ID A0A2K5IFU4_COLAP Unreviewed; 1025 AA.
AC A0A2K5IFU4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=RAS p21 protein activator 1 {ECO:0008006|Google:ProtNLM};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000015337.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000015337.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A2K5IFU4; -.
DR Ensembl; ENSCANT00000038270.1; ENSCANP00000015337.1; ENSCANG00000030680.1.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd08400; C2_Ras_p21A1; 1.
DR CDD; cd13260; PH_RASA1; 1.
DR CDD; cd05391; RasGAP_p120GAP; 1.
DR CDD; cd10354; SH2_Cterm_RasGAP; 1.
DR CDD; cd10353; SH2_Nterm_RasGAP; 1.
DR CDD; cd11788; SH3_RasGAP; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 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; IPR035842; RasGAP_C_SH2.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR035841; RasGAP_N_SH2.
DR InterPro; IPR035652; RasGAP_SH3.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10194:SF146; RAS GTPASE-ACTIVATING PROTEIN 1; 1.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00323; RasGAP; 1.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 172..263
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 270..332
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 329..419
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 452..555
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 555..668
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 726..920
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
SQ SEQUENCE 1025 AA; 114095 MW; 3C868A48523BF6A2 CRC64;
MMAAEAGSEE GGPVTAGAGG GGAAAGSSAY PAVCRVKIPA ALPMAAAPYP GLVETGVAGT
LGGGATLGSG FLGAGSVTGA LGGAGLTGGG TAAGVAGAAA GVGDMALTKL PTSLPAETLG
PGGGFPPLPP PPYLPPLGAG LGTVDEGDSL DGPEYEEEEV AIPLTAPPTN QWYHGKLDRT
IAEERLRQAG KSGSYLIRES DRRPGSFVLS FLSQMNVVNH FRIIAMCGDY YIGGRRFSSL
SDLIGYYSHV SCLLKGEKLL YPVAPPEPVE DRRRVRAILP YTKVPDTDEI SFLKGDMFIV
HNELEDGWMW VTNLRTDEQG LIVEDLVEEV VSFISKQEAY NLLMTVGQVC SFLVRPSDNT
PGDYSLYFRT NENIQRFKIC PTPNNQFMMG GRYYNSIGDI IDHYRKEQIV EGYYLKEPVP
MQDQEQVLND AVDGKEIYNT IRRKTKDAFY KNIVKKGYLL KKGKGKRWKN LYFILEGSDA
QLIYFESEKR ATKPKGLIDL SVCSVYVVHD SLFGRPNCFQ IVVQHFSEEH YIFYFAGETP
EQAEDWMKGL QAFCNLRKSS PGTSNKRLRQ VSSLVLHIEE AHKLPVKHFT NPYCNIYLNS
VQVAKTHARE GQNPVWSEEF VFDDLPPDIN RFEITLSNKT KKSKDPDILF MRCQLSRLQK
GHATDEWFLL SSHIPLKGIE PGSLRVRARY SMEKIMPEEE YSEFKELILQ KELHVVYALS
HVCGQDRTLL ASILLRIFLH EKLESLLLCT LNDREISMED EATTLFRATT LASTLMEQYM
KATATQFVHH ALKDSILKIM ESKQSCELSP SKLEKNEDVN TNLAHLLNIL SELVEKIFMA
SEILPPTLRY IYGCLQKSVQ HKWPTNTTMR TRVVSGFVFL RLICPAILNP RMFNIISDSP
SPIAARTLIL VAKSVQNLAN LVEFGAKEPY MEGVNPFIKS NKHRMIMFLD ELGNVPELPD
TTEHSRTDLS RDLAALHEIC VAHSDELRTL SNERGAQQHV LKKLLAITEL LQQKQNQYTK
TNDVR
//