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Database: UniProt
Entry: A0A2K6U6F9_SAIBB
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ID   A0A2K6U6F9_SAIBB        Unreviewed;      1071 AA.
AC   A0A2K6U6F9;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=SLIT-ROBO Rho GTPase activating protein 2 {ECO:0008006|Google:ProtNLM};
OS   Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000027489.1, ECO:0000313|Proteomes:UP000233220};
RN   [1] {ECO:0000313|Ensembl:ENSSBOP00000027489.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   RefSeq; XP_003930494.2; XM_003930445.2.
DR   AlphaFoldDB; A0A2K6U6F9; -.
DR   STRING; 39432.ENSSBOP00000027489; -.
DR   Ensembl; ENSSBOT00000044366.1; ENSSBOP00000027489.1; ENSSBOG00000029696.1.
DR   GeneID; 101028623; -.
DR   KEGG; sbq:101028623; -.
DR   CTD; 23380; -.
DR   GeneTree; ENSGT00950000182824; -.
DR   OrthoDB; 2904755at2759; -.
DR   Proteomes; UP000233220; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR   GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR   GO; GO:0060996; P:dendritic spine development; IEA:Ensembl.
DR   GO; GO:1904861; P:excitatory synapse assembly; IEA:Ensembl.
DR   GO; GO:0021816; P:extension of a leading process involved in cell motility in cerebral cortex radial glia guided migration; IEA:Ensembl.
DR   GO; GO:0046847; P:filopodium assembly; IEA:Ensembl.
DR   GO; GO:1904862; P:inhibitory synapse assembly; IEA:Ensembl.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR   GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd07682; F-BAR_srGAP2; 1.
DR   CDD; cd04383; RhoGAP_srGAP; 1.
DR   CDD; cd11955; SH3_srGAP1-3; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 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   PANTHER; PTHR14166; SLIT-ROBO RHO GTPASE ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR14166:SF6; SLIT-ROBO RHO GTPASE-ACTIVATING PROTEIN 2-RELATED; 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; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils};
KW   Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          22..325
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          489..679
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          728..787
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          181..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          698..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          793..819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          837..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          983..1012
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1029..1071
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          363..397
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        181..204
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..809
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        850..931
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1050..1071
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1071 AA;  120789 MW;  3F244D065F5D3CE7 CRC64;
     MTSPAKFKKD KEIIAEYDTQ VKEIRAQLTE QMKCLDQQCE LRVQLLQDLQ DFFRKKAEIE
     MDYSRNLEKL AERFLAKTRS TKDQQFKKDQ NVLSPVNCWN LLLNQVKRES RDHTTLSDIY
     LNNIIPRFVQ VSEDSGRLFK KSKEVGQQLQ DDLMKVLNEL YSVMKTYHMY NADSISAQSK
     LKEAEKQEEK QIGKSVKQED RQTPRSPDST ANVRIEEKHV RRSSVKKIEK MKEKRQAKYT
     ENKLKAIKAR NEYLLALEAT NASVFKYYIH DLSDLIDQCC DLGYHASLNR ALRTFLSAEL
     NLEQSKHEGL DAIENAVENL DATSDKQRLM EMYNNVFCPP MKFEFQPHMG DMASQLCAQQ
     PVQSELVQRC QQLQSRLSTL KIENEEVKKT MEATLQTIQD IVTVEDFDVS DCFQYSNSME
     SVKSTVSETF MSKPSIAKRR ANQQETEQFY FTKMKEYLEG RNLITKLQAK HDLLQKTLGE
     SQRTDCSLAR RSSTVRKQDS SQAIPLVVES CIRFISRHGL QHEGIFRVSG SQVEVNDIKN
     AFERGEDPLA GDQNDHDMDS IAGVLKLYFR GLEHPLFPKD IFHDLMACVT MDNLQERALH
     IRKVLLVLPK TTLIIMRYLF AFLSHLSQFS EENMMDPYNL AICFGPSLMS VPEGHDQVSC
     QAHVNELIKT IIIQHENIFP SPRELEGPVY SRGGSMEDYC DSPHGETTSV DDSTQDVTAE
     HHTSDDECEP IEAIAKFDYV GRTARELSFK KGASLLLYQR ASDDWWEGRH NGIDGLIPHQ
     YIVVQDTEDG VVERSSPKSE IEVISEPPEE KVTARAGASC PSGGHVADIY LANINKQRKR
     PESGSIRKTF RSDSHGLSSS LTDSSSPGVG ASCRPSSQPI MSQSLPKEGS DKCSISGHGS
     LNSISRHSSL KNRLDSPQIR KTATAGRSKS FNNHRPMDPE VIAQDIEATM NSALNELREL
     ERQSSVKHTP DVVLDTLEPL KTSPVVAPTS EPSSPLHTQL LKDPEPAFQR SASTAGDIAC
     AFRPVKSVKM AAPVKPPATR PKPAVFPKTN ATSPGVNSST SPQSTDKSCT V
//
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