IMPG2_CHICK
ID IMPG2_CHICK Reviewed; 1423 AA.
AC Q1XI86;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Interphotoreceptor matrix proteoglycan 2;
DE AltName: Full=Sialoprotein associated with cones and rods proteoglycan;
DE Short=Spacrcan;
DE Flags: Precursor;
GN Name=IMPG2;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RC TISSUE=Retina;
RX PubMed=16469746; DOI=10.1074/jbc.m508161200;
RA Inoue Y., Yoneda M., Zhao J., Miyaishi O., Ohno-Jinno A., Kataoka T.,
RA Isogai Z., Kimata K., Iwaki M., Zako M.;
RT "Molecular cloning and characterization of chick SPACRCAN.";
RL J. Biol. Chem. 281:10381-10388(2006).
CC -!- FUNCTION: Chondroitin sulfate- and hyaluronan-binding proteoglycan
CC involved in the organization of interphotoreceptor matrix.
CC {ECO:0000250|UniProtKB:Q9BZV3}.
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 retina. {ECO:0000269|PubMed:16469746}.
CC -!- DEVELOPMENTAL STAGE: Detected in retina at E12 with increased
CC expression up to a peak at E16. {ECO:0000269|PubMed:16469746}.
CC -!- PTM: Highly glycosylated (N- and O-linked carbohydrates).
CC {ECO:0000269|PubMed:16469746}.
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DR EMBL; AB204591; BAE92938.1; -; mRNA.
DR RefSeq; NP_001038104.2; NM_001044639.2.
DR STRING; 9031.ENSGALP00000036121; -.
DR PaxDb; Q1XI86; -.
DR GeneID; 418393; -.
DR KEGG; gga:418393; -.
DR CTD; 50939; -.
DR VEuPathDB; HostDB:geneid_418393; -.
DR eggNOG; ENOG502QT6W; Eukaryota.
DR InParanoid; Q1XI86; -.
DR OrthoDB; 112459at2759; -.
DR PhylomeDB; Q1XI86; -.
DR PRO; PR:Q1XI86; -.
DR Proteomes; UP000000539; 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; IEA:UniProtKB-SubCell.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0005540; F:hyaluronic acid binding; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cell projection; Disulfide bond; EGF-like domain; Extracellular matrix;
KW Glycoprotein; Heparin-binding; Membrane; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1423
FT /note="Interphotoreceptor matrix proteoglycan 2"
FT /id="PRO_0000320152"
FT TOPO_DOM 28..1289
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1290..1310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1311..1423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 245..358
FT /note="SEA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 1083..1196
FT /note="SEA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 1196..1234
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1237..1279
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 203..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..273
FT /note="Hyaluronan-binding motif involved in chondroitin
FT sulfate A-binding"
FT /evidence="ECO:0000250"
FT REGION 417..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1274
FT /note="Hyaluronan-binding motif involved in chondroitin
FT sulfate C-binding"
FT /evidence="ECO:0000250"
FT REGION 1322..1327
FT /note="Hyaluronan-binding motif involved in chondroitin
FT sulfate C-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 425..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1200..1211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1205..1222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1240..1253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1247..1263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1265..1278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1423 AA; 157540 MW; 770AB61AEC4E17FA CRC64;
MFAFLWKISL CLLVLGVITG DPQAVAAEEK QAKDASPTPQ LGVWQFASPS LPPELRKLHG
IVEAEQVNRH LLRRRKRSIL FPSGVKICPD ESVEQAIANH LKYFRLRVCQ ETVWEVFKTF
WDRLPEREEY HTWMSLCEEG TMSIFEMGMN FSQSEEHRSL IVKKLSYTKE AMAGSCTDWS
CGGTPTPASD ADATTLRDAA ANVPPPHEVS IESPPGGTSH EIEDADTTIN NEIKKEDEIP
VRPVTEQMIE FSIVIAGEKY SEELSDPDTA KYQLLSEQFV SQIQNVFEGL PGYKNIHVLE
FSSPEEDSGV EVHYAVTFDG EAISNATWDL INLHSNKVED NSFMGIEDNP TVVYTISDFQ
DYIAEILQKN ALLENTSLTL DPNSLQLINV KEILHPTQED PSWITEHPTV LEHVEFDDNT
FSAERPSADE STVSNTLPFD FTKPDSTLDS EESDDNEIRP RPESLDSEVS LIPEAPLSSE
ADVTSLPDGL XLADWNQTPA LVTAPVIEHD SLDSLEWLSA PDSSDEFEDT GLSDDFLLPS
SPSSHLVPEE PPSTDDYTAP LLSAPTVASS SVIETDTKRT VTAEKEVVTQ GSPADSSSAD
SLLHEXVEES PFPLEVHPVE GEXDIYLGDR MIFDDGSGSA FDGSGKGMEP SIWPWDVATL
EPVFYPGPDS WLDDDNDSLP FRTEDIPEGL ILDYILNSGN KLDDDPSKDE NEGVASIKEN
FLDESEIFVF PETTTQQVPL LQTGEPSSVE TSTQMETLSM DDDSFVKPSF VLEPPEDYSF
ADLPTGEDLF LPHSTGVSVE DTLLTSTVTL GXEDSLLTST VAFSVEQPEE SSVGQEIISE
AXEHQNEDRP TVEELFTAGQ SNVGEAATVG YLDKSSLETV LTAEPFEVST DTSTEEQQSL
DSSLADRDTG LAIRKPADVW PTDRVLEKTL DQTVQSAVPT AAQVSTAVPS LIHQATALEG
FAGQDGTEHD THVSMSISTI LNSYVTITAD TVELPSHLPP MTTTVSSSVV TLAKVGDETT
RVLDVSVDLD HVSMVSFSPE PSEEAKSMTD SHMELTTHAH STEMAGVAWP THEIHNSTPV
PSRALVVFFS LRVTNMMFSE DLFNKNSPEY KALEQRFLEL LVPYLQSNLT GFQNLEILNF
RNGSIVVNSR MKFAKPVPRN VTNAVYMILE DFCNTAYHTM NLAIDKYSLD VESGEQADPC
KFQACNEFSE CLVNRWSGEA ECVCNPGYLS IDGLPCNSIC DLQPNFCLND GKCDISPGQG
AICRCRVGEN WWYRGEHCEE YVSEPLVVGI AIASVAGFLL VASAVIFFLA RTLRDQYTKS
DTEDSQGQGD SLSSIENAVK YNPMYESDTT GYSHYYRRYP QLTSYSSTSA ETSTDYSSEE
IRHIYENSEL TKEEIQDRIR IIELYAKDRQ FAEFVRQHQM KLL
