IMPG1_RAT
ID IMPG1_RAT Reviewed; 798 AA.
AC Q9ET62;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 23-FEB-2022, entry version 88.
DE RecName: Full=Interphotoreceptor matrix proteoglycan 1;
DE AltName: Full=Mucin-like glycoprotein associated with photoreceptor cells;
DE AltName: Full=Sialoprotein associated with cones and rods;
DE Flags: Precursor;
GN Name=Impg1 {ECO:0000312|RGD:620499}; Synonyms=Mlgapc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11914607; DOI=10.1159/000048330;
RA Uehara F., Ohba N., Ozawa M.;
RT "Mucin-like glycoprotein associated with photoreceptor cells in the
RT postnatal developing rat retina.";
RL Ophthalmic Res. 34:63-69(2002).
CC -!- FUNCTION: Chondroitin sulfate-, heparin- and hyaluronan-binding protein
CC (By similarity). May serve to form a basic macromolecular scaffold
CC comprising the insoluble interphotoreceptor matrix (By similarity).
CC {ECO:0000250|UniProtKB:Q17R60, ECO:0000250|UniProtKB:Q8JIR8}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer
CC segment {ECO:0000250|UniProtKB:Q17R60}. Secreted, extracellular space,
CC extracellular matrix, interphotoreceptor matrix
CC {ECO:0000250|UniProtKB:Q17R60}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:Q8R1W8}.
CC -!- PTM: Highly glycosylated (N- and O-linked carbohydrates and sialic
CC acid). {ECO:0000250|UniProtKB:Q17R60}.
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DR EMBL; AB047843; BAB12253.1; -; mRNA.
DR RefSeq; NP_076448.1; NM_023958.1.
DR STRING; 10116.ENSRNOP00000017048; -.
DR GlyGen; Q9ET62; 7 sites.
DR PaxDb; Q9ET62; -.
DR GeneID; 66014; -.
DR KEGG; rno:66014; -.
DR UCSC; RGD:620499; rat.
DR CTD; 3617; -.
DR RGD; 620499; Impg1.
DR eggNOG; ENOG502QTXX; Eukaryota.
DR InParanoid; Q9ET62; -.
DR OrthoDB; 112459at2759; -.
DR PhylomeDB; Q9ET62; -.
DR PRO; PR:Q9ET62; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0033165; C:interphotoreceptor matrix; ISO:RGD.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
DR GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0005540; F:hyaluronic acid binding; ISS:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0007601; P:visual perception; IEA:InterPro.
DR InterPro; IPR039861; IMPG.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR PANTHER; PTHR12199; PTHR12199; 1.
DR Pfam; PF01390; SEA; 2.
DR SMART; SM00200; SEA; 2.
DR SUPFAM; SSF82671; SSF82671; 2.
DR PROSITE; PS50024; SEA; 2.
PE 2: Evidence at transcript level;
KW Cell projection; Extracellular matrix; Glycoprotein; Heparin-binding;
KW Hyaluronic acid; Receptor; Reference proteome; Repeat; Secreted;
KW Sialic acid; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..798
FT /note="Interphotoreceptor matrix proteoglycan 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000252240"
FT DOMAIN 238..360
FT /note="SEA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 574..687
FT /note="SEA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT REGION 741..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 624..632
FT /note="Heparin- and hyaluronan-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8JIR8"
FT COMPBIAS 741..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 595
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 798 AA; 89950 MW; 0CB9DE49182E347C CRC64;
MNLEIKHAIL VLWIFLQVQG IKDTSTKTHS SGTKNIDKAP RIETTESTSA VHKASTMKRL
FAVAKLRNKR SALFPAVNIC PRESLRQILE SLQEYYRLRV CQEIVWEAYR IFLDRVPDTE
EYQDWVSLCQ KETFCLFDIG KNFSNSQEHL DLLQQRIFQR SFSGRKDDMS PIEILGVPTT
APVLPIDVSS MSLRPFPLPP DDTDLKEVTI KDIQTPIAIR RAELESKPEP THVTEISSEE
KVEFSISLPN HRFKAELTNS RSPYYQELVG QSQLQLQKIF KKLPGFGEIR VLGFRPKKEE
DGSSSTEIQL MAIFKRDHAE SKGPESDLLS LDSNKIERER IHHGAIEDKQ PEAYLTAADL
KKLIIRLLDG DQPLVGGTVP FSDEVTEPLF RPVTQSELPK PLTDVTEDVT LSPELPFSEP
RLESVDIYGP YLPDSSWSRP VTASTSGVGN LPSFTPSIFA LDDQSSPPLM ATGPTAFIPT
LTLPISDYST VRQWPLEVSH WPESSSDREL STTSSHDTIR DLDEMDVSDT PALSEIAELS
GYDSAPDRFL EMTTPIPTLQ YVTXSSETIA AKGHELVVFF SLRVANMPFS YDLFNKSSLE
YQALEQRFTD LLVPYLRSNL TGFKQLEILS FRNGSVIVNS KVRFAKAVPY NLTQAVRGVL
EDLRSTAAQE LNLEIESYSL DIEPADQADP CKFLDCGKFA QCIKNELTEE AECRCRQGHE
SHGTLEYQEL NLCPPGKTCE ASQGQATPCR PPDHSTNQAR QPSVKKLQRQ QNKVVKKRNS
ELSATDFEEL DDQDWEGN
