ID A0A2K6EL59_PROCO Unreviewed; 766 AA.
AC A0A2K6EL59;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Rho GTPase activating protein 44 {ECO:0000313|Ensembl:ENSPCOP00000002464.1};
GN Name=ARHGAP44 {ECO:0000313|Ensembl:ENSPCOP00000002464.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000002464.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000002464.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A2K6EL59; -.
DR STRING; 379532.ENSPCOP00000002464; -.
DR Ensembl; ENSPCOT00000008499.1; ENSPCOP00000002464.1; ENSPCOG00000007455.1.
DR GeneTree; ENSGT00940000157296; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0031256; C:leading edge membrane; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0098886; P:modification of dendritic spine; IEA:Ensembl.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0035021; P:negative regulation of Rac protein signal transduction; IEA:Ensembl.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:0099152; P:regulation of neurotransmitter receptor transport, endosome to postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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 InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR047165; RHG17/44/SH3BP1-like.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR14130; 3BP-1 RELATED RHOGAP; 1.
DR PANTHER; PTHR14130:SF13; RHO GTPASE-ACTIVATING PROTEIN 44; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160}.
FT DOMAIN 1..200
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 206..396
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 418..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..531
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..695
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 83418 MW; C15AA4B64B5ACC8B CRC64;
MKKQFNRMRQ LANQTVGKKL PLTTLAQCLM EGSAILGDDT LLGKMLKLCG ETEDKLAQEL
IHFELQVERD VIEPLFLLAE VEIPNIQKQR KHLAKLVLDM DSSRTRWQQT SKSSGLSSSL
QPAGAKADAL REEMEEAANR VEICRDQLSA DMYSFVAKEI DYANYFQTLI KVQAEYHRKS
LTLLQAVLPQ IKAQQEAWVE KPSFGKPLEE HLTISGREIA FPIEACVTML LECGMQEEGL
FRVAPSASKL KKLKAALDCC VVDVQEYSAD PHAIAGALKS YLRELPEPLM TFELYDEWIQ
ASNIQEQDKK LQALWNACEK LPKANHNNIR YLIKFLSKLS EYQDINKMTP SNMAIVLGPN
LLWPQAEGNI TEMMTTVSLQ IVGIIEPIIQ HADWFFPGEI EFNITGNYGS PVHVNHNANY
SSMPSPDMDP ADRRQTEQAR RPLSVATDNM MLEFYKKDGL RKIQSMGVRV MDTSWVARRG
SSAGRKASCA PPSMQPPAPP AELAAPLQSL PSPLPEQPLD SPAPPALSPS GVGLQPGPER
TSTSKSKELS PGSGQKGSPG SSQGTAGAGT QPGAQPGASP SQPPADQSPH TLRKVSKKLA
PIPPKAPFGQ PGAVAEQCTG QPSPVSLSPT PPSTPSPYGL SYPQGYSLAS GQLSPAAAPP
LASPSVFTST LTKSRPTPKP RQRPTLPPPQ PPTVNLSASS PQSAESPLLD GVSPGESMST
DLVHFDIPSI HIELGSTLRL SPRERAQRHS VTDKRDEEEE SESTAL
//
