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RASL3_BOVIN
ID   RASL3_BOVIN             Reviewed;        1012 AA.
AC   A6QQ91;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=RAS protein activator like-3;
GN   Name=RASAL3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions as a Ras GTPase-activating protein. Plays an
CC       important role in the expansion and functions of natural killer T (NKT)
CC       cells in the liver by negatively regulating RAS activity and the down-
CC       stream ERK signaling pathway. {ECO:0000250|UniProtKB:Q8C2K5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86YV0}.
CC       Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q86YV0}.
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DR   EMBL; BC149708; AAI49709.1; -; mRNA.
DR   RefSeq; NP_001095706.1; NM_001102236.2.
DR   AlphaFoldDB; A6QQ91; -.
DR   SMR; A6QQ91; -.
DR   STRING; 9913.ENSBTAP00000015416; -.
DR   PaxDb; A6QQ91; -.
DR   PRIDE; A6QQ91; -.
DR   Ensembl; ENSBTAT00000015416; ENSBTAP00000015416; ENSBTAG00000011602.
DR   GeneID; 540027; -.
DR   KEGG; bta:540027; -.
DR   CTD; 64926; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011602; -.
DR   VGNC; VGNC:33739; RASAL3.
DR   eggNOG; KOG3508; Eukaryota.
DR   GeneTree; ENSGT00940000161423; -.
DR   HOGENOM; CLU_009167_0_0_1; -.
DR   InParanoid; A6QQ91; -.
DR   OMA; WGRHKSP; -.
DR   OrthoDB; 69536at2759; -.
DR   TreeFam; TF105303; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000011602; Expressed in mesenteric lymph node and 95 other tissues.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0098562; C:cytoplasmic side of membrane; IEA:Ensembl.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0051142; P:positive regulation of NK T cell proliferation; ISS:UniProtKB.
DR   GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.506.10; -; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR039360; Ras_GTPase.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR001936; RasGAP_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   PANTHER; PTHR10194; PTHR10194; 1.
DR   Pfam; PF00616; RasGAP; 2.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; GTPase activation; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1012
FT                   /note="RAS protein activator like-3"
FT                   /id="PRO_0000322565"
FT   DOMAIN          193..294
FT                   /note="PH"
FT   DOMAIN          285..405
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          459..651
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT   REGION          1..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          990..1012
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          889..989
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YV0"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YV0"
FT   MOD_RES         160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YV0"
FT   MOD_RES         162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C2K5"
FT   MOD_RES         163
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YV0"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C2K5"
FT   MOD_RES         212
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C2K5"
FT   MOD_RES         225
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C2K5"
FT   MOD_RES         229
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C2K5"
FT   MOD_RES         232
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YV0"
FT   MOD_RES         235
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C2K5"
FT   MOD_RES         788
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C2K5"
FT   MOD_RES         791
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C2K5"
SQ   SEQUENCE   1012 AA;  110755 MW;  D9D0A8F97EBCF271 CRC64;
     MDPPSPSRAS QTQPVAPSPL TSYRWHSGGG AEKGAGGFRW GRLAGWGRAQ SHQETTASSQ
     PAPRSLFRRV LSAPPKESRT SRLKISKSLW GKNKSPPLDS EPEPENPEPE PELEPLATQI
     PEAPTPDVPV WNIEAFTLLD GKLVLLGNED EGPRQPRMGS ASSESSIHVA SGNLKDPDRT
     PGKTDPEAAG PHQIHNVRGL LKRLKEKKKA KSELGASASR DGPPSALGSR ESLATISELD
     LGAERDVRVW PLHPSLLEEP HCFQVTWAGG SRCFSCRSAA ERDRWIEDLR RHFQPSQDNV
     EREETWLSVW VHEVKGLPRA AAAAPGVRTE LWLDGALLAR TTPRAGPGQL FWAERFHFEA
     LPPARRLSLR LRGAGPGDAV LGRVALALEE LGIPRAPAAG LERWFPLLGA PAGAALRARI
     RARRLRVLPS ERYKELAEFL TFHYARLCGA LELALSAQAK EELAAAMVRV LRATGRAQAL
     VTDLGTAELA RSGGREALLF RENTLATKAI DEYMKLVAQD YLQETLGQVV RRLCASTEDC
     EVDPSKCPAS DLPQHQSRLR NSCKEVFENI IHSYNWFPAE LGTVFSGWRE ACKARGSEAL
     GPRLVCASLF LRLLCPAILS PSLFGLALEH PAPGPARTLT LIAKVIQNLA NRAPFGEKEA
     YMSFMNTFLE DHGPAMQHFL DQVATVDADT APSGYQGSSD LALQLAVLHA QLCTIFAELD
     QATRDNLEPL PTILHAIEEG RPVPVTVPMC LPAPRTQGHS SISAGEKPGF LAPRDLPKHT
     PLISKSQSLR SVHGAGSWAR PRLEEEQPPR LPRPVKRTQS VPAGRPARRR PSAGPRPRPK
     GSLHAGPAPR GRPWTGASAS LPRKPSVPWQ RQMDQPRDKD QALGTHRPVG KLAELQCEVA
     ALRQDLKMLS GLVESLSTHI RSLSEQQEQL RTQLQLLDSR LREGTAKLDP GRDRSTNEGH
     RLKSLECRLA EIESTQAQLK DTIQNLQLLP RTSESQSQPV PLKAPCINGD TT
 
 
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