SRGP1_MOUSE
ID SRGP1_MOUSE Reviewed; 1062 AA.
AC Q91Z69; Q08E84;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=SLIT-ROBO Rho GTPase-activating protein 1;
DE Short=srGAP1;
DE AltName: Full=Rho GTPase-activating protein 13;
GN Name=Srgap1; Synonyms=Arhgap13;
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 [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 353-1062.
RX PubMed=11672528; DOI=10.1016/s0092-8674(01)00530-x;
RA Wong K., Ren X.R., Huang Y.Z., Xie Y., Liu G., Saito H., Tang H., Wen L.,
RA Brady-Kalnay S.M., Mei L., Wu J.Y., Xiong W.C., Rao Y.;
RT "Signal transduction in neuronal migration: roles of GTPase activating
RT proteins and the small GTPase Cdc42 in the Slit-Robo pathway.";
RL Cell 107:209-221(2001).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 725-776, AND INTERACTION WITH
RP ROBO1.
RX PubMed=16857672; DOI=10.1074/jbc.m604135200;
RA Li X., Chen Y., Liu Y., Gao J., Gao F., Bartlam M., Wu J.Y., Rao Z.;
RT "Structural basis of Robo proline-rich motif recognition by the srGAP1 Src
RT homology 3 domain in the Slit-Robo signaling pathway.";
RL J. Biol. Chem. 281:28430-28437(2006).
CC -!- FUNCTION: GTPase-activating protein for RhoA and Cdc42 small GTPases.
CC Together with CDC42 seems to be involved in the pathway mediating the
CC repulsive signaling of Robo and Slit proteins in neuronal migration.
CC SLIT2, probably through interaction with ROBO1, increases the
CC interaction of SRGAP1 with ROBO1 and inactivates CDC42 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (Probable). Forms a heterooligomer with SRGAP2 and
CC SRGAP3 through its F-BAR domain. Interacts with CDC42 and RHOA.
CC Interacts with FASLG (By similarity). Interacts (via SH3 domain) with
CC ROBO1. {ECO:0000250, ECO:0000269|PubMed:16857672, ECO:0000305}.
CC -!- DOMAIN: The F-BAR domain mediates oligomerization, binds membranes, and
CC constrains plasma membrane protrusions. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL27030.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC120892; AAI20893.1; -; mRNA.
DR EMBL; BC120893; AAI20894.1; -; mRNA.
DR EMBL; AY057898; AAL27030.1; ALT_INIT; mRNA.
DR CCDS; CCDS56751.1; -.
DR RefSeq; NP_001229340.1; NM_001242411.1.
DR PDB; 2GNC; X-ray; 1.80 A; A/B=725-776.
DR PDBsum; 2GNC; -.
DR AlphaFoldDB; Q91Z69; -.
DR SMR; Q91Z69; -.
DR BioGRID; 228239; 63.
DR IntAct; Q91Z69; 1.
DR STRING; 10090.ENSMUSP00000020322; -.
DR iPTMnet; Q91Z69; -.
DR PhosphoSitePlus; Q91Z69; -.
DR EPD; Q91Z69; -.
DR MaxQB; Q91Z69; -.
DR PaxDb; Q91Z69; -.
DR PeptideAtlas; Q91Z69; -.
DR PRIDE; Q91Z69; -.
DR ProteomicsDB; 257400; -.
DR Antibodypedia; 29129; 243 antibodies from 27 providers.
DR Ensembl; ENSMUST00000020322; ENSMUSP00000020322; ENSMUSG00000020121.
DR GeneID; 117600; -.
DR KEGG; mmu:117600; -.
DR UCSC; uc007hgc.2; mouse.
DR CTD; 57522; -.
DR MGI; MGI:2152936; Srgap1.
DR VEuPathDB; HostDB:ENSMUSG00000020121; -.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00950000182824; -.
DR InParanoid; Q91Z69; -.
DR TreeFam; TF315892; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 117600; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Srgap1; mouse.
DR EvolutionaryTrace; Q91Z69; -.
DR PRO; PR:Q91Z69; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q91Z69; protein.
DR Bgee; ENSMUSG00000020121; Expressed in cortical plate and 166 other tissues.
DR ExpressionAtlas; Q91Z69; baseline and differential.
DR Genevisible; Q91Z69; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; IDA:MGI.
DR GO; GO:0016477; P:cell migration; IDA:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; IBA:GO_Central.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
DR CDD; cd07683; F-BAR_srGAP1; 1.
DR CDD; cd11955; SH3_srGAP1-3; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035648; srGAP1/2/3_SH3.
DR InterPro; IPR037451; srGAP1_F-BAR.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; GTPase activation; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..1062
FT /note="SLIT-ROBO Rho GTPase-activating protein 1"
FT /id="PRO_0000056766"
FT DOMAIN 19..314
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 481..671
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 720..779
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 785..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 352..382
FT /evidence="ECO:0000255"
FT COILED 933..960
FT /evidence="ECO:0000255"
FT COMPBIAS 785..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6B7"
FT MOD_RES 812
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6B7"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6B7"
FT MOD_RES 909
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6B7"
FT MOD_RES 976
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6B7"
FT MOD_RES 978
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6B7"
FT MOD_RES 1009
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6B7"
FT CONFLICT 574
FT /note="F -> V (in Ref. 2; AAL27030)"
FT /evidence="ECO:0000305"
FT CONFLICT 721..724
FT /note="EPIE -> RGPSR (in Ref. 2; AAL27030)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="S -> G (in Ref. 2; AAL27030)"
FT /evidence="ECO:0000305"
FT STRAND 725..729
FT /evidence="ECO:0007829|PDB:2GNC"
FT STRAND 746..754
FT /evidence="ECO:0007829|PDB:2GNC"
FT STRAND 757..762
FT /evidence="ECO:0007829|PDB:2GNC"
FT STRAND 765..770
FT /evidence="ECO:0007829|PDB:2GNC"
FT HELIX 771..773
FT /evidence="ECO:0007829|PDB:2GNC"
SQ SEQUENCE 1062 AA; 121430 MW; D0FA749750A9081A CRC64;
MSTPSRFKKD KEIIAEYESQ VKEIRAQLVE QQKCLEQQTE MRVQLLQDLQ DFFRKKAEIE
TEYSRNLEKL AERFMAKTRS TKDHQQFKKD QNLLSPVNCW YLLLNQVRRE SKDHATLSDI
YLNNVIMRFM QISEDSTRMF KKSKEIAFQL HEDLMKVLNE LYTVMKTYHM YHSESISAES
KLKEAEKQEE KQIGRSGDPV FHIRLEERHQ RRSSVKKIEK MKEKRQAKYS ENKLKSIKAR
NEYLLTLEAT NASVFKYYIH DLSDLIDCCD LGYHASLNRA LRTYLSAEYN LETSRHEGLD
IIENAVDNLE PRSDKQRFME MYPAAFCPPM KFEFQSHMGD EVCQVSAQQP VQAELMLRNQ
QLQSRLATLK IESEEVKKTT EATLQTIQDM VTIEDYDVSE CFQHSRSTES VKSTVSETYL
SKPSIAKRRA NQQETEQFYF MKLREFLEGS NLITKLQAKH DLLQRTLGEG HRAEYMTTSR
GRRNSHARHQ DSGQVIPLIV ESCIRFINLY GLQHQGIFRV SGSQVEVNDI KNSFERGENP
LSDEQSNHDI NSVAGVLKLY FRGLENPLFP KERFTDLISC IRIDNLYERA LHIRKLLLTL
PRSVLIVMRY LFAFLNHLSQ YSDENMMDPY NLAICFGPTL MPVPEIQDQV SCQAHVNEIV
KTIIIHHETI FPDAKELDGP VYEKCMAGGD YCDSPYSEHG TLEEVDQDAG TEPHTSEDEC
EPIEAIAKFD YVGRSARELS FKKGASLLLY HRASEDWWEG RHNGIDGLVP HQYIVVQDMD
DTFSDTLSQK ADSEASSGPV TEDKSSSKDM NSPTDRHSDS YLARQRKRGE PPPPGRRPGR
TSDGHCPLHP PHALSNSSID LGSPNLASHP RGLLQNRGLN NDSPERRRRP GHGSLTNISR
HDSLKKIDSP PIRRSTSSGQ YTGFNDHKPL DPETIAQDIE ETMNTALNEL RELERQSTVK
HAPDVVLDTL EQVKNSPTPA TSTESLSPLH NVALRGSEPQ IRRSTSSSSE TMSTFKPMVA
PRMGVQLKPP ALRPKPAVLP KTNPTMGPAA PSQGPTDKSC TM
