ID A0A1S3LR89_SALSA Unreviewed; 1359 AA.
AC A0A1S3LR89;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Rho GTPase-activating protein 35-like isoform X2 {ECO:0000313|RefSeq:XP_013993099.1};
GN Name=LOC106567838 {ECO:0000313|RefSeq:XP_013993099.1};
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_013993099.1};
RN [1] {ECO:0000313|RefSeq:XP_013993099.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013993099.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_013993099.1; XM_014137624.1.
DR GeneID; 106567838; -.
DR OrthoDB; 5405671at2759; -.
DR Proteomes; UP000087266; Chromosome ssa13.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00882; Ras_like_GTPase; 1.
DR Gene3D; 1.10.10.440; FF domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039007; pG1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR032835; RhoGAP-FF1.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR045786; RhoGAP_pG1_pG2.
DR InterPro; IPR039006; RhoGAP_pG2.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR46005; RHO GTPASE-ACTIVATING PROTEIN 190; 1.
DR PANTHER; PTHR46005:SF5; RHO GTPASE-ACTIVATING PROTEIN 35B; 1.
DR Pfam; PF00071; Ras; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF16512; RhoGAP-FF1; 1.
DR Pfam; PF19518; RhoGAP_pG1_pG2; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00441; FF; 4.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF81698; FF domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51676; FF; 1.
DR PROSITE; PS51852; PG1; 1.
DR PROSITE; PS51853; PG2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 428..482
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 592..772
FT /note="PG1 pseudoGTPase"
FT /evidence="ECO:0000259|PROSITE:PS51852"
FT DOMAIN 800..968
FT /note="PG2 pseudoGTPase"
FT /evidence="ECO:0000259|PROSITE:PS51853"
FT DOMAIN 1262..1359
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 767..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..791
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1359 AA; 153572 MW; 466E52008A344CE2 CRC64;
MMAKKQDAKS PTYNLIVVGL SGTEKEKGQC GVGKSCLCNR FVRPSADDFY LDHTSVLSTS
DFGGRVVNND HFLFWGEVGR VVEEGPECRM HVVEQTEFID DQTFQPHRST AMQPYIKRAA
STKLASAEKL MYFCTDQLGL EQDFEQKQMP EGKIQADGFM LCVDVSRGMN RNFDDQLKFV
TNLYGQLSKT KKPIVLVLTK CDEGVERYIK DSHTFAITKK SLPVVETSAR SNINVDLAFI
ALVQLIDKSR GKPKIIPYFE ALKLQSQQIA LAKDRYEWLV NRVVKNHNET WLNTSRRMHS
SSEFKEYVFL EGTAKCKKLF QQHVYRLKQE HIERRRKIYL STLPLALSSL VPDLDEIDQL
SWSGVQKVLE SKQHFAHWFV VLEDSPWEDT SHIDNMEDER IPSDLLETAP AEYIFNAHLE
HLRNECKRAE MRQEFKHKLA CSPFVTPGKP WEEARSFIMN EDFYQWLEES EYLDLYNRHQ
KDIIDHAKED FQELLLEYSE LFYELEVDAK PSKEKMGAIQ DVLGEEQRFK TLQKLPAERD
ALVLKHIHFV YHPTKETCPS SPQCGDFKIE QLLASRFPTC YPFFNVKSHF GDIKADRINL
VILGKDGLAR EFANEIRTLC TNDDRYVLDG KMYELTLRPI EGNVRLPVNS FHTTTFTPHG
CLCLYNSKES LTYVVESIER LRESTIGRRD SHIAQLLTSL LLVTKRGVGT YADIGGETAL
GLITQGQQVA RRLQCSFLDP ASPGVGYGHN VNDSQINQVL RGLLDSRRSS SFSSSSPPLP
PKPPGPRDSP HQPSPEADIR IVMCLMCGDN YDVEQLLSPF LLPQHCRPTS NSGTSVILEQ
TVGPHKQVIE LSLLSYHASF SLRKSRLVHG YIAVYSARRK ASLETLCAFL CEIQDIIPVQ
LLAVGESQVE LTESESAREQ LVQGEELAQE IEGRFNSVVC GSGGVVGGLH RIEMFQHFLM
EVVEKRNIVE ATHMYDNVAE ACTNDTAYSP RCSSPSPGNM FLDSDVDDVE PSPPYFDGTL
TSHGGGFNLP DLDSSDVSVI SDISSFENKL NSKVPPQVRP KPTVTFDFRK VGRNPYNTDT
MGHRRSLPSA VTWVPGGDGG YDPSDYAEPM DAVSKPRPSN EEIIYSVPHD STQGKIITIR
NANRMHSNGN GSDSEADSSS LERCRKFSAA GVKPRLYRDR SKRLGKFSSF RTSFIGSDDE
MGALPKTKED EFGTLKGDII NEEGEDPKKR NILKSLRRTA KKTRPKPRPS IPKPLESNYF
GVPLVNVVFP DRPIPLFIDK CVHFIETTGL NTEGLYRVSG NKCEMESMQR QFDQDHGLDL
VEKDFAINTV AGALKAFFSE LPEPLVPCIL QVELLEAFR
//