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Rho GTPase-activating protein 32 (Brain-specific Rho GTPase-activating protein) (GAB-associated Cdc42/Rac GTPase-activating protein) (GC-GAP) (GTPase regulator interacting with TrkA) (Rho-type GTPase-activating protein 32) (Rho/Cdc42/Rac GTPase-activating protein RICS) (RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling) (p200RhoGAP) (p250GAP)

 RHG32_HUMAN             Reviewed;        2087 AA.
A7KAX9; I7H0B0; O94820; Q86YL6; Q8IUG4; Q9BWG3;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 1.
22-NOV-2017, entry version 105.
RecName: Full=Rho GTPase-activating protein 32;
AltName: Full=Brain-specific Rho GTPase-activating protein;
AltName: Full=GAB-associated Cdc42/Rac GTPase-activating protein;
AltName: Full=GC-GAP;
AltName: Full=GTPase regulator interacting with TrkA;
AltName: Full=Rho-type GTPase-activating protein 32;
AltName: Full=Rho/Cdc42/Rac GTPase-activating protein RICS;
AltName: Full=RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling;
AltName: Full=p200RhoGAP;
AltName: Full=p250GAP;
Name=ARHGAP32; Synonyms=GRIT, KIAA0712, RICS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
NTRK1; SHC3; BCAR1; EGFR; CRK AND CRKL, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, PHOSPHORYLATION, AND MUTAGENESIS OF ARG-407.
TISSUE=Brain;
PubMed=12446789; DOI=10.1128/MCB.22.24.8721-8734.2002;
Nakamura T., Komiya M., Sone K., Hirose E., Gotoh N., Morii H.,
Ohta Y., Mori N.;
"Grit, a GTPase-activating protein for the Rho family, regulates
neurite extension through association with the TrkA receptor and N-Shc
and CrkL/Crk adapter molecules.";
Mol. Cell. Biol. 22:8721-8734(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
CTNNB1, AND MUTAGENESIS OF ARG-407 AND LYS-447.
PubMed=12531901; DOI=10.1074/jbc.M208872200;
Okabe T., Nakamura T., Nishimura Y.N., Kohu K., Ohwada S.,
Morishita Y., Akiyama T.;
"RICS, a novel GTPase-activating protein for Cdc42 and Rac1, is
involved in the beta-catenin-N-cadherin and N-methyl-D-aspartate
receptor signaling.";
J. Biol. Chem. 278:9920-9927(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
GAB1 AND GAB2; BCAR1; CRK AND NCK1, AND SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=12819203; DOI=10.1074/jbc.M304594200;
Zhao C., Ma H., Bossy-Wetzel E., Lipton S.A., Zhang Z., Feng G.S.;
"GC-GAP, a Rho family GTPase-activating protein that interacts with
signaling adapters Gab1 and Gab2.";
J. Biol. Chem. 278:34641-34653(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING,
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-173 AND
ARG-407.
PubMed=17663722; DOI=10.1111/j.1365-2443.2007.01101.x;
Hayashi T., Okabe T., Nasu-Nishimura Y., Sakaue F., Ohwada S.,
Matsuura K., Akiyama T., Nakamura T.;
"PX-RICS, a novel splicing variant of RICS, is a main isoform
expressed during neural development.";
Genes Cells 12:929-939(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=9872452; DOI=10.1093/dnares/5.5.277;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XI.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:277-286(1998).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Colon, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, INTERACTION WITH FYN, AND PHOSPHORYLATION (ISOFORM 2).
PubMed=12788081; DOI=10.1016/S0006-291X(03)00923-9;
Taniguchi S., Liu H., Nakazawa T., Yokoyama K., Tezuka T.,
Yamamoto T.;
"p250GAP, a neural RhoGAP protein, is associated with and
phosphorylated by Fyn.";
Biochem. Biophys. Res. Commun. 306:151-155(2003).
[9]
FUNCTION, AND MUTAGENESIS OF ARG-407.
PubMed=12454018; DOI=10.1074/jbc.M207789200;
Moon S.Y., Zang H., Zheng Y.;
"Characterization of a brain-specific Rho GTPase-activating protein,
p200RhoGAP.";
J. Biol. Chem. 278:4151-4159(2003).
[10]
FUNCTION, INTERACTION WITH GRIN2B, AND MUTAGENESIS OF ARG-407.
PubMed=12857875; DOI=10.1091/mbc.E02-09-0623;
Nakazawa T., Watabe A.M., Tezuka T., Yoshida Y., Yokoyama K.,
Umemori H., Inoue A., Okabe S., Manabe T., Yamamoto T.;
"p250GAP, a novel brain-enriched GTPase-activating protein for Rho
family GTPases, is involved in the N-methyl-d-aspartate receptor
signaling.";
Mol. Biol. Cell 14:2921-2934(2003).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1203, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706 AND SER-892, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-952, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 367-577.
Structural genomics consortium (SGC);
"Crystal structure of the Rho-GAP domain of RICS.";
Submitted (SEP-2009) to the PDB data bank.
-!- FUNCTION: GTPase-activating protein (GAP) promoting GTP hydrolysis
on RHOA, CDC42 and RAC1 small GTPases. May be involved in the
differentiation of neuronal cells during the formation of neurite
extensions. Involved in NMDA receptor activity-dependent actin
reorganization in dendritic spines. May mediate cross-talks
between Ras- and Rho-regulated signaling pathways in cell growth
regulation. Isoform 2 has higher GAP activity (By similarity).
{ECO:0000250, ECO:0000269|PubMed:12446789,
ECO:0000269|PubMed:12454018, ECO:0000269|PubMed:12531901,
ECO:0000269|PubMed:12788081, ECO:0000269|PubMed:12819203,
ECO:0000269|PubMed:12857875, ECO:0000269|PubMed:17663722}.
-!- SUBUNIT: Interacts with NTRK1 (via cytoplasmic domain); the
interaction is independent of the phosphorylation state of NTRK1.
Interacts with SHC3 (via SH2 domain). Interacts with RASA1 (via
SH3 domain); the interaction is necessary for the Ras activation
and cell transforming activities of ARHGAP32 (By similarity).
Interacts with GAB1 and GAB2. Interacts with CRK and CRKL. Found
in a complex with CRKL and BCAR1; upon EGF stimulation BCAR1 may
be replaced by EGFR. Interacts with NCK1 (via SH3 domain); NCK1
recruits phosphorylated BCAR1 to the complex. Isoform 2 interacts
with FYN; the interaction appears to be dependent on tyrosine
phosphorylation of ARHGAP32. Interacts with EGFR; the interaction
requires EGF stimulation and is increased by SHC3. Interacts with
CDC42; the interaction requires constitutively active CDC42.
Interacts with CTNNB1, DLG4, CDH2 and GRIN2B (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q9NYB9:ABI2; NbExp=3; IntAct=EBI-308663, EBI-743598;
Q08117:AES; NbExp=3; IntAct=EBI-308663, EBI-717810;
Q86Y13:DZIP3; NbExp=3; IntAct=EBI-308663, EBI-948630;
P06241:FYN; NbExp=4; IntAct=EBI-308663, EBI-515315;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-308663, EBI-741037;
Q99750:MDFI; NbExp=3; IntAct=EBI-308663, EBI-724076;
O43639:NCK2; NbExp=3; IntAct=EBI-308663, EBI-713635;
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane, postsynaptic density {ECO:0000250|UniProtKB:Q811P8}.
Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q811P8}.
Cytoplasm, cell cortex {ECO:0000269|PubMed:12446789}. Endosome
membrane {ECO:0000269|PubMed:17663722}. Golgi apparatus membrane
{ECO:0000269|PubMed:17663722}. Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q811P8}. Membrane
{ECO:0000269|PubMed:17663722}. Note=Association to membrane via PX
domain (PubMed:17663722). Associated with cortical actin in
undifferentiated neuroblastoma cells, but localized to dendritic
spine and postsynaptic density after differentiation (By
similarity). Colocalizes with EGFR at the cell membrane upon EGF
treatment (PubMed:12446789). Colocalizes with GAB2 at the cell
membrane (PubMed:12819203). {ECO:0000250|UniProtKB:Q811P8,
ECO:0000269|PubMed:12446789, ECO:0000269|PubMed:12819203,
ECO:0000269|PubMed:17663722}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=PX-RICS;
IsoId=A7KAX9-1; Sequence=Displayed;
Name=2;
IsoId=A7KAX9-2; Sequence=VSP_034933;
Name=3;
IsoId=A7KAX9-3; Sequence=VSP_034934, VSP_034935, VSP_034936;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed
in brain and testis. Isoform 1 is also expressed in other tissues
such as lung, liver and spleen. {ECO:0000269|PubMed:12446789}.
-!- DOMAIN: The N-terminal PX domain interacts specifically with
phosphatidylinositides. {ECO:0000250}.
-!- PTM: Isoform 2 is phosphorylated on multiple tyrosine residues by
FYN. Phosphorylated tyrosine residues undergo dephosphorylation
after stimulation of NMDA receptors (By similarity).
Phosphorylated in vitro by CaMK2 in the presence of calmodulin and
calcium; which inhibits GAP activity (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the PX domain-containing GAP family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA34432.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB079856; BAC24802.1; -; mRNA.
EMBL; AY194287; AAO43677.1; -; mRNA.
EMBL; AB088416; BAM34446.1; -; mRNA.
EMBL; EF127492; ABO33171.1; -; mRNA.
EMBL; AB018255; BAA34432.2; ALT_INIT; mRNA.
EMBL; CH471065; EAW67740.1; -; Genomic_DNA.
EMBL; BC000277; AAH00277.2; -; mRNA.
EMBL; BC104898; AAI04899.1; -; mRNA.
EMBL; BC113429; AAI13430.1; -; mRNA.
CCDS; CCDS31718.1; -. [A7KAX9-2]
CCDS; CCDS44769.1; -. [A7KAX9-1]
RefSeq; NP_001136157.1; NM_001142685.1. [A7KAX9-1]
RefSeq; NP_055530.2; NM_014715.3. [A7KAX9-2]
UniGene; Hs.440379; -.
PDB; 3IUG; X-ray; 1.77 A; A/B=367-577.
PDBsum; 3IUG; -.
ProteinModelPortal; A7KAX9; -.
SMR; A7KAX9; -.
BioGrid; 115091; 43.
IntAct; A7KAX9; 23.
MINT; MINT-268455; -.
STRING; 9606.ENSP00000310561; -.
iPTMnet; A7KAX9; -.
PhosphoSitePlus; A7KAX9; -.
BioMuta; ARHGAP32; -.
EPD; A7KAX9; -.
MaxQB; A7KAX9; -.
PaxDb; A7KAX9; -.
PRIDE; A7KAX9; -.
Ensembl; ENST00000310343; ENSP00000310561; ENSG00000134909. [A7KAX9-1]
Ensembl; ENST00000392657; ENSP00000376425; ENSG00000134909. [A7KAX9-2]
Ensembl; ENST00000527272; ENSP00000432862; ENSG00000134909. [A7KAX9-2]
GeneID; 9743; -.
KEGG; hsa:9743; -.
UCSC; uc001qez.4; human. [A7KAX9-1]
CTD; 9743; -.
DisGeNET; 9743; -.
EuPathDB; HostDB:ENSG00000134909.18; -.
GeneCards; ARHGAP32; -.
H-InvDB; HIX0010264; -.
HGNC; HGNC:17399; ARHGAP32.
HPA; HPA038382; -.
HPA; HPA038389; -.
HPA; HPA061505; -.
MIM; 608541; gene.
neXtProt; NX_A7KAX9; -.
OpenTargets; ENSG00000134909; -.
PharmGKB; PA165543138; -.
eggNOG; KOG1449; Eukaryota.
eggNOG; ENOG410Y1FN; LUCA.
GeneTree; ENSGT00900000140777; -.
HOGENOM; HOG000090208; -.
HOVERGEN; HBG108407; -.
InParanoid; A7KAX9; -.
KO; K20647; -.
OMA; CDVDAYG; -.
OrthoDB; EOG091G02IN; -.
PhylomeDB; A7KAX9; -.
TreeFam; TF351451; -.
Reactome; R-HSA-194840; Rho GTPase cycle.
SignaLink; A7KAX9; -.
SIGNOR; A7KAX9; -.
ChiTaRS; ARHGAP32; human.
EvolutionaryTrace; A7KAX9; -.
GeneWiki; RICS_(gene); -.
GenomeRNAi; 9743; -.
PRO; PR:A7KAX9; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000134909; -.
ExpressionAtlas; A7KAX9; baseline and differential.
Genevisible; A7KAX9; HS.
GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
GO; GO:0005938; C:cell cortex; IBA:GO_Central.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 3.30.1520.10; -; 1.
InterPro; IPR001683; Phox.
InterPro; IPR036871; PX_dom_sf.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
Pfam; PF00787; PX; 1.
Pfam; PF00620; RhoGAP; 1.
Pfam; PF14604; SH3_9; 1.
SMART; SM00324; RhoGAP; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF48350; SSF48350; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF64268; SSF64268; 1.
PROSITE; PS50238; RHOGAP; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Cell projection; Complete proteome; Cytoplasm; Endoplasmic reticulum;
Endosome; Golgi apparatus; GTPase activation; Membrane; Methylation;
Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
SH3 domain; Synapse.
CHAIN 1 2087 Rho GTPase-activating protein 32.
/FTId=PRO_0000345203.
DOMAIN 131 245 PX; atypical.
DOMAIN 259 321 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 372 567 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
REGION 1391 1711 Interaction with GAB2.
{ECO:0000269|PubMed:12819203}.
REGION 1685 2087 Interaction with FYN.
{ECO:0000269|PubMed:12788081}.
COMPBIAS 1031 1036 Poly-Pro.
COMPBIAS 1305 1310 Poly-Pro.
MOD_RES 706 706 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 709 709 Phosphoserine.
{ECO:0000250|UniProtKB:Q811P8}.
MOD_RES 732 732 Phosphoserine.
{ECO:0000250|UniProtKB:Q811P8}.
MOD_RES 738 738 Phosphoserine.
{ECO:0000250|UniProtKB:Q811P8}.
MOD_RES 852 852 Phosphoserine.
{ECO:0000250|UniProtKB:Q811P8}.
MOD_RES 856 856 Phosphoserine.
{ECO:0000250|UniProtKB:Q811P8}.
MOD_RES 892 892 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 952 952 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1203 1203 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1523 1523 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q811P8}.
MOD_RES 1533 1533 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q811P8}.
MOD_RES 1585 1585 Phosphoserine.
{ECO:0000250|UniProtKB:Q811P8}.
MOD_RES 2037 2037 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q811P8}.
VAR_SEQ 1 349 Missing (in isoform 2).
{ECO:0000303|PubMed:12446789,
ECO:0000303|PubMed:12531901,
ECO:0000303|PubMed:12819203,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9872452}.
/FTId=VSP_034933.
VAR_SEQ 1 290 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034934.
VAR_SEQ 567 612 FSGRISMAMQEGAASLSRPKSLLVSSPSTKLLTLEEAQART
QAQVN -> LPHFSARTELIVPFPLRLLRKQFTPPLLGPMS
PLNPLVQITVCISI (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034935.
VAR_SEQ 613 2087 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034936.
MUTAGEN 173 173 Y->A: Loss of binding to phospholipids.
Cytoplasmic localization.
{ECO:0000269|PubMed:17663722}.
MUTAGEN 407 407 R->A: Mild effect on GAP activity and
neurite-promotion upon nerve growth
factor stimulation.
{ECO:0000269|PubMed:12446789,
ECO:0000269|PubMed:12454018,
ECO:0000269|PubMed:12531901,
ECO:0000269|PubMed:12857875,
ECO:0000269|PubMed:17663722}.
MUTAGEN 407 407 R->I: Loss of GAP activity.
{ECO:0000269|PubMed:12446789,
ECO:0000269|PubMed:12454018,
ECO:0000269|PubMed:12531901,
ECO:0000269|PubMed:12857875,
ECO:0000269|PubMed:17663722}.
MUTAGEN 407 407 R->M: Loss of GAP activity. In isoform 1,
no inhibitory effect on neurite
extension. {ECO:0000269|PubMed:12446789,
ECO:0000269|PubMed:12454018,
ECO:0000269|PubMed:12531901,
ECO:0000269|PubMed:12857875,
ECO:0000269|PubMed:17663722}.
MUTAGEN 447 447 K->A: Loss of GAP activity.
{ECO:0000269|PubMed:12531901}.
HELIX 374 381 {ECO:0000244|PDB:3IUG}.
HELIX 387 399 {ECO:0000244|PDB:3IUG}.
TURN 403 407 {ECO:0000244|PDB:3IUG}.
HELIX 412 423 {ECO:0000244|PDB:3IUG}.
TURN 433 437 {ECO:0000244|PDB:3IUG}.
HELIX 439 452 {ECO:0000244|PDB:3IUG}.
TURN 460 462 {ECO:0000244|PDB:3IUG}.
HELIX 463 470 {ECO:0000244|PDB:3IUG}.
STRAND 472 474 {ECO:0000244|PDB:3IUG}.
HELIX 475 486 {ECO:0000244|PDB:3IUG}.
HELIX 491 508 {ECO:0000244|PDB:3IUG}.
HELIX 511 514 {ECO:0000244|PDB:3IUG}.
HELIX 518 529 {ECO:0000244|PDB:3IUG}.
HELIX 553 561 {ECO:0000244|PDB:3IUG}.
HELIX 563 566 {ECO:0000244|PDB:3IUG}.
SEQUENCE 2087 AA; 230529 MW; 075E5B4902857D06 CRC64;
METESESSTL GDDSVFWLES EVIIQVTDCE EEEREEKFRK MKSSVHSEED DFVPELHRNV
HPRERPDWEE TLSAMARGAD VPEIPGDLTL KTCGSTASMK VKHVKKLPFT KGHFPKMAEC
AHFHYENVEF GSIQLSLSEE QNEVMKNGCE SKELVYLVQI ACQGKSWIVK RSYEDFRVLD
KHLHLCIYDR RFSQLSELPR SDTLKDSPES VTQMLMAYLS RLSAIAGNKI NCGPALTWME
IDNKGNHLLV HEESSINTPA VGAAHVIKRY TARAPDELTL EVGDIVSVID MPPKVLSTWW
RGKHGFQVGL FPGHCVELIN QKVPQSVTNS VPKPVSKKHG KLITFLRTFM KSRPTKQKLK
QRGILKERVF GCDLGEHLLN SGFEVPQVLQ SCTAFIERYG IVDGIYRLSG VASNIQRLRH
EFDSEHVPDL TKEPYVQDIH SVGSLCKLYF RELPNPLLTY QLYEKFSDAV SAATDEERLI
KIHDVIQQLP PPHYRTLEFL MRHLSLLADY CSITNMHAKN LAIVWAPNLL RSKQIESACF
SGTAAFMEVR IQSVVVEFIL NHVDVLFSGR ISMAMQEGAA SLSRPKSLLV SSPSTKLLTL
EEAQARTQAQ VNSPIVTENK YIEVGEGPAA LQGKFHTIIE FPLERKRPQN KMKKSPVGSW
RSFFNLGKSS SVSKRKLQRN ESEPSEMKAM ALKGGRAEGT LRSAKSEESL TSLHAVDGDS
KLFRPRRPRS SSDALSASFN GEMLGNRCNS YDNLPHDNES EEEGGLLHIP ALMSPHSAED
VDLSPPDIGV ASLDFDPMSF QCSPPKAESE CLESGASFLD SPGYSKDKPS ANKKDAETGS
SQCQTPGSTA SSEPVSPLQE KLSPFFTLDL SPTEDKSSKP SSFTEKVVYA FSPKIGRKLS
KSPSMSISEP ISVTLPPRVS EVIGTVSNTT AQNASSSTWD KCVEERDATN RSPTQIVKMK
TNETVAQEAY ESEVQPLDQV AAEEVELPGK EDQSVSSSQS KAVASGQTQT GAVTHDPPQD
SVPVSSVSLI PPPPPPKNVA RMLALALAES AQQASTQSLK RPGTSQAGYT NYGDIAVATT
EDNLSSSYSA VALDKAYFQT DRPAEQFHLQ NNAPGNCDHP LPETTATGDP THSNTTESGE
QHHQVDLTGN QPHQAYLSGD PEKARITSVP LDSEKSDDHV SFPEDQSGKN SMPTVSFLDQ
DQSPPRFYSG DQPPSYLGAS VDKLHHPLEF ADKSPTPPNL PSDKIYPPSG SPEENTSTAT
MTYMTTTPAT AQMSTKEASW DVAEQPTTAD FAAATLQRTH RTNRPLPPPP SQRSAEQPPV
VGQVQAATNI GLNNSHKVQG VVPVPERPPE PRAMDDPASA FISDSGAAAA QCPMATAVQP
GLPEKVRDGA RVPLLHLRAE SVPAHPCGFP APLPPTRMME SKMIAAIHSS SADATSSSNY
HSFVTASSTS VDDALPLPLP VPQPKHASQK TVYSSFARPD VTTEPFGPDN CLHFNMTPNC
QYRPQSVPPH HNKLEQHQVY GARSEPPASM GLRYNTYVAP GRNASGHHSK PCSRVEYVSS
LSSSVRNTCY PEDIPPYPTI RRVQSLHAPP SSMIRSVPIS RTEVPPDDEP AYCPRPLYQY
KPYQSSQARS DYHVTQLQPY FENGRVHYRY SPYSSSSSSY YSPDGALCDV DAYGTVQLRP
LHRLPNRDFA FYNPRLQGKS LYSYAGLAPR PRANVTGYFS PNDHNVVSMP PAADVKHTYT
SWDLEDMEKY RMQSIRRESR ARQKVKGPVM SQYDNMTPAV QDDLGGIYVI HLRSKSDPGK
TGLLSVAEGK ESRHAAKAIS PEGEDRFYRR HPEAEMDRAH HHGGHGSTQP EKPSLPQKQS
SLRSRKLPDM GCSLPEHRAH QEASHRQFCE SKNGPPYPQG AGQLDYGSKG IPDTSEPVSY
HNSGVKYAAS GQESLRLNHK EVRLSKEMER PWVRQPSAPE KHSRDCYKEE EHLTQSIVPP
PKPERSHSLK LHHTQNVERD PSVLYQYQPH GKRQSSVTVV SQYDNLEDYH SLPQHQRGVF
GGGGMGTYVP PGFPHPQSRT YATALGQGAF LPAELSLQHP ETQIHAE


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