位置:首页 > 蛋白库 > IMPG2_MOUSE
IMPG2_MOUSE
ID   IMPG2_MOUSE             Reviewed;        1243 AA.
AC   Q80XH2; Q810Y3; Q8C8E4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 128.
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   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]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=12589770; DOI=10.1016/s0014-4835(02)00273-7;
RA   Chen Q., Lee J.W., Nishiyama K., Shadrach K.G., Rayborn M.E.,
RA   Hollyfield J.G.;
RT   "SPACRCAN in the interphotoreceptor matrix of the mouse retina: molecular,
RT   developmental and promoter analysis.";
RL   Exp. Eye Res. 76:1-14(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 965-1243 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
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   [4]
RP   BINDING REGIONS, AND MUTAGENESIS OF ARG-255; ARG-263; ARG-1083; ARG-1091;
RP   1136-ARG--ARG-1139 AND ARG-1147.
RX   PubMed=15044457; DOI=10.1074/jbc.m401584200;
RA   Chen Q., Cai S., Shadrach K.G., Prestwich G.D., Hollyfield J.G.;
RT   "Spacrcan binding to hyaluronan and other glycosaminoglycans. Molecular and
RT   biochemical studies.";
RL   J. Biol. Chem. 279:23142-23150(2004).
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- 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:0000250|UniProtKB:Q9BZV3}.
CC   -!- SUBCELLULAR LOCATION: Photoreceptor outer segment membrane
CC       {ECO:0000269|PubMed:29777959}; Single-pass type I membrane protein
CC       {ECO:0000255}. Photoreceptor inner segment membrane
CC       {ECO:0000269|PubMed:29777959}; Single-pass type I membrane protein
CC       {ECO:0000255}. Secreted, extracellular space, extracellular matrix,
CC       interphotoreceptor matrix {ECO:0000269|PubMed:29777959}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80XH2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80XH2-2; Sequence=VSP_031612;
CC   -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level)
CC       (PubMed:12589770, PubMed:29777959). Expressed in the pineal gland
CC       (PubMed:12589770). {ECO:0000269|PubMed:12589770,
CC       ECO:0000269|PubMed:29777959}.
CC   -!- DEVELOPMENTAL STAGE: Increasing expression in retina from 15 dpc to
CC       adulthood: expressed at P8 when photoreceptor outer segments are in
CC       active stages of elongation; elevated expression at P10 in the
CC       developing IPM and at P15 in the region adjacent to the retina pigment
CC       epithelium (RPE). From P18 to P35, more homogeneously present in the
CC       IPM surrounding both cones and rods. {ECO:0000269|PubMed:12589770}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO21221.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAO21221.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY174061; AAO21221.1; ALT_SEQ; mRNA.
DR   EMBL; BC048863; AAH48863.1; -; mRNA.
DR   EMBL; AK047356; BAC33032.1; -; mRNA.
DR   CCDS; CCDS37358.1; -. [Q80XH2-1]
DR   RefSeq; NP_777365.2; NM_174876.3. [Q80XH2-1]
DR   AlphaFoldDB; Q80XH2; -.
DR   SMR; Q80XH2; -.
DR   STRING; 10090.ENSMUSP00000063648; -.
DR   GlyGen; Q80XH2; 15 sites.
DR   iPTMnet; Q80XH2; -.
DR   PhosphoSitePlus; Q80XH2; -.
DR   PaxDb; Q80XH2; -.
DR   PRIDE; Q80XH2; -.
DR   ProteomicsDB; 266977; -. [Q80XH2-1]
DR   ProteomicsDB; 266978; -. [Q80XH2-2]
DR   Antibodypedia; 32271; 51 antibodies from 20 providers.
DR   DNASU; 224224; -.
DR   Ensembl; ENSMUST00000069936; ENSMUSP00000063648; ENSMUSG00000035270. [Q80XH2-1]
DR   Ensembl; ENSMUST00000160116; ENSMUSP00000125135; ENSMUSG00000035270. [Q80XH2-2]
DR   GeneID; 224224; -.
DR   KEGG; mmu:224224; -.
DR   UCSC; uc007zmm.1; mouse. [Q80XH2-1]
DR   UCSC; uc012agq.1; mouse. [Q80XH2-2]
DR   CTD; 50939; -.
DR   MGI; MGI:3044955; Impg2.
DR   VEuPathDB; HostDB:ENSMUSG00000035270; -.
DR   eggNOG; ENOG502QT6W; Eukaryota.
DR   GeneTree; ENSGT00530000063503; -.
DR   HOGENOM; CLU_005111_0_0_1; -.
DR   InParanoid; Q80XH2; -.
DR   OMA; ESSIWPW; -.
DR   OrthoDB; 112459at2759; -.
DR   PhylomeDB; Q80XH2; -.
DR   TreeFam; TF331340; -.
DR   BioGRID-ORCS; 224224; 2 hits in 74 CRISPR screens.
DR   PRO; PR:Q80XH2; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q80XH2; protein.
DR   Bgee; ENSMUSG00000035270; Expressed in layer of retina and 37 other tissues.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0031012; C:extracellular matrix; TAS:MGI.
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; IDA:MGI.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IDA:MGI.
DR   GO; GO:0005540; F:hyaluronic acid binding; IDA:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:MGI.
DR   GO; GO:0007601; P:visual perception; IEA:InterPro.
DR   Gene3D; 3.30.70.960; -; 1.
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   Alternative splicing; Cell projection; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Heparin-binding; Membrane; Receptor;
KW   Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..1243
FT                   /note="Interphotoreceptor matrix proteoglycan 2"
FT                   /id="PRO_0000320150"
FT   TOPO_DOM        28..1106
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1107..1127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1128..1243
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          205..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   REGION          748..768
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   REGION          1128..1136
FT                   /note="Hyaluronan-binding motif involved in chondroitin
FT                   sulfate A- and C-binding"
FT   REGION          1139..1147
FT                   /note="Hyaluronan-binding motif involved in chondroitin
FT                   sulfate C-binding"
FT   REGION          1212..1220
FT                   /note="Hyaluronan-binding motif involved in chondroitin
FT                   sulfate A- and C-binding motif"
FT   COMPBIAS        205..232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..766
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
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        427
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        582
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        701
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        704
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        712
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        888
FT                   /note="O-linked (GalNAc...) threonine"
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"
FT   VAR_SEQ         381..489
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12589770"
FT                   /id="VSP_031612"
FT   MUTAGEN         255
FT                   /note="R->H: Decreased-binding affinity to hyaluronan."
FT                   /evidence="ECO:0000269|PubMed:15044457"
FT   MUTAGEN         263
FT                   /note="R->H: Decreased-binding affinity to hyaluronan."
FT                   /evidence="ECO:0000269|PubMed:15044457"
FT   MUTAGEN         1083
FT                   /note="R->Q: Decreased-binding affinity to hyaluronan."
FT                   /evidence="ECO:0000269|PubMed:15044457"
FT   MUTAGEN         1091
FT                   /note="R->Q: Decreased-binding affinity to hyaluronan."
FT                   /evidence="ECO:0000269|PubMed:15044457"
FT   MUTAGEN         1136..1139
FT                   /note="RRER->SSES: Most important decrease in binding
FT                   affinity to hyaluronan."
FT                   /evidence="ECO:0000269|PubMed:15044457"
FT   MUTAGEN         1147
FT                   /note="R->G: Important decrease in binding affinity to
FT                   hyaluronan."
FT                   /evidence="ECO:0000269|PubMed:15044457"
SQ   SEQUENCE   1243 AA;  138102 MW;  26C647136491E4D5 CRC64;
     MIMFLPVGRM SLGILILFLT GGNLVSASEE RQEPMHAVSV LSPEKSTDLS LPTRKRQLLD
     ATETGRRWLL RRRRSILFPN GVKICSSETV AEAVANHVKY FKARVCQEAI WEAFRTFWDR
     LPGRDEYRHW MNLCEDGVTS VFEMGAHFSQ SVEHRNLIMK KLAYTREAES SSCKDQSCGP
     ELSFPVPIGE TSTLTGAVSS ASYPGLASES SAASPQESIS NEIENVTEEP TQPAAEQIAE
     FSIQLLGKRY SEELRDPSSA LYRLLVEEFI SEVEKAFTGL PGYKGIRVLE FRAPEENDSG
     IDVHYAVTFN GEAISNTTWD LISLHSNKVE NHGLVEMDDK PTAVYTISNF RDYIAETLHQ
     NFLMGNSSLN PDPKSLQLIN VRGVLLPQTE DIVWNTQSSS LQVTTSSILD NTLQAEWLSA
     DTTTTTTTTI SPFGFSSSSP SATGRELQSQ SALRDVVSTS KLASPTKVVL SSLPEILGGS
     SLTLHSVTPA VLQPDLPVAP EGRTSGSFIL EDGLASTEEL EDTSIDGLPS SPLIQPVPKE
     TVPPMEDSDT ALLSTPHLTS SAIEDLTKDI GTPSGLESLA SNISDQLEVI PWFPDTSVEK
     DFIFESGLGS GSGKDVDVID WPWSETSLEK TTKPLSKSWS EEQDALLPTE GREKLHIDGR
     VDSTEQIIES SEHRYGDRPI HFIEEESHVR STIPIFVESA TPPTSPIFSK HTSDVPDIDS
     YSLTKPPFLP VTIAIPASTK KTDEVLKEDM VHTESSSHKE LDSEVPVSRP DMQPVWTMLP
     ESDTVWTRTS SLGKLSRDTL ASTPESTDRL WLKASMTQST ELPSTTHSTQ LEEEVIMAVQ
     DISLELDQVG TDYYQSELTE EQHGKADSYV EMSTSVHYTE MPIVALPTKG GVLSHTQTAG
     ALVVFFSLRV TNMLFSEDLF NKNSLEYKAL EQRFLELLVP YLQSNLSGFQ NLEILSFRNG
     SIVVNSRVRF AESAPPNVNK AMYRILEDFC TTAYQTMNLD IDKYSLDVES GDEANPCKFQ
     ACNEFSECLV NPWSGEAKCK CYPGYLSVDE LPCQSLCDLQ PDFCLNDGKC DIMPGHGAIC
     RCRVGSNWWY RGQHCEEFVS EPFVIGITIA SVVSFLLVAS AVVFFLVKML QAQNVRRERQ
     RPTSSSRHPD SLSSVENAMK YNPAYESHLA GCELYEKSYS QHPFYSSASE EVIGGLSREE
     IRQMYESSDL SKEEIQERMR ILELYANDPE FAAFVREHQM EEL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024