ID I3JQM5_ORENI Unreviewed; 1257 AA.
AC I3JQM5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Synapse defective Rho GTPase homolog 2 {ECO:0000313|Ensembl:ENSONIP00000011169.2};
GN Name=SYDE2 {ECO:0000313|Ensembl:ENSONIP00000011169.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000011169.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000011169.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; I3JQM5; -.
DR STRING; 8128.ENSONIP00000078230; -.
DR Ensembl; ENSONIT00000011178.2; ENSONIP00000011169.2; ENSONIG00000008886.2.
DR eggNOG; KOG1452; Eukaryota.
DR GeneTree; ENSGT01030000234635; -.
DR HOGENOM; CLU_005764_1_0_1; -.
DR TreeFam; TF323458; -.
DR Proteomes; UP000005207; Linkage group LG17.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR46150; RHO GTPASE-ACTIVATING PROTEIN 100F; 1.
DR PANTHER; PTHR46150:SF1; RHO GTPASE-ACTIVATING PROTEIN SYDE2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207}.
FT DOMAIN 651..770
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 808..1023
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 293..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1257 AA; 139004 MW; 6AA862B5780E301C CRC64;
MVGTVVAVHE SNANWNFDSR PTLETNARNY AARVCPNRML KNTEENAVIR NIESYDPDYA
GDVRGGLLSP TFFPTELEIC DVNMASLCAT EPSLTYPLDS EDDDYYDNEI LPFYETIRPM
TDSERAETVE LTQPGQDKGQ AGDSNSAQET DRLRNQLKEA YYLLINAMND INMDVQQIGG
GLTEQQATSS CSSHSRDSLC SRLSLKNRDS DSWSSGEDQS PQQVSDTDSL LLCLTGIVEV
GVKGRLKSKS MANLSFTKKP TLSRSTSDGE IRYQDAFSES VQACETQSAE ICDDQEAERG
EGGTEAGELS EPRVFCSAVS NEELLQDDGV EEERGGQLNE SSGSINSITS SSDSNTETAT
HQGHNNKQEL TELQTQVANT VNKGHGVTVN KMQEWMHKGR MLSSEMKQRI EGSSLPRGGG
QSQDRSCPQV NPGGCKPGAQ TSSRAGKSVK AKSQQHQQQQ PDCLDLPNAT SFSPPSSPNP
AKKSSSINWS FPDKIKSPRT VRKISMKMKK LPELSRKLSV KGTQNNSSSN GSSQLEPRAH
SPKANGSGSE VVLQTSGPPR LASSGGGQAS RNVISRYHLD SSVSTQHSFY KKKSSGSSKS
ASKGGYLSDG DSPELVAKSG KHGSGEGKGG KGKDTEGGGG NSRINGTELD IDAFRHYSFS
EQPKCSQYIS GLMSLHFYGA EDLKPPRIDS RDVYCAIQVD SVNKARTALL TCRTTFLDMD
HTFNIELENA QHLKLVVFSW EPTPRRHRVC CHGTVVLPAL FRVTRSHQLA VKLEPRGVIY
VKLSLMEQWQ NSLNGGPDGD REPQVFGVEV WRVVERENTG LMVPLLISKC INEIEKRGCQ
VVGLYRLCGS AAVKKELREA FERDSHAVEL CENTYPDINV ITGVLKDYLR ELPYPLINKQ
LYEAVLESMA ARPLRMGASG CENDQTDSEH TVSLLENLPE VERMMLRKLL DHLKLVASYQ
EMNKMTCQNL AVCFGPVLLS QRQEASCHTN RVFIDSEELA SALHFKKHIE VLHYLLQLWP
VVDPHGQSSS QPPAPSLVPT SSDLLSALPL RRRKERPQVL NLTGAEMAGV LRPKPGRLDS
PSNRYAGDWS GCGETYFPSE MLLPSSKEEA DYDDVPSEDI EATEEVQEKR EEARDGIQLK
VDCPVSDTAD EEQPQRREVG KEEETQEAVE EQEKLIESDS SNSGHPLEEE EQEHKVCNHI
LPPRLPKEHT YQAYMKIQDI SPVLSNRVNL RDLQESIDTL IGNLERELNK NKLNVGY
//
