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Protein

SLIT-ROBO Rho GTPase-activating protein 3

Gene

Srgap3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GTPase-activating protein for RAC1 and perhaps CDC42, but not for RhoA small GTPase. May attenuate RAC1 signaling in neurons (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
SLIT-ROBO Rho GTPase-activating protein 3
Short name:
srGAP3
Alternative name(s):
Rho GTPase-activating protein 14
WAVE-associated Rac GTPase-activating protein
Short name:
WRP
Gene namesi
Name:Srgap3
Synonyms:Arhgap14, Kiaa0411, Srgap2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2152938. Srgap3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10991099SLIT-ROBO Rho GTPase-activating protein 3PRO_0000056770Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei817 – 8171PhosphoserineCombined sources
Modified residuei820 – 8201PhosphoserineCombined sources
Modified residuei821 – 8211PhosphoserineCombined sources
Modified residuei837 – 8371PhosphoserineBy similarity
Modified residuei858 – 8581PhosphoserineCombined sources
Modified residuei954 – 9541PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ812A2.
PaxDbiQ812A2.
PRIDEiQ812A2.

PTM databases

iPTMnetiQ812A2.
PhosphoSiteiQ812A2.

Expressioni

Gene expression databases

CleanExiMM_SRGAP2.
MM_SRGAP3.

Interactioni

Subunit structurei

Homodimer (Probable). Forms a heterooligomer with SRGAP1 and SRGAP2 through its F-BAR domain. Interacts with WASF1. Probably interacts with ROBO1. Interacts with FASLG (By similarity).By similarityCurated

Protein-protein interaction databases

BioGridi234422. 1 interaction.
IntActiQ812A2. 2 interactions.
MINTiMINT-4135517.
STRINGi10090.ENSMUSP00000085712.

Structurei

3D structure databases

ProteinModelPortaliQ812A2.
SMRiQ812A2. Positions 749-800.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 314296F-BARPROSITE-ProRule annotationAdd
BLAST
Domaini506 – 694189Rho-GAPPROSITE-ProRule annotationAdd
BLAST
Domaini744 – 80360SH3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili352 – 39241Sequence analysisAdd
BLAST
Coiled coili952 – 98736Sequence analysisAdd
BLAST

Domaini

The F-BAR domain mediates oligomerization, binds membranes, and induces plasma membrane protrusions.By similarity

Sequence similaritiesi

Contains 1 F-BAR domain.PROSITE-ProRule annotation
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiKOG3565. Eukaryota.
ENOG410XS44. LUCA.
HOGENOMiHOG000039980.
HOVERGENiHBG051637.
InParanoidiQ812A2.
KOiK07526.
PhylomeDBiQ812A2.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q812A2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSQTKFKKD KEIIAEYEAQ IKEIRTQLVE QFKCLEQQSE SRLQLLQDLQ
60 70 80 90 100
EFFRRKAEIE LEYSRSLEKL AERFSSKIRS SREHQFKKDQ YLLSPVNCWY
110 120 130 140 150
LVLHQTRRES RDHATLNDIF MNNVIVRLSQ ISEDVIRLFK KSKEIGLQMH
160 170 180 190 200
EELLKVTNEL YTVMKTYHMY HAESISAESK LKEAEKQEEK QFNKSGELSM
210 220 230 240 250
NLLRHEDRPQ RRSSVKKIEK MKEKRQAKYS ENKLKCTKAR NDYLLNLAAT
260 270 280 290 300
NAAISKYYIH DVSDLIDCCD LGFHASLART FRTYLSAEYN LETSRHEGLD
310 320 330 340 350
VIENAVDNLD SRSDKHTVMD MCSQVFCPPL KFEFQPHMGD EVCQVSAQQP
360 370 380 390 400
VQTELLMRYH QLQSRLATLK IENEEVRKTL DATMQTLQDM LTVEDFDVSD
410 420 430 440 450
AFQHSRSTES IKSAASETYM SKINIAKRRA NQQETEMFYF TKFKEYVNGS
460 470 480 490 500
NLITKLQAKH DLLKQTLGEG ERAECGTTRP PCLPPKPQKM RRPRPLSVYS
510 520 530 540 550
HKLFNGSMEA FIKDSGQAIP LVAESCIRFI NLYGLQQQGI FRVPGSQVEV
560 570 580 590 600
NDIKNSFERG EDPLVDDQNE RDINSVAGVL KLYFRGLENP LFPKERFQDL
610 620 630 640 650
ISTIKLENPA DRVHPIQQIL ITLPRVVIVV MRYLFAFLNH LSQYSDENMM
660 670 680 690 700
DPYNLAICFG PTLMHIPDGQ DPVSCQAHVN EVIKTIIIHH EAIFPSPREL
710 720 730 740 750
EGPVYEKCMA GGEEYCDSPH SEPGTIDEVD HDNGTEPHTS DEEVEQIEAI
760 770 780 790 800
AKFDYVGRSP RELSFKKGAS LLLYHRASED WWEGRHNGVD GLIPHQYIVV
810 820 830 840 850
QDMDDAFSDS LSQKADSEAS SGPLLDDKAS SKNDLQSPTE HISDYGFGGV
860 870 880 890 900
MGRVRLRSDG AAIPRRRSGG DTHSPPRGLG PSIDTPPRAA ACPSSPHKIP
910 920 930 940 950
LSRGRIESPE KRRMATFGSA GSINYPDKKA LTEGLSMRST CGSTRHSSLG
960 970 980 990 1000
DHKSLEAEAL AEDIEKTMST ALHELRELER QNTVKQAPDV VLDTLEPLKN
1010 1020 1030 1040 1050
PPGPISSEPA SPLHTIVIRD PDAAMRRSSS SSTEMMTTFK PALSARLAGA
1060 1070 1080 1090
QLRPPPMRPV RPVVQHRSSS SSSSGVGSPA VTPTEKMFPN SSSDKSGTM
Length:1,099
Mass (Da):124,420
Last modified:June 1, 2003 - v1
Checksum:iC033CD7DE43C1B2C
GO

Sequence cautioni

The sequence AAK52474.1 differs from that shown. Reason: Frameshift at positions 90, 98, 104, 110 and 120. Curated
The sequence AAK52474.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC34580.1 differs from that shown.Intron retention.Curated
The sequence BAC65558.1 differs from that shown.Probable cloning artifact. Aberrant splice sites.Curated
The sequence BAC65558.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671L → V in AAK52474 (Ref. 4) Curated
Sequence conflicti122 – 1221N → T in AAK52474 (Ref. 4) Curated
Sequence conflicti523 – 5231A → V in BAC65558 (PubMed:12693553).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF496547 mRNA. Translation: AAM46845.1.
AK122276 mRNA. Translation: BAC65558.1. Sequence problems.
AK045508 mRNA. Translation: BAC32400.1.
AK051262 mRNA. Translation: BAC34580.1. Sequence problems.
AF338472 mRNA. Translation: AAK52474.1. Frameshift.
CCDSiCCDS39590.1.
RefSeqiNP_536696.4. NM_080448.4.
UniGeneiMm.236401.

Genome annotation databases

GeneIDi259302.
KEGGimmu:259302.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF496547 mRNA. Translation: AAM46845.1.
AK122276 mRNA. Translation: BAC65558.1. Sequence problems.
AK045508 mRNA. Translation: BAC32400.1.
AK051262 mRNA. Translation: BAC34580.1. Sequence problems.
AF338472 mRNA. Translation: AAK52474.1. Frameshift.
CCDSiCCDS39590.1.
RefSeqiNP_536696.4. NM_080448.4.
UniGeneiMm.236401.

3D structure databases

ProteinModelPortaliQ812A2.
SMRiQ812A2. Positions 749-800.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234422. 1 interaction.
IntActiQ812A2. 2 interactions.
MINTiMINT-4135517.
STRINGi10090.ENSMUSP00000085712.

PTM databases

iPTMnetiQ812A2.
PhosphoSiteiQ812A2.

Proteomic databases

MaxQBiQ812A2.
PaxDbiQ812A2.
PRIDEiQ812A2.

Protocols and materials databases

DNASUi259302.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi259302.
KEGGimmu:259302.

Organism-specific databases

CTDi9901.
MGIiMGI:2152938. Srgap3.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG3565. Eukaryota.
ENOG410XS44. LUCA.
HOGENOMiHOG000039980.
HOVERGENiHBG051637.
InParanoidiQ812A2.
KOiK07526.
PhylomeDBiQ812A2.

Miscellaneous databases

ChiTaRSiSrgap3. mouse.
NextBioi392051.
PROiQ812A2.
SOURCEiSearch...

Gene expression databases

CleanExiMM_SRGAP2.
MM_SRGAP3.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00611. FCH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The WRP component of the WAVE-1 complex attenuates Rac-mediated signalling."
    Soderling S.H., Binns K.L., Wayman G.A., Davee S.M., Ong S.H., Pawson T., Scott J.D.
    Nat. Cell Biol. 4:970-975(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Brain.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-671.
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-471.
    Strain: C57BL/6J.
    Tissue: Spinal ganglion.
  4. "Identification of a novel RhoGAP through analysis of an ecotropic MuLV integration site."
    Crowley M.R., Slon K.E., Nowak N.J., Asch H.L., Asch B.B.
    Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-1099.
    Strain: BALB/cJ.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817; SER-820; SER-821; SER-858 AND SER-954, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Testis.

Entry informationi

Entry nameiSRGP3_MOUSE
AccessioniPrimary (citable) accession number: Q812A2
Secondary accession number(s): Q80U09
, Q8BKP4, Q8BLD0, Q925I2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2003
Last modified: May 11, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.