ID   A0A2Y9JCZ7_ENHLU        Unreviewed;       850 AA.
AC   A0A2Y9JCZ7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Ras GTPase-activating protein 2 isoform X1 {ECO:0000313|RefSeq:XP_022358887.1};
GN   Name=LOC111147253 {ECO:0000313|RefSeq:XP_022358887.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022358887.1};
RN   [1] {ECO:0000313|RefSeq:XP_022358887.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022358887.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_022358887.1; XM_022503179.1.
DR   AlphaFoldDB; A0A2Y9JCZ7; -.
DR   KEGG; elk:111147253; -.
DR   Proteomes; UP000248482; 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; cd08401; C2A_RasA2_RasA3; 1.
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:UP000248482};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00432}.
FT   DOMAIN          20..138
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          149..289
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          356..550
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   DOMAIN          604..706
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          825..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   850 AA;  96596 MW;  ECE37754C4D7A5A7 CRC64;
     MAAAAPAAAA ASSEAPAATA TAEPEAGDED SREVRVLQSL RGKICEAKNL LPYLGPNKMR
     DCFCTINLDQ EEVYRTQVVE KSLSPFFSEE FYFEIPRTFQ YLSFYVYDKN VLQRDLRIGK
     VAIKKEDLCN HSGKETWFSL QPVDSNSEVQ GKVHLELKLN ELITENGTVC QQLVVHIMAC
     HGLPLINGQS CDPYATVSLV GPSRNDQKKT KVKKKTSNPQ FNEIFYFEVT RSSSYTRKSQ
     FQVEEEDIEK LEIRIDLWNN GNLVQDIFLG EIKVPVNVLR NDSSHQAWYL LQPRDNGNKS
     SKTDDLGSLR LNICYTEDYV LPSEYYGPLK TLLLKSPDVQ PISASAAYIL GEICRDKNDA
     VLPLVRLLLH HDKLVPFATA VAELDLKDTQ DANTIFRGNS LATRCLDEMM KIVGGHYLKV
     TLKPILDEIC ESSKSCEIDP IKLKEGDNVE NNKENLRYYV DKLFSTIVKS SMSCPTVMCD
     TFYSLRQMAT QRFPNDPHVQ YSAVSSFVFL RFFAVAVVSP HTFHLRPHHP DPQTVRTLTL
     ISKTIQTLGS WGSLSKSKSS FKETFMCEFF KMFQEEGYIV AVKKFLDEIS STETKESSGT
     SEPVHLKEGE MYKRAQGRTR IGKKNFKKRW FCLTSRELTY HKQPGSKDAI YTIPVKNILA
     VEKLEESSFN KKNMFQVIHM EKPLYVQANN CVEANEWIDV LCRVSRCNQN RLSFYHPSAY
     LNGNWLCCLE TSENALGCKP CTAGVPADIQ IDIDEDRETE RIYSLFTLSL LKLQKMEEAC
     GTIAVYQGPQ KEPDDYSNFV IEDSVTTFKT IQQIKSIIEK LDEPHEKYRK KRSSSAKYGS
     KENPIVGKTS
//