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IIGP5_RAT
ID   IIGP5_RAT               Reviewed;         463 AA.
AC   Q6AYF9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Interferon-inducible GTPase 5;
DE            EC=3.6.5.-;
DE   AltName: Full=Immunity-related GTPase cinema 1;
GN   Name=Irgc; Synonyms=Iigp5, Irgc1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246 AND SER-303, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. IRG family. {ECO:0000255|PROSITE-ProRule:PRU01053,
CC       ECO:0000305}.
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DR   EMBL; BC079034; AAH79034.1; -; mRNA.
DR   EMBL; BC079061; AAH79061.1; -; mRNA.
DR   RefSeq; NP_001014038.1; NM_001014016.1.
DR   RefSeq; XP_006228487.1; XM_006228425.3.
DR   RefSeq; XP_006228488.1; XM_006228426.3.
DR   RefSeq; XP_006228489.1; XM_006228427.3.
DR   RefSeq; XP_008757149.1; XM_008758927.2.
DR   AlphaFoldDB; Q6AYF9; -.
DR   SMR; Q6AYF9; -.
DR   STRING; 10116.ENSRNOP00000030295; -.
DR   CarbonylDB; Q6AYF9; -.
DR   iPTMnet; Q6AYF9; -.
DR   PhosphoSitePlus; Q6AYF9; -.
DR   PaxDb; Q6AYF9; -.
DR   PRIDE; Q6AYF9; -.
DR   Ensembl; ENSRNOT00000030900; ENSRNOP00000030295; ENSRNOG00000024257.
DR   Ensembl; ENSRNOT00000103829; ENSRNOP00000083551; ENSRNOG00000024257.
DR   Ensembl; ENSRNOT00000105042; ENSRNOP00000087872; ENSRNOG00000024257.
DR   Ensembl; ENSRNOT00000115582; ENSRNOP00000090201; ENSRNOG00000024257.
DR   Ensembl; ENSRNOT00000119560; ENSRNOP00000092074; ENSRNOG00000024257.
DR   Ensembl; ENSRNOT00000119898; ENSRNOP00000095705; ENSRNOG00000024257.
DR   GeneID; 308428; -.
DR   KEGG; rno:308428; -.
DR   UCSC; RGD:1311107; rat.
DR   CTD; 56269; -.
DR   RGD; 1311107; Irgc.
DR   eggNOG; ENOG502QS9R; Eukaryota.
DR   GeneTree; ENSGT00950000183007; -.
DR   HOGENOM; CLU_015342_2_0_1; -.
DR   InParanoid; Q6AYF9; -.
DR   OMA; QEIREHC; -.
DR   OrthoDB; 688334at2759; -.
DR   PhylomeDB; Q6AYF9; -.
DR   TreeFam; TF331897; -.
DR   PRO; PR:Q6AYF9; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000024257; Expressed in testis and 3 other tissues.
DR   ExpressionAtlas; Q6AYF9; baseline.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0035458; P:cellular response to interferon-beta; IBA:GO_Central.
DR   GO; GO:0006952; P:defense response; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR030385; G_IRG_dom.
DR   InterPro; IPR007743; Immunity-related_GTPase-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF05049; IIGP; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51716; G_IRG; 1.
PE   1: Evidence at protein level;
KW   GTP-binding; Hydrolase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..463
FT                   /note="Interferon-inducible GTPase 5"
FT                   /id="PRO_0000285267"
FT   DOMAIN          52..234
FT                   /note="IRG-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01053"
FT   REGION          409..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         61..68
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         86..90
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         168..170
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         215..217
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         246
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         303
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   463 AA;  50556 MW;  E1B59CDC966A2578 CRC64;
     MATSRLPAVP EEETTILMAK EELEALRTAF ESGDIPQAAS RLRELLATTE TTRLEVGVTG
     ESGAGKSSLI NALRGVGAED PGAALTGVVE TTMQPSPYPH PQFPDVTLWD LPGAGSPGCS
     ADKYLKEVDF GRYDFFLLVS PRRCGAVETR LASEILRQGK KFYFVRTKVD EDLAATRNQR
     PSGFSEAAVL QEIRDHCAER LRAAGLSDPR IFLVSNLSPN RYDFPMLVTT WEHDLPAHRR
     HAGLLSLPDI SLEALQKKKD MLQEQVLKTA LVSGVIQALP VPGLAAAYDD ALLIRSLRGY
     HRSFGLDDDS LAKLAEQVGK QAGDLRSVIR SPLANEVSPE TVLRLYSQSS DGAMRVARAF
     ERGIPVFGTL VAGGISFGTV YTMLQGCLNE MAEDAQRVRI KALEEDETQG EVSLEAAGDN
     AVEKRSSGEG TSEEAPLSTR RKLGLLLKYI LDSWKRRDLS EDK
 
 
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