LGSN_CANLF
ID LGSN_CANLF Reviewed; 574 AA.
AC Q1ZZS1;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Lengsin;
DE AltName: Full=Glutamate-ammonia ligase domain-containing protein 1;
GN Name=LGSN; Synonyms=GLULD1, LGS;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RA Wistow G.;
RL Submitted (FEB-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; DQ415892; ABD74632.1; -; mRNA.
DR RefSeq; NP_001041568.1; NM_001048103.1.
DR AlphaFoldDB; Q1ZZS1; -.
DR SMR; Q1ZZS1; -.
DR STRING; 9615.ENSCAFP00000062661; -.
DR PaxDb; Q1ZZS1; -.
DR PRIDE; Q1ZZS1; -.
DR Ensembl; ENSCAFT00845012846; ENSCAFP00845010011; ENSCAFG00845007217.
DR GeneID; 481862; -.
DR KEGG; cfa:481862; -.
DR CTD; 51557; -.
DR VEuPathDB; HostDB:ENSCAFG00845007217; -.
DR VGNC; VGNC:42656; LGSN.
DR eggNOG; KOG0683; Eukaryota.
DR GeneTree; ENSGT00390000013639; -.
DR InParanoid; Q1ZZS1; -.
DR OrthoDB; 1424442at2759; -.
DR Proteomes; UP000002254; Chromosome 12.
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..574
FT /note="Lengsin"
FT /id="PRO_0000365069"
FT DOMAIN 148..242
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 249..574
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 63955 MW; 89144B70B9596CAC CRC64;
MNDEGDLLQE NTRDEGNETE ASRMSKLRRT RKKVTKQHIF STEVGEMDVS NSKERIRSQM
VCHTLGNMSK PVVGPGSADS HLPQDDKDSE NQTTVIKPSP LKTSASAPCS EFNTNSNHAD
NTWEDTQIPT TPHLSSRMKH IKQEMAKNHL QFVRFEATDL HGVSRSKSIP AHFFQEKVIH
GVCMPRGYLE LIPNPKDDEV DHIRATCFNS DIVLMPELST FRVLPWAERT ARVICDTFTV
TGEPLLTSPR YIAKRQLSQL QDSGFSLLSA FIYDFCIFAV PEIINSKTIS FPASTLLNNH
DQPFIQELVD GLYHTGANVE SFSSSTRPGQ MEICFLPEFG ISSADNAFTL RTGVKEVARK
YNYIASFFIE TGFCNSGILS HSLWDVDGKK NMFCSSSGIE ELTITGKKWL AGLLKHSAAL
SCLMAPAVSC RKRYSKESKD LKESVPTTWG YNDNSCAFNI KCHGEKGTRI ENKLGSATAN
PYLVLAATVA AGLDGLQSSD GVLASPGDST DLYPSKPSEI PLKLEDALVA LEEDQCLRQA
LGETFIRYFV AMKKYDLENE ETDAERNKFL EYFI
