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Protein

Interphotoreceptor matrix proteoglycan 2

Gene

Impg2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Interphotoreceptor matrix proteoglycan 2
Alternative name(s):
PG10.2
Sialoprotein associated with cones and rods proteoglycan
Short name:
Spacrcan
Gene namesi
Name:Impg2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi708358. Impg2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini29 – 1104ExtracellularSequence analysisAdd BLAST1076
Transmembranei1105 – 1125HelicalSequence analysisAdd BLAST21
Topological domaini1126 – 1241CytoplasmicSequence analysisAdd BLAST116

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000032015129 – 1241Interphotoreceptor matrix proteoglycan 2Add BLAST1213

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi193O-linked (GalNAc...)Sequence analysis1
Glycosylationi225N-linked (GlcNAc...)Sequence analysis1
Glycosylationi231O-linked (GalNAc...)Sequence analysis1
Glycosylationi297N-linked (GlcNAc...)Sequence analysis1
Glycosylationi316N-linked (GlcNAc...)Sequence analysis1
Glycosylationi366N-linked (GlcNAc...)Sequence analysis1
Glycosylationi429O-linked (GalNAc...)Sequence analysis1
Glycosylationi430O-linked (GalNAc...)Sequence analysis1
Glycosylationi431O-linked (GalNAc...)Sequence analysis1
Glycosylationi817O-linked (GalNAc...)Sequence analysis1
Glycosylationi841N-linked (GlcNAc...)Sequence analysis1
Glycosylationi945N-linked (GlcNAc...)Sequence analysis1
Glycosylationi959N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1017 ↔ 1028PROSITE-ProRule annotation
Disulfide bondi1022 ↔ 1039PROSITE-ProRule annotation
Disulfide bondi1041 ↔ 1053PROSITE-ProRule annotation
Disulfide bondi1057 ↔ 1070PROSITE-ProRule annotation
Disulfide bondi1064 ↔ 1080PROSITE-ProRule annotation
Disulfide bondi1082 ↔ 1095PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP70628.
PRIDEiP70628.

PTM databases

PhosphoSitePlusiP70628.

Expressioni

Tissue specificityi

Expressed in the pineal gland and the outer layer of the retina.1 Publication

Developmental stagei

Expressed in the photoreceptor cells of the retina at E16 and in pineal gland at E21. Expressed at P5 in photoreceptor cells and P6 in the pineal gland at protein level.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000046981.

Structurei

3D structure databases

ProteinModelPortaliP70628.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini235 – 349SEA 1PROSITE-ProRule annotationAdd BLAST115
Domaini900 – 1013SEA 2PROSITE-ProRule annotationAdd BLAST114
Domaini1013 – 1054EGF-like 1PROSITE-ProRule annotationAdd BLAST42
Domaini1055 – 1096EGF-like 2PROSITE-ProRule annotationAdd BLAST42

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni255 – 263Hyaluronan-binding motif involved in chondroitin sulfate A-bindingBy similarity9
Regioni1083 – 1091Hyaluronan-binding motif involved in chondroitin sulfate C-bindingBy similarity9
Regioni1128 – 1136Hyaluronan-binding motif involved in chondroitin sulfate A- and C-bindingBy similarity9
Regioni1139 – 1145Hyaluronan-binding motif involved in chondroitin sulfate C-bindingBy similarity7
Regioni1210 – 1218Hyaluronan-binding motif involved in chondroitin sulfate A- and C-binding motifBy similarity9

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

eggNOGiENOG410IH0G. Eukaryota.
ENOG410Y9FF. LUCA.
HOGENOMiHOG000113064.
HOVERGENiHBG108006.
InParanoidiP70628.
PhylomeDBiP70628.

Family and domain databases

Gene3Di3.30.70.960. 2 hits.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR032975. IMPG2.
IPR000082. SEA_dom.
[Graphical view]
PANTHERiPTHR12199:SF4. PTHR12199:SF4. 1 hit.
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.

P70628-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIMFLPLGRI SLGILILFLT GGNLVSVSEE IQDRMHAVAV LSPKESTDLS
60 70 80 90 100
LPTRKRQLLD ATETGRRWPL RRRRSILFPN GVRICPSDTV AEAVANHVKY
110 120 130 140 150
FKARVCQEAI WEAFRTFWDR LPGREEYQYW MNLCEDGVTS VFEMGTQFSQ
160 170 180 190 200
SVEHRHLIME KLTYTKEAES SSCKDQACGP ELSSPVPIGE TSTLAGAVSS
210 220 230 240 250
ASYPGAASER SAASPQESIS NEIENVTEQP TPPAAEQIAE FSIQLLGKQY
260 270 280 290 300
SEELRDPSSA LYRLLVEEFI SEVEKAFTGL PGYKGIHVLD FRSPKENGSG
310 320 330 340 350
IDVHYAVTFN GEAISNTTWD LISLHSNKVE NHGLVELDDK PTAVYTISNF
360 370 380 390 400
RDYIAETLHQ NFLMGNSSLN PDPKSLQLIN VRGVLLPQTE EIVWNTQSSS
410 420 430 440 450
LQVTTSSILD NTLQAEWLSA DESITTTTTT TISPFGFSSG PPSATGRELH
460 470 480 490 500
SESTLGDIVS TPKLASPSKV VLSSSPEVLG GSSLTLHSVT PAVLQIDLPV
510 520 530 540 550
APEGRTSGSS ILEDDNTEES EDVSIDVLPS SSLIQPVPKE TVPPMEDSDM
560 570 580 590 600
ILLTSSPHLT SSVIEDLAKD ITTPSGLDSL ASRVSDKLDV SPWFPDTSVE
610 620 630 640 650
KEFIFESGLG SGSGKNVDVI DWPWSETSLE KTTEPLSKSW SEEQDTLLPT
660 670 680 690 700
ESIEKLHMYF TEQMIEPSAH RYGDGPIYFT EEESHVRSTI PIFAESATQP
710 720 730 740 750
TSLISSKHTS DVPDIDSYSV TKAPFLLATI ANTASTKETD EVNTLLKKGM
760 770 780 790 800
VQTEPSSPKG LDSKISVARP DMQPVWTILP ESDTVWARTS SLGKLSRDTL
810 820 830 840 850
VSTPESADRL WLKASMTQPA ELPPSTHSIQ LEDEVIMAVQ NISLELDQVG
860 870 880 890 900
TDYYQPELTQ EQNGKVDSYV EMPTHVHYTE MPLVAQPTKG GVLSRTQTAG
910 920 930 940 950
ALVVFFSLRV TNMLFSEDLF NKNSLEYKAL EQRFLELLVP YLQSNLSGFQ
960 970 980 990 1000
NLEILNFRNG SIVVNSRVKF AESVPPNVNN AIYMILEDFC TTAYQTMNLD
1010 1020 1030 1040 1050
IDKYSLDVES GDDANPCKFQ ACNEFSECLV NPWSGEAKCK CHPGYLSVDE
1060 1070 1080 1090 1100
LPCQSVCDLQ PDFCLNDGKC DVMPGHGAIC RCRVGSNWWY RGQHCEEFVS
1110 1120 1130 1140 1150
EPFVIGITIA SVVSLLLVAS AVVFFLAKML QAQNVRRERQ RPTNRQPDSL
1160 1170 1180 1190 1200
SSVENAMKYN PAYESRLAGC EQYEKPYSQH PFYSSASEEV IGGLSREEIR
1210 1220 1230 1240
QMYESSDLSK EEIQERMRIL ELYANDPEFA AFVREHEMEE L
Length:1,241
Mass (Da):137,547
Last modified:February 26, 2008 - v2
Checksum:iBC0FD39E72F0D727
GO

Sequence cautioni

The sequence AAC52891 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76717 mRNA. Translation: AAC52891.1. Different initiation.
UniGeneiRn.10612.

Genome annotation databases

UCSCiRGD:708358. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76717 mRNA. Translation: AAC52891.1. Different initiation.
UniGeneiRn.10612.

3D structure databases

ProteinModelPortaliP70628.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000046981.

PTM databases

PhosphoSitePlusiP70628.

Proteomic databases

PaxDbiP70628.
PRIDEiP70628.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:708358. rat.

Organism-specific databases

RGDi708358. Impg2.

Phylogenomic databases

eggNOGiENOG410IH0G. Eukaryota.
ENOG410Y9FF. LUCA.
HOGENOMiHOG000113064.
HOVERGENiHBG108006.
InParanoidiP70628.
PhylomeDBiP70628.

Miscellaneous databases

PROiP70628.

Family and domain databases

Gene3Di3.30.70.960. 2 hits.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR032975. IMPG2.
IPR000082. SEA_dom.
[Graphical view]
PANTHERiPTHR12199:SF4. PTHR12199:SF4. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiIMPG2_RAT
AccessioniPrimary (citable) accession number: P70628
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: November 2, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.