ID A0A093NVD5_PYGAD Unreviewed; 836 AA.
AC A0A093NVD5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Rho GTPase-activating protein 12 {ECO:0000313|EMBL:KFW68126.1};
DE Flags: Fragment;
GN ORFNames=AS28_03963 {ECO:0000313|EMBL:KFW68126.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW68126.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW68126.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW68126.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KL225148; KFW68126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093NVD5; -.
DR STRING; 9238.A0A093NVD5; -.
DR Proteomes; UP000054081; Unassembled WGS sequence.
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 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 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000054081};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 12..74
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 260..293
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 359..386
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 464..565
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 646..834
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 196..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW68126.1"
FT NON_TER 836
FT /evidence="ECO:0000313|EMBL:KFW68126.1"
SQ SEQUENCE 836 AA; 95061 MW; 221B7D70BC0F7441 CRC64;
IEMADKGGKI LPGQLYIEVE YDYEYEAKDK KIVIKQGEKY ILVKKTNDDW WQVKRDENSK
PFYVPAQYVK EIPRKALMPP VKQASMLPNN SLKLTHGLQR STENVNKSPE LSSFGKSSPV
QVSCLVRDAN QNLGPNNSPG QTLGLSLDLT QNNGKLNNEL QSPKVSNQYR TVSMGHFPCP
EFLEIEKTSF LHEQTVAGEG SEKIHQDSES GDELSSSSTE QVQPTTPPSQ GRPDSPVYAN
LQELKISQSA LPPLPTSAPV QINGEWETHK DTTGRCYYYN RGSQERTWKP PRWARDASIN
KGDSQSHADH EHLSSEENDH SSCYSQSDSQ YGSPPKGWSE ELDEHGQTLY TNDYTNEKWL
KHADEQGRPY YYSADGSRSE WELPKYNASP QQQRDIIKSR SLDRRLQEPI VLTKWRHSTI
VLDTNDKESS TASKASFPEN ESSPSSPKHQ ATGQEKYGLL NVTKITENGK KVRKNWMSSW
AVLQGSSLLF TKTQGSGTGW FGVNQSKPEF TVDLKGALID WASKDKSSKK NVIELKTRQG
TELLIQSDND SFINEWYKVL NYTINNQVVE SDEALEDDVP DSPGVEKQDK EKENKDSKKL
RLKAPSNIDS TDQKKTKTKL KKFLTRRPTL QAVREKGYIK DQVFGSNLTS LCQRENSTVP
KFVKLCIEHV EEHGLDVDGL YRVSGNLAVI QKLRFAVNHD EKLDLNDSKW EDIHVITGAL
KMFFRELPEP LFTYNHFNDF VNAIKQEPRQ RVHAVKDLIK QLPKPNQDTM QVLFRHLKRV
VENGEKNRMT YQSVAIVFGP TLLKPEKETG NIAVHTVYQN QIVELILLEL NSVFGR
//
