GNL1_MOUSE
ID GNL1_MOUSE Reviewed; 607 AA.
AC P36916; E9QPZ9; Q91Z20;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Guanine nucleotide-binding protein-like 1;
DE AltName: Full=GTP-binding protein MMR1;
GN Name=Gnl1; Synonyms=Gna-rs1, Mmr1;
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] (ISOFORM 2).
RX PubMed=1478666; DOI=10.1016/s0888-7543(05)80105-3;
RA Denizot F., Mattei M.-G., Vernet C., Pontarotti P., Chimini G.;
RT "YAC-assisted cloning of a putative G-protein mapping to the MHC class I
RT region.";
RL Genomics 14:857-862(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=129; TISSUE=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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-324, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Possible regulatory or functional link with the
CC histocompatibility cluster. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P36916-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P36916-2; Sequence=VSP_026994, VSP_026995;
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; X65026; CAA46160.1; -; mRNA.
DR EMBL; AC112970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010298; AAH10298.1; -; mRNA.
DR CCDS; CCDS37606.1; -. [P36916-1]
DR RefSeq; NP_032162.2; NM_008136.2. [P36916-1]
DR AlphaFoldDB; P36916; -.
DR BioGRID; 199960; 5.
DR IntAct; P36916; 2.
DR MINT; P36916; -.
DR STRING; 10090.ENSMUSP00000084450; -.
DR iPTMnet; P36916; -.
DR PhosphoSitePlus; P36916; -.
DR SwissPalm; P36916; -.
DR EPD; P36916; -.
DR jPOST; P36916; -.
DR MaxQB; P36916; -.
DR PaxDb; P36916; -.
DR PeptideAtlas; P36916; -.
DR PRIDE; P36916; -.
DR ProteomicsDB; 267642; -. [P36916-1]
DR ProteomicsDB; 267643; -. [P36916-2]
DR Antibodypedia; 26307; 253 antibodies from 30 providers.
DR DNASU; 14670; -.
DR Ensembl; ENSMUST00000087200; ENSMUSP00000084450; ENSMUSG00000024429. [P36916-1]
DR GeneID; 14670; -.
DR KEGG; mmu:14670; -.
DR UCSC; uc008cjo.1; mouse. [P36916-1]
DR CTD; 2794; -.
DR MGI; MGI:95764; Gnl1.
DR VEuPathDB; HostDB:ENSMUSG00000024429; -.
DR eggNOG; KOG1424; Eukaryota.
DR GeneTree; ENSGT00940000158047; -.
DR HOGENOM; CLU_013649_1_1_1; -.
DR InParanoid; P36916; -.
DR OMA; CDFPVRP; -.
DR PhylomeDB; P36916; -.
DR TreeFam; TF324569; -.
DR BioGRID-ORCS; 14670; 14 hits in 76 CRISPR screens.
DR ChiTaRS; Gnl1; mouse.
DR PRO; PR:P36916; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P36916; protein.
DR Bgee; ENSMUSG00000024429; Expressed in superior frontal gyrus and 232 other tissues.
DR Genevisible; P36916; MM.
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:MGI.
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 Alternative splicing; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..607
FT /note="Guanine nucleotide-binding protein-like 1"
FT /id="PRO_0000122442"
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:0007744|PubMed:21183079"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36915"
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:21183079"
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"
FT VAR_SEQ 1..177
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1478666"
FT /id="VSP_026994"
FT VAR_SEQ 178..183
FT /note="WRQLWR -> MEAAVA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1478666"
FT /id="VSP_026995"
FT CONFLICT 245
FT /note="C -> R (in Ref. 1; CAA46160 and 3; AAH10298)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="K -> Q (in Ref. 1; CAA46160)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="A -> R (in Ref. 1; CAA46160)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 68771 MW; 10D417265D727082 CRC64;
MPRKKPFSVK QKKKQLQDKR ERKRGLQDGL RSSSNSRSGS RERREEQTDT SDGESVTHHI
RRLNQQPSQG LGPRGYDPNR YRLHFERDSR EEVERRKRAA REQVLQPVSA EVLELDIREV
YQPGSVLDFP RRPPWSYEMS KEQLMSQEER SFQEYLGKIH GAYTSEKLSY FEHNLETWRQ
LWRVLEMSDI VLLITDIRHP VVNFPPALYE YVTGELGLAL VLVLNKVDLA PPALVVAWKH
YFHQCYPQLH IVLFTSFPRD TRTPQEPGGV LKKNRRRGKG WTRALGPEQL LRACEAITVG
KVDLSSWREK IARDVAGASW GNVSGEEEEE EDGPAVLVEQ LTDSAMEPTG PSRERYKDGV
VTIGCIGFPN VGKSSLINGL VGRKVVSVSR TPGHTRYFQT YFLTPSVKLC DCPGLIFPSL
LPRQLQVLAG IYPIAQIQEP YTSVGYLASR IPVQALLHLR HPEAEDPSAE HPWCAWDICE
AWAEKRGYKT AKAARNDVYR AANSLLRLAV DGRLSLCFYP PGYSEQRGTW ESHPETAELV
LSQGRVGPAG DEEEEEEEEL SSSCEEEGEE DRDADEEGEG DEDTPTSDPG SCLTARNPYA
LLGEDEC
