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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
 
 
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