CSPG4_MOUSE
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 03-AUG-2022, entry version 155.
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, Spleen,
RC 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 GlyGen; Q8VHY0; 16 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8VHY0; -.
DR PhosphoSitePlus; Q8VHY0; -.
DR MaxQB; Q8VHY0; -.
DR PaxDb; Q8VHY0; -.
DR PeptideAtlas; Q8VHY0; -.
DR PRIDE; Q8VHY0; -.
DR ProteomicsDB; 284040; -. [Q8VHY0-1]
DR ProteomicsDB; 284041; -. [Q8VHY0-2]
DR ProteomicsDB; 284042; -. [Q8VHY0-3]
DR Antibodypedia; 1108; 696 antibodies from 40 providers.
DR DNASU; 121021; -.
DR Ensembl; ENSMUST00000035661; ENSMUSP00000038909; ENSMUSG00000032911. [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 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; YCRTSNP; -.
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; 2 hits in 75 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 tissues.
DR Genevisible; Q8VHY0; MM.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006954; P:inflammatory response; ISO: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 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 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"
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
