IMPG1_BOVIN
ID IMPG1_BOVIN Reviewed; 794 AA.
AC Q9GMS5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-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; Synonyms=MLGAPC;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10937595;
RA Uehara F., Ohba N., Ozawa M.;
RT "Isolation and characterization of mucinlike glycoprotein associated with
RT photoreceptor cells.";
RL Invest. Ophthalmol. Vis. Sci. 41:2759-2765(2000).
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}.
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DR EMBL; AB047844; BAB12254.1; -; mRNA.
DR RefSeq; NP_776787.1; NM_174362.2.
DR AlphaFoldDB; Q9GMS5; -.
DR SMR; Q9GMS5; -.
DR STRING; 9913.ENSBTAP00000028218; -.
DR PaxDb; Q9GMS5; -.
DR PRIDE; Q9GMS5; -.
DR GeneID; 281866; -.
DR KEGG; bta:281866; -.
DR CTD; 3617; -.
DR eggNOG; ENOG502QTXX; Eukaryota.
DR InParanoid; Q9GMS5; -.
DR OrthoDB; 112459at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0033165; C:interphotoreceptor matrix; IEA:UniProtKB-SubCell.
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:0007601; P:visual perception; IEA:InterPro.
DR Gene3D; 3.30.70.960; -; 1.
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..794
FT /note="Interphotoreceptor matrix proteoglycan 1"
FT /id="PRO_0000252237"
FT DOMAIN 236..357
FT /note="SEA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 579..692
FT /note="SEA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT REGION 202..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 629..637
FT /note="Heparin- and hyaluronan-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8JIR8"
FT COMPBIAS 332..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 425
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 794 AA; 89378 MW; 4965FD322FA95841 CRC64;
MHLEAARVIF FLWIFLQVQG IKDLSIKIYG SEIKDIDNAP RTEATKNTAK TYKVSTMRRI
FDLAKHRTKR SAFFPTGVKV CPQESMEQIL ASLQAYYRLR VCQEAVWEAY RIFLDRLPEP
GEYQDWVSVC QQETFCLFDI GKNFSNSQEH LDLLQQRMKQ RNFLERKDEV VTKETLGELG
QTPGLQQTLP VSHPGPCLSL PMTTAQRNPQ LHPSRTPRVP TRERKIEFTD AAEDALEQKV
ELSISLANQK FKSELDNSQS PYYLEVAAKS QLQMQKIFKK LPGFKEIHVS GFRPKKERDG
TSSTEMQLTA IFKKGKAEAK SPASDPLSLD SNKIESEGDP RGTTEEEKQR ELYPTASELR
KLISRALEED QSLDVGTIQF TDEIVGSLPS LDPDTQLVLP TLLTDITKDA TLSPELPLGQ
PRLETVDRAG HSPPGASPTD GWSPPAMTST SLSETLPFFT ASSVFPQTDQ SATDIMSIDQ
TVLIPRLTVP TDDYSAISPL VPEISHLPTS SEDWLSTSSQ DTMEYLDGVD LTKTPTSSEG
PRNSVGMFPA WIIFLENITP DPGLRYITTS AMTVAARGRE LVVFFSLRVA NVPFSTDLFN
KSSLEYQALE QRFTQLLVPN LRSNLTGFKQ LEILNFRNGS VIVNSKVRFA KSVPYNLTKA
VRGVLEDFRS TAAQQLDLEI DSYSLDVEPA DQADPCKFLA CGEFAQCVRN EWTEEAECRC
RSGTQALVLP IEDCEDIPGK GTPCRSLDQS KNQVYEPGVK KFQRQQDNKV TMKRKFELLT
IGYEEFNYQD WEGN
