ID U3J4N3_ANAPP Unreviewed; 1265 AA.
AC U3J4N3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 2.
DT 24-JAN-2024, entry version 65.
DE SubName: Full=RAS protein activator like 2 {ECO:0000313|Ensembl:ENSAPLP00000014460.2};
GN Name=RASAL2 {ECO:0000313|Ensembl:ENSAPLP00000014460.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000014460.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000014460.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000014460.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; U3J4N3; -.
DR STRING; 8840.ENSAPLP00000014460; -.
DR Ensembl; ENSAPLT00000015237.2; ENSAPLP00000014460.2; ENSAPLG00000014584.2.
DR GeneTree; ENSGT00940000157702; -.
DR HOGENOM; CLU_001727_1_0_1; -.
DR OMA; HAAQMDH; -.
DR Proteomes; UP000016666; Chromosome 8.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:2000257; P:regulation of protein activation cascade; IEA:Ensembl.
DR GO; GO:0002021; P:response to dietary excess; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
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; 1.
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:UP000016666}.
FT DOMAIN 44..292
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 283..401
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 461..653
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 121..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1105..1178
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 148..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..981
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1079
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1265 AA; 142232 MW; B06A5E7163B29C64 CRC64;
MEAPPAAGEP PAWAAEALAE PELGSDELEA AAGGALDRVL LESVCQQQGW LRVYDVKGPP
THRLSCGQSP YTDTTTWERK YCILTDSQLV LLNREKEVPM DGAQEPQDAT KGRCLRRTVS
VPSEGQFPEY PPDGAAKLEV PAERSPRRRS ISGTSTSEKT NSMDAANTSP FKVPGFFSKR
LKGSIKRTKS QSKLDRNTSF RLPSLRNADD RSRGLPKLKE SRSHESLLSP GSAVEALDLG
SEEKVFVKPL HSSILGQDFC FEVTYSSGSK CFSCSSAAER DKWMENLRRT VQPNKDNCRR
AENVLRLWII EAKDLAPKKK YFCELCLDDT LFARTTSKTK ADNIFWGEHF EFYGLPPLHS
ITVHIYKDVE KKKKKDKNNY VGLVNIPMAS VTGRQFVEKW YPVSTPTPNK GKSGGPSIRI
KSRYQTITIL PMEQYKEFAE FVTSNYTMLC SVLEPVISVR NKEEMACALV HILQSTGRAK
DFLTDLVMSE VDRCGEHDVL IFRENTLATK AIEEYLKLVG QKYLHDALGE FIKALYESDE
NCEVDPSKCS SSELTDHQSN LKMCCELAFC KIINSYCVFP RELKEVFASW KQQCLSRGKQ
DISERLISAS LFLRFLCPAI MSPSLFSLMQ EYPDDRTSRT LTLIAKVIQN LANFAKFGNK
EEYMAFMNDF LEHEWGGMKR FLLEISNPDT ISNMPGFEGY IDLGRELSVL HSLLWEVVSQ
LDKATVAKLG PLPRILADIT KSMTNPTPIQ QQLRRFTEHS SSPNVSGSLS SGLQKIFEDP
TDGDLHKLKS PTQENVDGYF RGKTLLLVQQ ASTQSMTYSD KDERESILPN GRSISLMDLQ
DPHTAHSDHA SIMHDVPLRL AGSQLSITQV ANIKQLWEAQ STPQSAPQVR RPLHPALNQQ
GSLQPLSFQN PVYHLNNPPP PMPKASVDSS LENLSTASSR SRSNSEDFKL SGPSNSSMED
FTKRSTQSED FSRRHTVTDK HVPIALPRQN SSSQAQIRKM DQGLGARAKA PQSLPHSASL
RSTGSMSGVS GAMVTEPIQN GSRSRQQSSS SRESPVPKVR AIQRQQTQQV QSPVDSATMS
PVERTAAWVL NNGQYEEVEE DAEQNPDEAK HAEKYEQEIA KLKERLKVSS RRLEEYERRL
LVQEQQMQKL LMEYKSRLED SEERLRRQQE EKDSQMKSII SRLMAVEEEL KKDHAEMQAV
IDAKQKIIDA QEKRIVSLDS ANTRLMSALT QVKERYSMQV RNGISPTNPT KLSITENGEF
KNSSC
//
