ID A0A2U3YEE1_LEPWE Unreviewed; 1280 AA.
AC A0A2U3YEE1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Ras GTPase-activating protein nGAP isoform X4 {ECO:0000313|RefSeq:XP_006742067.1};
GN Name=RASAL2 {ECO:0000313|RefSeq:XP_006742067.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006742067.1};
RN [1] {ECO:0000313|RefSeq:XP_006742067.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006742067.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_006742067.1; XM_006742004.2.
DR AlphaFoldDB; A0A2U3YEE1; -.
DR GeneID; 102731896; -.
DR CTD; 9462; -.
DR OrthoDB; 22721at2759; -.
DR Proteomes; UP000245341; Unplaced.
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; 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:UP000245341}.
FT DOMAIN 75..306
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 297..415
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 475..667
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1107..1193
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 162..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1280 AA; 143949 MW; 539C923A7301F810 CRC64;
MELSPSSGGA AEALSWPEMF PGLESDSPLP PEELEAVVPV GGAVAGGMLD RIFLESVCQQ
QSWVRVYDVK GPPTHRLSCG QSPYTETTTW ERKYCILTDS QLVLLNKEKE IPVEGGQEQQ
TDSSKGRCLR RTVSVPSEGQ FPEYPPEGAT KLEVPAERSP RRRSISGTST SEKPNSMDTV
NTSPFKVPGF FSKRLKGSIK RTKSQSKLDR NTSFRLPSLR NADDRARGLP KLKESRSHES
LLSPCSAVEC LDLGRGEPVS VKPLHSSVLG QDFCFEVTYL SGSKCFSCNS ASERDKWMEN
LRRTVQPNKD NCRRAENVLR LWIIEAKDLA PKKKYFCELC LDDTLFARTT SKTKADNIFW
GEHFEFYSLP PLHSITVHIY KDVEKKKKKD KNNYVGLVNI PTASVTGRQF VEKWYPVSTP
TPNKGKTGGP SIRIKSRFQT ITILPMEQYK EFAEFVTSNY TMLCSVLEPV ISVRNKEELA
CALVHILQST GRAKDFLTDL VMSEVDRCGE HDVLIFRENT IATKSIEEYL KLVGQQYLHD
ALGEFIKALY ESDENCEVDP SKCSSSELID HQSNLKMCCE LAFCKIINSY CVFPRELREV
FASWKQQCLN RGKQDISERL ISASLFLRFL CPAIMSPSLF NLMQEYPDDR TSRTLTLIAK
VIQNLANFAK FGNKEEYMAF MNDFLEHEWG GMKRFLLEIS NPDTISNTPG FDGYIDLGRE
LSVLHSLLWE VVSQLDKATV AKLGPLPRVL ADITKSLTNP TPIQQQLRRF TEHNSSPNVS
GSLSSGLQKI FEDPTDSDLH KLKSPSQDNT DSYFRGKTLL LVQQASSQSM TYSEKDEKES
SLPNGRSISL MDLQDPHAAQ VEHASVMLDV PMRLTGSQLS ITQVASIKQL RETQSTPQSA
PQVRRPLHPA LNQPGSLQPL SFQNPVYHLN NPIPAMPKAS VDSSLENLST ASSRSQSNSE
DFKLSGPSNS SMEDFTKRST QSEDFSRRHT VPDRHIPLAL PRQSSTGQAP IRKMDQAGLG
ARAKALPSLP HSASLRSTGS MSVASAALVA EPLQNGSRSR QQSSSSRESP VPKVRAIQRQ
QTQQVQSPVD SATMSPVERT AAWVLNNGQY EEDVEETEQN QDESKHAEKY EQEITKLKER
LRVSSRRLEE YERRLLVQEQ QMQKLLLEYK ARLEDSEERL RRQQEEKDSQ MKSIISRLMA
VEEELKKDHA EMQAVIDAKQ KIIDAQEKRI VSLDSANTRL MSALTQVKER YSMQVRNGIS
PTNPTKLSIT ENGEFKNSSC
//
