ID A0A2U3XEB6_LEPWE Unreviewed; 574 AA.
AC A0A2U3XEB6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Lengsin {ECO:0000256|ARBA:ARBA00039404};
DE AltName: Full=Glutamate-ammonia ligase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00042675};
GN Name=LGSN {ECO:0000313|RefSeq:XP_006729678.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006729678.1};
RN [1] {ECO:0000313|RefSeq:XP_006729678.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006729678.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00037583}.
CC -!- SUBUNIT: Dodecamer. Interacts with BFSP2 and VIM.
CC {ECO:0000256|ARBA:ARBA00038790}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330,
CC ECO:0000256|RuleBase:RU000384}.
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DR RefSeq; XP_006729678.1; XM_006729615.1.
DR AlphaFoldDB; A0A2U3XEB6; -.
DR STRING; 9713.A0A2U3XEB6; -.
DR GeneID; 102741342; -.
DR KEGG; lww:102741342; -.
DR CTD; 51557; -.
DR OrthoDB; 344272at2759; -.
DR Proteomes; UP000245341; Unplaced.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR008147; Gln_synt_N.
DR InterPro; IPR036651; Gln_synt_N_sf.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR PANTHER; PTHR43407; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR43407:SF1; LENGSIN; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000245341}.
FT DOMAIN 148..242
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 249..574
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 64001 MW; 23C18B807E1BE593 CRC64;
MNDEGDLLQE DTRDEGNETE ASRMSKLRRT RKKVTKQHVF STEVGETDMS NSKERIRNQM
VCHKLGDVNK PVVGPGSADS HLQQDDKDSE NQTTVIKPSP LQTSASAPCR EFNTNSNHTD
NTRDGTQIPT TPYLSSRMKH IKQEMSKNHL QFVRFEATDL HGVSRSKSIP AQFFQEKVIH
GVCMPRGYLE LIPNPKDEEV DHIRATCFNS DIVLMPELST FRVLPWAERT ARVICDTFTV
TGEPLLTSPR YIAKSQLSQL QDSGFSLLSA FIYDFCIFAV PEIINSKTIS FPASTLLNNH
DQPFIQELVD GLYHTGANVE SFSSSTRPGQ MEICFLPEFG INAADNAFTL RTGVKEVARK
YNYIASFFIE TGFCNSGILS HSLWDVGGKK NMFCINSGVE ELTITGKKWL AGLLKHSAAL
SCLMAPAVSC RKRYSKESKD LKDSVPTTWG YNDNSCAFNI KCHGEKGTRI ENKLGSATAN
PYLVLAATVA AGLDGLQSSD GVLAGPDGST DFYQAKSSEI PLKLEDALVA LEEDQCLRQA
LGETFIRYFV AMKKYELENE ETDAERNKFL EYFI
//
