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Database: UniProt
Entry: P70628
LinkDB: P70628
Original site: P70628 
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   07-NOV-2018, entry version 111.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   the 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.,
RA   Young W.S. III, Hollyfield J.G.;
RT   "SPACRCAN in the developing retina and pineal gland of the rat:
RT   spatial and temporal pattern of gene expression and protein
RT   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-
CC       sensitive photoreceptor outer segment. Binds heparin.
CC       {ECO:0000269|PubMed:11406817}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in the pineal gland and the outer
CC       layer of the retina. {ECO:0000269|PubMed:8883960}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the photoreceptor cells of the
CC       retina at E16 and in pineal gland at E21. Expressed at P5 in
CC       photoreceptor 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};
DR   EMBL; U76717; AAC52891.1; ALT_INIT; mRNA.
DR   UniGene; Rn.10612; -.
DR   ProteinModelPortal; P70628; -.
DR   SMR; P70628; -.
DR   STRING; 10116.ENSRNOP00000046981; -.
DR   PhosphoSitePlus; P70628; -.
DR   PaxDb; P70628; -.
DR   PRIDE; P70628; -.
DR   UCSC; RGD:708358; rat.
DR   RGD; 708358; Impg2.
DR   eggNOG; ENOG410IH0G; Eukaryota.
DR   eggNOG; ENOG410Y9FF; LUCA.
DR   HOGENOM; HOG000113064; -.
DR   HOVERGEN; HBG108006; -.
DR   InParanoid; P70628; -.
DR   PhylomeDB; P70628; -.
DR   PRO; PR:P70628; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033165; C:interphotoreceptor matrix; IEA:InterPro.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR   GO; GO:0007601; P:visual perception; IEA:InterPro.
DR   Gene3D; 3.30.70.960; -; 1.
DR   InterPro; IPR013032; EGF-like_CS.
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   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Heparin-binding; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     28       {ECO:0000255}.
FT   CHAIN        29   1241       Interphotoreceptor matrix proteoglycan 2.
FT                                /FTId=PRO_0000320151.
FT   TOPO_DOM     29   1104       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1105   1125       Helical. {ECO:0000255}.
FT   TOPO_DOM   1126   1241       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      235    349       SEA 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00188}.
FT   DOMAIN      900   1013       SEA 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00188}.
FT   DOMAIN     1013   1054       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1055   1096       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REGION      255    263       Hyaluronan-binding motif involved in
FT                                chondroitin sulfate A-binding.
FT                                {ECO:0000250}.
FT   REGION     1083   1091       Hyaluronan-binding motif involved in
FT                                chondroitin sulfate C-binding.
FT                                {ECO:0000250}.
FT   REGION     1128   1136       Hyaluronan-binding motif involved in
FT                                chondroitin sulfate A- and C-binding.
FT                                {ECO:0000250}.
FT   REGION     1139   1145       Hyaluronan-binding motif involved in
FT                                chondroitin sulfate C-binding.
FT                                {ECO:0000250}.
FT   REGION     1210   1218       Hyaluronan-binding motif involved in
FT                                chondroitin sulfate A- and C-binding
FT                                motif. {ECO:0000250}.
FT   CARBOHYD    193    193       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    225    225       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    231    231       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    297    297       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    316    316       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    366    366       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    429    429       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    430    430       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    431    431       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    817    817       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    841    841       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    945    945       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    959    959       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID   1017   1028       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1022   1039       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1041   1053       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1057   1070       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1064   1080       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1082   1095       {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
//
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