CSPG4_HUMAN
ID CSPG4_HUMAN Reviewed; 2322 AA.
AC Q6UVK1; D3DW77; Q92675;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Chondroitin sulfate proteoglycan 4;
DE AltName: Full=Chondroitin sulfate proteoglycan NG2;
DE AltName: Full=Melanoma chondroitin sulfate proteoglycan;
DE AltName: Full=Melanoma-associated chondroitin sulfate proteoglycan;
DE Flags: Precursor;
GN Name=CSPG4; Synonyms=MCSP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Melanoma;
RX PubMed=8790396; DOI=10.1073/pnas.93.18.9710;
RA Pluschke G., Vanek M., Evans A., Dittmar T., Schmid P., Itin P.,
RA Filardo E.J., Reisfeld R.A.;
RT "Molecular cloning of a human melanoma-associated chondroitin sulfate
RT proteoglycan.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9710-9715(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Melanoma;
RX PubMed=15210734; DOI=10.1083/jcb.200403174;
RA Yang J., Price M.A., Neudauer C.L., Wilson C., Ferrone S., Xia H., Iida J.,
RA Simpson M.A., McCarthy J.B.;
RT "Melanoma chondroitin sulfate proteoglycan enhances FAK and ERK activation
RT by distinct mechanisms.";
RL J. Cell Biol. 165:881-891(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH ITGA4.
RX PubMed=9488735; DOI=10.1074/jbc.273.10.5955;
RA Iida J., Meijne A.M.L., Oegema T.R. Jr., Yednock T.A., Kovach N.L.,
RA Furcht L.T., McCarthy J.B.;
RT "A role of chondroitin sulfate glycosaminoglycan binding site in
RT alpha4beta1 integrin-mediated melanoma cell adhesion.";
RL J. Biol. Chem. 273:5955-5962(1998).
RN [6]
RP INTERACTION WITH BCAR1; CDC42 AND ACK1, AND FUNCTION.
RX PubMed=10587647; DOI=10.1038/70302;
RA Eisenmann K.M., McCarthy J.B., Simpson M.A., Keely P.J., Guan J.-L.,
RA Tachibana K., Lim L., Manser E., Furcht L.T., Iida J.;
RT "Melanoma chondroitin sulphate proteoglycan regulates cell spreading
RT through Cdc42, Ack-1 and p130cas.";
RL Nat. Cell Biol. 1:507-513(1999).
RN [7]
RP INTERACTION WITH MMP16, AND FUNCTION.
RX PubMed=11278606; DOI=10.1074/jbc.m010053200;
RA Iida J., Pei D., Kang T., Simpson M.A., Herlyn M., Furcht L.T.,
RA McCarthy J.B.;
RT "Melanoma chondroitin sulfate proteoglycan regulates matrix
RT metalloproteinase-dependent human melanoma invasion into type I collagen.";
RL J. Biol. Chem. 276:18786-18794(2001).
RN [8]
RP IDENTIFICATION OF CSPG REPEATS.
RX PubMed=12220645; DOI=10.1016/s0014-5793(02)03195-2;
RA Staub E., Hinzmann B., Rosenthal A.;
RT "A novel repeat in the melanoma-associated chondroitin sulfate proteoglycan
RT defines a new protein family.";
RL FEBS Lett. 527:114-118(2002).
RN [9]
RP INTERACTION WITH ITGA3; ITGB1 AND LGALS3.
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 [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2075.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
RP INTERACTION WITH C.DIFFICILE TCDB (MICROBIAL INFECTION).
RX PubMed=25547119; DOI=10.1038/cr.2014.169;
RA Yuan P., Zhang H., Cai C., Zhu S., Zhou Y., Yang X., He R., Li C., Guo S.,
RA Li S., Huang T., Perez-Cordon G., Feng H., Wei W.;
RT "Chondroitin sulfate proteoglycan 4 functions as the cellular receptor for
RT Clostridium difficile toxin B.";
RL Cell Res. 25:157-168(2015).
RN [12]
RP INTERACTION WITH C.DIFFICILE TCDB (MICROBIAL INFECTION).
RX PubMed=27680706; DOI=10.1038/nature19799;
RA Tao L., Zhang J., Meraner P., Tovaglieri A., Wu X., Gerhard R., Zhang X.,
RA Stallcup W.B., Miao J., He X., Hurdle J.G., Breault D.T., Brass A.L.,
RA Dong M.;
RT "Frizzled proteins are colonic epithelial receptors for C. difficile toxin
RT B.";
RL Nature 538:350-355(2016).
RN [13]
RP INTERACTION WITH C.DIFFICILE TCDB (MICROBIAL INFECTION).
RX PubMed=31233493; DOI=10.1371/journal.pbio.3000311;
RA Simeon R., Jiang M., Chamoun-Emanuelli A.M., Yu H., Zhang Y., Meng R.,
RA Peng Z., Jakana J., Zhang J., Feng H., Chen Z.;
RT "Selection and characterization of ultrahigh potency designed ankyrin
RT repeat protein inhibitors of C. difficile toxin B.";
RL PLoS Biol. 17:e3000311-e3000311(2019).
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:10587647, ECO:0000269|PubMed:11278606,
CC ECO:0000269|PubMed:15210734}.
CC -!- SUBUNIT: Interacts with the first PDZ domain of MPDZ. Interacts with
CC PRKCA. Binds TNC, laminin-1, COL5A1 and COL6A2. Interacts with PLG and
CC angiostatin. Binds FGF2 and PDGFA. Interacts with GRIP1, GRIP2 and
CC GRIA2. Forms a ternary complex with GRIP1 and GRIA2 (By similarity).
CC Interacts with LGALS3 and the integrin composed of ITGB1 and ITGA3.
CC Interacts with ITGA4 through its chondroitin sulfate glycosaminoglycan.
CC Interacts with BCAR1, CDC42 and ACK1. Interacts with MMP16.
CC {ECO:0000250, ECO:0000269|PubMed:10587647, ECO:0000269|PubMed:11278606,
CC ECO:0000269|PubMed:15181153, ECO:0000269|PubMed:9488735}.
CC -!- SUBUNIT: (Microbial infection) Interacts with C.difficile toxin TcdB,
CC suggesting that it may act as a receptor for TcdB.
CC {ECO:0000269|PubMed:25547119, ECO:0000269|PubMed:27680706,
CC ECO:0000269|PubMed:31233493}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q00657};
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. Localizes
CC to the plasma membrane of oligodendrocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q00657, ECO:0000250|UniProtKB:Q8VHY0}.
CC -!- TISSUE SPECIFICITY: Detected only in malignant melanoma cells.
CC {ECO:0000269|PubMed:8790396}.
CC -!- PTM: O-glycosylated; contains glycosaminoglycan chondroitin sulfate
CC which are required for proper localization and function in stress fiber
CC formation (By similarity). Involved in interaction with MMP16 and
CC ITGA4. {ECO:0000250, ECO:0000269|PubMed:16335952}.
CC -!- PTM: Phosphorylation by PRKCA regulates its subcellular location and
CC function in cell motility. {ECO:0000250}.
CC -!- MISCELLANEOUS: Valuable marker for several incompletely differentiated
CC precursor cells.
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DR EMBL; X96753; CAA65529.1; -; mRNA.
DR EMBL; AY359468; AAQ62842.1; -; mRNA.
DR EMBL; AC105020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471136; EAW99239.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99240.1; -; Genomic_DNA.
DR CCDS; CCDS10284.1; -.
DR RefSeq; NP_001888.2; NM_001897.4.
DR PDB; 7ML7; EM; 3.17 A; B=30-764.
DR PDB; 7N8X; EM; 3.40 A; B=411-550.
DR PDB; 7N9Y; EM; 4.80 A; B=411-550.
DR PDBsum; 7ML7; -.
DR PDBsum; 7N8X; -.
DR PDBsum; 7N9Y; -.
DR AlphaFoldDB; Q6UVK1; -.
DR SMR; Q6UVK1; -.
DR BioGRID; 107846; 146.
DR CORUM; Q6UVK1; -.
DR IntAct; Q6UVK1; 23.
DR MINT; Q6UVK1; -.
DR STRING; 9606.ENSP00000312506; -.
DR GlyConnect; 2028; 1 N-Linked glycan (1 site).
DR GlyGen; Q6UVK1; 18 sites, 2 N-linked glycans (1 site), 3 O-linked glycans (2 sites).
DR iPTMnet; Q6UVK1; -.
DR PhosphoSitePlus; Q6UVK1; -.
DR BioMuta; CSPG4; -.
DR DMDM; 296434468; -.
DR EPD; Q6UVK1; -.
DR jPOST; Q6UVK1; -.
DR MassIVE; Q6UVK1; -.
DR MaxQB; Q6UVK1; -.
DR PaxDb; Q6UVK1; -.
DR PeptideAtlas; Q6UVK1; -.
DR PRIDE; Q6UVK1; -.
DR ProteomicsDB; 67431; -.
DR ABCD; Q6UVK1; 53 sequenced antibodies.
DR Antibodypedia; 1108; 696 antibodies from 40 providers.
DR DNASU; 1464; -.
DR Ensembl; ENST00000308508.5; ENSP00000312506.5; ENSG00000173546.7.
DR GeneID; 1464; -.
DR KEGG; hsa:1464; -.
DR MANE-Select; ENST00000308508.5; ENSP00000312506.5; NM_001897.5; NP_001888.2.
DR UCSC; uc002baw.3; human.
DR CTD; 1464; -.
DR DisGeNET; 1464; -.
DR GeneCards; CSPG4; -.
DR HGNC; HGNC:2466; CSPG4.
DR HPA; ENSG00000173546; Low tissue specificity.
DR MIM; 601172; gene.
DR neXtProt; NX_Q6UVK1; -.
DR OpenTargets; ENSG00000173546; -.
DR PharmGKB; PA26963; -.
DR VEuPathDB; HostDB:ENSG00000173546; -.
DR eggNOG; KOG3597; Eukaryota.
DR GeneTree; ENSGT00940000154091; -.
DR HOGENOM; CLU_000473_1_0_1; -.
DR InParanoid; Q6UVK1; -.
DR OMA; YCRTSNP; -.
DR OrthoDB; 219190at2759; -.
DR PhylomeDB; Q6UVK1; -.
DR TreeFam; TF316876; -.
DR PathwayCommons; Q6UVK1; -.
DR Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-HSA-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-HSA-2024101; CS/DS degradation.
DR Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
DR Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
DR Reactome; R-HSA-3595172; Defective CHST3 causes SEDCJD.
DR Reactome; R-HSA-3595174; Defective CHST14 causes EDS, musculocontractural type.
DR Reactome; R-HSA-3595177; Defective CHSY1 causes TPBS.
DR Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
DR SignaLink; Q6UVK1; -.
DR SIGNOR; Q6UVK1; -.
DR BioGRID-ORCS; 1464; 24 hits in 1070 CRISPR screens.
DR ChiTaRS; CSPG4; human.
DR GeneWiki; CSPG4; -.
DR GenomeRNAi; 1464; -.
DR Pharos; Q6UVK1; Tbio.
DR PRO; PR:Q6UVK1; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q6UVK1; protein.
DR Bgee; ENSG00000173546; Expressed in tendon of biceps brachii and 131 other tissues.
DR Genevisible; Q6UVK1; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR GO; GO:0015026; F:coreceptor activity; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0008347; P:glial cell migration; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0097178; P:ruffle assembly; IEA:Ensembl.
DR GO; GO:0006929; P:substrate-dependent cell migration; IEA:Ensembl.
DR GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
DR CDD; cd00110; LamG; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR039005; CSPG_rpt.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS51854; CSPG; 15.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 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..2322
FT /note="Chondroitin sulfate proteoglycan 4"
FT /id="PRO_0000041962"
FT TOPO_DOM 30..2224
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00657"
FT TRANSMEM 2225..2245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2246..2322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00657"
FT DOMAIN 30..192
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 202..380
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REPEAT 428..523
FT /note="CSPG 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 553..645
FT /note="CSPG 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 662..764
FT /note="CSPG 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 783..878
FT /note="CSPG 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 898..989
FT /note="CSPG 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1018..1110
FT /note="CSPG 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1126..1216
FT /note="CSPG 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1238..1337
FT /note="CSPG 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1356..1449
FT /note="CSPG 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1473..1563
FT /note="CSPG 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1581..1679
FT /note="CSPG 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1704..1803
FT /note="CSPG 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1832..1924
FT /note="CSPG 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1941..2029
FT /note="CSPG 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 2038..2147
FT /note="CSPG 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REGION 30..639
FT /note="Globular or compact configuration stabilized by
FT disulfide bonds"
FT REGION 30..639
FT /note="Neurite growth inhibition"
FT /evidence="ECO:0000250"
FT REGION 574..1040
FT /note="Interaction with COL6A2"
FT /evidence="ECO:0000250"
FT REGION 631..1446
FT /note="Interaction with COL5A1"
FT /evidence="ECO:0000250"
FT REGION 1586..2221
FT /note="Neurite growth inhibition"
FT /evidence="ECO:0000250"
FT REGION 1587..2221
FT /note="Cysteine-containing"
FT REGION 2182..2206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2320..2322
FT /note="PDZ-binding"
FT MOD_RES 2252
FT /note="Phosphothreonine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:Q00657"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 995
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1909
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2016
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2034
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2040
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2075
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT DISULFID 169..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 354..380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT VARIANT 1703
FT /note="R -> H (in dbSNP:rs8023621)"
FT /id="VAR_061733"
FT CONFLICT 5..6
FT /note="PR -> RG (in Ref. 1; CAA65529 and 2; AAQ62842)"
FT /evidence="ECO:0000305"
FT CONFLICT 477..478
FT /note="RH -> HY (in Ref. 1; CAA65529)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="P -> L (in Ref. 1; CAA65529)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="R -> C (in Ref. 1; CAA65529)"
FT /evidence="ECO:0000305"
FT CONFLICT 715..717
FT /note="QGA -> HST (in Ref. 1; CAA65529)"
FT /evidence="ECO:0000305"
FT CONFLICT 942
FT /note="H -> L (in Ref. 1; CAA65529)"
FT /evidence="ECO:0000305"
FT CONFLICT 1208
FT /note="R -> E (in Ref. 1; CAA65529)"
FT /evidence="ECO:0000305"
FT CONFLICT 1405
FT /note="A -> P (in Ref. 1; CAA65529)"
FT /evidence="ECO:0000305"
FT CONFLICT 1557
FT /note="R -> P (in Ref. 1; CAA65529)"
FT /evidence="ECO:0000305"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:7ML7"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:7ML7"
FT STRAND 437..443
FT /evidence="ECO:0007829|PDB:7ML7"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:7ML7"
FT STRAND 452..456
FT /evidence="ECO:0007829|PDB:7ML7"
FT TURN 458..462
FT /evidence="ECO:0007829|PDB:7ML7"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:7ML7"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:7ML7"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:7ML7"
FT HELIX 496..500
FT /evidence="ECO:0007829|PDB:7ML7"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:7ML7"
FT STRAND 516..524
FT /evidence="ECO:0007829|PDB:7ML7"
FT HELIX 533..536
FT /evidence="ECO:0007829|PDB:7ML7"
FT STRAND 538..547
FT /evidence="ECO:0007829|PDB:7ML7"
SQ SEQUENCE 2322 AA; 250537 MW; 0B4F39AFC5ADD3CA CRC64;
MQSGPRPPLP APGLALALTL TMLARLASAA SFFGENHLEV PVATALTDID LQLQFSTSQP
EALLLLAAGP ADHLLLQLYS GRLQVRLVLG QEELRLQTPA ETLLSDSIPH TVVLTVVEGW
ATLSVDGFLN ASSAVPGAPL EVPYGLFVGG TGTLGLPYLR GTSRPLRGCL HAATLNGRSL
LRPLTPDVHE GCAEEFSASD DVALGFSGPH SLAAFPAWGT QDEGTLEFTL TTQSRQAPLA
FQAGGRRGDF IYVDIFEGHL RAVVEKGQGT VLLHNSVPVA DGQPHEVSVH INAHRLEISV
DQYPTHTSNR GVLSYLEPRG SLLLGGLDAE ASRHLQEHRL GLTPEATNAS LLGCMEDLSV
NGQRRGLREA LLTRNMAAGC RLEEEEYEDD AYGHYEAFST LAPEAWPAME LPEPCVPEPG
LPPVFANFTQ LLTISPLVVA EGGTAWLEWR HVQPTLDLME AELRKSQVLF SVTRGARHGE
LELDIPGAQA RKMFTLLDVV NRKARFIHDG SEDTSDQLVL EVSVTARVPM PSCLRRGQTY
LLPIQVNPVN DPPHIIFPHG SLMVILEHTQ KPLGPEVFQA YDPDSACEGL TFQVLGTSSG
LPVERRDQPG EPATEFSCRE LEAGSLVYVH RGGPAQDLTF RVSDGLQASP PATLKVVAIR
PAIQIHRSTG LRLAQGSAMP ILPANLSVET NAVGQDVSVL FRVTGALQFG ELQKQGAGGV
EGAEWWATQA FHQRDVEQGR VRYLSTDPQH HAYDTVENLA LEVQVGQEIL SNLSFPVTIQ
RATVWMLRLE PLHTQNTQQE TLTTAHLEAT LEEAGPSPPT FHYEVVQAPR KGNLQLQGTR
LSDGQGFTQD DIQAGRVTYG ATARASEAVE DTFRFRVTAP PYFSPLYTFP IHIGGDPDAP
VLTNVLLVVP EGGEGVLSAD HLFVKSLNSA SYLYEVMERP RHGRLAWRGT QDKTTMVTSF
TNEDLLRGRL VYQHDDSETT EDDIPFVATR QGESSGDMAW EEVRGVFRVA IQPVNDHAPV
QTISRIFHVA RGGRRLLTTD DVAFSDADSG FADAQLVLTR KDLLFGSIVA VDEPTRPIYR
FTQEDLRKRR VLFVHSGADR GWIQLQVSDG QHQATALLEV QASEPYLRVA NGSSLVVPQG
GQGTIDTAVL HLDTNLDIRS GDEVHYHVTA GPRWGQLVRA GQPATAFSQQ DLLDGAVLYS
HNGSLSPRDT MAFSVEAGPV HTDATLQVTI ALEGPLAPLK LVRHKKIYVF QGEAAEIRRD
QLEAAQEAVP PADIVFSVKS PPSAGYLVMV SRGALADEPP SLDPVQSFSQ EAVDTGRVLY
LHSRPEAWSD AFSLDVASGL GAPLEGVLVE LEVLPAAIPL EAQNFSVPEG GSLTLAPPLL
RVSGPYFPTL LGLSLQVLEP PQHGALQKED GPQARTLSAF SWRMVEEQLI RYVHDGSETL
TDSFVLMANA SEMDRQSHPV AFTVTVLPVN DQPPILTTNT GLQMWEGATA PIPAEALRST
DGDSGSEDLV YTIEQPSNGR VVLRGAPGTE VRSFTQAQLD GGLVLFSHRG TLDGGFRFRL
SDGEHTSPGH FFRVTAQKQV LLSLKGSQTL TVCPGSVQPL SSQTLRASSS AGTDPQLLLY
RVVRGPQLGR LFHAQQDSTG EALVNFTQAE VYAGNILYEH EMPPEPFWEA HDTLELQLSS
PPARDVAATL AVAVSFEAAC PQRPSHLWKN KGLWVPEGQR ARITVAALDA SNLLASVPSP
QRSEHDVLFQ VTQFPSRGQL LVSEEPLHAG QPHFLQSQLA AGQLVYAHGG GGTQQDGFHF
RAHLQGPAGA SVAGPQTSEA FAITVRDVNE RPPQPQASVP LRLTRGSRAP ISRAQLSVVD
PDSAPGEIEY EVQRAPHNGF LSLVGGGLGP VTRFTQADVD SGRLAFVANG SSVAGIFQLS
MSDGASPPLP MSLAVDILPS AIEVQLRAPL EVPQALGRSS LSQQQLRVVS DREEPEAAYR
LIQGPQYGHL LVGGRPTSAF SQFQIDQGEV VFAFTNFSSS HDHFRVLALA RGVNASAVVN
VTVRALLHVW AGGPWPQGAT LRLDPTVLDA GELANRTGSV PRFRLLEGPR HGRVVRVPRA
RTEPGGSQLV EQFTQQDLED GRLGLEVGRP EGRAPGPAGD SLTLELWAQG VPPAVASLDF
ATEPYNAARP YSVALLSVPE AARTEAGKPE SSTPTGEPGP MASSPEPAVA KGGFLSFLEA
NMFSVIIPMC LVLLLLALIL PLLFYLRKRN KTGKHDVQVL TAKPRNGLAG DTETFRKVEP
GQAIPLTAVP GQGPPPGGQP DPELLQFCRT PNPALKNGQY WV
