ID A0A1S3NRK4_SALSA Unreviewed; 821 AA.
AC A0A1S3NRK4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Ras GTPase-activating protein 2 {ECO:0000313|RefSeq:XP_014017870.1};
GN Name=rasa2 {ECO:0000313|RefSeq:XP_014017870.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014017870.1};
RN [1] {ECO:0000313|RefSeq:XP_014017870.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014017870.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_014017870.1; XM_014162395.1.
DR AlphaFoldDB; A0A1S3NRK4; -.
DR STRING; 8030.ENSSSAP00000083590; -.
DR PaxDb; 8030-ENSSSAP00000083590; -.
DR Ensembl; ENSSSAT00000117375; ENSSSAP00000083590; ENSSSAG00000065814.
DR GeneID; 106580875; -.
DR KEGG; sasa:106580875; -.
DR CTD; 5922; -.
DR OMA; GKICQAK; -.
DR OrthoDB; 24454at2759; -.
DR Proteomes; UP000087266; Chromosome ssa20.
DR Bgee; ENSSSAG00000065814; Expressed in head kidney and 13 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; 1.
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:UP000087266};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00432}.
FT DOMAIN 1..115
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 126..266
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 331..525
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT DOMAIN 580..681
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 797..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 821 AA; 93519 MW; 2AE57BCA271A3E8A CRC64;
MAEEEDTRIR ILQSLRGKIC EGKNLGPCSG PNRQRDLCTF CTISLDQEEV FRTKVFDKSL
SPFYGEDFYF EIPRPFQCLS FYVFAKGVFQ RDLPVGKVSI RKEELCKFSG KEHWFGLQPV
DPNSEVQGKV HLEMRLNELI IENGSMCQQL LVRIIECQGL PLISGQNCDP YATVSLVGPA
RSDQKKTKVK KKTSDPQFEE TFNFEVTRPN SYTKKSNFPV EEEDIEKLEI KVDLWNNGNL
AQDVFLGETR VSVKILRNDH IHRAWYLLQP KGNGKSKTDD LGSLRLNVTY IEDNVLPSAC
YTPLRTLLLK SPDIKPISAS AAHILGDICR ERYEAVLPVV RLLLHHSRLV PFVSAITVLE
LENTQEANTI FRGNSLATRC IDDMMKIVGR SYLTVTLKPV LDEICESNKT CEIDPIKLKE
GDNVEVNKEN LQGYVQKVFS SITQSSSSCP PLMCDVFRSL RHMASKRFPD DPHVQYSAVS
SFVFLRFFAV AVLSPHTFQL RPHHPDLEVS RTLTLISKTI QTLGSWGSLS KNKLSSFKES
YMYDFFKSFQ EDKCIEKVKK FLDEISSNVS KESSGVEDSV VLKEGEIQKR AQGRKRIGKR
NFKKRWLRVT NRELSYHKHR GKEALCIIPV KDIRAVEKLY ESAFNRKNMF QVLHSEKPLY
VQAGNCVEAS EWVEVLSQVS RCNPDRLGTF HPSAYVAGAW LCCRSLSDSQ PGCKPCTPTL
LANLQLDIDC DRETERIFSL LTSSYSKLQK MEDACASIAV YQGPPKEQDD YSLFTIQDPK
ETFHTVRQIT HILEELQREH DTRSGTAQYG SQENPIVGKT S
//
