CSPG4_RAT
ID CSPG4_RAT Reviewed; 2326 AA.
AC Q00657;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 161.
DE RecName: Full=Chondroitin sulfate proteoglycan 4;
DE AltName: Full=Chondroitin sulfate proteoglycan NG2;
DE AltName: Full=HSN tumor-specific antigen;
DE Flags: Precursor;
GN Name=Cspg4; Synonyms=Ng2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-47; 1011-1016 AND
RP 1466-1477, SUBCELLULAR LOCATION, TOPOLOGY, AND GLYCOSYLATION.
RC TISSUE=Neuron;
RX PubMed=1906475; DOI=10.1083/jcb.114.2.359;
RA Nishiyama A., Dahlin K.J., Prince J.T., Johnstone S.R., Stallcup W.B.;
RT "The primary structure of NG2, a novel membrane-spanning proteoglycan.";
RL J. Cell Biol. 114:359-371(1991).
RN [2]
RP SEQUENCE REVISION TO 2047-2096.
RA Nishiyama A., Dahlin K.J., Prince J.T., Johnstone S.R., Stallcup W.B.;
RL J. Cell Biol. 145:1115-1115(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 556-573 AND 657-667.
RX PubMed=8077056; DOI=10.1002/ijc.2910580514;
RA Leger O., Johnson-Leger C., Jackson E., Coles B., Dean C.;
RT "The chondroitin sulfate proteoglycan NG2 is a tumour-specific antigen on
RT the chemically induced rat chondrosarcoma HSN.";
RL Int. J. Cancer 58:700-705(1994).
RN [4]
RP INTERACTION WITH COL6A2, AND SUBCELLULAR LOCATION.
RX PubMed=2269670; DOI=10.1083/jcb.111.6.3177;
RA Stallcup W.B., Dahlin K., Healy P.;
RT "Interaction of the NG2 chondroitin sulfate proteoglycan with type VI
RT collagen.";
RL J. Cell Biol. 111:3177-3188(1990).
RN [5]
RP INTERACTION WITH COL6A2, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=8305732; DOI=10.1091/mbc.4.11.1097;
RA Nishiyama A., Stallcup W.B.;
RT "Expression of NG2 proteoglycan causes retention of type VI collagen on the
RT cell surface.";
RL Mol. Biol. Cell 4:1097-1108(1993).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=8590808; DOI=10.1091/mbc.6.12.1819;
RA Nishiyama A., Lin X.-H., Stallcup W.B.;
RT "Generation of truncated forms of the NG2 proteoglycan by cell surface
RT proteolysis.";
RL Mol. Biol. Cell 6:1819-1832(1995).
RN [7]
RP INTERACTION WITH COL5A1; COL6A2; TNC AND LAMININ-1.
RX PubMed=8824254; DOI=10.1074/jbc.271.42.26110;
RA Burg M.A., Tillet E., Timpl R., Stallcup W.B.;
RT "Binding of the NG2 proteoglycan to type VI collagen and other
RT extracellular matrix molecules.";
RL J. Biol. Chem. 271:26110-26116(1996).
RN [8]
RP INTERACTION WITH COL6A2, GLYCOSYLATION, DOMAIN, AND FUNCTION.
RX PubMed=9281375; DOI=10.1006/excr.1997.3674;
RA Burg M.A., Nishiyama A., Stallcup W.B.;
RT "A central segment of the NG2 proteoglycan is critical for the ability of
RT glioma cells to bind and migrate toward type VI collagen.";
RL Exp. Cell Res. 235:254-264(1997).
RN [9]
RP INTERACTION WITH COL5A1 AND COL6A2, AND DOMAIN.
RX PubMed=9099729; DOI=10.1074/jbc.272.16.10769;
RA Tillet E., Ruggiero F., Nishiyama A., Stallcup W.B.;
RT "The membrane-spanning proteoglycan NG2 binds to collagens V and VI through
RT the central nonglobular domain of its core protein.";
RL J. Biol. Chem. 272:10769-10776(1997).
RN [10]
RP INTERACTION WITH FGF2 AND PDGFA.
RX PubMed=10358027; DOI=10.1074/jbc.274.24.16831;
RA Goretzki L., Burg M.A., Grako K.A., Stallcup W.B.;
RT "High-affinity binding of basic fibroblast growth factor and platelet-
RT derived growth factor-AA to the core protein of the NG2 proteoglycan.";
RL J. Biol. Chem. 274:16831-16837(1999).
RN [11]
RP INTERACTION WITH PLG, AND FUNCTION.
RX PubMed=10889192; DOI=10.1074/jbc.m002290200;
RA Goretzki L., Lombardo C.R., Stallcup W.B.;
RT "Binding of the NG2 proteoglycan to kringle domains modulates the
RT functional properties of angiostatin and plasmin(ogen).";
RL J. Biol. Chem. 275:28625-28633(2000).
RN [12]
RP INTERACTION WITH MPDZ.
RX PubMed=10967549;
RX DOI=10.1002/1097-4644(20001101)79:2<213::aid-jcb50>3.0.co;2-g;
RA Barritt D.S., Pearn M.T., Zisch A.H., Lee S.S., Javier R.T., Pasquale E.B.,
RA Stallcup W.B.;
RT "The multi-PDZ domain protein MUPP1 is a cytoplasmic ligand for the
RT membrane-spanning proteoglycan NG2.";
RL J. Cell. Biochem. 79:213-224(2000).
RN [13]
RP MUTAGENESIS OF SER-999 AND SER-1342, SUBCELLULAR LOCATION, GLYCOSYLATION AT
RP SER-999, AND FUNCTION.
RX PubMed=11493670; DOI=10.1242/jcs.114.12.2315;
RA Stallcup W.B., Dahlin-Huppe K.;
RT "Chondroitin sulfate and cytoplasmic domain-dependent membrane targeting of
RT the NG2 proteoglycan promotes retraction fiber formation and cell
RT polarization.";
RL J. Cell Sci. 114:2315-2325(2001).
RN [14]
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 [15]
RP DOMAINS, AND FUNCTION.
RX PubMed=12514214; DOI=10.1523/jneurosci.23-01-00175.2003;
RA Ughrin Y.M., Chen Z.J., Levine J.M.;
RT "Multiple regions of the NG2 proteoglycan inhibit neurite growth and induce
RT growth cone collapse.";
RL J. Neurosci. 23:175-186(2003).
RN [16]
RP PHOSPHORYLATION AT THR-2256, INTERACTION WITH PRKCA, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF THR-2256; THR-2265 AND THR-2278, AND FUNCTION.
RX PubMed=15504744; DOI=10.1074/jbc.m411045200;
RA Makagiansar I.T., Williams S., Dahlin-Huppe K., Fukushi J., Mustelin T.,
RA Stallcup W.B.;
RT "Phosphorylation of NG2 proteoglycan by protein kinase C-alpha regulates
RT polarized membrane distribution and cell motility.";
RL J. Biol. Chem. 279:55262-55270(2004).
RN [17]
RP INTERACTION WITH LGALS3; ITGB1 AND ITGA3, 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).
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:10889192, ECO:0000269|PubMed:11493670,
CC ECO:0000269|PubMed:12514214, ECO:0000269|PubMed:15181153,
CC ECO:0000269|PubMed:15504744, ECO:0000269|PubMed:8305732,
CC ECO:0000269|PubMed:9281375}.
CC -!- SUBUNIT: Interacts with GRIP1, GRIP2 and GRIA2. Forms a ternary complex
CC with GRIP1 and GRIA2. Interacts with ITGA4 through its chondroitin
CC sulfate glycosaminoglycan. Interacts with BCAR1, CDC42 and ACK1.
CC Interacts with MMP16 (By similarity). Interacts with the first PDZ
CC domain of MPDZ. Interacts with PRKCA. Interacts with LGALS3 and the
CC integrin composed of ITGB1 and ITGA3. Binds TNC, laminin-1, COL5A1 and
CC COL6A2. Interacts with PLG and angiostatin. Binds FGF2 and PDGFA.
CC {ECO:0000250, ECO:0000269|PubMed:10358027, ECO:0000269|PubMed:10889192,
CC ECO:0000269|PubMed:10967549, ECO:0000269|PubMed:15181153,
CC ECO:0000269|PubMed:15504744, ECO:0000269|PubMed:2269670,
CC ECO:0000269|PubMed:8305732, ECO:0000269|PubMed:8824254,
CC ECO:0000269|PubMed:9099729, ECO:0000269|PubMed:9281375}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15504744,
CC ECO:0000269|PubMed:1906475}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:1906475}; Extracellular side
CC {ECO:0000269|PubMed:1906475}. Apical cell membrane
CC {ECO:0000269|PubMed:15504744}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:1906475}; Extracellular side
CC {ECO:0000269|PubMed:1906475}. Cell projection, lamellipodium membrane
CC {ECO:0000269|PubMed:15504744}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:1906475}; Extracellular side
CC {ECO:0000269|PubMed:1906475}. Cell surface {ECO:0000269|PubMed:2269670,
CC ECO:0000269|PubMed:8305732, ECO:0000269|PubMed:8590808}. Note=Localizes
CC to the plasma membrane of oligodendrocytes (By similarity). Localized
CC at the apical plasma membrane it relocalizes to the lamellipodia of
CC astrocytoma upon phosphorylation by PRKCA (PubMed:15504744). Localizes
CC to the retraction fibers (PubMed:11493670). A fraction may undergo cell
CC surface proteolysis and secretion. {ECO:0000250|UniProtKB:Q8VHY0,
CC ECO:0000269|PubMed:11493670, ECO:0000269|PubMed:15504744}.
CC -!- TISSUE SPECIFICITY: Neural cells and also extraneural tissues,
CC especially in the developing mesenchyme.
CC -!- DEVELOPMENTAL STAGE: The level of expression is highest on immature,
CC proliferating cells and decreases as these cells differentiate.
CC -!- PTM: N-glycosylated.
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.
CC -!- PTM: Phosphorylation by PRKCA regulates its subcellular location and
CC function in cell motility. {ECO:0000269|PubMed:15504744}.
CC -!- MISCELLANEOUS: Valuable marker for several incompletely differentiated
CC precursor cells.
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DR EMBL; X56541; CAA39884.2; -; mRNA.
DR PIR; S16025; A61208.
DR RefSeq; NP_112284.1; NM_031022.1.
DR AlphaFoldDB; Q00657; -.
DR SMR; Q00657; -.
DR BioGRID; 249551; 1.
DR STRING; 10116.ENSRNOP00000023326; -.
DR GlyGen; Q00657; 16 sites.
DR iPTMnet; Q00657; -.
DR PhosphoSitePlus; Q00657; -.
DR PaxDb; Q00657; -.
DR PRIDE; Q00657; -.
DR ABCD; Q00657; 8 sequenced antibodies.
DR GeneID; 81651; -.
DR KEGG; rno:81651; -.
DR UCSC; RGD:619942; rat.
DR CTD; 1464; -.
DR RGD; 619942; Cspg4.
DR eggNOG; KOG3597; Eukaryota.
DR InParanoid; Q00657; -.
DR OrthoDB; 219190at2759; -.
DR PhylomeDB; Q00657; -.
DR Reactome; R-RNO-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-RNO-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-RNO-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-RNO-2024101; CS/DS degradation.
DR PRO; PR:Q00657; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:RGD.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0005518; F:collagen binding; IPI:UniProtKB.
DR GO; GO:0015026; F:coreceptor activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0008347; P:glial cell migration; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IMP:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
DR GO; GO:0016322; P:neuron remodeling; IDA:RGD.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0010226; P:response to lithium ion; IEP:RGD.
DR GO; GO:0097178; P:ruffle assembly; ISO:RGD.
DR GO; GO:0006929; P:substrate-dependent cell migration; ISO:RGD.
DR GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:RGD.
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 Angiogenesis; Cell membrane; Cell projection; Developmental protein;
KW Differentiation; Direct protein sequencing; 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:0000269|PubMed:1906475"
FT CHAIN 30..2326
FT /note="Chondroitin sulfate proteoglycan 4"
FT /id="PRO_0000026695"
FT TOPO_DOM 30..2225
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:1906475"
FT TRANSMEM 2226..2250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2251..2326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:1906475"
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 ECO:0000269|PubMed:12220645"
FT REPEAT 554..646
FT /note="CSPG 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 663..765
FT /note="CSPG 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 784..882
FT /note="CSPG 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 902..993
FT /note="CSPG 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1022..1114
FT /note="CSPG 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1130..1220
FT /note="CSPG 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1242..1341
FT /note="CSPG 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1360..1453
FT /note="CSPG 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1477..1567
FT /note="CSPG 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1585..1683
FT /note="CSPG 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1708..1807
FT /note="CSPG 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1836..1928
FT /note="CSPG 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 1945..2033
FT /note="CSPG 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
FT REPEAT 2042..2151
FT /note="CSPG 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201,
FT ECO:0000269|PubMed:12220645"
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 REGION 575..1044
FT /note="Interaction with COL6A2"
FT REGION 632..1450
FT /note="Interaction with COL5A1"
FT REGION 1590..2225
FT /note="Neurite growth inhibition"
FT REGION 1591..2225
FT /note="Cysteine-containing"
FT REGION 2187..2210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2324..2326
FT /note="PDZ-binding"
FT COMPBIAS 2192..2210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2256
FT /note="Phosphothreonine; by PKC/PRKCA"
FT /evidence="ECO:0000269|PubMed:15504744"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 999
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:11493670"
FT CARBOHYD 1135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1913
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2020
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2038
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2044
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2079
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 170..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 355..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT MUTAGEN 999
FT /note="S->A: No chondroitin sulfate attachment. Loss of
FT localization to the retraction fibers."
FT /evidence="ECO:0000269|PubMed:11493670"
FT MUTAGEN 1342
FT /note="S->A: No effect on chondroitin sulfate attachment."
FT /evidence="ECO:0000269|PubMed:11493670"
FT MUTAGEN 2256
FT /note="T->E: Localized to the lamellipodia. Increases cell
FT motility independently of PRKCA activation."
FT /evidence="ECO:0000269|PubMed:15504744"
FT MUTAGEN 2256
FT /note="T->V: Apically localized. Loss of PRKCA-dependent
FT cell motility."
FT /evidence="ECO:0000269|PubMed:15504744"
FT MUTAGEN 2265
FT /note="T->E: Behaves as wild-type."
FT /evidence="ECO:0000269|PubMed:15504744"
FT MUTAGEN 2265
FT /note="T->V: Behaves as wild-type."
FT /evidence="ECO:0000269|PubMed:15504744"
FT MUTAGEN 2278
FT /note="T->E: Behaves as wild-type."
FT /evidence="ECO:0000269|PubMed:15504744"
FT MUTAGEN 2278
FT /note="T->V: Behaves as wild-type."
FT /evidence="ECO:0000269|PubMed:15504744"
FT CONFLICT 1391..1392
FT /note="LG -> FP (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2326 AA; 251909 MW; FA3E3BCEDB7E5EF5 CRC64;
MLLSPGHPLS APALALILTL ALLVRSTAPA SFFGENHLEV PVPSALTRVD LLLQFSTSQP
EALLLLAAGQ TDHLLLQLQS GHLQVRLALG QNELSLQTPA DTVLSDSTTH TVVLTVSNSW
AVLSVDGVLN TSAPIPKASH LKVPYGLFVG SSGSLDLPYL KGISRPLRGC LHSAILNGRN
LLRPLTPDVH EGCAEEFSAG DEVGLGFSGP HSLAAFPAWS TREEGTLEFT LTTRSQQAPL
AFQAGDKRGN FIYVDIFEGH LRAVVEKGQG TMLLRNSVPV ADGQPHEVSV HIDVHRLEIS
VDQYPTRTFN RGVLSYLEPR GSLLLGGLDT EASRHLQEHR LGLTPGAANI SLVGCIEDFS
VNGRRLGLRD AWLTRDMAAG CRPEEDEYEE EVYGPFEAFS TLAPEAWPVM DLPEPCVPEP
GLPAVFANFT QLLTISPLVV AEGGTAWLEW RHVQPTLDLT EAELRKSQVL FSVSQGARHG
ELELDIPGAQ TRKMFTLLDV VNRKARFVHD GSEDTSDQLM LEVSVTSRAP VPSCLRRGQI
YILPIQVNPV NDPPRIVFPH GSLMVILEHT QKPLGPEIFQ AYDPDSACEG LTIQLLGVSA
SVPVEHRDQP GEPVTEFSCR DLEAGNIVYV HRGGPAQDLT FRVSDGMQAS GPATLKVVAV
RPAIQILHNT GLRLAQGSAA AILPANLSVE TNAVGQDVSV LFRVTGTLQF GELQKQGAGG
VEGTEWWDTL AFHQRDVEQG RVRYLSTDPQ HHTQDTVEDL TLEVQVGQET LSNLSFPVTI
QRATVWMLQL EPLHTQNPHQ ETLTSAHLEA SLEEEGEGGP YPHIFHYELV QAPRRGNLLL
QGTRLSDGQS FSQSDLQAGR VTYRATTRTS EAAEDSFRFR VTSPPHFSPL YTFPIHIGGD
PNAPVLTNVL LMVPEGGEGV LSADHLFVKS LNSASYLYEV MEQPHHGSLA WRDPKGRATP
VTSFTNEDLL HGRLVYQHDD SETIEDDIPF VATRQGEGSG DMAWEEVRGV FRVAIQPVND
HAPVQTISRV FHVARGGQRL LTTDDVAFSD ADSGFSDAQL VLTRKDLLFG SIVAMEEPTR
PIYRFTQEDL RKKQVLFVHS GADHGWLQLQ VSDGQHQATA MLEVQASEPY LHVANSSSLV
VPQGGQGTID TAVLHLDTNL DIRSGNEVHY HVTAGPHWGQ LLRDGQSVTS FSQRDLLDGA
ILYSHNGSLS PQDTLALSVA AGPVHTSTVL QVTIALEGPL APLQLVQHKR IYVFQGEAAE
IRRDQLEVVQ EAVLPADIMF SLRSPPNAGY LVMVSHGASA DGPPSLDPVQ RFSQEAINSG
RVLYLHSRPG AWSDSFSLDV ASGLGDPLEG ISVELEVLPT VIPLDVQNFS VPEGGTRTLA
PPLIQITGPY LGTLPGLVLQ VLEPPQHGAL QKEDRPQDGT LSTFSWREVE EQLIRYVHDG
SETQTDGFIL LANASEMDRQ SQPMAFTITI LPVNDQPPVI TTNTGLQIWE GAIVPIPPEA
LRGIDSDSGP EDLVYTIEQP SNGRIALRVA PDAEAHRFTQ AQLDSGLVLF SHRGALEGGF
HFDLSDGVHT SPGHFFRVVA QKQVLLSLEG SRKLTVCPES VQPLSSQSLS ASSSTGSDPR
HLLYQVVRGP QLGRLLHAQQ GSAEEALVNF TQAEVNAGNI LYEHEISSEP FWEAHDTIGL
LLSSSPARDL AATLAVTVSF DAACPQRPSR LWRNKGLWVP EGQRAKITVA ALDAANLLAS
VPASQRGRHD VLFQITQFPT RGQLLVSEEP LHARRPHFLQ SELTAGQLVY AHGGGGTQQD
GFRFRAHLQG PTGASVAGPQ TSEAFVITVR DVNERPPQPQ ASIPLRITRG SRAPVSRAQL
SVVDPDSAPG EIEYEVQRAP HNGFLSLAGD NTGPVTHFTQ ADVDAGRLAF VANGSSVAGV
FQLSMSDGAS PPIPMSLAVD VLPSTIEVQL RAPLEVPQAL GRSSLSRQQL QVISDREEPD
VAYRLTQGPL YGQVLVGGQP ASAFSQLQVD QGDVVFAFTN FSSSQDHFKV LALARGVNAS
ATVNVTVQAL LHVWAGGPWP QGTTLRLDPT VLDASELANR TGSMPRFRLL EGPRYGRVVR
VSQGRAESRT NQLVEDFTQQ DLEEGRLGLE VGRPEGRSTG PTGDRLTLEL QATGVPPAVA
LLDFATEPYH AAKFYKVTLL SVPEAARTET EKTGKSTPTG QPGQAASSPM PTVAKSGFLG
FLEANMFSVI IPVCLVLLLL ALILPLLFYL RKRNKTGKHD VQVLTAKPRN GLAGDTETFR
KVEPGQAIPL TTVPGQGPPP GGQPDPELLQ FCRTPNPALR NGQYWV
