Cspg4
entrez
81651
canonical
uniprot
Q00657
canonical
ensembl
ENSRNOG00000017208
resolver
ensp
ENSRNOP00000023326
resolver
enst
ENSRNOT00000023326
resolver
genesymbol
Cspg4
resolver
genesymbol_syn
Ng2
resolver
uniprot
F1LS79
resolver
uniprot_entry
CSPG4_RAT
resolver
uniprot_entry
F1LS79_RAT
resolver
amino_acid_sequence
MLLSPGHPLSAPALALILTLALLVRSTAPASFFGENHLEVPVPSALTRVDLLLQFSTSQPEALLLLAAGQTDHLLLQLQSGHLQVRLALGQNELSLQTPADTVLSDSTTHTVVLTVSNSWAVLSVDGVLNTSAPIPKASHLKVPYGLFVGSSGSLDLPYLKGISRPLRGCLHSAILNGRNLLRPLTPDVHEGCAEEFSAGDEVGLGFSGPHSLAAFPAWSTREEGTLEFTLTTRSQQAPLAFQAGDKRGNFIYVDIFEGHLRAVVEKGQGTMLLRNSVPVADGQPHEVSVHIDVHRLEISVDQYPTRTFNRGVLSYLEPRGSLLLGGLDTEASRHLQEHRLGLTPGAANISLVGCIEDFSVNGRRLGLRDAWLTRDMAAGCRPEEDEYEEEVYGPFEAFSTLAPEAWPVMDLPEPCVPEPGLPAVFANFTQLLTISPLVVAEGGTAWLEWRHVQPTLDLTEAELRKSQVLFSVSQGARHGELELDIPGAQTRKMFTLLDVVNRKARFVHDGSEDTSDQLMLEVSVTSRAPVPSCLRRGQIYILPIQVNPVNDPPRIVFPHGSLMVILEHTQKPLGPEIFQAYDPDSACEGLTIQLLGVSASVPVEHRDQPGEPVTEFSCRDLEAGNIVYVHRGGPAQDLTFRVSDGMQASGPATLKVVAVRPAIQILHNTGLRLAQGSAAAILPANLSVETNAVGQDVSVLFRVTGTLQFGELQKQGAGGVEGTEWWDTLAFHQRDVEQGRVRYLSTDPQHHTQDTVEDLTLEVQVGQETLSNLSFPVTIQRATVWMLQLEPLHTQNPHQETLTSAHLEASLEEEGEGGPYPHIFHYELVQAPRRGNLLLQGTRLSDGQSFSQSDLQAGRVTYRATTRTSEAAEDSFRFRVTSPPHFSPLYTFPIHIGGDPNAPVLTNVLLMVPEGGEGVLSADHLFVKSLNSASYLYEVMEQPHHGSLAWRDPKGRATPVTSFTNEDLLHGRLVYQHDDSETIEDDIPFVATRQGEGSGDMAWEEVRGVFRVAIQPVNDHAPVQTISRVFHVARGGQRLLTTDDVAFSDADSGFSDAQLVLTRKDLLFGSIVAMEEPTRPIYRFTQEDLRKKQVLFVHSGADHGWLQLQVSDGQHQATAMLEVQASEPYLHVANSSSLVVPQGGQGTIDTAVLHLDTNLDIRSGNEVHYHVTAGPHWGQLLRDGQSVTSFSQRDLLDGAILYSHNGSLSPQDTLALSVAAGPVHTSTVLQVTIALEGPLAPLQLVQHKRIYVFQGEAAEIRRDQLEVVQEAVLPADIMFSLRSPPNAGYLVMVSHGASADGPPSLDPVQRFSQEAINSGRVLYLHSRPGAWSDSFSLDVASGLGDPLEGISVELEVLPTVIPLDVQNFSVPEGGTRTLAPPLIQITGPYLGTLPGLVLQVLEPPQHGALQKEDRPQDGTLSTFSWREVEEQLIRYVHDGSETQTDGFILLANASEMDRQSQPMAFTITILPVNDQPPVITTNTGLQIWEGAIVPIPPEALRGIDSDSGPEDLVYTIEQPSNGRIALRVAPDAEAHRFTQAQLDSGLVLFSHRGALEGGFHFDLSDGVHTSPGHFFRVVAQKQVLLSLEGSRKLTVCPESVQPLSSQSLSASSSTGSDPRHLLYQVVRGPQLGRLLHAQQGSAEEALVNFTQAEVNAGNILYEHEISSEPFWEAHDTIGLLLSSSPARDLAATLAVTVSFDAACPQRPSRLWRNKGLWVPEGQRAKITVAALDAANLLASVPASQRGRHDVLFQITQFPTRGQLLVSEEPLHARRPHFLQSELTAGQLVYAHGGGGTQQDGFRFRAHLQGPTGASVAGPQTSEAFVITVRDVNERPPQPQASIPLRITRGSRAPVSRAQLSVVDPDSAPGEIEYEVQRAPHNGFLSLAGDNTGPVTHFTQADVDAGRLAFVANGSSVAGVFQLSMSDGASPPIPMSLAVDVLPSTIEVQLRAPLEVPQALGRSSLSRQQLQVISDREEPDVAYRLTQGPLYGQVLVGGQPASAFSQLQVDQGDVVFAFTNFSSSQDHFKVLALARGVNASATVNVTVQALLHVWAGGPWPQGTTLRLDPTVLDASELANRTGSMPRFRLLEGPRYGRVVRVSQGRAESRTNQLVEDFTQQDLEEGRLGLEVGRPEGRSTGPTGDRLTLELQATGVPPAVALLDFATEPYHAAKFYKVTLLSVPEAARTETEKTGKSTPTGQPGQAASSPMPTVAKSGFLGFLEANMFSVIIPVCLVLLLLALILPLLFYLRKRNKTGKHDVQVLTAKPRNGLAGDTETFRKVEPGQAIPLTTVPGQGPPPGGQPDPELLQFCRTPNPALRNGQYWV
uniprot
proteins
function
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. Also functions 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. {ECO:0000269|PubMed:10889192, ECO:0000269|PubMed:11493670, ECO:0000269|PubMed:12514214, ECO:0000269|PubMed:15181153, ECO:0000269|PubMed:15504744, ECO:0000269|PubMed:8305732, ECO:0000269|PubMed:9281375}.
uniprot
proteins
mass_dalton
251909
uniprot
proteins
mutagenesis
MUTAGEN 999; /note="S->A: No chondroitin sulfate attachment. Loss of localization to the retraction fibers."; /evidence="ECO:0000269|PubMed:11493670"; MUTAGEN 1342; /note="S->A: No effect on chondroitin sulfate attachment."; /evidence="ECO:0000269|PubMed:11493670"; MUTAGEN 2256; /note="T->E: Localized to the lamellipodia. Increases cell motility independently of PRKCA activation."; /evidence="ECO:0000269|PubMed:15504744"; MUTAGEN 2256; /note="T->V: Apically localized. Loss of PRKCA-dependent cell motility."; /evidence="ECO:0000269|PubMed:15504744"; MUTAGEN 2265; /note="T->E: Behaves as wild-type."; /evidence="ECO:0000269|PubMed:15504744"; MUTAGEN 2265; /note="T->V: Behaves as wild-type."; /evidence="ECO:0000269|PubMed:15504744"; MUTAGEN 2278; /note="T->E: Behaves as wild-type."; /evidence="ECO:0000269|PubMed:15504744"; MUTAGEN 2278; /note="T->V: Behaves as wild-type."; /evidence="ECO:0000269|PubMed:15504744
uniprot
proteins
post_translational_modification
PTM: N-glycosylated.; PTM: 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.; PTM: Phosphorylation by PRKCA regulates its subcellular location and function in cell motility. {ECO:0000269|PubMed:15504744}.
uniprot
proteins
pubmed
10358027
uniprot
proteins
pubmed
10889192
uniprot
proteins
pubmed
10967549
uniprot
proteins
pubmed
11493670
uniprot
proteins
pubmed
12220645
uniprot
proteins
pubmed
12514214
uniprot
proteins
pubmed
15181153
uniprot
proteins
pubmed
15504744
uniprot
proteins
pubmed
1906475
uniprot
proteins
pubmed
2269670
uniprot
proteins
pubmed
8077056
uniprot
proteins
pubmed
8305732
uniprot
proteins
pubmed
8590808
uniprot
proteins
pubmed
8824254
uniprot
proteins
pubmed
9099729
uniprot
proteins
pubmed
9281375
uniprot
proteins
sequence_length
2326
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15504744, ECO:0000269|PubMed:1906475}; Single-pass type I membrane protein {ECO:0000269|PubMed:1906475}; Extracellular side {ECO:0000269|PubMed:1906475}. Apical cell membrane {ECO:0000269|PubMed:15504744}; Single-pass type I membrane protein {ECO:0000269|PubMed:1906475}; Extracellular side {ECO:0000269|PubMed:1906475}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:15504744}; Single-pass type I membrane protein {ECO:0000269|PubMed:1906475}; Extracellular side {ECO:0000269|PubMed:1906475}. Cell surface {ECO:0000269|PubMed:2269670, ECO:0000269|PubMed:8305732, ECO:0000269|PubMed:8590808}. Note=Localizes to the plasma membrane of oligodendrocytes (By similarity). Localized at the apical plasma membrane it relocalizes to the lamellipodia of astrocytoma upon phosphorylation by PRKCA (PubMed:15504744). Localizes to the retraction fibers (PubMed:11493670). A fraction may undergo cell surface proteolysis and secretion. {ECO:0000250|UniProtKB:Q8VHY0, ECO:0000269|PubMed:11493670, ECO:0000269|PubMed:15504744}.
uniprot
proteins
transmembrane_region
TRANSMEM 2226..2250; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins