ID A0A091DK80_FUKDA Unreviewed; 1269 AA.
AC A0A091DK80;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Ras GTPase-activating protein nGAP {ECO:0000313|EMBL:KFO30675.1};
GN ORFNames=H920_07915 {ECO:0000313|EMBL:KFO30675.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO30675.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO30675.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO30675.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN122390; KFO30675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DK80; -.
DR STRING; 885580.ENSFDAP00000008763; -.
DR eggNOG; KOG3508; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR CDD; cd04013; C2_SynGAP_like; 1.
DR CDD; cd05136; RasGAP_DAB2IP; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR021887; DAB2P_C.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR PANTHER; PTHR10194:SF52; RAS GTPASE-ACTIVATING PROTEIN NGAP; 1.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12004; DAB2P_C; 1.
DR Pfam; PF00616; RasGAP; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT DOMAIN 57..288
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 279..397
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 457..649
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 117..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1096..1182
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 144..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1269 AA; 143192 MW; 1FF52622809EA3E3 CRC64;
MFPGLESDSP LPPEDLEAVV PVSGAVAGGM LDRILLESVC QQQSWVRVYD VKGPPTHRLS
CGQSPYTETT TWERKYCILT DSQLVLLNKE KEIPMEGGQE QHTDSTKGRC LRRTVSVPSE
GQFPEYPPEG TSKLEVPAER SPRRRSISGT STSEKPSSMD TANTSPFKVP GFFSKRLKGS
IKRTKSQSKL DRNTSFRLPS LRNTDERSRG LPKLKESRSH ESLLSPCSAV ECLDLGRGEP
VSVKPLHSSI LGQDFCFEVT YLSGSKCFSC NSASERDKWM ENLRRTVQPN KDNCRRAENV
LRLWIIEAKD LAPKKKYFCE LCLDDTLFAR TTSKTKADNI FWGEHFEFYS LPPLHSITVH
IYKDVEKKKK KDKNNYVGLV NIPTASVTGR QFVEKWYPVS TPTPNKGKTG GPSIRIKSRF
QTITILPMEQ YKEFAEFITS NYTMLCSVLE PVISVRNKEE LACALVHILQ STGRAKDFLT
DLVMSEVDRC GEHDVLIFRE NTIATKSIEE YLKLVGQQYL HDALGEFIKA LYESDENCEV
DPSKCSSSEL IDHQSNLKMC CELAFCKIIN SYCVFPRELK EVFASWKQQC LTRGKQDISE
RLISASLFLR FLCPAIMSPS LFNLMQEYPD DRTSRTLTLI AKVIQNLANF AKFGNKEEYM
AFMNDFLEHE WGGMKRFLLE ISNPDTISNT PGFDGYIDLG RELSVLHSLL WEVVSQLDKG
DNSFLQATVA KLGPLPRVLA DITKSLTNPT PIQQQLRRFT EHNSSPNVSG SLSSGLQKIF
EDPADSDLHK LKSPSQDNTD SYFRGKTLLL VQQASSQSMT YSEKDEKESS LPNGRSISLM
DLQDTHAVQM EHASVMLDVP MRLMGSQLSI TQVASIKQLR ETQSTPQSAP QVRRPLHPAL
NQPGSLQPLS FQNPVYHLNN PIPAMPKASV DSSLENLSTA SSRSQSNSED FKLSGPSNSS
MEDFTKRSTQ SEDFSRRHNM PDRHIPLVLP RQNSTGQTQI RKMDQATLGA RARAPPSLPH
SASLRSTGSM SVASAALVAE PVQNGSRSRQ QSSSSRESPV PKVRAIQRQQ TQQVQSPVDS
ATMSPVERTA AWVLNNGQYE EDVEETEQNQ DEAKHAEKYE QEISKLKERL RVSSRRLEEY
ERRLLVQEQQ MQKLLLEYKA RLEDSEERLR RQQEEKDSQM KSIISRLMAV EEELKKDHAE
MQAVIDAKQK IIDAQEKRIV SLDSANTRLM SALTQVKERY SMQVRNGISP TNPTKLSITE
NGEFKNSSC
//
