LGSN_MOUSE
ID LGSN_MOUSE Reviewed; 563 AA.
AC Q8CIX8; Q149K1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Lengsin;
DE AltName: Full=Glutamate-ammonia ligase domain-containing protein 1;
DE AltName: Full=Lens glutamine synthase-like;
GN Name=Lgsn; Synonyms=Gluld1, Lgs;
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].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RA Wistow G., Wyatt K.;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 INTERACTION WITH BFSP2 AND VIM, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18178558; DOI=10.1074/jbc.m709144200;
RA Wyatt K., Gao C., Tsai J.-Y., Fariss R.N., Ray S., Wistow G.;
RT "A role for lengsin, a recruited enzyme, in terminal differentiation in the
RT vertebrate lens.";
RL J. Biol. Chem. 283:6607-6615(2008).
RN [4]
RP STRUCTURE BY ELECTRON MICROSCOPY (17.0 ANGSTROMS) OF 141-563, AND SUBUNIT.
RX PubMed=17161372; DOI=10.1016/j.str.2006.10.008;
RA Wyatt K., White H.E., Wang L., Bateman O.A., Slingsby C., Orlova E.V.,
RA Wistow G.;
RT "Lengsin is a survivor of an ancient family of class I glutamine
RT synthetases re-engineered by evolution for a role in the vertebrate lens.";
RL Structure 14:1823-1834(2006).
CC -!- FUNCTION: May act as a component of the cytoskeleton or as a chaperone
CC for the reorganization of intermediate filament proteins during
CC terminal differentiation in the lens. Does not seem to have enzymatic
CC activity. {ECO:0000269|PubMed:18178558}.
CC -!- SUBUNIT: Dodecamer. Interacts with BFSP2 AND VIM.
CC {ECO:0000269|PubMed:17161372, ECO:0000269|PubMed:18178558}.
CC -!- TISSUE SPECIFICITY: Expressed in lens. {ECO:0000269|PubMed:18178558}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; AF545851; AAN38298.1; -; mRNA.
DR EMBL; BC117745; AAI17746.1; -; mRNA.
DR EMBL; BC117746; AAI17747.1; -; mRNA.
DR EMBL; BC128067; AAI28068.1; -; mRNA.
DR CCDS; CCDS14859.1; -.
DR RefSeq; NP_705829.1; NM_153601.1.
DR PDB; 2J9I; EM; 17.00 A; A/B/C/D/E/F/G/H/I/J/K/L=141-563.
DR PDBsum; 2J9I; -.
DR AlphaFoldDB; Q8CIX8; -.
DR SMR; Q8CIX8; -.
DR DIP; DIP-29169N; -.
DR STRING; 10090.ENSMUSP00000059871; -.
DR PhosphoSitePlus; Q8CIX8; -.
DR MaxQB; Q8CIX8; -.
DR PaxDb; Q8CIX8; -.
DR PRIDE; Q8CIX8; -.
DR ProteomicsDB; 290025; -.
DR Antibodypedia; 49358; 34 antibodies from 14 providers.
DR DNASU; 266744; -.
DR Ensembl; ENSMUST00000062560; ENSMUSP00000059871; ENSMUSG00000050217.
DR GeneID; 266744; -.
DR KEGG; mmu:266744; -.
DR UCSC; uc007ank.1; mouse.
DR CTD; 51557; -.
DR MGI; MGI:2672844; Lgsn.
DR VEuPathDB; HostDB:ENSMUSG00000050217; -.
DR eggNOG; KOG0683; Eukaryota.
DR GeneTree; ENSGT00390000013639; -.
DR HOGENOM; CLU_017290_0_2_1; -.
DR InParanoid; Q8CIX8; -.
DR OMA; TFYTHPE; -.
DR OrthoDB; 1424442at2759; -.
DR PhylomeDB; Q8CIX8; -.
DR TreeFam; TF331605; -.
DR BioGRID-ORCS; 266744; 4 hits in 73 CRISPR screens.
DR EvolutionaryTrace; Q8CIX8; -.
DR PRO; PR:Q8CIX8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8CIX8; protein.
DR Bgee; ENSMUSG00000050217; Expressed in lens of camera-type eye and 3 other tissues.
DR ExpressionAtlas; Q8CIX8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.10.20.70; -; 1.
DR InterPro; IPR036651; Gln_synt_N.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR Pfam; PF00120; Gln-synt_C; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..563
FT /note="Lengsin"
FT /id="PRO_0000153283"
FT DOMAIN 137..231
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 238..563
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 62164 MW; BAA6409CE90345AA CRC64;
MTDEGDLAQE DTAKDEGNVT EGSRMSKLRR ARRKVTKPHL CSMDGEEIAK ANSSEMSRNQ
IADLSKPGSA ESWSSHSAKD AYHPTPVVKP SLPSALAGAP DAEFSPNTDP TRYNAQSFNP
PQLSARMKHI KQEMAKNHLQ FVRFEATDLH GVSRSKSIPA QFFQEKVIHG VFMPRGYLEL
MPNPKDNEVN HIRATCFNSD IVLMPELSTF RVLPWAERTA RVICDTFTVT GEPLLTSPRY
IAKRQLRQLQ DAGFCLLSAF IYDFCIFGVP EVINSKTISF PASTLLSNHD QPFMQELVEG
LYQTGANVES FSSSTRPGQM EICFLPEFGI SSADNAFTLR TGLQEVARRY NYIASLVIET
GFCNSGILSH SIWDVGGKTN MFCSGSGVER LTLTGKKWLA GLLKHSAALS CLMAPAVNCR
KRYCKDSRDL KDSVPTTWGY NDNSCALNIK CHGEKGTQIE NKLGSATANP YLVLAATVAA
GLDGLQSSDG AAAGSDESQD LYQPEPSEIP LKMEDALAAL EQDECLKQAL GETFIRYFVA
MKKYELENEE TDAEGNKFLE YFI
