ID   A0A2K6QS69_RHIRO        Unreviewed;       807 AA.
AC   A0A2K6QS69;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=RAS p21 protein activator 2 {ECO:0000313|Ensembl:ENSRROP00000031606.1};
GN   Name=RASA2 {ECO:0000313|Ensembl:ENSRROP00000031606.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000031606.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000031606.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A2K6QS69; -.
DR   Ensembl; ENSRROT00000056022.1; ENSRROP00000031606.1; ENSRROG00000039486.1.
DR   GeneTree; ENSGT00940000158201; -.
DR   OMA; GKICQAK; -.
DR   Proteomes; UP000233200; Unplaced.
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:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:InterPro.
DR   CDD; cd04010; C2B_RasA3; 1.
DR   CDD; cd13370; PH_GAP1m_mammal-like; 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; IPR037773; RASA2_PH.
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   PRINTS; PR00402; TECBTKDOMAIN.
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   Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00432}.
FT   DOMAIN          1..96
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          107..247
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          314..508
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   DOMAIN          562..663
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          782..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   807 AA;  92314 MW;  07E34F6958108E82 CRC64;
     TATAIPWAQA ILTPQPLKDC FCTINLDQEE VYRTQVVEKS LSPFFSEEFY FEIPRTFQYL
     SFYVYDKNVL QRDLRIGKVA IKKEDLCHHS GKETWFSLQP VDSNSEVQGK VHLELKLNEL
     ITENGTVCQQ LVVHIKACHG LPLINGQSCD PYATVSLVGP SRNDQKKTKV KKKTSNPQFN
     EIFYFEVTRS SSYTRKSQFQ VEEEDIEKLE IRIDLWNNGN LVQDVFLGEI KVPVNVLRTD
     SSHQAWYLLQ PRDNGNKSSK TDDLGSLRLN ICYTEDYVLP SEYYGPLKTL LLKSPDVQPI
     SASAAYILSE ICRDKNDAVL PLVRLLLHHD KLVPFATAVA ELDLKDTQDA NTIFRGNSLA
     TRCLDEMMKI VGGHYLKVTL KPILDEICDS SKSCEIDPIK LKEGDNVENN KENLRYYVDK
     LFSTIVKSSM SCPTVMCDIF YSLRQMATQR FPNDPHVQYS AVSSFVFLRF FAVAVVSPHT
     FHLRPHHPDA QTIRTLTLIS KTIQTLGSWG SLSKSKSSFK ETFMCEFFKM FQEEGYIMAV
     KKFLDEISST ETKESSGTSE PVHLKEGEMY KRAQGRTRIG KKNFKKRWFC LTSRELTYHK
     QPGKDAIYTI PVKNILAVEK LEESSFNKKN MFQVIHTEKP LYVQANNCVE ANEWIDVLCR
     VSRCNQNRLS FYHPSVYLNG NWLCCQETGE NTLGCKPCTA GVPADIQIDI DEDRETERIY
     SLFTLSLLKL QKMEEACGTI AVYQGPQKEP DDYSNFVIED SVTTFKTIQQ IKSIIEKLDE
     PHEKYRKKRS SSAKYGSKEN PIVGKAS
//