IMPG1_CHICK
ID IMPG1_CHICK Reviewed; 928 AA.
AC Q8JIR8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Interphotoreceptor matrix proteoglycan 1;
DE AltName: Full=Sialoprotein associated with cones and rods;
DE Short=SPACR;
DE Flags: Precursor;
GN Name=IMPG1 {ECO:0000250|UniProtKB:Q17R60};
GN Synonyms=SPACR {ECO:0000312|EMBL:BAC00947.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC00947.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RC TISSUE=Retina {ECO:0000312|EMBL:BAC00947.1};
RX PubMed=11991949; DOI=10.1074/jbc.m201279200;
RA Zako M., Iwaki M., Yoneda M., Miyaishi O., Zhao J., Suzuki Y., Takeuchi M.,
RA Miyake G., Ikagawa H., Kimata K.;
RT "Molecular cloning and characterization of chick sialoprotein associated
RT with cones and rods, a developmentally regulated glycoprotein of
RT interphotoreceptor matrix.";
RL J. Biol. Chem. 277:25592-25600(2002).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF LEU-777; LYS-785; GLN-786;
RP GLU-788 AND ARG-793.
RX PubMed=18466325; DOI=10.1111/j.1471-4159.2008.05468.x;
RA Zhao J., Yoneda M., Takeyama M., Miyaishi O., Inoue Y., Kataoka T.,
RA Ohno-Jinno A., Isogai Z., Kimata K., Iwaki M., Zako M.;
RT "Characterization of a motif for specific binding to hyaluronan in chicken
RT SPACR.";
RL J. Neurochem. 106:1117-1124(2008).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF LEU-777; LYS-785; GLN-786;
RP GLU-788 AND ARG-793.
RX PubMed=18786170; DOI=10.1111/j.1471-4159.2008.05669.x;
RA Zhao J., Yoneda M., Takeyama M., Inoue Y., Kataoka T., Ohno-Jinno A.,
RA Isogai Z., Iwaki M., Zako M.;
RT "Competitive binding of heparin with hyaluronan to a specific motif in
RT SPACR.";
RL J. Neurochem. 107:823-831(2008).
CC -!- FUNCTION: Chondroitin sulfate-, heparin- and hyaluronan-binding protein
CC (PubMed:11991949, PubMed:18466325, PubMed:18786170). May serve to form
CC a basic macromolecular scaffold comprising the insoluble
CC interphotoreceptor matrix (By similarity).
CC {ECO:0000250|UniProtKB:Q17R60, ECO:0000269|PubMed:11991949,
CC ECO:0000269|PubMed:18466325, ECO:0000269|PubMed:18786170}.
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:11991949}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:Q8R1W8}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the retina (at protein
CC level) (PubMed:11991949, PubMed:18466325, PubMed:18786170). Localizes
CC to the photoreceptor layer of the interphotoreceptor matrix of the
CC retina (at protein level) (PubMed:11991949).
CC {ECO:0000269|PubMed:11991949, ECO:0000269|PubMed:18466325,
CC ECO:0000269|PubMed:18786170}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected in embryonic retina
CC at 15 dpc and increases with developmental age.
CC {ECO:0000269|PubMed:11991949}.
CC -!- PTM: Highly glycosylated (N- and O-linked carbohydrates and sialic
CC acid). {ECO:0000269|PubMed:11991949}.
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DR EMBL; AB070714; BAC00947.1; -; mRNA.
DR RefSeq; NP_989572.1; NM_204241.1.
DR AlphaFoldDB; Q8JIR8; -.
DR SMR; Q8JIR8; -.
DR STRING; 9031.ENSGALP00000025572; -.
DR PaxDb; Q8JIR8; -.
DR Ensembl; ENSGALT00000025619; ENSGALP00000025572; ENSGALG00000015897.
DR GeneID; 374088; -.
DR KEGG; gga:374088; -.
DR CTD; 3617; -.
DR VEuPathDB; HostDB:geneid_374088; -.
DR eggNOG; ENOG502QTXX; Eukaryota.
DR GeneTree; ENSGT00530000063503; -.
DR HOGENOM; CLU_005111_1_0_1; -.
DR InParanoid; Q8JIR8; -.
DR OMA; FCIFDIG; -.
DR OrthoDB; 112459at2759; -.
DR PhylomeDB; Q8JIR8; -.
DR PRO; PR:Q8JIR8; -.
DR Proteomes; UP000000539; Chromosome 3.
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; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR GO; GO:0005540; F:hyaluronic acid binding; IDA:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:InterPro.
DR Gene3D; 3.30.70.960; -; 2.
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 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..928
FT /note="Interphotoreceptor matrix proteoglycan 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000252241"
FT DOMAIN 231..356
FT /note="SEA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 735..848
FT /note="SEA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT REGION 26..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 785..793
FT /note="Heparin- and hyaluronan-binding"
FT /evidence="ECO:0000269|PubMed:18466325,
FT ECO:0000269|PubMed:18786170"
FT COMPBIAS 164..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 794
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 812
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 777
FT /note="L->R: Increases binding of hyaluronan and heparin."
FT /evidence="ECO:0000269|PubMed:18466325,
FT ECO:0000269|PubMed:18786170"
FT MUTAGEN 785
FT /note="K->N: Reduces binding of hyaluronan and heparin."
FT /evidence="ECO:0000269|PubMed:18466325,
FT ECO:0000269|PubMed:18786170"
FT MUTAGEN 786
FT /note="Q->T: No effect on binding of hyaluronan or
FT heparin."
FT /evidence="ECO:0000269|PubMed:18466325,
FT ECO:0000269|PubMed:18786170"
FT MUTAGEN 788
FT /note="E->V: Increases binding of hyaluronan and heparin."
FT /evidence="ECO:0000269|PubMed:18466325,
FT ECO:0000269|PubMed:18786170"
FT MUTAGEN 793
FT /note="R->S: Reduces binding of hyaluronan and heparin."
FT /evidence="ECO:0000269|PubMed:18466325,
FT ECO:0000269|PubMed:18786170"
SQ SEQUENCE 928 AA; 102684 MW; 4DBB800528C56CA2 CRC64;
MHLKTGLIFL AICLALQVQG SREIPSKTNH GEAKQLADAS GSDKTERTTK RSRVSTIRRI
FDMAKHRTKR SPFFSTGVKI CPQESVKQIL ASHQAYYRLR VCQEAVWEAF RIFLDRIPDT
SEYQNWVTAC QRETFCIFDI GKNFSNSQEH LEIIQRRVKH RTFQERKDEI STDKTGGKKL
EDIPSVSTGP PSASLSTYTL VPNGTLLNEI VNETKTPVKE LGTNTVPELP AEQMVEFSVT
LTDQEYTAEL SDPNSPQYRQ LAAKFQLQMQ KIFEKLPGFK EIHVLGFKQK KEKDGSSSTI
ARYMVNFERD GSEIKSTADD ISTIGSNKVE NEKVPLSAKE EREISATKLT VTDLQQLVAT
ALHEDRSLPV DLGTLRFTDE PIKPSSDFDN DIQGMVTIPL AGPDLDDTIS AELPLVYPSP
ITVDQTRDIF VDEFTTGITD LSREIGGPED FDSNFITSEP AFPTKPSREP PHDRSPDTED
ITTDYQRFTV PFSALVSTDS PAKPEDSYLP PPADESDSND LITDESPTEQ VITPAVYTTG
SFTLPTFLQA TDKDTEAEMK KELVGVTEPL FKEADRDSLS GQAVKMMDEL ESSGDDILVT
TSTYKTLPFL IGSSDLFATQ PEVTFAAALP PDQTLLPTVT SPFYSHSVVI DQSPEVPDTL
MPAAASALPD RASTGVQDIA AELDGAGVKS TAVLDEAEHG SGYISVQTTE PAEVTQAPTL
KYVTTSSMTT AAKGKELVVF FSLRVTNMHF SDDLFNRSSQ EYKALEQQFM QLLLPYLQSN
LTGFKQLEIL NFRNGSVIVN SKMKFARTVP YNITEAVHCV LEDFCDAAAQ HLNLEIDSYS
LDIEPADQAD PCKFMACDEF SKCIMNEWTK EADCLCKPGY ASQDGLPCRS LCEMEPHLCD
NGGKCELVPG RGAVCRSPDQ FTEPGLTS
