ID V9KA11_CALMI Unreviewed; 879 AA.
AC V9KA11;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Rho GTPase activating protein 12 {ECO:0000313|EMBL:AFO94691.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO94691.1};
RN [1] {ECO:0000313|EMBL:AFO94691.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ovary {ECO:0000313|EMBL:AFO94691.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
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DR EMBL; JW862174; AFO94691.1; -; mRNA.
DR AlphaFoldDB; V9KA11; -.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd13233; PH_ARHGAP9-like; 1.
DR CDD; cd04403; RhoGAP_ARHGAP27_15_12_9; 1.
DR CDD; cd12070; SH3_ARHGAP12; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035491; ARHGAP12_SH3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR23176:SF107; RHO GTPASE-ACTIVATING PROTEIN 12; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF16618; SH3-WW_linker; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 2: Evidence at transcript level;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 14..76
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 270..303
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 370..397
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 495..606
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 687..876
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 100..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 879 AA; 100125 MW; E16CD18C496DA864 CRC64;
MAEKDGKPNL PIIPGQMWIE VEYDYEYEAK DRKISIKQGE KYILVKKTNN DWWQVKKEET
SKLFYLPAQY VKELPRKALM PPVKHGPSCV KSAALNVDTK PLQDSTESPY KPLDYSNSFK
SSTGPLQSQP TDLDTSQIHH RDQGLLHLQT AVQDSAKTST QSYGPGESES QYPRVPNQTW
NLGAGRSQSS DSMDGENSLY DPSYEWTSES SGRQHQDSES GDEFSSSSTE QLQTPSPAGP
TRPDSPVYAN LQDLKMSQAN LPPVPKSSPI QVLGDWEMHK DATGRTYYYN KGSQERSWKP
PRGTRDSINK EHGSQGDSIN HAHHITDENS RSTFSSYSDN QFDSPPRGWS EEMDERGQTL
YVSEYTNEKW MKHTDDQGRR YFYSTDGSKS EWELPQYNIS AKQQEIIGKS RSLDRKPAEP
LVLTNWRHST YTGGPLDLEK FTTKKHKRNS SEHLCAPPSY LYSQHPDQES STSPKPVHDN
NNEPPLSPKS PQPSLTEKYG LLNVTKITDN GKKVRKNWTS SWTVLQGSSL LFAKNQGSGW
KFGSNQSKPE FTVDLRGAAI EWASKDKSSK KNVLELRTRQ GTELLIQLDN DATIAEWHKA
LEITIGNQTE PDEIFEDDLP ESPGIDKHDK DKNNKDLKKS RQVKSSFSME NADQKKTKTK
LKKFLTRRPT LQAVRDKGYI KDQVFGCNLD SLCQRENTTI PQFVKMCIDH VEKEGLDIDG
LYRVSGNLAV IQKLRFAVNH DEKLDLKDSK WEDINVITGA LKMFFRELPE PLFTYHLFND
FVNAIKNPDY KQRVQDIKEL IRQLPKPNHD TMQILFQHLG KIVANGELNR MTTQSVAIVF
GPTLLKPEKE TGNIAVHMVY QNQIVELILT EYETVFGRS
//