LGSN_RABIT
ID LGSN_RABIT Reviewed; 571 AA.
AC Q0GA40;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Lengsin;
DE AltName: Full=Glutamate-ammonia ligase domain-containing protein 1;
GN Name=LGSN; Synonyms=GLULD1, LGS;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RA Wistow G.;
RT "Rabbit lengsin.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Dodecamer. Interacts with BFSP2 AND VIM. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; DQ885946; ABI35898.1; -; mRNA.
DR RefSeq; NP_001075696.1; NM_001082227.1.
DR AlphaFoldDB; Q0GA40; -.
DR SMR; Q0GA40; -.
DR STRING; 9986.ENSOCUP00000018240; -.
DR GeneID; 100009041; -.
DR KEGG; ocu:100009041; -.
DR CTD; 51557; -.
DR eggNOG; KOG0683; Eukaryota.
DR InParanoid; Q0GA40; -.
DR OrthoDB; 1424442at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic 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 2: Evidence at transcript level;
KW Reference proteome.
FT CHAIN 1..571
FT /note="Lengsin"
FT /id="PRO_0000365070"
FT DOMAIN 145..239
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 246..571
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT REGION 1..129
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 46..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 571 AA; 63751 MW; E399E7F63466BAA5 CRC64;
MNDEGDLLQE DTARDEVNET EASRMSKLRK TRKKVTKPHD YSTEVGEMDI SNSNERIRSQ
MLCHQLGDTS KPVAGPSSSE TRVSQDDKDS PDQTMVMKPL PPQTASVPSG EHNTNSDCTR
DSTQILTPPQ LSSRMKHIKQ EMAKNHLQFV QFEASDLHGV SRSKSIPAHF FQEKVIHGVF
MPRGYLELIP NPKDNEVNHI RATCFNNDIV LMPELSTFRV LPWAERTARV ICDTFTVTGE
PLLTSPRYIA KRQLNQLQDC GFSLLSAFIY DFCIFGVPEI INSKTISFAA STLVNNHDQP
FMQELVDGLY HTGASVESFS SSTRPGQMEI CFLPEFGISS ADNAFTLRTG VKEVARKYNY
IASFFIETGF CNSGILSHSL WDVDGKKNMF CNSSGVEQLT IIGKKWLAGL LKHSAALSCL
MAPAVSCRKR YSKETKDLKE SVPTTWGYND NSCAFNIKCH GDKGARIENK LGSATANPYL
VLAATVAAGL DGLQSNLDDL AGPDDSTDLF QSEPSEIPLK LEDALVALEE DECLREALGE
TFIRYFVAMK KYELENEETD AERNKFLEYF I