SRGP3_MOUSE
ID SRGP3_MOUSE Reviewed; 1099 AA.
AC Q812A2; Q80U09; Q8BKP4; Q8BLD0; Q925I2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=SLIT-ROBO Rho GTPase-activating protein 3;
DE Short=srGAP3;
DE AltName: Full=Rho GTPase-activating protein 14;
DE AltName: Full=WAVE-associated Rac GTPase-activating protein;
DE Short=WRP;
GN Name=Srgap3; Synonyms=Arhgap14, Kiaa0411, Srgap2;
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].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=12447388; DOI=10.1038/ncb886;
RA Soderling S.H., Binns K.L., Wayman G.A., Davee S.M., Ong S.H., Pawson T.,
RA Scott J.D.;
RT "The WRP component of the WAVE-1 complex attenuates Rac-mediated
RT signalling.";
RL Nat. Cell Biol. 4:970-975(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-671.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-471.
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-1099.
RC STRAIN=BALB/cJ;
RA Crowley M.R., Slon K.E., Nowak N.J., Asch H.L., Asch B.B.;
RT "Identification of a novel RhoGAP through analysis of an ecotropic MuLV
RT integration site.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817; SER-820; SER-821;
RP SER-858 AND SER-954, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, 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: GTPase-activating protein for RAC1 and perhaps CDC42, but not
CC for RhoA small GTPase. May attenuate RAC1 signaling in neurons (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (Probable). Forms a heterooligomer with SRGAP1 and
CC SRGAP2 through its F-BAR domain. Interacts with WASF1. Probably
CC interacts with ROBO1. Interacts with FASLG (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- DOMAIN: The F-BAR domain mediates oligomerization, binds membranes, and
CC induces plasma membrane protrusions. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK52474.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK52474.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC34580.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAC65558.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC65558.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact. Aberrant splice sites.; Evidence={ECO:0000305};
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DR EMBL; AF496547; AAM46845.1; -; mRNA.
DR EMBL; AK122276; BAC65558.1; ALT_SEQ; mRNA.
DR EMBL; AK045508; BAC32400.1; -; mRNA.
DR EMBL; AK051262; BAC34580.1; ALT_SEQ; mRNA.
DR EMBL; AF338472; AAK52474.1; ALT_FRAME; mRNA.
DR CCDS; CCDS39590.1; -.
DR RefSeq; NP_536696.4; NM_080448.4.
DR AlphaFoldDB; Q812A2; -.
DR SMR; Q812A2; -.
DR BioGRID; 234422; 15.
DR IntAct; Q812A2; 4.
DR STRING; 10090.ENSMUSP00000085712; -.
DR iPTMnet; Q812A2; -.
DR PhosphoSitePlus; Q812A2; -.
DR MaxQB; Q812A2; -.
DR PaxDb; Q812A2; -.
DR PRIDE; Q812A2; -.
DR ProteomicsDB; 257069; -.
DR DNASU; 259302; -.
DR GeneID; 259302; -.
DR KEGG; mmu:259302; -.
DR CTD; 9901; -.
DR MGI; MGI:2152938; Srgap3.
DR eggNOG; KOG3565; Eukaryota.
DR InParanoid; Q812A2; -.
DR PhylomeDB; Q812A2; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 259302; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Srgap3; mouse.
DR PRO; PR:Q812A2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q812A2; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0030336; P:negative regulation of cell migration; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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 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 Coiled coil; GTPase activation; Phosphoprotein; Reference proteome;
KW SH3 domain.
FT CHAIN 1..1099
FT /note="SLIT-ROBO Rho GTPase-activating protein 3"
FT /id="PRO_0000056770"
FT DOMAIN 19..314
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 506..694
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 744..803
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 470..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 352..392
FT /evidence="ECO:0000255"
FT COILED 952..987
FT /evidence="ECO:0000255"
FT COMPBIAS 809..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43295"
FT MOD_RES 858
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 954
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 67
FT /note="L -> V (in Ref. 4; AAK52474)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="N -> T (in Ref. 4; AAK52474)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="A -> V (in Ref. 2; BAC65558)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1099 AA; 124420 MW; C033CD7DE43C1B2C CRC64;
MSSQTKFKKD KEIIAEYEAQ IKEIRTQLVE QFKCLEQQSE SRLQLLQDLQ EFFRRKAEIE
LEYSRSLEKL AERFSSKIRS SREHQFKKDQ YLLSPVNCWY LVLHQTRRES RDHATLNDIF
MNNVIVRLSQ ISEDVIRLFK KSKEIGLQMH EELLKVTNEL YTVMKTYHMY HAESISAESK
LKEAEKQEEK QFNKSGELSM NLLRHEDRPQ RRSSVKKIEK MKEKRQAKYS ENKLKCTKAR
NDYLLNLAAT NAAISKYYIH DVSDLIDCCD LGFHASLART FRTYLSAEYN LETSRHEGLD
VIENAVDNLD SRSDKHTVMD MCSQVFCPPL KFEFQPHMGD EVCQVSAQQP VQTELLMRYH
QLQSRLATLK IENEEVRKTL DATMQTLQDM LTVEDFDVSD AFQHSRSTES IKSAASETYM
SKINIAKRRA NQQETEMFYF TKFKEYVNGS NLITKLQAKH DLLKQTLGEG ERAECGTTRP
PCLPPKPQKM RRPRPLSVYS HKLFNGSMEA FIKDSGQAIP LVAESCIRFI NLYGLQQQGI
FRVPGSQVEV NDIKNSFERG EDPLVDDQNE RDINSVAGVL KLYFRGLENP LFPKERFQDL
ISTIKLENPA DRVHPIQQIL ITLPRVVIVV MRYLFAFLNH LSQYSDENMM DPYNLAICFG
PTLMHIPDGQ DPVSCQAHVN EVIKTIIIHH EAIFPSPREL EGPVYEKCMA GGEEYCDSPH
SEPGTIDEVD HDNGTEPHTS DEEVEQIEAI AKFDYVGRSP RELSFKKGAS LLLYHRASED
WWEGRHNGVD GLIPHQYIVV QDMDDAFSDS LSQKADSEAS SGPLLDDKAS SKNDLQSPTE
HISDYGFGGV MGRVRLRSDG AAIPRRRSGG DTHSPPRGLG PSIDTPPRAA ACPSSPHKIP
LSRGRIESPE KRRMATFGSA GSINYPDKKA LTEGLSMRST CGSTRHSSLG DHKSLEAEAL
AEDIEKTMST ALHELRELER QNTVKQAPDV VLDTLEPLKN PPGPISSEPA SPLHTIVIRD
PDAAMRRSSS SSTEMMTTFK PALSARLAGA QLRPPPMRPV RPVVQHRSSS SSSSGVGSPA
VTPTEKMFPN SSSDKSGTM
