ID A0A674IR32_9SAUR Unreviewed; 1408 AA.
AC A0A674IR32;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 10-JUN-2026, entry version 24.
DE SubName: Full=Rho GTPase-activating protein SYDE2-like {ECO:0000313|Ensembl:ENSTMTP00000011420.1};
GN Name=LOC113405012 {ECO:0000313|Ensembl:ENSTMTP00000011420.1};
OS Terrapene triunguis (Three-toed box turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Emydidae; Terrapene.
OX NCBI_TaxID=2587831 {ECO:0000313|Ensembl:ENSTMTP00000011420.1, ECO:0000313|Proteomes:UP000472274};
RN [1] {ECO:0000313|Ensembl:ENSTMTP00000011420.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSTMTP00000011420.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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DR RefSeq; XP_026511636.1; XM_026655851.2.
DR Ensembl; ENSTMTT00000011805.1; ENSTMTP00000011420.1; ENSTMTG00000008273.1.
DR GeneID; 113405012; -.
DR GeneTree; ENSGT01030000234635; -.
DR InParanoid; A0A674IR32; -.
DR Proteomes; UP000472274; Unplaced.
DR GO; GO:0097060; C:synaptic membrane; IEA:TreeGrafter.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; IEA:TreeGrafter.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR FunFam; 1.10.555.10:FF:000031; rho GTPase-activating protein 100F isoform X6; 1.
DR FunFam; 2.60.40.150:FF:000195; Synapse defective Rho GTPase homolog 2; 1.
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; IPR052118; Rho-GAP_regulator.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR057459; SYDE1/2_C2.
DR PANTHER; PTHR46150; RHO GTPASE-ACTIVATING PROTEIN 100F; 1.
DR PANTHER; PTHR46150:SF1; RHO GTPASE-ACTIVATING PROTEIN SYDE2; 1.
DR Pfam; PF25336; C2_SYDE; 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 GTPase activation {ECO:0000256|ARBA:ARBA00022468, ECO:0000256|PROSITE-
KW ProRule:PRU00172}; Reference proteome {ECO:0000313|Proteomes:UP000472274}.
FT DOMAIN 873..992
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1029..1244
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1279..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..18
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..52
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..95
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..221
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..273
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..359
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..772
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..837
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1338
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1408 AA; 151881 MW; 5055367A267A8CAF CRC64;
MADPLRRTLS KLRGRRSQRG AAAGAHPRGG TGAPQGKAQQ QPPARGAPCA QPRSREVSAP
PGAGSQEESG QRQPGWPRRG KAPRGPAALG EGTPGAPAPP GCTPGDPAPQ PVSAPARRAP
EGEEGDYYDN ETLPWGCRPA EAQGLPAARA RGRGEGRLAG PRESTGRLQS QLQEAYYLLI
HAMHDLPPAS PACAGGFPQP VASCGAAESS DAWSSSSGEG SPQQQVSATA WPPPPGQGSA
GRPGQLVPPG RGAQSLGSLP LLPPGRPAKP PPLQRCLSDS VIRYHPVEPA LGHLLQGEPP
GPAWDRGGSD APAAAECSLS CGESRGTGSR QAELLLLSAQ GSAPQEAAAG GGLPAACPGS
RPHAPQSPFR PPAVSVGKLQ KWVCKGRLLS LGMKGRVGAG ASSADPRAIG TGAALPAQPD
LGEERPATPP AWRGHGSKAL AAPPDQRVLL TDLIENIYIS STSGRELKIL MASEVPEHNP
QLDSITVSKK RNWLHQSTLK APNLEEENIC KKMQGNTIHV PKSSSPLPGP KLPPVPPKSP
IGQECPARTS SFVTAVHHST NPSVLRNCTL DFSEDNDADD EGEIWYNPIP EDDEPDFPRV
HCFTGKNSVN LDSHTTSFKM LPGSDLIKVM GHNKGLPYFS ESAGDNQMAQ ACEINQADSI
HSTEYVQLHK QSFVCKTQSA TAIEESPAFK YCSAGSGIVP ANKAEAGATE ISPPSPNPLK
KGGSINWPFP DKIKSPRTVR KLSMKMKKLP ELSRKLSIKG TSSSNSSDNP SSLLKGDCQD
TSHATSLPSS GNATAAASRN VISRYHLDSS VSSQHGYKKK SSGSSKSSSK GGYLSDGDSP
ELIAKSGKHG SVSRFGKGKE TLPSNNNKTE IDIDAFRHYS FSDQPKCSQY ISGLMSVHFY
GAEDLKPPRM DSKDVFCAIQ VDSVNKARTA LLTCRTTFLD MDHTFNIEIE NAQHLKLVVF
SWEPTPRKNR VCCHGTVVLP TLFRVTKTHQ LAVKLEPRGL IYVKLTLIEQ WENSLDGLVA
DREPVIFGVD ARKVVEKENV GLMVPLLMQK CIVEIEKRGC QVVGLYRLCG SAAVKKELRE
AFERDSKAVT LCENQYPDIN VITGVLKDYL RELPSPLITK QLYETVLDAM VKNPLKMTAS
GCENDPSDSE HTVALLDCLP DVEKATLKML LDHLKLVASY HEVNKMTCQN LAVCFGPVLL
SQRQETSNHN NRVFTDSEEL ASALDFKKHI EVLHYLLQLW PVQCSTAKES TYSNMFPGNQ
SSLNYLRPKK QRPQMLNLSS TEMSGVLRPR PARLDSPSSN RYAGDWSSCG ENYFLNPKET
LNEADYDDVP SEDTESGEDC SKVDGPDRLI EHAKSMSKEH TFQTYLTMQT IDSAVDHRVN
LKDLQESIDT LIGNLERELN KNKLNITY
//
