ID A0A452HKB7_9SAUR Unreviewed; 989 AA.
AC A0A452HKB7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=SLIT-ROBO Rho GTPase activating protein 2 {ECO:0008006|Google:ProtNLM};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000015363.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000015363.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A452HKB7; -.
DR Ensembl; ENSGAGT00000017546.1; ENSGAGP00000015363.1; ENSGAGG00000010110.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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:UP000291020};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 7..251
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 413..602
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 651..710
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 616..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 300..334
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 767..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 989 AA; 111412 MW; A8D935DF46A00DC4 CRC64;
MSSPTRKKLQ LTRFIRTQLI EQLKCLDQQC ELRVQLLQDL QDFFRKKAEI EMDYSRNLEK
LAERFLAKTR STKDQQFKKD QNVLSPVNCW NLLLNQVKRE SRDHTTLSDI YLNNIIPRFV
QVSEDSGRLF KKSKEVGLQL QEDLMKVLNE LYTVMKTYHM YNADSISAQS KLKEAEKQEE
KQIGKSVKFE EKHVRRSSVK KIEKMKEKRQ AKYTENKLKA IKARNEYLLA LEATNASVFK
YYIHDLSDLI DVSVLLLGLM SFPLTPLCAS PSLTPFPPQK GHLFDSHLGV SQLCAQQPVQ
SELVQRCQQL QSRLSTLKIE NEEVKKTMEA TLQTIQDIVT IEDFDVSDCF QYSNSMESVK
STVSETFMSK PSIAKRRANQ QETEQFYFTK MKEYLEGRNL ITKLQAKHDL LQKTLGESKS
GTRFQAIPLV VESCIRFISR HGLQHEGIFR VSGSQVEVND IKNAFERGED PLAGDQNDHD
MDSIAGVLKL YFRGLEHPLF PKEIFHDLIA CVTMDNLQER ALHIRKVLLS LPKTTLIVMR
YLFAFLSHLS QFSEENMMDP YNLAICFGPT LMSVPEGHDQ VSCQAHVNEL IKTIIIQHEN
IFPGLRELEG PVYSRGGSTE DYCESPHGET ASAEDSVQDI AAEHHTSDDE CEPIEAIAKF
DYIGRTAREL SFKKGASLLL YQRASDDWWE GRHNGIDGLI PHQYIVVQDT EDGSSERSSP
KSEIEINSET SILRYGPSPT PACTDLFCFC VGRQRKRPES GSIRRAFRQS DSHGLASSLV
EPASPGATAS SRPSSQPIMS PSLPKEVPDK CSSSGHGSLN SISRHSSLKN RIDSPQIRKT
VTAGRSKSFN NHRPMDPEVI VQDIEATMNT ALNELRELER QSSVKHTPDV VLDTLEPLKT
SPVVAPTSEP SSPLHTQILK DSEPAFQRSA STAGDIPCAF RPVKSVKMAA QVKPPATRPK
PAVFPKTNAT SPGVASSASQ QPTDKSCTV
//
