ID V8PFS1_OPHHA Unreviewed; 1288 AA.
AC V8PFS1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Rho GTPase-activating protein 29 {ECO:0000256|ARBA:ARBA00040783};
DE AltName: Full=Rho-type GTPase-activating protein 29 {ECO:0000256|ARBA:ARBA00042921};
DE Flags: Fragment;
GN Name=arhgap29 {ECO:0000313|EMBL:ETE72732.1};
GN ORFNames=L345_01436 {ECO:0000313|EMBL:ETE72732.1};
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:ETE72732.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE72732.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE72732.1};
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 -!- 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:ETE72732.1}.
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; AZIM01000186; ETE72732.1; -; Genomic_DNA.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20816; C1_GMIP-like; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR15228:SF7; RHO GTPASE-ACTIVATING PROTEIN 29; 1.
DR PANTHER; PTHR15228; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 216..485
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 669..714
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 728..942
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 588..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 321..362
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 388..425
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 588..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE72732.1"
SQ SEQUENCE 1288 AA; 144145 MW; 7A958177B2A76C48 CRC64;
MLRQNSDSNK CGLGLTKLST SNLFPISNTG KRGMGRNTKS NSLNSISSNF DGYDNIIVDP
DYIMQLVNDV RKFADVLLNL REAITSENQN CLHQFVHERL GEVLRVLKAI INKHPNLYSV
DVLSAAGTVI AKVRAVNFKE INEEKREVLS EIFSSIDLLA FTFGNAVSDC LMGDVDNGSG
LGHQVSRQSQ SFENLCTDSG VSLHEGVQST GHLNAEEIDS VLLKNDNGIK SALSYAKAWS
KYAKDIIVWV EKKINLEMEC AKNLAKVAET TKTIIVSQDY MPFQSIFMNA FQNDIENSLL
WQQTAVALQT NKFLQPLLGR KNELDRQRKE IKELWQREEK KMQELESSVR KAKQLYLQRQ
EEYEKARSTT LRAEDDYITS NWGFTKDTSK IEKKRKLEEE ALQKAEEANE HFKTSKAEVE
EKRNNLENFK SVILTQLREQ IYQCDLTLKA ATVNLFQIQH TQCVSMPVNC QLLCERAKLY
DPGKKLFEYV KNLPKYDVPT ESVCFETQTS QVGGVFGEQS NNVSASQVCI PQCSGDYPIQ
LLDDTTSPAY LCSQKIGDKR SLSSTDVSAV RGLPPFRSWS VGNQSWGMCS DSESAGGSSE
SRSVDSPSAS PGDFKRLPRT PSIGTMSSAD DLDEREAPSP DCGLNDLAAE IASTPGPFRN
TLLSKAAQTH KLRKLRSPSK CRECDSLVVF HGAECEECSL SCHKKCLETL AIQCGHKKLH
GKLHLFGVEF TQVSKNSQDG IPFIIRKCTS EIESRALNVK GIYRVNGAKS RVEKLCQSFE
NGKDLVELSE LNAHDISNVL KLFLRQLPEP LILSRFYNEF IGLAKESQNI NEELDRKQMR
PKLNKQPVCI ELNRIILKIK DLLKLLPTAN RNTLQFLLAH LCRVSEQSDE NKMSACNLGI
IFGPTLIRPR ETDATLSLSS LVDYPYQARM VELLITHYEK IFDTAQEHSS AATESDENSF
CIKKSTSTLE RKLSLGKQNS LSESTSVLTL ENDTVPIKKS DDKATPVSDQ DNGKHDPETE
DGVKSDQLIR PKHQIIKVQM RCQKSKPFLR PVSLPLGPML PSCILNEQNF QNASLNPDKL
GKSLVIEDIS ETQALSSANA GSRISCYDPH TQKKTWDKQY KQYDITSKTA KIMTNIHENL
TQESVNTCAL NASSNFVNNS VNAILLCKPY TGPITTVREA STPVVTLKKP RCFQPPGETF
YKPSANNNAK TNGESSASKC CAAVIHNDMP GLGVNPGLDH GFLDSSSQHR KEQKSTFETL
SPTDLKPAYQ RLRPKRMQEL EHREAHFV
//