ID A0A2K5DKS0_AOTNA Unreviewed; 1071 AA.
AC A0A2K5DKS0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=SLIT-ROBO Rho GTPase activating protein 2 {ECO:0008006|Google:ProtNLM};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000021497.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000021497.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_012314724.1; XM_012459301.1.
DR AlphaFoldDB; A0A2K5DKS0; -.
DR STRING; 37293.ENSANAP00000021497; -.
DR Ensembl; ENSANAT00000039385.1; ENSANAP00000021497.1; ENSANAG00000028268.1.
DR GeneID; 105722102; -.
DR CTD; 23380; -.
DR GeneTree; ENSGT00950000182824; -.
DR OrthoDB; 2904755at2759; -.
DR Proteomes; UP000233020; 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:UP000233020};
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 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 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; 120803 MW; F5A9EE4B6BDE6415 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 EDSTQDVTAE
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
//
