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Q9BZV3

- IMPG2_HUMAN

UniProt

Q9BZV3 - IMPG2_HUMAN

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Protein

Interphotoreceptor matrix proteoglycan 2

Gene

IMPG2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: UniProtKB
  2. heparin binding Source: UniProtKB-KW
  3. hyaluronic acid binding Source: UniProtKB

GO - Biological processi

  1. visual perception Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:IMPG2
Synonyms:IPM200
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:18362. IMPG2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 10991077ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1100 – 112021HelicalSequence AnalysisAdd
BLAST
Topological domaini1121 – 1241121CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. proteinaceous extracellular matrix Source: UniProtKB
  3. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti124 – 1241F → L in MACLP-IMPG2. 1 Publication
VAR_064336

Keywords - Diseasei

Disease mutation, Retinitis pigmentosa

Organism-specific databases

MIMi613581. phenotype.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA29866.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 12411219Interphotoreceptor matrix proteoglycan 2PRO_0000320149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi190 – 1901O-linked (GalNAc...)Sequence Analysis
Glycosylationi192 – 1921O-linked (GalNAc...)Sequence Analysis
Glycosylationi301 – 3011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi320 – 3201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi544 – 5441O-linked (GalNAc...)Sequence Analysis
Glycosylationi556 – 5561O-linked (GalNAc...)Sequence Analysis
Glycosylationi942 – 9421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi956 – 9561N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1014 ↔ 1025PROSITE-ProRule annotation
Disulfide bondi1019 ↔ 1036PROSITE-ProRule annotation
Disulfide bondi1038 ↔ 1050PROSITE-ProRule annotation
Disulfide bondi1054 ↔ 1067PROSITE-ProRule annotation
Disulfide bondi1061 ↔ 1077PROSITE-ProRule annotation
Disulfide bondi1079 ↔ 1092PROSITE-ProRule annotation

Post-translational modificationi

Highly glycosylated (N- and O-linked carbohydrates).1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9BZV3.
PRIDEiQ9BZV3.

PTM databases

PhosphoSiteiQ9BZV3.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ9BZV3.
CleanExiHS_IMPG2.
ExpressionAtlasiQ9BZV3. baseline and differential.
GenevestigatoriQ9BZV3.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000193391.

Structurei

3D structure databases

ProteinModelPortaliQ9BZV3.
SMRiQ9BZV3. Positions 1012-1093.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini239 – 353115SEA 1PROSITE-ProRule annotationAdd
BLAST
Domaini897 – 1010114SEA 2PROSITE-ProRule annotationAdd
BLAST
Domaini1010 – 105142EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini1052 – 109342EGF-like 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni259 – 2679Hyaluronan-binding motif involved in chondroitin sulfate A-bindingBy similarity
Regioni1080 – 10889Hyaluronan-binding motif involved in chondroitin sulfate C-bindingBy similarity
Regioni1125 – 11339Hyaluronan-binding motif involved in chondroitin sulfate A- and C-bindingBy similarity
Regioni1136 – 114510Hyaluronan-binding motif involved in chondroitin sulfate C-bindingBy similarity
Regioni1210 – 12189Hyaluronan-binding motif involved in chondroitin sulfate A- and C-binding motifBy similarity

Sequence similaritiesi

Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 2 SEA domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG17485.
GeneTreeiENSGT00530000063503.
HOGENOMiHOG000113064.
HOVERGENiHBG108006.
InParanoidiQ9BZV3.
OMAiWPWSETS.
OrthoDBiEOG7TXKFR.
PhylomeDBiQ9BZV3.
TreeFamiTF331340.

Family and domain databases

Gene3Di3.30.70.960. 2 hits.
InterProiIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR000082. SEA_dom.
[Graphical view]
PfamiPF01390. SEA. 2 hits.
[Graphical view]
SMARTiSM00200. SEA. 2 hits.
[Graphical view]
SUPFAMiSSF82671. SSF82671. 2 hits.
PROSITEiPS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS50024. SEA. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9BZV3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIMFPLFGKI SLGILIFVLI EGDFPSLTAQ TYLSIEEIQE PKSAVSFLLP
60 70 80 90 100
EESTDLSLAT KKKQPLDRRE TERQWLIRRR RSILFPNGVK ICPDESVAEA
110 120 130 140 150
VANHVKYFKV RVCQEAVWEA FRTFWDRLPG REEYHYWMNL CEDGVTSIFE
160 170 180 190 200
MGTNFSESVE HRSLIMKKLT YAKETVSSSE LSSPVPVGDT STLGDTTLSV
210 220 230 240 250
PHPEVDAYEG ASESSLERPE ESISNEIENV IEEATKPAGE QIAEFSIHLL
260 270 280 290 300
GKQYREELQD SSSFHHQHLE EEFISEVENA FTGLPGYKEI RVLEFRSPKE
310 320 330 340 350
NDSGVDVYYA VTFNGEAISN TTWDLISLHS NKVENHGLVE LDDKPTVVYT
360 370 380 390 400
ISNFRDYIAE TLQQNFLLGN SSLNPDPDSL QLINVRGVLR HQTEDLVWNT
410 420 430 440 450
QSSSLQATPS SILDNTFQAA WPSADESITS SIPPLDFSSG PPSATGRELW
460 470 480 490 500
SESPLGDLVS THKLAFPSKM GLSSSPEVLE VSSLTLHSVT PAVLQTGLPV
510 520 530 540 550
ASEERTSGSH LVEDGLANVE ESEDFLSIDS LPSSSFTQPV PKETIPSMED
560 570 580 590 600
SDVSLTSSPY LTSSIPFGLD SLTSKVKDQL KVSPFLPDAS MEKELIFDGG
610 620 630 640 650
LGSGSGQKVD LITWPWSETS SEKSAEPLSK PWLEDDDSLL PAEIEDKKLV
660 670 680 690 700
LVDKMDSTDQ ISKHSKYEHD DRSTHFPEEE PLSGPAVPIF ADTAAESASL
710 720 730 740 750
TLPKHISEVP GVDDYSVTKA PLILTSVAIS ASTDKSDQAD AILREDMEQI
760 770 780 790 800
TESSNYEWFD SEVSMVKPDM QTLWTILPES ERVWTRTSSL EKLSRDILAS
810 820 830 840 850
TPQSADRLWL SVTQSTKLPP TTISTLLEDE VIMGVQDISL ELDRIGTDYY
860 870 880 890 900
QPEQVQEQNG KVGSYVEMST SVHSTEMVSV AWPTEGGDDL SYTQTSGALV
910 920 930 940 950
VFFSLRVTNM MFSEDLFNKN SLEYKALEQR FLELLVPYLQ SNLTGFQNLE
960 970 980 990 1000
ILNFRNGSIV VNSRMKFANS VPPNVNNAVY MILEDFCTTA YNTMNLAIDK
1010 1020 1030 1040 1050
YSLDVESGDE ANPCKFQACN EFSECLVNPW SGEAKCRCFP GYLSVEERPC
1060 1070 1080 1090 1100
QSLCDLQPDF CLNDGKCDIM PGHGAICRCR VGENWWYRGK HCEEFVSEPV
1110 1120 1130 1140 1150
IIGITIASVV GLLVIFSAII YFFIRTLQAH HDRSERESPF SGSSRQPDSL
1160 1170 1180 1190 1200
SSIENAVKYN PVYESHRAGC EKYEGPYPQH PFYSSASGDV IGGLSREEIR
1210 1220 1230 1240
QMYESSELSR EEIQERMRVL ELYANDPEFA AFVREQQVEE V
Length:1,241
Mass (Da):138,621
Last modified:May 18, 2010 - v3
Checksum:iE72D7BFB84824078
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51P → L in AAF13154. (PubMed:10702256)Curated
Sequence conflicti77 – 771I → T in AAF13154. (PubMed:10702256)Curated
Sequence conflicti668 – 6681E → V in AAF13154. (PubMed:10702256)Curated
Sequence conflicti715 – 7151Y → C in AAF06999. (PubMed:10542133)Curated
Sequence conflicti1012 – 10121N → T in AAG49889. (PubMed:10542133)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti124 – 1241F → L in MACLP-IMPG2. 1 Publication
VAR_064336
Natural varianti344 – 3441K → N.
Corresponds to variant rs34375459 [ dbSNP | Ensembl ].
VAR_039144
Natural varianti674 – 6741T → I.3 Publications
Corresponds to variant rs571391 [ dbSNP | Ensembl ].
VAR_039145
Natural varianti1013 – 10131P → L.1 Publication
Corresponds to variant rs116450347 [ dbSNP | Ensembl ].
VAR_039146

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF173155 mRNA. Translation: AAF06999.1.
AF271379
, 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.
CCDSiCCDS2940.1.
RefSeqiNP_057331.2. NM_016247.3.
UniGeneiHs.209249.

Genome annotation databases

EnsembliENST00000193391; ENSP00000193391; ENSG00000081148.
GeneIDi50939.
KEGGihsa:50939.
UCSCiuc003duq.2. human.

Polymorphism databases

DMDMi296439325.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF173155 mRNA. Translation: AAF06999.1 .
AF271379
, 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.
CCDSi CCDS2940.1.
RefSeqi NP_057331.2. NM_016247.3.
UniGenei Hs.209249.

3D structure databases

ProteinModelPortali Q9BZV3.
SMRi Q9BZV3. Positions 1012-1093.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000193391.

Chemistry

DrugBanki DB08818. Hyaluronan.

PTM databases

PhosphoSitei Q9BZV3.

Polymorphism databases

DMDMi 296439325.

Proteomic databases

PaxDbi Q9BZV3.
PRIDEi Q9BZV3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000193391 ; ENSP00000193391 ; ENSG00000081148 .
GeneIDi 50939.
KEGGi hsa:50939.
UCSCi uc003duq.2. human.

Organism-specific databases

CTDi 50939.
GeneCardsi GC03M100944.
GeneReviewsi IMPG2.
H-InvDB HIX0030730.
HGNCi HGNC:18362. IMPG2.
MIMi 607056. gene.
613581. phenotype.
neXtProti NX_Q9BZV3.
Orphaneti 791. Retinitis pigmentosa.
PharmGKBi PA29866.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG17485.
GeneTreei ENSGT00530000063503.
HOGENOMi HOG000113064.
HOVERGENi HBG108006.
InParanoidi Q9BZV3.
OMAi WPWSETS.
OrthoDBi EOG7TXKFR.
PhylomeDBi Q9BZV3.
TreeFami TF331340.

Miscellaneous databases

ChiTaRSi IMPG2. human.
GenomeRNAii 50939.
NextBioi 53387.
PROi Q9BZV3.
SOURCEi Search...

Gene expression databases

Bgeei Q9BZV3.
CleanExi HS_IMPG2.
ExpressionAtlasi Q9BZV3. baseline and differential.
Genevestigatori Q9BZV3.

Family and domain databases

Gene3Di 3.30.70.960. 2 hits.
InterProi IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR000082. SEA_dom.
[Graphical view ]
Pfami PF01390. SEA. 2 hits.
[Graphical view ]
SMARTi SM00200. SEA. 2 hits.
[Graphical view ]
SUPFAMi SSF82671. SSF82671. 2 hits.
PROSITEi PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS50024. SEA. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: VARIANT MACLP-IMPG2 LEU-124, INVOLVEMENT IN RP56.

Entry informationi

Entry nameiIMPG2_HUMAN
AccessioniPrimary (citable) accession number: Q9BZV3
Secondary accession number(s): A8MWT5, Q9UKD4, Q9UKK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 18, 2010
Last modified: November 26, 2014
This is version 87 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3