SRGP2_DANRE
ID SRGP2_DANRE Reviewed; 1100 AA.
AC B0S6J3; Q0IHZ9;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=SLIT-ROBO Rho GTPase-activating protein 2;
DE Short=srGAP2;
GN Name=srgap2; ORFNames=si:dkey-85p17.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Postsynaptic RAC1 GTPase activating protein (GAP) that plays
CC a key role in neuronal morphogenesis and migration mainly during
CC development of the cerebral cortex. Regulates excitatory and inhibitory
CC synapse maturation and density in cortical pyramidal neurons.
CC Mechanistically, acts by binding and deforming membranes, thereby
CC regulating actin dynamics to regulate cell migration and
CC differentiation. {ECO:0000250|UniProtKB:Q91Z67}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q91Z67}.
CC Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q91Z67}.
CC Postsynaptic density {ECO:0000250|UniProtKB:Q91Z67}. Postsynaptic cell
CC membrane {ECO:0000250|UniProtKB:Q91Z67}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:O75044}. Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:Q91Z67}. Nucleus {ECO:0000250|UniProtKB:D4A208}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q91Z67}.
CC -!- DOMAIN: The F-BAR domain mediates oligomerization, binds membranes, and
CC induces plasma membrane protrusions. {ECO:0000250|UniProtKB:O75044}.
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DR EMBL; BX537291; CAQ14643.1; -; Genomic_DNA.
DR EMBL; CR848745; CAQ14643.1; JOINED; Genomic_DNA.
DR EMBL; BC122886; AAI22887.1; -; mRNA.
DR RefSeq; NP_001041700.1; NM_001048235.1.
DR RefSeq; XP_009304269.1; XM_009305994.2.
DR AlphaFoldDB; B0S6J3; -.
DR SMR; B0S6J3; -.
DR STRING; 7955.ENSDARP00000045390; -.
DR PaxDb; B0S6J3; -.
DR PeptideAtlas; B0S6J3; -.
DR PRIDE; B0S6J3; -.
DR Ensembl; ENSDART00000045391; ENSDARP00000045390; ENSDARG00000032161.
DR Ensembl; ENSDART00000190095; ENSDARP00000155791; ENSDARG00000032161.
DR GeneID; 556198; -.
DR KEGG; dre:556198; -.
DR CTD; 23380; -.
DR ZFIN; ZDB-GENE-060915-2; srgap2.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00950000182824; -.
DR HOGENOM; CLU_005715_0_0_1; -.
DR InParanoid; B0S6J3; -.
DR OMA; XEDPLAG; -.
DR OrthoDB; 1245523at2759; -.
DR PhylomeDB; B0S6J3; -.
DR TreeFam; TF315892; -.
DR Reactome; R-DRE-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DRE-9013148; CDC42 GTPase cycle.
DR Reactome; R-DRE-9013149; RAC1 GTPase cycle.
DR Reactome; R-DRE-9013406; RHOQ GTPase cycle.
DR Reactome; R-DRE-9013420; RHOU GTPase cycle.
DR Reactome; R-DRE-9013423; RAC3 GTPase cycle.
DR Reactome; R-DRE-9035034; RHOF GTPase cycle.
DR PRO; PR:B0S6J3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 11.
DR Bgee; ENSDARG00000032161; Expressed in zone of skin and 21 other tissues.
DR ExpressionAtlas; B0S6J3; baseline.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0044327; C:dendritic spine head; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; ISS:UniProtKB.
DR GO; GO:0060996; P:dendritic spine development; ISS:UniProtKB.
DR GO; GO:0046847; P:filopodium assembly; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IBA:GO_Central.
DR GO; GO:2001223; P:negative regulation of neuron migration; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
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 InterPro; IPR030252; srGAP2.
DR PANTHER; PTHR14166:SF6; PTHR14166:SF6; 1.
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 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; GTPase activation; Membrane; Neurogenesis; Nucleus;
KW Postsynaptic cell membrane; Reference proteome; SH3 domain; Synapse.
FT CHAIN 1..1100
FT /note="SLIT-ROBO Rho GTPase-activating protein 2"
FT /id="PRO_0000418883"
FT DOMAIN 19..324
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 496..680
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 738..797
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 181..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..201
FT /evidence="ECO:0000255"
FT COILED 363..400
FT /evidence="ECO:0000255"
FT COILED 945..972
FT /evidence="ECO:0000255"
FT COMPBIAS 894..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 317
FT /note="E -> K (in Ref. 2; AAI22887)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1100 AA; 123568 MW; 9A5753F6023D4211 CRC64;
MTSPAKFRKD KEIIAEYETQ VKEIRAQLVE QLKCLDQQCE LRVQLLQDLQ DFFRKKAEIE
MDYSRNLEKL AERFLAKTRY TKDPQFKKEQ NILSPVNCWN LLLAQVKRES RDHATLSDLY
LNNIIPRFAQ ISEDSGRLFK KSKEVGLQLQ EDLMKVLNEL YTVMKTYHMY NMDSINAESK
LKEAEKQEEK QMSRSVRHEE KQTPRSPDSL TNIKIEDKHV RRSSVKKIEK MKEKRQAKYT
ENKLKAIKAR NEYLLALEAT NSCVFKYYIH DLSDLIDCCD LGYHASLNRA LRTYLSAEFN
VETSKHGGLE TIENAAENLE ANSDKQRLME TYNNVFCPPM RFDFQSHMGD MVGHLCAQQP
VQGELIQRCQ QLQSRLSTLN IENEEVKKTM EATLQTIQDM VTIEDFDVTD CFHHSNSMES
VKSTVSESFM SKPSLAKRRA NQQETEQFYF TKLKEFLEGR NLITKLQAKH DLIQKTLGES
QKTDYCLASG RRDSTVRKQE AIQIIPLMVE SCIRFISRHG LHHEGIFRVS GSQVEVNDIK
NAFERGEDPL AGDQNDHDMD SIAGVLKLYF RGLENALFPK EVFHDLMSCV SIESLQERAV
HIRKVLLSLP SNILVIMRYL FAFLNHLSQY SDDNMMDPYN LAICFGPTLM SVPEGHDQVS
CQAHVNELIK TIIIHHESIF PGPRELEGPV YDRGGAPEEY CDSPHIEPPL VDEPAPDTVS
VIHNSDDVKS GPLTVSESDP IEAIARFDYS GRTNRELSFK KGASLLLYSR ASDDWWEGRH
NGTEGLVPHQ YIVVQDMPDG YAGRGSPKAD LEGSHDSVEE KVSTRASASS PTGGHVADIY
LANLNKLRKR PEATSIRRTI RPVEEGSSGA AGGLKTSSMP AGGLAKDSSD KRPVSAHSVL
NSITRHSSLK TKVEGPQVRK STPTGRSKSF SNHRPLDPEV IAQVEHSSQD IEATMNTALS
ELRELERQSN VKHAPDVVLD TLEQLKSGGT SEPSSPLHSR LLREAESSQH PLQRSASSAS
DMPSTFRPSK TTGPKSPLSS MTTASGSTFR DNKPPATRPK PVVFPKSSSA GGSPAMGSPT
TTIPPTPPPP PPPTDKSCPV
