ID   CSPG4_MOUSE             Reviewed;        2327 AA.
AC   Q8VHY0; G5E892; Q5DTG1; Q8BPI8; Q8CE79;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 3.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Chondroitin sulfate proteoglycan 4;
DE   AltName: Full=Chondroitin sulfate proteoglycan NG2;
DE   AltName: Full=Proteoglycan AN2;
DE   Flags: Precursor;
GN   Name=Cspg4; Synonyms=An2, Kiaa4232, Ng2;
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 1), INTERACTION WITH GRIP1; GRIP2 AND
RP   GRIA2, MUTAGENESIS OF GLN-2324; TYR-2325; TRP-2326 AND VAL-2327, DOMAIN,
RP   AND SUBCELLULAR LOCATION.
RC   TISSUE=Oligodendrocyte;
RX   PubMed=12458226; DOI=10.1074/jbc.m210010200;
RA   Stegmueller J., Werner H., Nave K.-A., Trotter J.;
RT   "The proteoglycan NG2 is complexed with alpha-amino-3-hydroxy-5-methyl-4-
RT   isoxazolepropionic acid (AMPA) receptors by the PDZ glutamate receptor
RT   interaction protein (GRIP) in glial progenitor cells. Implications for
RT   glial-neuronal signaling.";
RL   J. Biol. Chem. 278:3590-3598(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Skin;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 999-2327 (ISOFORM 3).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10036240; DOI=10.1242/jcs.112.6.905;
RA   Grako K.A., Ochiya T., Barritt D., Nishiyama A., Stallcup W.B.;
RT   "PDGF (alpha)-receptor is unresponsive to PDGF-AA in aortic smooth muscle
RT   cells from the NG2 knockout mouse.";
RL   J. Cell Sci. 112:905-915(1999).
RN   [7]
RP   TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=15181153; DOI=10.1091/mbc.e04-03-0236;
RA   Fukushi J., Makagiansar I.T., Stallcup W.B.;
RT   "NG2 proteoglycan promotes endothelial cell motility and angiogenesis via
RT   engagement of galectin-3 and alpha3beta1 integrin.";
RL   Mol. Biol. Cell 15:3580-3590(2004).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130; ASN-1369; ASN-1454;
RP   ASN-2021 AND ASN-2080.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA   Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Proteoglycan playing a role in cell proliferation and
CC       migration which stimulates endothelial cells motility during
CC       microvascular morphogenesis. May also inhibit neurite outgrowth and
CC       growth cone collapse during axon regeneration. Cell surface receptor
CC       for collagen alpha 2(VI) which may confer cells ability to migrate on
CC       that substrate. Binds through its extracellular N-terminus growth
CC       factors, extracellular matrix proteases modulating their activity. May
CC       regulate MPP16-dependent degradation and invasion of type I collagen
CC       participating in melanoma cells invasion properties. May modulate the
CC       plasminogen system by enhancing plasminogen activation and inhibiting
CC       angiostatin. Functions also as a signal transducing protein by binding
CC       through its cytoplasmic C-terminus scaffolding and signaling proteins.
CC       May promote retraction fiber formation and cell polarization through
CC       Rho GTPase activation. May stimulate alpha-4, beta-1 integrin-mediated
CC       adhesion and spreading by recruiting and activating a signaling cascade
CC       through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling
CC       cascades. {ECO:0000269|PubMed:10036240, ECO:0000269|PubMed:15181153}.
CC   -!- SUBUNIT: Interacts with ITGA4 through its chondroitin sulfate
CC       glycosaminoglycan. Interacts with BCAR1, CDC42 and ACK1. Interacts with
CC       MMP16. Interacts with the first PDZ domain of MPDZ. Interacts with
CC       PRKCA. Interacts with LGALS3 and the integrin composed of ITGB1 and
CC       ITGA3. Binds TNC, laminin-1, COL5A1 and COL6A2. Interacts with PLG and
CC       angiostatin. Binds FGF2 and PDGFA (By similarity). Interacts with
CC       GRIP1, GRIP2 and GRIA2. Forms a ternary complex with GRIP1 and GRIA2.
CC       {ECO:0000250, ECO:0000269|PubMed:12458226}.
CC   -!- INTERACTION:
CC       Q8VHY0; P23819: Gria2; NbExp=2; IntAct=EBI-8327479, EBI-77538;
CC       Q8VHY0; Q925T6: Grip1; NbExp=7; IntAct=EBI-8327479, EBI-537752;
CC       Q8VHY0; Q9WTW1: Grip2; Xeno; NbExp=2; IntAct=EBI-8327479, EBI-936045;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12458226};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q00657};
CC       Extracellular side {ECO:0000250|UniProtKB:Q00657}. Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q00657}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:Q00657}; Extracellular side
CC       {ECO:0000250|UniProtKB:Q00657}. Cell projection, lamellipodium membrane
CC       {ECO:0000250|UniProtKB:Q00657}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:Q00657}; Extracellular side
CC       {ECO:0000250|UniProtKB:Q00657}. Cell surface
CC       {ECO:0000250|UniProtKB:Q00657}. Note=Localized at the apical plasma
CC       membrane it relocalizes to the lamellipodia of astrocytoma upon
CC       phosphorylation by PRKCA. Localizes to the retraction fibers. A
CC       fraction may undergo cell surface proteolysis and secretion (By
CC       similarity). Localizes to the plasma membrane of oligodendrocytes
CC       (PubMed:12458226). {ECO:0000250|UniProtKB:Q00657,
CC       ECO:0000269|PubMed:12458226}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8VHY0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VHY0-2; Sequence=VSP_015656;
CC       Name=3;
CC         IsoId=Q8VHY0-3; Sequence=VSP_015657, VSP_015658;
CC   -!- TISSUE SPECIFICITY: Expressed in microcascular pericytes and not
CC       endothelial cells. {ECO:0000269|PubMed:15181153}.
CC   -!- PTM: O-glycosylated; contains glycosaminoglycan chondroitin sulfate
CC       which are required for proper localization and function in stress fiber
CC       formation. Involved in interaction with MMP16 and ITGA4 (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylation by PRKCA regulates its subcellular location and
CC       function in cell motility. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice are unresponsive to PDGF-AA through PDGF-
CC       alpha receptor. {ECO:0000269|PubMed:10036240}.
CC   -!- MISCELLANEOUS: Valuable marker for several incompletely differentiated
CC       precursor cells.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC26150.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF352400; AAL37505.1; -; mRNA.
DR   EMBL; AK028844; BAC26150.1; ALT_SEQ; mRNA.
DR   EMBL; AK075625; BAC35866.1; -; mRNA.
DR   EMBL; AC126257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466522; EDL25876.1; -; Genomic_DNA.
DR   EMBL; AK220559; BAD90326.1; -; mRNA.
DR   CCDS; CCDS23211.1; -. [Q8VHY0-1]
DR   RefSeq; NP_620570.2; NM_139001.2. [Q8VHY0-1]
DR   AlphaFoldDB; Q8VHY0; -.
DR   SMR; Q8VHY0; -.
DR   BioGRID; 228250; 7.
DR   CORUM; Q8VHY0; -.
DR   IntAct; Q8VHY0; 4.
DR   MINT; Q8VHY0; -.
DR   STRING; 10090.ENSMUSP00000038909; -.
DR   GlyConnect; 2213; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q8VHY0; 16 sites, 1 glycan.
DR   GlyGen; Q8VHY0; 17 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q8VHY0; -.
DR   PhosphoSitePlus; Q8VHY0; -.
DR   MaxQB; Q8VHY0; -.
DR   PaxDb; 10090-ENSMUSP00000038909; -.
DR   PeptideAtlas; Q8VHY0; -.
DR   ProteomicsDB; 284040; -. [Q8VHY0-1]
DR   ProteomicsDB; 284041; -. [Q8VHY0-2]
DR   ProteomicsDB; 284042; -. [Q8VHY0-3]
DR   Pumba; Q8VHY0; -.
DR   Antibodypedia; 1108; 881 antibodies from 41 providers.
DR   DNASU; 121021; -.
DR   Ensembl; ENSMUST00000035661.7; ENSMUSP00000038909.6; ENSMUSG00000032911.7. [Q8VHY0-1]
DR   GeneID; 121021; -.
DR   KEGG; mmu:121021; -.
DR   UCSC; uc009ptl.1; mouse. [Q8VHY0-1]
DR   UCSC; uc009ptn.1; mouse. [Q8VHY0-3]
DR   UCSC; uc009pto.1; mouse. [Q8VHY0-2]
DR   AGR; MGI:2153093; -.
DR   CTD; 1464; -.
DR   MGI; MGI:2153093; Cspg4.
DR   VEuPathDB; HostDB:ENSMUSG00000032911; -.
DR   eggNOG; KOG3597; Eukaryota.
DR   GeneTree; ENSGT00940000154091; -.
DR   HOGENOM; CLU_000473_1_0_1; -.
DR   InParanoid; Q8VHY0; -.
DR   OMA; PWPQGTT; -.
DR   OrthoDB; 4072625at2759; -.
DR   PhylomeDB; Q8VHY0; -.
DR   TreeFam; TF316876; -.
DR   Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR   Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR   Reactome; R-MMU-2022923; Dermatan sulfate biosynthesis.
DR   Reactome; R-MMU-2024101; CS/DS degradation.
DR   BioGRID-ORCS; 121021; 3 hits in 80 CRISPR screens.
DR   ChiTaRS; Cspg4; mouse.
DR   PRO; PR:Q8VHY0; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q8VHY0; Protein.
DR   Bgee; ENSMUSG00000032911; Expressed in humerus cartilage element and 212 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042995; C:cell projection; IDA:MGI.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0001726; C:ruffle; IDA:MGI.
DR   GO; GO:0005518; F:collagen binding; ISO:MGI.
DR   GO; GO:0015026; F:coreceptor activity; IDA:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0008347; P:glial cell migration; IDA:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR   GO; GO:0016322; P:neuron remodeling; ISO:MGI.
DR   GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR   GO; GO:0097178; P:ruffle assembly; IDA:MGI.
DR   GO; GO:0006929; P:substrate-dependent cell migration; IGI:MGI.
DR   GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
DR   CDD; cd00110; LamG; 2.
DR   Gene3D; 2.60.120.200; -; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR039005; CSPG_rpt.
DR   InterPro; IPR001791; Laminin_G.
DR   PANTHER; PTHR45739:SF12; CHONDROITIN SULFATE PROTEOGLYCAN 4-LIKE ISOFORM X2; 1.
DR   PANTHER; PTHR45739; MATRIX PROTEIN, PUTATIVE-RELATED; 1.
DR   Pfam; PF16184; Cadherin_3; 13.
DR   Pfam; PF00054; Laminin_G_1; 1.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   SMART; SM00282; LamG; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   PROSITE; PS51854; CSPG; 15.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 2.
DR   Genevisible; Q8VHY0; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Angiogenesis; Cell membrane; Cell projection;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Membrane; Phosphoprotein; Proteoglycan; Reference proteome; Repeat; Signal;
KW   Tissue remodeling; Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..2327
FT                   /note="Chondroitin sulfate proteoglycan 4"
FT                   /id="PRO_0000041963"
FT   TOPO_DOM        30..2229
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00657"
FT   TRANSMEM        2230..2250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2251..2327
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00657"
FT   DOMAIN          30..193
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          203..381
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   REPEAT          429..524
FT                   /note="CSPG 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          554..646
FT                   /note="CSPG 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          663..765
FT                   /note="CSPG 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          784..883
FT                   /note="CSPG 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          903..994
FT                   /note="CSPG 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1023..1115
FT                   /note="CSPG 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1131..1221
FT                   /note="CSPG 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1243..1342
FT                   /note="CSPG 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1361..1454
FT                   /note="CSPG 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1478..1568
FT                   /note="CSPG 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1586..1684
FT                   /note="CSPG 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1709..1808
FT                   /note="CSPG 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1837..1929
FT                   /note="CSPG 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1946..2034
FT                   /note="CSPG 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          2043..2152
FT                   /note="CSPG 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REGION          30..640
FT                   /note="Globular or compact configuration stabilized by
FT                   disulfide bonds"
FT   REGION          30..640
FT                   /note="Neurite growth inhibition"
FT                   /evidence="ECO:0000250"
FT   REGION          575..1045
FT                   /note="Interaction with COL6A2"
FT                   /evidence="ECO:0000250"
FT   REGION          632..1451
FT                   /note="Interaction with COL5A1"
FT                   /evidence="ECO:0000250"
FT   REGION          1591..2226
FT                   /note="Neurite growth inhibition"
FT                   /evidence="ECO:0000250"
FT   REGION          1592..2226
FT                   /note="Cysteine-containing"
FT   REGION          2190..2210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           2325..2327
FT                   /note="PDZ-binding"
FT   COMPBIAS        2195..2209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2257
FT                   /note="Phosphothreonine; by PKC/PRKCA"
FT                   /evidence="ECO:0000250|UniProtKB:Q00657"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19656770"
FT   CARBOHYD        349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        686
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        773
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1000
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6UVK1"
FT   CARBOHYD        1136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1369
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19656770"
FT   CARBOHYD        1454
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19656770"
FT   CARBOHYD        1650
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1914
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2021
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19656770"
FT   CARBOHYD        2039
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2045
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2080
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19656770"
FT   DISULFID        170..193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DISULFID        355..381
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   VAR_SEQ         1..1666
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_015656"
FT   VAR_SEQ         1657..1694
FT                   /note="NAGNILYEHEMSSEPFWEAHDTIGLLLSSPPARDLAAT -> RASLLSHHTD
FT                   PNLTSGGCQLEHPPHWQLASLDPVPAQG (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_015657"
FT   VAR_SEQ         1695..2327
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_015658"
FT   MUTAGEN         2324
FT                   /note="Q->G: No effect on interaction with GRIP1 and
FT                   GRIP2."
FT                   /evidence="ECO:0000269|PubMed:12458226"
FT   MUTAGEN         2325
FT                   /note="Y->F: No effect on interaction with GRIP1 and
FT                   GRIP2."
FT                   /evidence="ECO:0000269|PubMed:12458226"
FT   MUTAGEN         2325
FT                   /note="Y->G: Loss of interaction with GRIP1 and GRIP2."
FT                   /evidence="ECO:0000269|PubMed:12458226"
FT   MUTAGEN         2326
FT                   /note="W->G: Loss of interaction with GRIP1 and GRIP2."
FT                   /evidence="ECO:0000269|PubMed:12458226"
FT   MUTAGEN         2327
FT                   /note="V->G: Loss of interaction with GRIP1 and GRIP2."
FT                   /evidence="ECO:0000269|PubMed:12458226"
FT   CONFLICT        1058
FT                   /note="D -> V (in Ref. 1; AAL37505)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1113
FT                   /note="S -> P (in Ref. 5; BAD90326)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1427
FT                   /note="W -> R (in Ref. 1; AAL37505)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1520
FT                   /note="Q -> E (in Ref. 1; AAL37505)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1546
FT                   /note="S -> G (in Ref. 1; AAL37505)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1929
FT                   /note="G -> E (in Ref. 1; AAL37505)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2000
FT                   /note="Q -> R (in Ref. 1; AAL37505)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2011
FT                   /note="D -> H (in Ref. 2; BAC26150)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2093
FT                   /note="G -> E (in Ref. 1; AAL37505)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2248
FT                   /note="L -> H (in Ref. 1; AAL37505)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2300
FT                   /note="P -> S (in Ref. 1; AAL37505)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2327 AA;  252309 MW;  C101DF60FCE3A7BC CRC64;
     MLLGPGHPLS APALALALTL ALLVRSTAPA SFFGENHLEV PVPSALTRVD LLLQFSTSQP
     EALLLLAAGQ DDHLLLQLHS GCLQVRLALG QKELKLQTPA DTVLSDSAPH TVVLTVSDSW
     AVLSVDGVLN TSAPIPRASH LKATYGLFVG SSGSLDLPYL KGISRPLRGC LHSAILNGRN
     LLRPLTSDVH EGCAEEFSAG DEVGLGFSGP HSLAAFPAWS TREEGTLEFT LTTRSQQAPL
     AFQAGDKRGN FIYVDIFEGH LRAVVEKGQG TMLLRNSVPV ADGQPHEVSV HIDVHRLEIS
     VDQYPTRTFN RGVLSYLEPR GSLLLGGLDT EASRHLQEHR LGLAPGAANI SLVGCIEDFS
     VNGRRQGLRD AWLTRDMSAG CRPEEDEYEE EVYGPYETFS TLAPEAWPAM ELPEPCIPEP
     GLPAVFANFT QLLTISPLVV AEGGTAWLEW RHVQPTLDLT EAELRKSQVL FSVSQSARHG
     DLELDILGAQ TRKMFTLLDV VNRKARFVHD GSEDTSDQLM LEVSVTARAP VPSCLRRGQI
     YILPIQVNPV NDPPRIIFPH GSLMVILEHT QKPLGPEIFQ AYDPDSACEG LTFQLLGVSS
     GVPVEHRDQP GEPATEFSCR ELEVGDIVYV HRGGPAQDLT FRVSDGMQAS APATLKVVAV
     RPAIQILHNT GLHLAQGSAA AILPANLSVE TNAVGQDVSV LFRVTGTLQF GELQKQGAGG
     VEGTEWWDTL AFHQRDVEQG RVRYLSTDPQ HHTQDTVEDL ILEVQVGQET LSNLSFPVTI
     QRATVWMLRL EPLHTQNPHQ ETLTPAHLEA SLEEEEEEGS PQPHTFHYEL VQAPRRGNLL
     LQGTRLSDGE SFSQSDLQAG RVTYRATMRT SEAADDSFRF RVTSPPHFSP LYTFPIHIGG
     DPNAPVLTNV LLMVPEGGEG VLSADHLFVK SLNSASYLYE VMEQPHHGKL AWRDPKGKST
     PVTSFTNEDL LHGRLVYQHD DSETIEDDIP FVATRQGEGS GDMAWEEVRG VFRVAIQPVN
     DHAPVQTISR VFHVARGGQR LLTTDDVAFS DADSGFSDAQ LVLTRKDLLF GSIVAMEEPT
     RPIYRFTQED LRKKQVLFVH SGADHGWLQL QVSDGQHQAT AMLEVQASEP YLHVANSSSL
     VVPQGGQGTI DTAVLQLDTN LDIRSGNEVH YHVTAGPQWG QLLRDGQSVT SFSQRDLLDG
     AILYSHNGSL SPQDTLAFSV AAGPVHTNTF LQVTIALEGP LAPLQLVQHK KIYVFQGEAA
     EIRRDQLEVV QEAVLPADIM FSLRSPPNAG YLVMVSHGAS AEEPPSLDPV QSFSQEAVNS
     GRVLYLHSRP GAWSDSFSLD VASGLGDPLE GISVELEVLP TVIPLDVQNF SVPEGGTRTL
     APPLVQITGP YFPTLPGLVL QVLEPPQHGA LQKEDHSQDG SLSTFSWREV EEQLIRYVHD
     GSETQTDAFV LLANASEMDR QSQPVAFTIT ILPVNDQPPV LTTNTGLQIW EGAIVPIPPE
     ALRGTDNDSG PEDLVYTIEQ PSNGRIALRV APDTEVHRFT QAQLDSGLVL FSHRGALEGG
     FHFDLSDGAH TSPGHFFRVV AQKQALLSLE GTRKLTVCPE SVQPLSSQSL SASSSTGADP
     RHLLYRVVRG PQLGRLLHAQ QGSAEEVLVN FTQAEVNAGN ILYEHEMSSE PFWEAHDTIG
     LLLSSPPARD LAATLAVMVS FDAACPQRPS RLWKNKGLWV PEGQRAKITV AALDAANLLA
     SVPASQRSRH DVLFQVTQFP TRGQLLVSEE PLHARRPYFL QSELAAGQLV YAHGGGGTQQ
     DGFRFRAHLQ GPTGTSVAGP QTSEAFVITV RDVNERPPQP QASIPLRVTR GSRAPVSRAQ
     LSVVDPDSAP GEIEYEVQRA PHNGFLSLAG DNTGPVTHFT QADVDAGRLA FVANGSSVAG
     VFQLSMSDGA SPPIPMSLAV DVLPSTIEVQ LRAPLEVPQA LGRTSLSRQQ LQVISDREEP
     DVAYRLTQGP LYGQLLVGGQ PASAFSQLQV DQGDVVFVFT NFSSSQDHFK VVALARGVNA
     SATVNVTVQA LLHVWAGGPW PQGTTLRLDP TVLDASELAN RTGSMPHFRL LAGPRYGRVV
     RVSQGRTESR SNQLVEHFTQ RDLEEGQLGL EVGKPEGRST GPAGDRLTLE LWAKGVPPAV
     ALLDFATEPY HAAKSYSVAL LSVPEAVRTE TEKPGRSVPT GQPGQAASSP VPTAAKGGFL
     GFLEANMFSI IIPVCLILLL LALILPLLFY LRKRNKTGKH DVQVLTAKPR NGLAGDTETF
     RKVEPGQAIP LITVPGQGPP PGGQPDPELL QFCRTPNPAL RNGQYWV
//