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Database: UniProt
Entry: A0A2K5CHM0_AOTNA
LinkDB: A0A2K5CHM0_AOTNA
Original site: A0A2K5CHM0_AOTNA 
ID   A0A2K5CHM0_AOTNA        Unreviewed;       738 AA.
AC   A0A2K5CHM0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   10-JUN-2026, entry version 36.
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};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000008154.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000008154.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   AlphaFoldDB; A0A2K5CHM0; -.
DR   STRING; 37293.ENSANAP00000008154; -.
DR   Ensembl; ENSANAT00000025934.1; ENSANAP00000008154.1; ENSANAG00000022113.1.
DR   GeneTree; ENSGT01030000234635; -.
DR   Proteomes; UP000233020; 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:1901165; P:positive regulation of trophoblast cell migration; IEA:Ensembl.
DR   GO; GO:0051493; P:regulation of cytoskeleton organization; IEA:Ensembl.
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; IPR000008; C2_dom.
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; PS50004; C2; 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:UP000233020}.
FT   DOMAIN          252..369
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          401..607
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          629..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..74
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..134
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..150
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..224
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   738 AA;  80058 MW;  3862ABB184702EF5 CRC64;
     MAEPLLRKTF SRLRGREKLP RKKSDAKERG ERGSVREEGS PSPARPRRPR GRSAGRSGGG
     SPSPEASRSP ARGAYLQSLE PSSRRWVLGG AKPTEDTSLG PGAPGSGEPA GEIWYNPIPE
     EDPKPPASEP PGPQPDSAEP EGPASQGAAP ASPPTKASRT KSPGPARRLS IKMKKLPELR
     RRLSLRGPRA GRERERAAPA GSVISRYHLD SSVGGPGRAA GSGGTQSPRT GYLSDGDSPE
     RPAGLPSPTS FQPYEVGPTA RAPPAALWGR LSLHLYGLGG LRPAPGATPR DLCCLLQVDG
     EARARTGPLR GGPDFLRLDH TFHLELEAAQ LLRALVLAWD PGVRRHRPCA QGTVLLPTVF
     RGCQAQQLAV RLEPQGLLYA KLTLSEQQEA PATAEPRVFG LPLPLLVERE RPPGQVPLII
     QKCVGQIERR GLRVVGLYRL CGSAAVKKEL RDAFERDSAA VCLSEDLYPD INVITGILKD
     YLRELPTPLI TQPLYQVVLE AMAHDPPNRG PPTTDSTRGL LSCLPDVERA TLTLLLDHLR
     LVSSFHAYNR MTPQNLAVCF GPVLLPARQA PTRSRARSSG PGLTSAVDFK RHIEVLHYLL
     QSWPDPHLPP EAPDVAPYLR PKRQPALHLP LADPEVVSRP RGRGGPESPP SNRYAGDWSV
     CGRDFLPCGR DFLSGPDYDH VTGSDSEDED EEAGEPRITA DFEDDFDAPF NPHLNLKDFD
     ALILDLEREL SKQINVCL
//
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