Q8VHY0 (CSPG4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chondroitin sulfate proteoglycan 4

Alternative name(s):
Chondroitin sulfate proteoglycan NG2
Proteoglycan AN2

Gene names

Name:	Cspg4
Synonyms:	An2, Kiaa4232, Ng2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2327 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. May also inhibit neurite outgrowth and growth cone collapse during axon regeneration. Cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. Binds through its extracellular N-terminus growth factors, extracellular matrix proteases modulating their activity. May regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. May modulate the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. Functions also as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. May promote retraction fiber formation and cell polarization through Rho GTPase activation. May stimulate alpha-4, beta-1 integrin-mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling cascades. Ref.6 Ref.7
Subunit structure	Interacts with ITGA4 through its chondroitin sulfate glycosaminoglycan. Interacts with BCAR1, CDC42 and ACK1. Interacts with MMP16. Interacts with the first PDZ domain of MPDZ. Interacts with PRKCA. Interacts with LGALS3 and the integrin composed of ITGB1 and ITGA3. Binds TNC, laminin-1, COL5A1 and COL6A2. Interacts with PLG and angiostatin. Binds FGF2 and PDGFA By similarity. Interacts with GRIP1, GRIP2 and GRIA2. Forms a ternary complex with GRIP1 and GRIA2. Ref.1
Subcellular location	Apical cell membrane; Single-pass type I membrane protein; Extracellular side. Cell projection › lamellipodium membrane; Single-pass type I membrane protein; Extracellular side. Note: Localized at the apical plasma membrane it relocalizes to the lamellipodia of astrocytoma upon phosphorylation by PRKCA. Localizes to the retraction fibers. A fraction may undergo cell surface proteolysis and secretion By similarity. Localizes to the plasma membrane of oligodendrocytes. Ref.1
Tissue specificity	Expressed in microcascular pericytes and not endothelial cells. Ref.7
Post-translational modification	O-glycosylated; contains glycosaminoglycan chondroitin sulfate which are required for proper localization and function in stress fiber formation. Involved in interaction with MMP16 and ITGA4 By similarity. Phosphorylation by PRKCA regulates its subcellular location and function in cell motility By similarity.
Disruption phenotype	Mice are unresponsive to PDGF-AA through PDGF-alpha receptor. Ref.6
Miscellaneous	Valuable marker for several incompletely differentiated precursor cells.
Sequence similarities	Contains 15 CSPG (NG2) repeats. Contains 2 laminin G-like domains.
Sequence caution	The sequence BAC26150.1 differs from that shown. Reason: Frameshift at position 1889.

Ontologies

Keywords
Biological process	Angiogenesis Differentiation Tissue remodeling
Cellular component	Cell membrane Cell projection Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Developmental protein Transducer
PTM	Disulfide bond Glycoprotein Phosphoprotein Proteoglycan
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of MAPK activity Inferred from mutant phenotype PubMed 11668599. Source: MGI angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Inferred from mutant phenotype PubMed 11668599. Source: MGI glial cell migration Inferred from direct assay PubMed 10366628. Source: MGI intracellular signal transduction Inferred from electronic annotation. Source: Compara positive regulation of peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara tissue remodeling Inferred from electronic annotation. Source: UniProtKB-KW transmembrane receptor protein tyrosine kinase signaling pathway Inferred from mutant phenotype PubMed 11668599. Source: MGI
Cellular_component	apical plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW lamellipodium membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay PubMed 11668599. Source: MGI
Molecular_function	signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8VHY0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8VHY0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1666: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q8VHY0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1657-1694: NAGNILYEHE...SPPARDLAAT → RASLLSHHTD...ASLDPVPAQG
     1695-2327: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 29	29	Potential
	Chain	30 – 2327	2298	Chondroitin sulfate proteoglycan 4		PRO_0000041963
Regions
	Topological domain	30 – 2229	2200	Extracellular Potential
	Transmembrane	2230 – 2250	21	Helical; Potential
	Topological domain	2251 – 2327	77	Cytoplasmic Potential
	Domain	30 – 193	164	Laminin G-like 1
	Domain	203 – 381	179	Laminin G-like 2
	Repeat	431 – 524	94	CSPG 1
	Repeat	557 – 644	88	CSPG 2
	Repeat	666 – 765	100	CSPG 3
	Repeat	793 – 883	91	CSPG 4
	Repeat	905 – 994	90	CSPG 5
	Repeat	1025 – 1113	89	CSPG 6
	Repeat	1133 – 1221	89	CSPG 7
	Repeat	1246 – 1342	97	CSPG 8
	Repeat	1365 – 1454	90	CSPG 9
	Repeat	1481 – 1566	86	CSPG 10
	Repeat	1588 – 1684	97	CSPG 11
	Repeat	1712 – 1808	97	CSPG 12
	Repeat	1840 – 1927	88	CSPG 13
	Repeat	1949 – 2034	86	CSPG 14
	Repeat	2053 – 2152	100	CSPG 15
	Region	30 – 640	611	Globular or compact configuration stabilized by disulfide bonds
	Region	30 – 640	611	Neurite growth inhibition By similarity
	Region	575 – 1045	471	Interaction with COL6A2 By similarity
	Region	632 – 1451	820	Interaction with COL5A1 By similarity
	Region	1591 – 2226	636	Neurite growth inhibition By similarity
	Region	1592 – 2226	635	Cysteine-containing
	Motif	2325 – 2327	3	PDZ-binding
	Compositional bias	640 – 1591	952	Gly/Ser-rich (glycosaminoglycan attachment domain)
Amino acid modifications
	Modified residue	2257	1	Phosphothreonine; by PKC/PRKCA By similarity
	Glycosylation	130	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	349	1	N-linked (GlcNAc...) Potential
	Glycosylation	428	1	N-linked (GlcNAc...) Potential
	Glycosylation	686	1	N-linked (GlcNAc...) Potential
	Glycosylation	773	1	N-linked (GlcNAc...) Potential
	Glycosylation	1000	1	O-linked (Xyl...) (chondroitin sulfate) By similarity
	Glycosylation	1136	1	N-linked (GlcNAc...) Potential
	Glycosylation	1207	1	N-linked (GlcNAc...) Potential
	Glycosylation	1369	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	1454	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	1650	1	N-linked (GlcNAc...) Potential
	Glycosylation	1914	1	N-linked (GlcNAc...) Potential
	Glycosylation	2021	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	2039	1	N-linked (GlcNAc...) Potential
	Glycosylation	2045	1	N-linked (GlcNAc...) Potential
	Glycosylation	2080	1	N-linked (GlcNAc...) Ref.8
	Disulfide bond	170 ↔ 193		By similarity
	Disulfide bond	355 ↔ 381		By similarity
Natural variations
	Alternative sequence	1 – 1666	1666	Missing in isoform 2.		VSP_015656
	Alternative sequence	1657 – 1694	38	NAGNI…DLAAT → RASLLSHHTDPNLTSGGCQL EHPPHWQLASLDPVPAQG in isoform 3.		VSP_015657
	Alternative sequence	1695 – 2327	633	Missing in isoform 3.		VSP_015658
Experimental info
	Mutagenesis	2324	1	Q → G: No effect on interaction with GRIP1 and GRIP2. Ref.1
	Mutagenesis	2325	1	Y → F: No effect on interaction with GRIP1 and GRIP2. Ref.1
	Mutagenesis	2325	1	Y → G: Loss of interaction with GRIP1 and GRIP2. Ref.1
	Mutagenesis	2326	1	W → G: Loss of interaction with GRIP1 and GRIP2. Ref.1
	Mutagenesis	2327	1	V → G: Loss of interaction with GRIP1 and GRIP2. Ref.1
	Sequence conflict	1058	1	D → V in AAL37505. Ref.1
	Sequence conflict	1113	1	S → P in BAD90326. Ref.5
	Sequence conflict	1427	1	W → R in AAL37505. Ref.1
	Sequence conflict	1520	1	Q → E in AAL37505. Ref.1
	Sequence conflict	1546	1	S → G in AAL37505. Ref.1
	Sequence conflict	1929	1	G → E in AAL37505. Ref.1
	Sequence conflict	2000	1	Q → R in AAL37505. Ref.1
	Sequence conflict	2011	1	D → H in BAC26150. Ref.2
	Sequence conflict	2093	1	G → E in AAL37505. Ref.1
	Sequence conflict	2248	1	L → H in AAL37505. Ref.1
	Sequence conflict	2300	1	P → S in AAL37505. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 3, 2012. Version 3. Checksum: C101DF60FCE3A7BC	FASTA	2,327	252,309
	10 20 30 40 50 60 MLLGPGHPLS APALALALTL ALLVRSTAPA SFFGENHLEV PVPSALTRVD LLLQFSTSQP 70 80 90 100 110 120 EALLLLAAGQ DDHLLLQLHS GCLQVRLALG QKELKLQTPA DTVLSDSAPH TVVLTVSDSW 130 140 150 160 170 180 AVLSVDGVLN TSAPIPRASH LKATYGLFVG SSGSLDLPYL KGISRPLRGC LHSAILNGRN 190 200 210 220 230 240 LLRPLTSDVH EGCAEEFSAG DEVGLGFSGP HSLAAFPAWS TREEGTLEFT LTTRSQQAPL 250 260 270 280 290 300 AFQAGDKRGN FIYVDIFEGH LRAVVEKGQG TMLLRNSVPV ADGQPHEVSV HIDVHRLEIS 310 320 330 340 350 360 VDQYPTRTFN RGVLSYLEPR GSLLLGGLDT EASRHLQEHR LGLAPGAANI SLVGCIEDFS 370 380 390 400 410 420 VNGRRQGLRD AWLTRDMSAG CRPEEDEYEE EVYGPYETFS TLAPEAWPAM ELPEPCIPEP 430 440 450 460 470 480 GLPAVFANFT QLLTISPLVV AEGGTAWLEW RHVQPTLDLT EAELRKSQVL FSVSQSARHG 490 500 510 520 530 540 DLELDILGAQ TRKMFTLLDV VNRKARFVHD GSEDTSDQLM LEVSVTARAP VPSCLRRGQI 550 560 570 580 590 600 YILPIQVNPV NDPPRIIFPH GSLMVILEHT QKPLGPEIFQ AYDPDSACEG LTFQLLGVSS 610 620 630 640 650 660 GVPVEHRDQP GEPATEFSCR ELEVGDIVYV HRGGPAQDLT FRVSDGMQAS APATLKVVAV 670 680 690 700 710 720 RPAIQILHNT GLHLAQGSAA AILPANLSVE TNAVGQDVSV LFRVTGTLQF GELQKQGAGG 730 740 750 760 770 780 VEGTEWWDTL AFHQRDVEQG RVRYLSTDPQ HHTQDTVEDL ILEVQVGQET LSNLSFPVTI 790 800 810 820 830 840 QRATVWMLRL EPLHTQNPHQ ETLTPAHLEA SLEEEEEEGS PQPHTFHYEL VQAPRRGNLL 850 860 870 880 890 900 LQGTRLSDGE SFSQSDLQAG RVTYRATMRT SEAADDSFRF RVTSPPHFSP LYTFPIHIGG 910 920 930 940 950 960 DPNAPVLTNV LLMVPEGGEG VLSADHLFVK SLNSASYLYE VMEQPHHGKL AWRDPKGKST 970 980 990 1000 1010 1020 PVTSFTNEDL LHGRLVYQHD DSETIEDDIP FVATRQGEGS GDMAWEEVRG VFRVAIQPVN 1030 1040 1050 1060 1070 1080 DHAPVQTISR VFHVARGGQR LLTTDDVAFS DADSGFSDAQ LVLTRKDLLF GSIVAMEEPT 1090 1100 1110 1120 1130 1140 RPIYRFTQED LRKKQVLFVH SGADHGWLQL QVSDGQHQAT AMLEVQASEP YLHVANSSSL 1150 1160 1170 1180 1190 1200 VVPQGGQGTI DTAVLQLDTN LDIRSGNEVH YHVTAGPQWG QLLRDGQSVT SFSQRDLLDG 1210 1220 1230 1240 1250 1260 AILYSHNGSL SPQDTLAFSV AAGPVHTNTF LQVTIALEGP LAPLQLVQHK KIYVFQGEAA 1270 1280 1290 1300 1310 1320 EIRRDQLEVV QEAVLPADIM FSLRSPPNAG YLVMVSHGAS AEEPPSLDPV QSFSQEAVNS 1330 1340 1350 1360 1370 1380 GRVLYLHSRP GAWSDSFSLD VASGLGDPLE GISVELEVLP TVIPLDVQNF SVPEGGTRTL 1390 1400 1410 1420 1430 1440 APPLVQITGP YFPTLPGLVL QVLEPPQHGA LQKEDHSQDG SLSTFSWREV EEQLIRYVHD 1450 1460 1470 1480 1490 1500 GSETQTDAFV LLANASEMDR QSQPVAFTIT ILPVNDQPPV LTTNTGLQIW EGAIVPIPPE 1510 1520 1530 1540 1550 1560 ALRGTDNDSG PEDLVYTIEQ PSNGRIALRV APDTEVHRFT QAQLDSGLVL FSHRGALEGG 1570 1580 1590 1600 1610 1620 FHFDLSDGAH TSPGHFFRVV AQKQALLSLE GTRKLTVCPE SVQPLSSQSL SASSSTGADP 1630 1640 1650 1660 1670 1680 RHLLYRVVRG PQLGRLLHAQ QGSAEEVLVN FTQAEVNAGN ILYEHEMSSE PFWEAHDTIG 1690 1700 1710 1720 1730 1740 LLLSSPPARD LAATLAVMVS FDAACPQRPS RLWKNKGLWV PEGQRAKITV AALDAANLLA 1750 1760 1770 1780 1790 1800 SVPASQRSRH DVLFQVTQFP TRGQLLVSEE PLHARRPYFL QSELAAGQLV YAHGGGGTQQ 1810 1820 1830 1840 1850 1860 DGFRFRAHLQ GPTGTSVAGP QTSEAFVITV RDVNERPPQP QASIPLRVTR GSRAPVSRAQ 1870 1880 1890 1900 1910 1920 LSVVDPDSAP GEIEYEVQRA PHNGFLSLAG DNTGPVTHFT QADVDAGRLA FVANGSSVAG 1930 1940 1950 1960 1970 1980 VFQLSMSDGA SPPIPMSLAV DVLPSTIEVQ LRAPLEVPQA LGRTSLSRQQ LQVISDREEP 1990 2000 2010 2020 2030 2040 DVAYRLTQGP LYGQLLVGGQ PASAFSQLQV DQGDVVFVFT NFSSSQDHFK VVALARGVNA 2050 2060 2070 2080 2090 2100 SATVNVTVQA LLHVWAGGPW PQGTTLRLDP TVLDASELAN RTGSMPHFRL LAGPRYGRVV 2110 2120 2130 2140 2150 2160 RVSQGRTESR SNQLVEHFTQ RDLEEGQLGL EVGKPEGRST GPAGDRLTLE LWAKGVPPAV 2170 2180 2190 2200 2210 2220 ALLDFATEPY HAAKSYSVAL LSVPEAVRTE TEKPGRSVPT GQPGQAASSP VPTAAKGGFL 2230 2240 2250 2260 2270 2280 GFLEANMFSI IIPVCLILLL LALILPLLFY LRKRNKTGKH DVQVLTAKPR NGLAGDTETF 2290 2300 2310 2320 RKVEPGQAIP LITVPGQGPP PGGQPDPELL QFCRTPNPAL RNGQYWV
	Isoform 2 [UniParc]. Checksum: DA679F6CCF894532	FASTA	661	70,843
	10 20 30 40 50 60 MSSEPFWEAH DTIGLLLSSP PARDLAATLA VMVSFDAACP QRPSRLWKNK GLWVPEGQRA 70 80 90 100 110 120 KITVAALDAA NLLASVPASQ RSRHDVLFQV TQFPTRGQLL VSEEPLHARR PYFLQSELAA 130 140 150 160 170 180 GQLVYAHGGG GTQQDGFRFR AHLQGPTGTS VAGPQTSEAF VITVRDVNER PPQPQASIPL 190 200 210 220 230 240 RVTRGSRAPV SRAQLSVVDP DSAPGEIEYE VQRAPHNGFL SLAGDNTGPV THFTQADVDA 250 260 270 280 290 300 GRLAFVANGS SVAGVFQLSM SDGASPPIPM SLAVDVLPST IEVQLRAPLE VPQALGRTSL 310 320 330 340 350 360 SRQQLQVISD REEPDVAYRL TQGPLYGQLL VGGQPASAFS QLQVDQGDVV FVFTNFSSSQ 370 380 390 400 410 420 DHFKVVALAR GVNASATVNV TVQALLHVWA GGPWPQGTTL RLDPTVLDAS ELANRTGSMP 430 440 450 460 470 480 HFRLLAGPRY GRVVRVSQGR TESRSNQLVE HFTQRDLEEG QLGLEVGKPE GRSTGPAGDR 490 500 510 520 530 540 LTLELWAKGV PPAVALLDFA TEPYHAAKSY SVALLSVPEA VRTETEKPGR SVPTGQPGQA 550 560 570 580 590 600 ASSPVPTAAK GGFLGFLEAN MFSIIIPVCL ILLLLALILP LLFYLRKRNK TGKHDVQVLT 610 620 630 640 650 660 AKPRNGLAGD TETFRKVEPG QAIPLITVPG QGPPPGGQPD PELLQFCRTP NPALRNGQYW V
	Isoform 3 [UniParc]. Checksum: 52625A76C5070FBB	FASTA	1,694	184,393
	10 20 30 40 50 60 MLLGPGHPLS APALALALTL ALLVRSTAPA SFFGENHLEV PVPSALTRVD LLLQFSTSQP 70 80 90 100 110 120 EALLLLAAGQ DDHLLLQLHS GCLQVRLALG QKELKLQTPA DTVLSDSAPH TVVLTVSDSW 130 140 150 160 170 180 AVLSVDGVLN TSAPIPRASH LKATYGLFVG SSGSLDLPYL KGISRPLRGC LHSAILNGRN 190 200 210 220 230 240 LLRPLTSDVH EGCAEEFSAG DEVGLGFSGP HSLAAFPAWS TREEGTLEFT LTTRSQQAPL 250 260 270 280 290 300 AFQAGDKRGN FIYVDIFEGH LRAVVEKGQG TMLLRNSVPV ADGQPHEVSV HIDVHRLEIS 310 320 330 340 350 360 VDQYPTRTFN RGVLSYLEPR GSLLLGGLDT EASRHLQEHR LGLAPGAANI SLVGCIEDFS 370 380 390 400 410 420 VNGRRQGLRD AWLTRDMSAG CRPEEDEYEE EVYGPYETFS TLAPEAWPAM ELPEPCIPEP 430 440 450 460 470 480 GLPAVFANFT QLLTISPLVV AEGGTAWLEW RHVQPTLDLT EAELRKSQVL FSVSQSARHG 490 500 510 520 530 540 DLELDILGAQ TRKMFTLLDV VNRKARFVHD GSEDTSDQLM LEVSVTARAP VPSCLRRGQI 550 560 570 580 590 600 YILPIQVNPV NDPPRIIFPH GSLMVILEHT QKPLGPEIFQ AYDPDSACEG LTFQLLGVSS 610 620 630 640 650 660 GVPVEHRDQP GEPATEFSCR ELEVGDIVYV HRGGPAQDLT FRVSDGMQAS APATLKVVAV 670 680 690 700 710 720 RPAIQILHNT GLHLAQGSAA AILPANLSVE TNAVGQDVSV LFRVTGTLQF GELQKQGAGG 730 740 750 760 770 780 VEGTEWWDTL AFHQRDVEQG RVRYLSTDPQ HHTQDTVEDL ILEVQVGQET LSNLSFPVTI 790 800 810 820 830 840 QRATVWMLRL EPLHTQNPHQ ETLTPAHLEA SLEEEEEEGS PQPHTFHYEL VQAPRRGNLL 850 860 870 880 890 900 LQGTRLSDGE SFSQSDLQAG RVTYRATMRT SEAADDSFRF RVTSPPHFSP LYTFPIHIGG 910 920 930 940 950 960 DPNAPVLTNV LLMVPEGGEG VLSADHLFVK SLNSASYLYE VMEQPHHGKL AWRDPKGKST 970 980 990 1000 1010 1020 PVTSFTNEDL LHGRLVYQHD DSETIEDDIP FVATRQGEGS GDMAWEEVRG VFRVAIQPVN 1030 1040 1050 1060 1070 1080 DHAPVQTISR VFHVARGGQR LLTTDDVAFS DADSGFSDAQ LVLTRKDLLF GSIVAMEEPT 1090 1100 1110 1120 1130 1140 RPIYRFTQED LRKKQVLFVH SGADHGWLQL QVSDGQHQAT AMLEVQASEP YLHVANSSSL 1150 1160 1170 1180 1190 1200 VVPQGGQGTI DTAVLQLDTN LDIRSGNEVH YHVTAGPQWG QLLRDGQSVT SFSQRDLLDG 1210 1220 1230 1240 1250 1260 AILYSHNGSL SPQDTLAFSV AAGPVHTNTF LQVTIALEGP LAPLQLVQHK KIYVFQGEAA 1270 1280 1290 1300 1310 1320 EIRRDQLEVV QEAVLPADIM FSLRSPPNAG YLVMVSHGAS AEEPPSLDPV QSFSQEAVNS 1330 1340 1350 1360 1370 1380 GRVLYLHSRP GAWSDSFSLD VASGLGDPLE GISVELEVLP TVIPLDVQNF SVPEGGTRTL 1390 1400 1410 1420 1430 1440 APPLVQITGP YFPTLPGLVL QVLEPPQHGA LQKEDHSQDG SLSTFSWREV EEQLIRYVHD 1450 1460 1470 1480 1490 1500 GSETQTDAFV LLANASEMDR QSQPVAFTIT ILPVNDQPPV LTTNTGLQIW EGAIVPIPPE 1510 1520 1530 1540 1550 1560 ALRGTDNDSG PEDLVYTIEQ PSNGRIALRV APDTEVHRFT QAQLDSGLVL FSHRGALEGG 1570 1580 1590 1600 1610 1620 FHFDLSDGAH TSPGHFFRVV AQKQALLSLE GTRKLTVCPE SVQPLSSQSL SASSSTGADP 1630 1640 1650 1660 1670 1680 RHLLYRVVRG PQLGRLLHAQ QGSAEEVLVN FTQAEVRASL LSHHTDPNLT SGGCQLEHPP 1690 HWQLASLDPV PAQG

References

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[1]	"The proteoglycan NG2 is complexed with alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors by the PDZ glutamate receptor interaction protein (GRIP) in glial progenitor cells. Implications for glial-neuronal signaling." Stegmueller J., Werner H., Nave K.-A., Trotter J. J. Biol. Chem. 278:3590-3598(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH GRIP1; GRIP2 AND GRIA2, MUTAGENESIS OF GLN-2324; TYR-2325; TRP-2326 AND VAL-2327, DOMAIN, SUBCELLULAR LOCATION. Tissue: Oligodendrocyte.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Embryo and Skin.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H. Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 999-2327 (ISOFORM 3). Tissue: Fetal brain.
[6]	"PDGF (alpha)-receptor is unresponsive to PDGF-AA in aortic smooth muscle cells from the NG2 knockout mouse." Grako K.A., Ochiya T., Barritt D., Nishiyama A., Stallcup W.B. J. Cell Sci. 112:905-915(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]	"NG2 proteoglycan promotes endothelial cell motility and angiogenesis via engagement of galectin-3 and alpha3beta1 integrin." Fukushi J., Makagiansar I.T., Stallcup W.B. Mol. Biol. Cell 15:3580-3590(2004) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, FUNCTION.
[8]	"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation." Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B. Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130; ASN-1369; ASN-1454; ASN-2021 AND ASN-2080, MASS SPECTROMETRY. Tissue: Myoblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF352400 mRNA. Translation: AAL37505.1. AK028844 mRNA. Translation: BAC26150.1. Sequence problems. AK075625 mRNA. Translation: BAC35866.1. AC126257 Genomic DNA. No translation available. CH466522 Genomic DNA. Translation: EDL25876.1. AK220559 mRNA. Translation: BAD90326.1.
IPI	IPI00128915. IPI00554856. IPI00648223.
RefSeq	NP_620570.2. NM_139001.2.
UniGene	Mm.41329.
3D structure databases
ProteinModelPortal	Q8VHY0.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1787512.
PTM databases
PhosphoSite	Q8VHY0.
Proteomic databases
PaxDb	Q8VHY0.
PRIDE	Q8VHY0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000035661; ENSMUSP00000038909; ENSMUSG00000032911.
GeneID	121021.
KEGG	mmu:121021.
UCSC	uc009ptl.1. mouse.
Organism-specific databases
CTD	1464.
MGI	MGI:2153093. Cspg4.
Rouge	Search...
Phylogenomic databases
eggNOG	NOG261397.
GeneTree	ENSGT00550000074429.
HOGENOM	HOG000170195.
HOVERGEN	HBG081360.
InParanoid	Q8VHY0.
KO	K08115.
OMA	RPIYRFT.
OrthoDB	EOG42BX7N.
Gene expression databases
CleanEx	MM_CSPG4.
Genevestigator	Q8VHY0.
GermOnline	ENSMUSG00000032911. Mus musculus.
Family and domain databases
Gene3D	2.60.120.200. 2 hits.
InterPro	IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR027210. Cspg4. IPR001791. Laminin_G. [Graphical view]
PANTHER	PTHR32539:SF0. PTHR32539:SF0. 1 hit.
Pfam	PF00054. Laminin_G_1. 1 hit. PF02210. Laminin_G_2. 1 hit. [Graphical view]
SMART	SM00282. LamG. 2 hits. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 2 hits.
PROSITE	PS50025. LAM_G_DOMAIN. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	369752.
SOURCE	Search...

Entry information

Entry name

CSPG4_MOUSE

Accession

Primary (citable) accession number: Q8VHY0
Secondary accession number(s): G5E892 , Q5DTG1, Q8BPI8, Q8CE79

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	October 3, 2012
Last modified:	May 29, 2013
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program