ID A0A3P8NYD7_ASTCA Unreviewed; 844 AA.
AC A0A3P8NYD7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=RAS p21 protein activator 2 {ECO:0000313|Ensembl:ENSACLP00000009759.1};
GN Name=RASA2 {ECO:0000313|Ensembl:ENSACLP00000009759.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000009759.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000009759.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000009759.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3P8NYD7; -.
DR STRING; 8154.ENSACLP00000009759; -.
DR Ensembl; ENSACLT00000009983.1; ENSACLP00000009759.1; ENSACLG00000006649.1.
DR GeneTree; ENSGT00940000158201; -.
DR OMA; GKICQAK; -.
DR Proteomes; UP000265100; Chromosome 14.
DR Bgee; ENSACLG00000006649; Expressed in brain and 4 other cell types or tissues.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd05394; RasGAP_RASA2; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001562; Znf_Btk_motif.
DR PANTHER; PTHR10194:SF21; RAS GTPASE-ACTIVATING PROTEIN 2; 1.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR Pfam; PF00779; BTK; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00616; RasGAP; 2.
DR SMART; SM00107; BTK; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS51113; ZF_BTK; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00432}.
FT DOMAIN 20..140
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 151..289
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 355..549
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT DOMAIN 603..704
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 822..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 95922 MW; 4DD951DBF3C37E6A CRC64;
LPAFINGYDK PALNAPEQRQ KSALTMAEDD DAKIRILQSL RGKICEAKNL GSVSGPNRQR
DLCTFCTISL DQEEVFRTKV FDKSVCPFYG EDFYFEIPRP FQCLSFYVYA KSVFQRDLPV
GKVSIRKDDL CKYSGKENWF SLQTVDPNSE VQGKVHLEMR LSEVITENGS TGQHISVRII
ECKELPLISG QNCDPYATVS LVGPARSDQK KTKVKKKTSN PHFEETFFFE VTRSYSRRTQ
FNVEEEDIEK LEIKVDLWNN ENLAQDVFLG ETRVPVKILQ SDHIHKAWYL LQPKGNGNKS
KSDDLGSLRL KLTYIEDTVL PSACYTPLCT LLLKSPDVKP ISASAAHILG DICRERYEVV
LPMVRLLLHN NRFVPFVSAV AALELDNTQE ANTIFRGNSL ATRCIDDMMK IVGKNYLSVT
LKPVIDEICE SNKTCEIDPI KLKEGDNVEV NKENLQGYVQ KVFSSITQSS SNCPPLMCDV
FRSLRHLACK RFPGDPHVQY SAVSSFVFLR FFAVAVLSPH SFQLRSHHPD PEISRTLTLI
SKTIQTLGSW GSLSKKLSSF KETYMYDFFK SFQEEKCIEK VKKFLDEISS NVSKESSGLE
DAVVLKEGEV QKRAQGRKPP GMKTFKKRWL RLTNRELSYH KHKGKDADRT INVKNIRAVE
KVDESAFNRK NMFQVVHSEK PLYVQAGNCV EASEWLEVLS QVSRCNEGRL ATFHPSNYTS
GAWQCCQSLS SNAPGCKPCT TTMLANLQLD IDCDREAERI FSLLSANDTK LQSMEDACAS
LAVYQGPQRE PEEYSKFTIQ EPKETFHTLK QLRNIMEELQ RQHNSRNDVR QYGSLDNPIV
GKTS
//
