GNL1_RAT
ID GNL1_RAT Reviewed; 607 AA.
AC Q6MG06;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Guanine nucleotide-binding protein-like 1;
GN Name=Gnl1;
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48; THR-50; SER-51 AND
RP SER-324, AND 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 -!- FUNCTION: Possible regulatory or functional link with the
CC histocompatibility cluster. {ECO:0000250}.
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs described
CC by a G4-G1-G3 pattern.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; BX883048; CAE84041.1; -; Genomic_DNA.
DR EMBL; BC129081; AAI29082.1; -; mRNA.
DR RefSeq; NP_997665.1; NM_212500.3.
DR AlphaFoldDB; Q6MG06; -.
DR IntAct; Q6MG06; 1.
DR STRING; 10116.ENSRNOP00000045697; -.
DR iPTMnet; Q6MG06; -.
DR PhosphoSitePlus; Q6MG06; -.
DR jPOST; Q6MG06; -.
DR PaxDb; Q6MG06; -.
DR PRIDE; Q6MG06; -.
DR GeneID; 309593; -.
DR KEGG; rno:309593; -.
DR UCSC; RGD:1303051; rat.
DR CTD; 2794; -.
DR RGD; 1303051; Gnl1.
DR VEuPathDB; HostDB:ENSRNOG00000000798; -.
DR eggNOG; KOG1424; Eukaryota.
DR InParanoid; Q6MG06; -.
DR OMA; CDFPVRP; -.
DR OrthoDB; 839833at2759; -.
DR PhylomeDB; Q6MG06; -.
DR TreeFam; TF324569; -.
DR PRO; PR:Q6MG06; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000798; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; Q6MG06; baseline and differential.
DR Genevisible; Q6MG06; RN.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR043358; GNL1-like.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45709; PTHR45709; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..607
FT /note="Guanine nucleotide-binding protein-like 1"
FT /id="PRO_0000295691"
FT DOMAIN 178..418
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..584
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 225..228
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 367..374
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 411..415
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
SQ SEQUENCE 607 AA; 68707 MW; B384481372E3F92D CRC64;
MPRKKPFSVK QKKKQLQDKR ERKRGLQDGL RSSSNSRSGS RERREEQTDT SDGESVTHHI
RRLNQQPSQG LGPRGYDPNR YRLHFERDSR EEVERRKRAA REQVLQPVSA EMLELDIQEV
YQPGSVLDFP RRPPWSYEMS KEQLMSQEER SFQEYLGKIH GAYTSEKLSY FEHNLETWRQ
LWRVLEMSDI VLLITDIRHP VVNFPPALYE YVTGELGLAL VLVLNKVDLA PPALVVAWKH
YFHQHYPQLH IVLFTSFPRD TRTPQEPGSV LKKSRRRGRG WTRALGPEQL LRACEAITVG
KVDLSSWREK IARDVAGASW GNVSGEEEEE EDGPAVLVEQ QTDSAMEPTG PSRERYKDGV
VTIGCVGFPN VGKSSLINGL VGRKVVSVSR TPGHTRYFQT YFLTPSVKLC DCPGLIFPSL
LPRQLQVLAG IYPIAQIQEP YTSVGYLACR IPVQALLHLR HPEAEDPSAE HPWCAWDVCE
AWAEKRGYKT AKAARNDVYR AANSLLRLAV DGRLSLCFHP PGYSEQRGTW ESHAETAELV
LSQGRVGPAG DEEEEEEEEL SSSCEEEGEE DRDADEEGEG DEDTPTSDTG SCLAARNPYA
LLGEGEC
