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Chondroitin sulfate proteoglycan 4 (Chondroitin sulfate proteoglycan NG2) (Proteoglycan AN2)

 CSPG4_MOUSE             Reviewed;        2327 AA.
Q8VHY0; G5E892; Q5DTG1; Q8BPI8; Q8CE79;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 3.
23-MAY-2018, entry version 131.
RecName: Full=Chondroitin sulfate proteoglycan 4;
AltName: Full=Chondroitin sulfate proteoglycan NG2;
AltName: Full=Proteoglycan AN2;
Flags: Precursor;
Name=Cspg4; Synonyms=An2, Kiaa4232, Ng2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH GRIP1; GRIP2
AND GRIA2, MUTAGENESIS OF GLN-2324; TYR-2325; TRP-2326 AND VAL-2327,
DOMAIN, AND SUBCELLULAR LOCATION.
TISSUE=Oligodendrocyte;
PubMed=12458226; DOI=10.1074/jbc.M210010200;
Stegmueller J., Werner H., Nave K.-A., Trotter J.;
"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.";
J. Biol. Chem. 278:3590-3598(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Embryo, and Skin;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 999-2327 (ISOFORM 3).
TISSUE=Fetal brain;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
Koga H.;
"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.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10036240;
Grako K.A., Ochiya T., Barritt D., Nishiyama A., Stallcup W.B.;
"PDGF (alpha)-receptor is unresponsive to PDGF-AA in aortic smooth
muscle cells from the NG2 knockout mouse.";
J. Cell Sci. 112:905-915(1999).
[7]
TISSUE SPECIFICITY, AND FUNCTION.
PubMed=15181153; DOI=10.1091/mbc.E04-03-0236;
Fukushi J., Makagiansar I.T., Stallcup W.B.;
"NG2 proteoglycan promotes endothelial cell motility and angiogenesis
via engagement of galectin-3 and alpha3beta1 integrin.";
Mol. Biol. Cell 15:3580-3590(2004).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130; ASN-1369; ASN-1454;
ASN-2021 AND ASN-2080.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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. {ECO:0000269|PubMed:10036240,
ECO:0000269|PubMed:15181153}.
-!- SUBUNIT: 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. {ECO:0000250,
ECO:0000269|PubMed:12458226}.
-!- INTERACTION:
P23819:Gria2; NbExp=2; IntAct=EBI-8327479, EBI-77538;
Q925T6:Grip1; NbExp=7; IntAct=EBI-8327479, EBI-537752;
Q9WTW1:Grip2 (xeno); NbExp=2; IntAct=EBI-8327479, EBI-936045;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12458226};
Single-pass type I membrane protein
{ECO:0000250|UniProtKB:Q00657}; Extracellular side
{ECO:0000250|UniProtKB:Q00657}. Apical cell membrane
{ECO:0000250|UniProtKB:Q00657}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q00657}; Extracellular side
{ECO:0000250|UniProtKB:Q00657}. Cell projection, lamellipodium
membrane {ECO:0000250|UniProtKB:Q00657}; Single-pass type I
membrane protein {ECO:0000250|UniProtKB:Q00657}; Extracellular
side {ECO:0000250|UniProtKB:Q00657}. Cell surface
{ECO:0000250|UniProtKB:Q00657}. 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
(PubMed:12458226). {ECO:0000250|UniProtKB:Q00657,
ECO:0000269|PubMed:12458226}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8VHY0-1; Sequence=Displayed;
Name=2;
IsoId=Q8VHY0-2; Sequence=VSP_015656;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8VHY0-3; Sequence=VSP_015657, VSP_015658;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in microcascular pericytes and not
endothelial cells. {ECO:0000269|PubMed:15181153}.
-!- 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 (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylation by PRKCA regulates its subcellular location
and function in cell motility. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice are unresponsive to PDGF-AA through
PDGF-alpha receptor. {ECO:0000269|PubMed:10036240}.
-!- MISCELLANEOUS: Valuable marker for several incompletely
differentiated precursor cells.
-!- SEQUENCE CAUTION:
Sequence=BAC26150.1; Type=Frameshift; Positions=1889; Evidence={ECO:0000305};
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EMBL; AF352400; AAL37505.1; -; mRNA.
EMBL; AK028844; BAC26150.1; ALT_SEQ; mRNA.
EMBL; AK075625; BAC35866.1; -; mRNA.
EMBL; AC126257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466522; EDL25876.1; -; Genomic_DNA.
EMBL; AK220559; BAD90326.1; -; mRNA.
CCDS; CCDS23211.1; -. [Q8VHY0-1]
RefSeq; NP_620570.2; NM_139001.2. [Q8VHY0-1]
UniGene; Mm.41329; -.
ProteinModelPortal; Q8VHY0; -.
SMR; Q8VHY0; -.
BioGrid; 228250; 1.
CORUM; Q8VHY0; -.
IntAct; Q8VHY0; 5.
MINT; Q8VHY0; -.
STRING; 10090.ENSMUSP00000038909; -.
iPTMnet; Q8VHY0; -.
PhosphoSitePlus; Q8VHY0; -.
PaxDb; Q8VHY0; -.
PeptideAtlas; Q8VHY0; -.
PRIDE; Q8VHY0; -.
Ensembl; ENSMUST00000035661; ENSMUSP00000038909; ENSMUSG00000032911. [Q8VHY0-1]
GeneID; 121021; -.
KEGG; mmu:121021; -.
UCSC; uc009ptl.1; mouse. [Q8VHY0-1]
UCSC; uc009ptn.1; mouse. [Q8VHY0-3]
UCSC; uc009pto.1; mouse. [Q8VHY0-2]
CTD; 1464; -.
MGI; MGI:2153093; Cspg4.
eggNOG; KOG3597; Eukaryota.
eggNOG; ENOG410XQ29; LUCA.
GeneTree; ENSGT00550000074429; -.
HOGENOM; HOG000170195; -.
HOVERGEN; HBG081360; -.
InParanoid; Q8VHY0; -.
KO; K08115; -.
OMA; EPFWEAH; -.
OrthoDB; EOG091G00BN; -.
TreeFam; TF316876; -.
Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
Reactome; R-MMU-2022923; Dermatan sulfate biosynthesis.
Reactome; R-MMU-2024101; CS/DS degradation.
ChiTaRS; Cspg4; mouse.
PRO; PR:Q8VHY0; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032911; -.
CleanEx; MM_CSPG4; -.
Genevisible; Q8VHY0; MM.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0042995; C:cell projection; IDA:MGI.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
GO; GO:0000187; P:activation of MAPK activity; IMP:MGI.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; IMP:MGI.
GO; GO:0008347; P:glial cell migration; IDA:MGI.
GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IMP:MGI.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR039005; CSPG_rpt.
InterPro; IPR001791; Laminin_G.
Pfam; PF00054; Laminin_G_1; 1.
Pfam; PF02210; Laminin_G_2; 1.
SMART; SM00282; LamG; 2.
SUPFAM; SSF49899; SSF49899; 2.
PROSITE; PS51854; CSPG; 15.
PROSITE; PS50025; LAM_G_DOMAIN; 2.
1: Evidence at protein level;
Alternative splicing; Angiogenesis; Cell membrane; Cell projection;
Complete proteome; Developmental protein; Differentiation;
Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Proteoglycan;
Reference proteome; Repeat; Signal; Tissue remodeling; Transducer;
Transmembrane; Transmembrane helix.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 2327 Chondroitin sulfate proteoglycan 4.
/FTId=PRO_0000041963.
TOPO_DOM 30 2229 Extracellular.
{ECO:0000250|UniProtKB:Q00657}.
TRANSMEM 2230 2250 Helical. {ECO:0000255}.
TOPO_DOM 2251 2327 Cytoplasmic.
{ECO:0000250|UniProtKB:Q00657}.
DOMAIN 30 193 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 203 381 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
REPEAT 429 524 CSPG 1. {ECO:0000255|PROSITE-
ProRule:PRU01201}.
REPEAT 554 646 CSPG 2. {ECO:0000255|PROSITE-
ProRule:PRU01201}.
REPEAT 663 765 CSPG 3. {ECO:0000255|PROSITE-
ProRule:PRU01201}.
REPEAT 784 883 CSPG 4. {ECO:0000255|PROSITE-
ProRule:PRU01201}.
REPEAT 903 994 CSPG 5. {ECO:0000255|PROSITE-
ProRule:PRU01201}.
REPEAT 1023 1115 CSPG 6. {ECO:0000255|PROSITE-
ProRule:PRU01201}.
REPEAT 1131 1221 CSPG 7. {ECO:0000255|PROSITE-
ProRule:PRU01201}.
REPEAT 1243 1342 CSPG 8. {ECO:0000255|PROSITE-
ProRule:PRU01201}.
REPEAT 1361 1454 CSPG 9. {ECO:0000255|PROSITE-
ProRule:PRU01201}.
REPEAT 1478 1568 CSPG 10. {ECO:0000255|PROSITE-
ProRule:PRU01201}.
REPEAT 1586 1684 CSPG 11. {ECO:0000255|PROSITE-
ProRule:PRU01201}.
REPEAT 1709 1808 CSPG 12. {ECO:0000255|PROSITE-
ProRule:PRU01201}.
REPEAT 1837 1929 CSPG 13. {ECO:0000255|PROSITE-
ProRule:PRU01201}.
REPEAT 1946 2034 CSPG 14. {ECO:0000255|PROSITE-
ProRule:PRU01201}.
REPEAT 2043 2152 CSPG 15. {ECO:0000255|PROSITE-
ProRule:PRU01201}.
REGION 30 640 Globular or compact configuration
stabilized by disulfide bonds.
REGION 30 640 Neurite growth inhibition. {ECO:0000250}.
REGION 575 1045 Interaction with COL6A2. {ECO:0000250}.
REGION 632 1451 Interaction with COL5A1. {ECO:0000250}.
REGION 1591 2226 Neurite growth inhibition. {ECO:0000250}.
REGION 1592 2226 Cysteine-containing.
MOTIF 2325 2327 PDZ-binding.
COMPBIAS 640 1591 Gly/Ser-rich (glycosaminoglycan
attachment domain).
MOD_RES 2257 2257 Phosphothreonine; by PKC/PRKCA.
{ECO:0000250|UniProtKB:Q00657}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 349 349 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 428 428 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 686 686 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 773 773 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1000 1000 O-linked (Xyl...) (chondroitin sulfate)
serine. {ECO:0000250}.
CARBOHYD 1136 1136 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1207 1207 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1369 1369 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 1454 1454 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 1650 1650 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1914 1914 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2021 2021 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 2039 2039 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2045 2045 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2080 2080 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
DISULFID 170 193 {ECO:0000255|PROSITE-ProRule:PRU00122}.
DISULFID 355 381 {ECO:0000255|PROSITE-ProRule:PRU00122}.
VAR_SEQ 1 1666 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_015656.
VAR_SEQ 1657 1694 NAGNILYEHEMSSEPFWEAHDTIGLLLSSPPARDLAAT ->
RASLLSHHTDPNLTSGGCQLEHPPHWQLASLDPVPAQG
(in isoform 3). {ECO:0000303|Ref.5}.
/FTId=VSP_015657.
VAR_SEQ 1695 2327 Missing (in isoform 3).
{ECO:0000303|Ref.5}.
/FTId=VSP_015658.
MUTAGEN 2324 2324 Q->G: No effect on interaction with GRIP1
and GRIP2. {ECO:0000269|PubMed:12458226}.
MUTAGEN 2325 2325 Y->F: No effect on interaction with GRIP1
and GRIP2. {ECO:0000269|PubMed:12458226}.
MUTAGEN 2325 2325 Y->G: Loss of interaction with GRIP1 and
GRIP2. {ECO:0000269|PubMed:12458226}.
MUTAGEN 2326 2326 W->G: Loss of interaction with GRIP1 and
GRIP2. {ECO:0000269|PubMed:12458226}.
MUTAGEN 2327 2327 V->G: Loss of interaction with GRIP1 and
GRIP2. {ECO:0000269|PubMed:12458226}.
CONFLICT 1058 1058 D -> V (in Ref. 1; AAL37505).
{ECO:0000305}.
CONFLICT 1113 1113 S -> P (in Ref. 5; BAD90326).
{ECO:0000305}.
CONFLICT 1427 1427 W -> R (in Ref. 1; AAL37505).
{ECO:0000305}.
CONFLICT 1520 1520 Q -> E (in Ref. 1; AAL37505).
{ECO:0000305}.
CONFLICT 1546 1546 S -> G (in Ref. 1; AAL37505).
{ECO:0000305}.
CONFLICT 1929 1929 G -> E (in Ref. 1; AAL37505).
{ECO:0000305}.
CONFLICT 2000 2000 Q -> R (in Ref. 1; AAL37505).
{ECO:0000305}.
CONFLICT 2011 2011 D -> H (in Ref. 2; BAC26150).
{ECO:0000305}.
CONFLICT 2093 2093 G -> E (in Ref. 1; AAL37505).
{ECO:0000305}.
CONFLICT 2248 2248 L -> H (in Ref. 1; AAL37505).
{ECO:0000305}.
CONFLICT 2300 2300 P -> S (in Ref. 1; AAL37505).
{ECO:0000305}.
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


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