ID A0A6P3RLU3_PTEVA Unreviewed; 649 AA.
AC A0A6P3RLU3;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 10-JUN-2026, entry version 22.
DE RecName: Full=Rho GTPase-activating protein SYDE1 {ECO:0000256|ARBA:ARBA00074687};
DE AltName: Full=Synapse defective protein 1 homolog 1 {ECO:0000256|ARBA:ARBA00075368};
GN Name=SYDE1 {ECO:0000313|RefSeq:XP_011382417.1};
OS Pteropus vampyrus (Large flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC Pteropodidae; Pteropodinae; Pteropus.
OX NCBI_TaxID=132908 {ECO:0000313|Proteomes:UP000515202, ECO:0000313|RefSeq:XP_011382417.1};
RN [1] {ECO:0000313|RefSeq:XP_011382417.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_011382417.1};
RG RefSeq;
RL Submitted (JAN-2026) to UniProtKB.
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases. As a GCM1
CC downstream effector, it is involved in placental development and
CC positively regulates trophoblast cells migration. It regulates
CC cytoskeletal remodeling by controlling the activity of Rho GTPases
CC including RHOA, CDC42 and RAC1. {ECO:0000256|ARBA:ARBA00057607}.
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DR RefSeq; XP_011382417.1; XM_011384115.2.
DR AlphaFoldDB; A0A6P3RLU3; -.
DR GeneID; 105308252; -.
DR CTD; 85360; -.
DR OrthoDB; 120383at2759; -.
DR Proteomes; UP000515202; 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:000051; Synapse defective Rho GTPase homolog 1; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
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:SF2; RHO GTPASE-ACTIVATING PROTEIN SYDE1; 1.
DR Pfam; PF25336; C2_SYDE; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468, ECO:0000256|PROSITE-
KW ProRule:PRU00172}; Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000515202}.
FT DOMAIN 313..519
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..71
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 71101 MW; CAB4C2C4A7A15518 CRC64;
MAEPLLRKTF SRLRGREKLP RKKSDAKERG RPAQHLEPST TEPEPQAPER AQAGAEGPPS
PEASRSPARG AYLQSLEPSS RRWVLGGAKQ PEEATLGPGG PGSGEPAGEI WYNPIPEEDP
RPLAPEPPEP QPGLAEPEGP ALQGVAPASP PTKASRTKSP GPARRLSMKM KKLPELRRRL
SLRGTRAGRD RERAAPEGSV ISRYHLDSSV DGVARARTGP LRGGPDFLRL DHTFHLELEA
ARLLRALVLA WDPGVHRHRP CAQGIVLLPT VFRGCQAQQL AVHLEPQGLL YAKLTLSEQQ
EAPDTAEPRV FGLPLPLLVE REQPPGQVPL IIQKCVGQIE RRGLRVVGLY RLCGSAAVKK
ELRDAFERDS AAVCLSEDLY PDINVITGIL KDYLRELPTP LITQPLYQVV LEAMAQGPPS
RVPPSADGTR GLLSCLPDVE RATLTLLLDH LRLVSSFHAH NRMTAQNLAV CFGPVLLPAR
QAPTRPCIRS SGPGLANAVD FKRHIEVLHY LLQAWPDPSR SPEAPDLAPY LRPKRQPSLR
LPLAGPEVVT RPRGRGGPES PPSNRYAGDW SVCGRDFLPC GRDFLSGPDY DHVTGSDSDE
DEEAGERRGA ADFEDDFEAP FNPHLNLKDF DALILDLERE LSKQINVCL
//
