IMPG2_RAT
ID IMPG2_RAT Reviewed; 1241 AA.
AC P70628;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Interphotoreceptor matrix proteoglycan 2;
DE AltName: Full=PG10.2;
DE AltName: Full=Sialoprotein associated with cones and rods proteoglycan;
DE Short=Spacrcan;
DE Flags: Precursor;
GN Name=Impg2;
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], AND TISSUE SPECIFICITY.
RX PubMed=8883960; DOI=10.1016/0169-328x(96)00107-6;
RA Wang X., Brownstein M.J., Young W.S. III;
RT "Sequence analysis of PG10.2, a gene expressed in the pineal gland and the
RT outer nuclear layer of the retina.";
RL Brain Res. Mol. Brain Res. 41:269-278(1996).
RN [2]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=11406817; DOI=10.1002/cne.1035;
RA Foletta V.C., Nishiyama K., Rayborn M.E., Shadrach K.G., Young W.S. III,
RA Hollyfield J.G.;
RT "SPACRCAN in the developing retina and pineal gland of the rat: spatial and
RT temporal pattern of gene expression and protein synthesis.";
RL J. Comp. Neurol. 435:354-363(2001).
CC -!- FUNCTION: Chondroitin sulfate- and hyaluronan-binding proteoglycan
CC involved in the organization of interphotoreceptor matrix; may
CC participate in the maturation and maintenance of the light-sensitive
CC photoreceptor outer segment. Binds heparin.
CC {ECO:0000269|PubMed:11406817}.
CC -!- SUBCELLULAR LOCATION: Photoreceptor outer segment membrane
CC {ECO:0000250|UniProtKB:Q80XH2}; Single-pass type I membrane protein
CC {ECO:0000255}. Photoreceptor inner segment membrane
CC {ECO:0000250|UniProtKB:Q80XH2}; Single-pass type I membrane protein
CC {ECO:0000255}. Secreted, extracellular space, extracellular matrix,
CC interphotoreceptor matrix {ECO:0000250|UniProtKB:Q80XH2}.
CC -!- TISSUE SPECIFICITY: Expressed in the pineal gland and the outer layer
CC of the retina. {ECO:0000269|PubMed:8883960}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the photoreceptor cells of the retina
CC at E16 and in pineal gland at E21. Expressed at P5 in photoreceptor
CC cells and P6 in the pineal gland at protein level.
CC {ECO:0000269|PubMed:11406817}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52891.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U76717; AAC52891.1; ALT_INIT; mRNA.
DR AlphaFoldDB; P70628; -.
DR SMR; P70628; -.
DR STRING; 10116.ENSRNOP00000046981; -.
DR GlyGen; P70628; 13 sites.
DR PhosphoSitePlus; P70628; -.
DR PaxDb; P70628; -.
DR UCSC; RGD:708358; rat.
DR RGD; 708358; Impg2.
DR eggNOG; ENOG502QT6W; Eukaryota.
DR InParanoid; P70628; -.
DR PhylomeDB; P70628; -.
DR PRO; PR:P70628; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033165; C:interphotoreceptor matrix; ISO:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; ISO:RGD.
DR GO; GO:0005540; F:hyaluronic acid binding; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; ISO:RGD.
DR GO; GO:0007601; P:visual perception; IEA:InterPro.
DR Gene3D; 3.30.70.960; -; 2.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR039861; IMPG.
DR InterPro; IPR032975; IMPG2.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR PANTHER; PTHR12199; PTHR12199; 1.
DR PANTHER; PTHR12199:SF4; PTHR12199:SF4; 1.
DR Pfam; PF01390; SEA; 2.
DR SMART; SM00200; SEA; 2.
DR SUPFAM; SSF82671; SSF82671; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50024; SEA; 2.
PE 2: Evidence at transcript level;
KW Cell projection; Disulfide bond; EGF-like domain; Extracellular matrix;
KW Glycoprotein; Heparin-binding; Membrane; Receptor; Reference proteome;
KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1241
FT /note="Interphotoreceptor matrix proteoglycan 2"
FT /id="PRO_0000320151"
FT TOPO_DOM 29..1104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1105..1125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1126..1241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 235..349
FT /note="SEA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 900..1013
FT /note="SEA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 1013..1054
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1055..1096
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 206..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..263
FT /note="Hyaluronan-binding motif involved in chondroitin
FT sulfate A-binding"
FT /evidence="ECO:0000250"
FT REGION 431..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1091
FT /note="Hyaluronan-binding motif involved in chondroitin
FT sulfate C-binding"
FT /evidence="ECO:0000250"
FT REGION 1128..1136
FT /note="Hyaluronan-binding motif involved in chondroitin
FT sulfate A- and C-binding"
FT /evidence="ECO:0000250"
FT REGION 1139..1145
FT /note="Hyaluronan-binding motif involved in chondroitin
FT sulfate C-binding"
FT /evidence="ECO:0000250"
FT REGION 1210..1218
FT /note="Hyaluronan-binding motif involved in chondroitin
FT sulfate A- and C-binding motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 206..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 193
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 817
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 841
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 945
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 959
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1017..1028
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1022..1039
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1041..1053
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1057..1070
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1064..1080
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1082..1095
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1241 AA; 137547 MW; BC0FD39E72F0D727 CRC64;
MIMFLPLGRI SLGILILFLT GGNLVSVSEE IQDRMHAVAV LSPKESTDLS LPTRKRQLLD
ATETGRRWPL RRRRSILFPN GVRICPSDTV AEAVANHVKY FKARVCQEAI WEAFRTFWDR
LPGREEYQYW MNLCEDGVTS VFEMGTQFSQ SVEHRHLIME KLTYTKEAES SSCKDQACGP
ELSSPVPIGE TSTLAGAVSS ASYPGAASER SAASPQESIS NEIENVTEQP TPPAAEQIAE
FSIQLLGKQY SEELRDPSSA LYRLLVEEFI SEVEKAFTGL PGYKGIHVLD FRSPKENGSG
IDVHYAVTFN GEAISNTTWD LISLHSNKVE NHGLVELDDK PTAVYTISNF RDYIAETLHQ
NFLMGNSSLN PDPKSLQLIN VRGVLLPQTE EIVWNTQSSS LQVTTSSILD NTLQAEWLSA
DESITTTTTT TISPFGFSSG PPSATGRELH SESTLGDIVS TPKLASPSKV VLSSSPEVLG
GSSLTLHSVT PAVLQIDLPV APEGRTSGSS ILEDDNTEES EDVSIDVLPS SSLIQPVPKE
TVPPMEDSDM ILLTSSPHLT SSVIEDLAKD ITTPSGLDSL ASRVSDKLDV SPWFPDTSVE
KEFIFESGLG SGSGKNVDVI DWPWSETSLE KTTEPLSKSW SEEQDTLLPT ESIEKLHMYF
TEQMIEPSAH RYGDGPIYFT EEESHVRSTI PIFAESATQP TSLISSKHTS DVPDIDSYSV
TKAPFLLATI ANTASTKETD EVNTLLKKGM VQTEPSSPKG LDSKISVARP DMQPVWTILP
ESDTVWARTS SLGKLSRDTL VSTPESADRL WLKASMTQPA ELPPSTHSIQ LEDEVIMAVQ
NISLELDQVG TDYYQPELTQ EQNGKVDSYV EMPTHVHYTE MPLVAQPTKG GVLSRTQTAG
ALVVFFSLRV TNMLFSEDLF NKNSLEYKAL EQRFLELLVP YLQSNLSGFQ NLEILNFRNG
SIVVNSRVKF AESVPPNVNN AIYMILEDFC TTAYQTMNLD IDKYSLDVES GDDANPCKFQ
ACNEFSECLV NPWSGEAKCK CHPGYLSVDE LPCQSVCDLQ PDFCLNDGKC DVMPGHGAIC
RCRVGSNWWY RGQHCEEFVS EPFVIGITIA SVVSLLLVAS AVVFFLAKML QAQNVRRERQ
RPTNRQPDSL SSVENAMKYN PAYESRLAGC EQYEKPYSQH PFYSSASEEV IGGLSREEIR
QMYESSDLSK EEIQERMRIL ELYANDPEFA AFVREHEMEE L
