ID V8NLW9_OPHHA Unreviewed; 1221 AA.
AC V8NLW9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Rho GTPase-activating protein 35 {ECO:0000313|EMBL:ETE63289.1};
DE Flags: Fragment;
GN Name=ARHGAP35 {ECO:0000313|EMBL:ETE63289.1};
GN ORFNames=L345_10945 {ECO:0000313|EMBL:ETE63289.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE63289.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE63289.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE63289.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE63289.1}.
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DR EMBL; AZIM01002818; ETE63289.1; -; Genomic_DNA.
DR AlphaFoldDB; V8NLW9; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR CDD; cd22221; pseudoGTPaseD_p190RhoGAP-A; 1.
DR CDD; cd00882; Ras_like_GTPase; 1.
DR Gene3D; 1.10.10.440; FF domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039007; pG1.
DR InterPro; IPR032835; RhoGAP-FF1.
DR InterPro; IPR045786; RhoGAP_pG1_pG2.
DR InterPro; IPR039006; RhoGAP_pG2.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR46005; RHO GTPASE-ACTIVATING PROTEIN 190; 1.
DR PANTHER; PTHR46005:SF1; RHO GTPASE-ACTIVATING PROTEIN 35; 1.
DR Pfam; PF00071; Ras; 1.
DR Pfam; PF16512; RhoGAP-FF1; 1.
DR Pfam; PF19518; RhoGAP_pG1_pG2; 1.
DR SMART; SM00441; FF; 4.
DR SUPFAM; SSF81698; FF domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51676; FF; 3.
DR PROSITE; PS51852; PG1; 1.
DR PROSITE; PS51853; PG2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 268..325
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 427..481
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 483..548
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 590..765
FT /note="PG1 pseudoGTPase"
FT /evidence="ECO:0000259|PROSITE:PS51852"
FT DOMAIN 781..945
FT /note="PG2 pseudoGTPase"
FT /evidence="ECO:0000259|PROSITE:PS51853"
FT REGION 967..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 411..438
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 967..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE63289.1"
FT NON_TER 1221
FT /evidence="ECO:0000313|EMBL:ETE63289.1"
SQ SEQUENCE 1221 AA; 139182 MW; 7B70320C9A2CB2AD CRC64;
MARKQDVRIP TYNISVVGLS GTEKEKGQCG IGKSCLCNRF VRPRADDFHL DHTSVLSTSD
FGGRVVNNDH FLYWGEVVRS LEDCVECKMH VVEQTEFIDD QTFQPHRSTA LQPYIKRAAA
TKLASAEKLM YFCTDQLGLE QDFEQKQMPD GKLLVDGFLL CIDVSRGMNR NFDEQLKFVT
NLYNQLTKTK KPTVVVLTKC DEGVERYIRD AHTFVFSKKN LQVVETSARS NVNVDLAFST
LVQLIDKSRG KTKIIPYFEA LKQQSQQIAA AKDKYEWLVS RIVKNHNETW SNVSRKMQSS
PEYQDYVYLE GTQKAKKLFL QHIFRLKQEH IERRKKMYLA MLPLAFDALI PNLDEINHLS
CIKVEKLLET KPDFLKWFVV LEETPWDATS HIDNMENDRI PFDVMDTLPA QQLYETHLEK
LRNERKRAEM RRAFKENLET SPFITPGKPW EEARSFIMNE DFYMWLEESV YMDIYGRHQK
QIIEKAKEDF QELLLEYSEL FYELELDAKP SKEKMGVIQD VLGEEQRFKA LQKLQAERDA
LILKHIHFVY HPTKDTCPSC PACVDAKIEH LISSRFIRPS DRNQKNLLSD SNIDRINLVI
LGKDGLAREL ANEIRALCTN DDKYVIDGKM YELSLRPIEG NVRLPVNSFQ TPTFQPHGCL
CLYNSKESLS YVVESIEKSR ESTLSRRDNH LAHLPLTLIL VNKRGDTSGE TLHSLIQQGQ
QIASKLQCVF LDPASTGIGY GRNINEKQIS QVLKGLLDSK RNLNLMSSTA SLKDLADIDL
RIVMCLLCGD PFNADDILLP VLQSQTCRPS PSGSSNSVLL EYPIGPHKRR IELSLLSFHS
AFSIRKSWLV HGYILFYSAK RKASLAMLRA FLCEVQDIIP VQIVALTEGS IDVLDNDLSR
EQLTEGEEIA QDIEGKFTSI PCSQPQHKLE VFHLFFKDVV ERKNIIEATH MYDNAAEACS
TTEEVFNSPR AGSPLCNSNL QDSEEDVEPP SYSPFRDDSS MPTLSKDLSK LSMELEGNDG
LSVFSVMSTF ESKLNNKVPP PVKPKPAVHF DITKGDLSYL EQGHREGQRK PVSSSSWPPT
DGFDPSDYAE PMDAVVKPRN EEENIYSVPH DSTQGKIITI RNINKTQSNG SGNGSDSEMD
TSSLERGRKV SLTTKPVLYR TRCTRLGRFA SFRTSFSIGS DDELGPIRKK EEDQTSQGYK
GDNAVIPYET TDEDPRKRNI L
//
