TAGAP_MOUSE
ID TAGAP_MOUSE Reviewed; 714 AA.
AC B2RWW0; Q8K2L9; Q920D6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=T-cell activation Rho GTPase-activating protein;
DE AltName: Full=T-cell activation GTPase-activating protein;
GN Name=Tagap;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=16116428; DOI=10.1038/ng1617;
RA Bauer H., Willert J., Koschorz B., Herrmann B.G.;
RT "The t complex-encoded GTPase-activating protein Tagap1 acts as a
RT transmission ratio distorter in mice.";
RL Nat. Genet. 37:969-973(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May function as a GTPase-activating protein. May play a role
CC in transmission ratio distortion (TRD) in mouse, in which heterozygous
CC males for t-locus transmit their t-carrying chromosome to 95% or more
CC of their offspring. {ECO:0000269|PubMed:16116428}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC {ECO:0000269|PubMed:16116428}.
CC -!- DEVELOPMENTAL STAGE: Expressed in testis at 7 dpc.
CC {ECO:0000269|PubMed:16116428}.
CC -!- CAUTION: Previously thought to be the same gene as Tagap1. These are
CC distinct loci that encode proteins with identical C-termini but each
CC with a unique N-terminus. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC150728; AAI50729.1; -; mRNA.
DR EMBL; BC030886; AAH30886.1; -; mRNA.
DR EMBL; BC039780; AAH39780.1; -; mRNA.
DR CCDS; CCDS28379.1; -.
DR RefSeq; NP_666080.1; NM_145968.2.
DR AlphaFoldDB; B2RWW0; -.
DR SMR; B2RWW0; -.
DR BioGRID; 215423; 22.
DR IntAct; B2RWW0; 18.
DR STRING; 10090.ENSMUSP00000047431; -.
DR iPTMnet; B2RWW0; -.
DR PhosphoSitePlus; B2RWW0; -.
DR EPD; B2RWW0; -.
DR jPOST; B2RWW0; -.
DR PaxDb; B2RWW0; -.
DR PRIDE; B2RWW0; -.
DR ProteomicsDB; 262926; -.
DR DNASU; 72536; -.
DR Ensembl; ENSMUST00000036370; ENSMUSP00000047431; ENSMUSG00000033450.
DR GeneID; 72536; -.
DR KEGG; mmu:72536; -.
DR UCSC; uc008air.2; mouse.
DR CTD; 117289; -.
DR MGI; MGI:3615484; Tagap.
DR VEuPathDB; HostDB:ENSMUSG00000033450; -.
DR eggNOG; KOG4724; Eukaryota.
DR GeneTree; ENSGT00940000157993; -.
DR HOGENOM; CLU_014209_1_0_1; -.
DR InParanoid; B2RWW0; -.
DR OMA; HRDSKEP; -.
DR OrthoDB; 148399at2759; -.
DR PhylomeDB; B2RWW0; -.
DR TreeFam; TF331062; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 72536; 3 hits in 72 CRISPR screens.
DR PRO; PR:B2RWW0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; B2RWW0; protein.
DR Bgee; ENSMUSG00000033450; Expressed in granulocyte and 52 other tissues.
DR Genevisible; B2RWW0; MM.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 2: Evidence at transcript level;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome.
FT CHAIN 1..714
FT /note="T-cell activation Rho GTPase-activating protein"
FT /id="PRO_0000056720"
FT DOMAIN 88..277
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 290..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N103"
FT CONFLICT 345
FT /note="Q -> H (in Ref. 1; AAI50729)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="V -> M (in Ref. 1; AAI50729)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="A -> T (in Ref. 1; AAI50729)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="A -> V (in Ref. 1; AAI50729)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 714 AA; 78920 MW; 35925DE6885B4CAD CRC64;
MKLISSLDGS KTLNANNMET LIECQSEGDI KVPPLLTSCE SEDSICQLTE IKKRKKVLSW
PSLMRKLSPS SDFSGSLEPE LKVSLFDQPL SIICGENDTL PRPIQDILTI LCLKGPSTEG
IFRKAASEKA RKELKEGLNC GVSVNLKQLP VHLLAVVFKD FLRGIPLKLL SCDLFEDWMG
ALEKPTEEDR IEALKQVAGG LPRPNLLLLR HLLYVLHLIS KNAEVNKMDS SNLAICIGPN
MLTLKNDQSL SFQAQKDLNN KVKILVEFLI DNCFEIFGEN IRTRSRITSD DSLEHTDSSD
VSTLQNDSAY DSNDPDVEPT SGAASPNRQL EGPTPTMAGL DTRGQRDTCE SSSESSVSMV
VRLKSSIVQQ DRRFSEPNMS PSRECLVGPT SKQKLARSED SFTLSQDASC SEGDEAEDPF
TEEVFPAVDS KPKRPVDLKI KNWTQGLASP QGHITKAFSR SSPGESLGSS PVPSPSCPKR
NFFTRHQSFT TKTDKTKPQR EIRKHSMSFS FASHKKVLPR TSSIGSEKSK DFSRDQLQKD
LRKESQLSGR IVQENESEIQ SQTSLGFSLS GTWALSVDNT FQLVDMRKPG SPPSYEEAIY
YQTSGLTAYG GQTVGSMRSR MFKPSTAVPP VPSHHGGDLS EGTPGGHRLS SVTEHWTHSQ
TVHVSIETQG RSELHQLRTV SESMQKAKLD CLGPQHSHLV FEADQLCCAR ESYI
