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Database: UniProt
Entry: V9KA11_CALMI
LinkDB: V9KA11_CALMI
Original site: V9KA11_CALMI 
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
//
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