ID A0A3Q3B694_KRYMA Unreviewed; 1249 AA.
AC A0A3Q3B694;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Ras/Rap GTPase-activating protein SynGAP-like {ECO:0000313|Ensembl:ENSKMAP00000019699.1};
GN Name=SYNGAP1 {ECO:0000313|Ensembl:ENSKMAP00000019699.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000019699.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000019699.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3Q3B694; -.
DR STRING; 37003.ENSKMAP00000019699; -.
DR Ensembl; ENSKMAT00000019964.1; ENSKMAP00000019699.1; ENSKMAG00000014642.1.
DR GeneTree; ENSGT00940000158438; -.
DR OMA; SHVFPRE; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:InterPro.
DR GO; GO:0036269; P:swimming behavior; IEA:Ensembl.
DR CDD; cd04013; C2_SynGAP_like; 1.
DR CDD; cd13375; PH_SynGAP; 1.
DR CDD; cd05136; RasGAP_DAB2IP; 1.
DR CDD; cd22265; UDM1_RNF168; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR021887; DAB2P_C.
DR InterPro; IPR011993; PH-like_dom_sf.
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 InterPro; IPR037779; SynGAP_PH.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR PANTHER; PTHR10194:SF25; RAS_RAP GTPASE-ACTIVATING PROTEIN SYNGAP; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12004; DAB2P_C; 1.
DR Pfam; PF00616; RasGAP; 2.
DR SMART; SM00239; C2; 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:UP000264800};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1249
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018697903"
FT DOMAIN 156..190
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 181..299
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 366..558
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 700..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1164..1223
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 700..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..1042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1249 AA; 140947 MW; B6C97B08562B2741 CRC64;
MSSGFILVNF LSLPHLCCFA LGHVVSYLTG DAPLPLADHR ARRKSIATGK QPSMEVPPTA
PLQPFRQSSF LSKRLKGSIK RAKSQPKLDR TSSFRHMILP RFRSADQDRT RLMQSFKESH
SHESLLSPSS AAEALDLTLD EDAIIKPVHS SILGQEYCFE VTTASGTKCF ACRSAAERDK
WIENLQRAVK PNKDNSRRVD NVLKLWIIEA RELPAKKRYY CELCLDDMLY ARTTSKPRTD
TVFWGEHFEF NNLPAVRNLR LHLYKETDKK RRKEKSTYLG LVSIPISSIT GRQFVEQWYP
VIQPSVLTKG AGVGGGKIIN ASLRLKSRFQ TMNILPMELY KEFAEYVTNN YRTLCAVLEP
VLSVKSKEEV ACALVHILQS TGKAKDFLSD MAMCEVDRFI DREHLIFREN TLATKAIEEY
LKLIGHKYLK DAIGEFIRAL YESEENCEVD PMRIPPSVLP DHQANLRMCC ELALCKIVNS
HCVFPRELKE VFASWRVRCA ERGREDISDR LISGSLFLRF LCPAIMSPSL FNLTQEYPDE
QTSRTLTLIA KVVQNLANFS KFGNKEEYMC FMNEFLEMEW GSMQQFLYEI SNLDSVSNAG
GFEGYIDLGR ELSILHSLLW EVMAQLSKDA IIKLGPLPRL LNDISMALRN PHLQRQPSHQ
TDRVQDRQMD RLLSRPSFNR GISSEFQNLM MRDLNSSIDI TRLPSPTSTG GVMPSRSQMS
FQDRDHPHRV SKDMFYVSRP PLARSSPAYC TSSSDITEPD PKVLNVYKSV SMMDLQDSRM
NSVSNLQSVD MLNSSQASIA GMGSFGGSQL RAGGRLSAGS GGSSMSGGLR LSQLSQMGTT
TDSLSQQQQQ QAAAMRYPLS FQNPLFHLAT ADGPQQQQLH HQHSRAQPPA PLLLAPEPEP
SHQTYIPQFA HGGFSRSEDL STLRTRDSHL GQPSIIHSHS YSDDYSRADY ARRQMSMHVQ
DNLQQQQEMM GMASQTGTSH SSLATTPPST VQPMRQSSVA PPPSQRVKSQ TSHQLSVSSA
AAPASSGKSR PQSGNLLQSP ESGYGGRQHG PRQLSVKDNT APGLPHQQSS VREGGSPQGT
TSQSTQQSPQ QQSQQHLLKP TMSKQGSQTP STLNPPTPAN ERTVAWVSNM PHLSADIESS
RIDREEFKLK EYSKSMDESR MDRVREYEEE INCLKERLIM SHKKLEEYER RLLVQEQQTN
KILLQYQNRL EDSERRLRQQ QMEKDSQIKG IINRKFEILP VLKNKLFGI
//
