ID A0A3P8XBD7_ESOLU Unreviewed; 952 AA.
AC A0A3P8XBD7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=SLIT-ROBO Rho GTPase-activating protein 3 {ECO:0000313|Ensembl:ENSELUP00000000893.2};
GN Name=SRGAP3 {ECO:0000313|Ensembl:ENSELUP00000000893.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000000893.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000000893.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000000893.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3P8XBD7; -.
DR Ensembl; ENSELUT00000018303.2; ENSELUP00000000893.2; ENSELUG00000002479.2.
DR GeneTree; ENSGT00950000182824; -.
DR Proteomes; UP000265140; LG17.
DR Bgee; ENSELUG00000002479; Expressed in brain and 11 other cell types or tissues.
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:SF8; SLIT-ROBO RHO GTPASE-ACTIVATING PROTEIN 3; 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|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 19..315
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 474..661
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 709..768
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 686..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 360..387
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 687..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..888
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 952 AA; 107722 MW; AB0102618B315C94 CRC64;
MSSHTRVKKD KEIIGEYETQ VKEIRNQLVE QFRCLEQQSE SRLQLLQDLQ EFFRRKAELQ
LEYARGLDKL AERFTSKIRS SREHQHFKKD QNLLSTVNCW YLVLNQTRRE SRDHATLSDL
YNNNVIVRLA HVGEDVIRLF KKSKDIGVQM HEELVKVTNE LYTVMKTYHM YHTESIAAEG
KLKEAEKQEE KQIGKVNDVT TSLLRPDDRP QRRSCIKKME KMKEKRQAKY SENKLKCTKA
RNDYLLNLAA TNALVAKYYI HDVSDMIDCC DLGYHASLAR SLRTYLSAEY SLETSRHEGL
DQLEGAVDAM DVRGDKHRVM DMYSQIFCPP ARFDYQPHMG DEVCQLSAQQ PVQTELLMRH
HQLQSRLATL KIENEEVRKT LDATMQTLQD MLTVEDFDVS EAFQHSQSTE SVKSASSDSY
MSKINVAKRR ANQQETEGFY FTKFKEYLNG SNLIVKLQAK HDLLKQTLGE GEDNFLTHLV
DSGQAIPVVV ESCVRYINLY GLQQQGIFRI PGSQVEVNDI KNSFERGEDP LVDDQSDHDI
MAVAGVLKLY FRGLENPLFP KELFLDLMST IKVDSGAERA HHLQQIILTL PRPVIIVMRY
LFAFLNHLSQ YSDENMMDPY NLAICFGPTL MPIPDHHDPV TCQTHVNEII KTIIVHNEVI
FPSHHELDGP VYEKCMTGGE EYCDSPHSET GAVDEVDNGT EPHTSDDDLE QIEAIARFDY
VGRTPRELSF KKGASLLLYL RASDDWWEGR HNGVDGLIPH QYIVVQDLIS SDCVCVFQDI
EKTMNTALHE LRELERQNVA KHPPDVVLDT LEPLKQQHSS CPGPGSTPEP SGSPLHANTM
AIRDPEAALR RSSSSSSSET MSTFKPSLSA RRPSAPLRPP PVRPLRPAPV HPGHGQGQGR
GQGGQGGQRS SSSSSSGLGS PASVTPTDRV FPKAPSPSPS TSSSSSDKQG NM
//
