IMPG1_MOUSE
ID IMPG1_MOUSE Reviewed; 798 AA.
AC Q8R1W8; Q9CTP8; Q9ES62; Q9ET31;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Interphotoreceptor matrix proteoglycan 1;
DE AltName: Full=Interphotoreceptor matrix proteoglycan of 150 kDa;
DE Short=IPM-150;
DE AltName: Full=Sialoprotein associated with cones and rods;
DE Flags: Precursor;
GN Name=Impg1 {ECO:0000312|MGI:MGI:1926876};
GN Synonyms=Spacr {ECO:0000303|PubMed:10995555};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG32162.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10995555; DOI=10.1006/exer.2000.0888;
RA Lee J.W., Chen Q., Rayborn M.E., Shadrach K.G., Crabb J.W., Rodriguez I.R.,
RA Hollyfield J.G.;
RT "SPACR in the interphotoreceptor matrix of the mouse retina: molecular,
RT biochemical and immunohistochemical characterization.";
RL Exp. Eye Res. 71:341-352(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAG00796.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10958699;
RA Kuehn M.H., Wietecki D.T., Hageman G.S.;
RT "Molecular characterization of the murine orthologue of the human retinal
RT proteoglycan IPM 150.";
RL Mol. Vis. 6:148-156(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH22970.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye {ECO:0000312|EMBL:AAH22970.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAB32231.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-293 (ISOFORM 3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB32231.3};
RC TISSUE=Retina {ECO:0000312|EMBL:BAB32231.3};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29777959; DOI=10.1016/j.actbio.2018.05.023;
RA Felemban M., Dorgau B., Hunt N.C., Hallam D., Zerti D., Bauer R., Ding Y.,
RA Collin J., Steel D., Krasnogor N., Al-Aama J., Lindsay S., Mellough C.,
RA Lako M.;
RT "Extracellular matrix component expression in human pluripotent stem cell-
RT derived retinal organoids recapitulates retinogenesis in vivo and reveals
RT an important role for IMPG1 and CD44 in the development of photoreceptors
RT and interphotoreceptor matrix.";
RL Acta Biomater. 74:207-221(2018).
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:0000269|PubMed:10995555, ECO:0000269|PubMed:29777959}.
CC Photoreceptor inner segment {ECO:0000269|PubMed:10995555}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:10958699, ECO:0000269|PubMed:15489334};
CC IsoId=Q8R1W8-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:10995555};
CC IsoId=Q8R1W8-2; Sequence=VSP_052171;
CC Name=3 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8R1W8-3; Sequence=VSP_052172;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the retina (at protein
CC level). {ECO:0000269|PubMed:10958699, ECO:0000269|PubMed:10995555,
CC ECO:0000269|PubMed:29777959}.
CC -!- PTM: Highly glycosylated (N- and O-linked carbohydrates and sialic
CC acid). {ECO:0000250|UniProtKB:Q17R60}.
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DR EMBL; AF229929; AAG32162.1; -; mRNA.
DR EMBL; AF266478; AAG00796.1; -; mRNA.
DR EMBL; BC022970; AAH22970.1; -; mRNA.
DR EMBL; AK020862; BAB32231.3; -; mRNA.
DR CCDS; CCDS57685.1; -. [Q8R1W8-1]
DR RefSeq; NP_071299.3; NM_022016.3. [Q8R1W8-1]
DR RefSeq; XP_006511391.1; XM_006511328.3. [Q8R1W8-1]
DR AlphaFoldDB; Q8R1W8; -.
DR BioGRID; 210997; 3.
DR STRING; 10090.ENSMUSP00000108876; -.
DR GlyGen; Q8R1W8; 12 sites.
DR iPTMnet; Q8R1W8; -.
DR PhosphoSitePlus; Q8R1W8; -.
DR PaxDb; Q8R1W8; -.
DR PRIDE; Q8R1W8; -.
DR ProteomicsDB; 267334; -. [Q8R1W8-1]
DR ProteomicsDB; 267335; -. [Q8R1W8-2]
DR ProteomicsDB; 267336; -. [Q8R1W8-3]
DR Antibodypedia; 55141; 41 antibodies from 11 providers.
DR DNASU; 63859; -.
DR Ensembl; ENSMUST00000085289; ENSMUSP00000082395; ENSMUSG00000032343. [Q8R1W8-3]
DR Ensembl; ENSMUST00000113250; ENSMUSP00000108876; ENSMUSG00000032343. [Q8R1W8-1]
DR GeneID; 63859; -.
DR KEGG; mmu:63859; -.
DR UCSC; uc009qvi.2; mouse. [Q8R1W8-1]
DR CTD; 3617; -.
DR MGI; MGI:1926876; Impg1.
DR VEuPathDB; HostDB:ENSMUSG00000032343; -.
DR eggNOG; ENOG502QTXX; Eukaryota.
DR GeneTree; ENSGT00530000063503; -.
DR HOGENOM; CLU_005111_1_0_1; -.
DR InParanoid; Q8R1W8; -.
DR OMA; FCIFDIG; -.
DR OrthoDB; 112459at2759; -.
DR PhylomeDB; Q8R1W8; -.
DR TreeFam; TF331340; -.
DR BioGRID-ORCS; 63859; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Impg1; mouse.
DR PRO; PR:Q8R1W8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8R1W8; protein.
DR Bgee; ENSMUSG00000032343; Expressed in retinal neural layer and 7 other tissues.
DR ExpressionAtlas; Q8R1W8; baseline and differential.
DR Genevisible; Q8R1W8; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0033165; C:interphotoreceptor matrix; IDA:MGI.
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; IMP:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Extracellular matrix; Glycoprotein;
KW Heparin-binding; Hyaluronic acid; Receptor; Reference proteome; Repeat;
KW Secreted; 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_0000252239"
FT DOMAIN 235..357
FT /note="SEA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 575..688
FT /note="SEA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT REGION 424..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 625..633
FT /note="Heparin- and hyaluronan-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8JIR8"
FT COMPBIAS 431..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..766
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 174
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 634
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10995555"
FT /id="VSP_052171"
FT VAR_SEQ 23..99
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052172"
FT CONFLICT 3
FT /note="L -> F (in Ref. 2; AAG00796)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="L -> F (in Ref. 2; AAG00796)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="K -> I (in Ref. 1; AAG32162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 798 AA; 89474 MW; E875FB5587389D4C CRC64;
MNLQIKHAIF VLGIFLQVQG IKDTSIKIFS SEIKNIDKTP RIETIESTST VHKVSTMKRI
FDLPKLRTKR SALFPAANIC PQESLRQILA SLQEYYRLRV CQEVVWEAYR IFLDRIPDTE
EYQDWVSLCQ KETFCLFDIG KNFSNSQEHL DLLQQRIKQR SFPGRKDETA SMETLEAPTE
APVVPTDVSR MSLGPFPLPS DDTDLKEILS VTLKDIQKPT TESKTEPIHV SEFSSEEKVE
FSISLPNHRF KAELTNSGSP YYQELVGQSQ LQLQKIFKKL PGFGEIRVLG FRPKKEEDGS
SSTEIQLMAI FKRDHAEAKS PDSHLLSLDS NKIESERIHH GVIEDKQPET YLTATDLKKL
IIQLLDGDLS LVEGKIPFGD EVTGTLFRPV TEPDLPKPLA DVTEDATLSP ELPFVEPRLE
AVDREGSELP GMSSKDSSWS PPVSASISRS ENLPSFTPSI FSLDAQSPPP LMTTGPTALI
PKPTLPTIDY STIRQLPLES SHWPASSSDR ELITSSHDTI RDLDGMDVSD TPALSEISEL
SGYDSASGQF LEMTTPIPTV RFITTSSETI ATKGQELVVF FSLRVANMPF SYDLFNKSSL
EYQALEQRFT DLLVPYLRSN LTGFKQLEIL SFRNGSVIVN SKVRFAKAVP YNLTQAVRGV
LEDLRSTAAQ GLNLEIESYS LDIEPADQAD PCKLLDCGKF AQCVKNEWTE EAECRCRQGH
ESHGTLDYQT LNLCPPGKTC VAGREQATPC RPPDHSTNQA QEPGVKKLRQ QNKVVKKRNS
KLSAIGFEEF EDQDWEGN
