Hyaluronan-binding motif involved in chondroitin sulfate A- and C-binding By similarity
Region1136 – 114510Hyaluronan-binding motif involved in chondroitin sulfate C-binding By similarity
Region1210 – 12189Hyaluronan-binding motif involved in chondroitin sulfate A- and C-binding motif By similarity

Amino acid modifications

Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation1901O-linked (GalNAc...) Potential
Glycosylation1921O-linked (GalNAc...) Potential
Glycosylation3011N-linked (GlcNAc...) Potential
Glycosylation3201N-linked (GlcNAc...) Potential
Glycosylation3701N-linked (GlcNAc...) Potential
Glycosylation5441O-linked (GalNAc...) Potential
Glycosylation5561O-linked (GalNAc...) Potential
Glycosylation9421N-linked (GlcNAc...) Potential
Glycosylation9561N-linked (GlcNAc...) Potential
Disulfide bond1014 ↔ 1025 By similarity
Disulfide bond1019 ↔ 1036 By similarity
Disulfide bond1038 ↔ 1050 By similarity
Disulfide bond1054 ↔ 1067 By similarity
Disulfide bond1061 ↔ 1077 By similarity
Disulfide bond1079 ↔ 1092 By similarity

Natural variations

Natural variant1241F → L in MACLP-IMPG2. Ref.5
VAR_064336
Natural variant3441K → N.
Corresponds to variant rs34375459 [ dbSNP | Ensembl ].
VAR_039144
Natural variant6741T → I. Ref.1 Ref.2 Ref.4
Corresponds to variant rs571391 [ dbSNP | Ensembl ].
VAR_039145
Natural variant10131P → L. Ref.4
Corresponds to variant rs116450347 [ dbSNP | Ensembl ].
VAR_039146

Experimental info

Sequence conflict51P → L in AAF13154. Ref.2
Sequence conflict771I → T in AAF13154. Ref.2
Sequence conflict6681E → V in AAF13154. Ref.2
Sequence conflict7151Y → C in AAF06999. Ref.1
Sequence conflict10121N → T in AAG49889. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9BZV3 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: E72D7BFB84824078

FASTA1,241138,621
        10         20         30         40         50         60 
MIMFPLFGKI SLGILIFVLI EGDFPSLTAQ TYLSIEEIQE PKSAVSFLLP EESTDLSLAT 

        70         80         90        100        110        120 
KKKQPLDRRE TERQWLIRRR RSILFPNGVK ICPDESVAEA VANHVKYFKV RVCQEAVWEA 

       130        140        150        160        170        180 
FRTFWDRLPG REEYHYWMNL CEDGVTSIFE MGTNFSESVE HRSLIMKKLT YAKETVSSSE 

       190        200        210        220        230        240 
LSSPVPVGDT STLGDTTLSV PHPEVDAYEG ASESSLERPE ESISNEIENV IEEATKPAGE 

       250        260        270        280        290        300 
QIAEFSIHLL GKQYREELQD SSSFHHQHLE EEFISEVENA FTGLPGYKEI RVLEFRSPKE 

       310        320        330        340        350        360 
NDSGVDVYYA VTFNGEAISN TTWDLISLHS NKVENHGLVE LDDKPTVVYT ISNFRDYIAE 

       370        380        390        400        410        420 
TLQQNFLLGN SSLNPDPDSL QLINVRGVLR HQTEDLVWNT QSSSLQATPS SILDNTFQAA 

       430        440        450        460        470        480 
WPSADESITS SIPPLDFSSG PPSATGRELW SESPLGDLVS THKLAFPSKM GLSSSPEVLE 

       490        500        510        520        530        540 
VSSLTLHSVT PAVLQTGLPV ASEERTSGSH LVEDGLANVE ESEDFLSIDS LPSSSFTQPV 

       550        560        570        580        590        600 
PKETIPSMED SDVSLTSSPY LTSSIPFGLD SLTSKVKDQL KVSPFLPDAS MEKELIFDGG 

       610        620        630        640        650        660 
LGSGSGQKVD LITWPWSETS SEKSAEPLSK PWLEDDDSLL PAEIEDKKLV LVDKMDSTDQ 

       670        680        690        700        710        720 
ISKHSKYEHD DRSTHFPEEE PLSGPAVPIF ADTAAESASL TLPKHISEVP GVDDYSVTKA 

       730        740        750        760        770        780 
PLILTSVAIS ASTDKSDQAD AILREDMEQI TESSNYEWFD SEVSMVKPDM QTLWTILPES 

       790        800        810        820        830        840 
ERVWTRTSSL EKLSRDILAS TPQSADRLWL SVTQSTKLPP TTISTLLEDE VIMGVQDISL 

       850        860        870        880        890        900 
ELDRIGTDYY QPEQVQEQNG KVGSYVEMST SVHSTEMVSV AWPTEGGDDL SYTQTSGALV 

       910        920        930        940        950        960 
VFFSLRVTNM MFSEDLFNKN SLEYKALEQR FLELLVPYLQ SNLTGFQNLE ILNFRNGSIV 

       970        980        990       1000       1010       1020 
VNSRMKFANS VPPNVNNAVY MILEDFCTTA YNTMNLAIDK YSLDVESGDE ANPCKFQACN 

      1030       1040       1050       1060       1070       1080 
EFSECLVNPW SGEAKCRCFP GYLSVEERPC QSLCDLQPDF CLNDGKCDIM PGHGAICRCR 

      1090       1100       1110       1120       1130       1140 
VGENWWYRGK HCEEFVSEPV IIGITIASVV GLLVIFSAII YFFIRTLQAH HDRSERESPF 

      1150       1160       1170       1180       1190       1200 
SGSSRQPDSL SSIENAVKYN PVYESHRAGC EKYEGPYPQH PFYSSASGDV IGGLSREEIR 

      1210       1220       1230       1240 
QMYESSELSR EEIQERMRVL ELYANDPEFA AFVREQQVEE V 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization and genomic mapping of human IPM 200, a second member of a novel family of proteoglycans."
Kuehn M.H., Hageman G.S.
Mol. Cell Biol. Res. Commun. 2:103-110(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, VARIANT ILE-674.
[2]"SPACRCAN, a novel human interphotoreceptor matrix hyaluronan-binding proteoglycan synthesized by photoreceptors and pinealocytes."
Acharya S., Foletta V.C., Lee J.W., Rayborn M.E., Rodriguez I.R., Young W.S. III, Hollyfield J.G.
J. Biol. Chem. 275:6945-6955(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 82-86; 123-127 AND 582-593, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, FUNCTION, GLYCOSYLATION, VARIANT ILE-674.
[3]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Organization of the human IMPG2 gene and its evaluation as a candidate gene in age-related macular degeneration and other retinal degenerative disorders."
Kuehn M.H., Stone E.M., Hageman G.S.
Invest. Ophthalmol. Vis. Sci. 42:3123-3129(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ILE-674 AND LEU-1013.
[5]"Mutations in IMPG2, encoding interphotoreceptor matrix proteoglycan 2, cause autosomal-recessive retinitis pigmentosa."
Bandah-Rozenfeld D., Collin R.W., Banin E., van den Born L.I., Coene K.L., Siemiatkowska A.M., Zelinger L., Khan M.I., Lefeber D.J., Erdinest I., Testa F., Simonelli F., Voesenek K., Blokland E.A., Strom T.M., Klaver C.C., Qamar R., Banfi S. expand/collapse author list , Cremers F.P., Sharon D., den Hollander A.I.
Am. J. Hum. Genet. 87:199-208(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MACLP-IMPG2 LEU-124, INVOLVEMENT IN RP56.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF173155 mRNA. Translation: AAF06999.1.
AF271379 expand/collapse EMBL AC list , AF271363, AF271364, AF271365, AF271366, AF271367, AF271368, AF271369, AF271370, AF271371, AF271372, AF271373, AF271374, AF271375, AF271376, AF271377, AF271378 Genomic DNA. Translation: AAG49889.1.
AF157624 mRNA. Translation: AAF13154.1.
AC068764 Genomic DNA. No translation available.
CCDSCCDS2940.1.
RefSeqNP_057331.2. NM_016247.3.
UniGeneHs.209249.

3D structure databases

ProteinModelPortalQ9BZV3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000193391.

PTM databases

PhosphoSiteQ9BZV3.

Polymorphism databases

DMDM296439325.

Proteomic databases

PaxDbQ9BZV3.
PRIDEQ9BZV3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000193391; ENSP00000193391; ENSG00000081148.
GeneID50939.
KEGGhsa:50939.
UCSCuc003duq.2. human.

Organism-specific databases

CTD50939.
GeneCardsGC03M100944.
GeneReviewsIMPG2.
H-InvDBHIX0030730.
HGNCHGNC:18362. IMPG2.
MIM607056. gene.
613581. phenotype.
neXtProtNX_Q9BZV3.
Orphanet791. Retinitis pigmentosa.
PharmGKBPA29866.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG17485.
HOGENOMHOG000113064.
HOVERGENHBG108006.
InParanoidQ9BZV3.
OMAWPWSETS.
OrthoDBEOG7TXKFR.
PhylomeDBQ9BZV3.
TreeFamTF331340.

Gene expression databases

ArrayExpressQ9BZV3.
BgeeQ9BZV3.
CleanExHS_IMPG2.
GenevestigatorQ9BZV3.

Family and domain databases

Gene3D3.30.70.960. 2 hits.
InterProIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR000082. SEA_dom.
[Graphical view]
PfamPF01390. SEA. 2 hits.
[Graphical view]
SMARTSM00200. SEA. 2 hits.
[Graphical view]
SUPFAMSSF82671. SSF82671. 2 hits.
PROSITEPS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS50024. SEA. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi50939.
NextBio53387.
PROQ9BZV3.
SOURCESearch...

Entry information

Entry nameIMPG2_HUMAN
AccessionPrimary (citable) accession number: Q9BZV3
Secondary accession number(s): A8MWT5, Q9UKD4, Q9UKK5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM