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Database: UniProt
Entry: P46410
LinkDB: P46410
Original site: P46410 
ID   GLNA_PIG                Reviewed;         373 AA.
AC   P46410;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   01-OCT-2014, entry version 81.
DE   RecName: Full=Glutamine synthetase;
DE            Short=GS;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate decarboxylase;
DE            EC=4.1.1.15;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=GLUL; Synonyms=GLNS;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Johnstone R.W., Loveland B.E.;
RT   "The cloning and nucleotide sequence of porcine glutamine synthetase
RT   cDNA.";
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential for proliferation of fetal skin fibroblasts.
CC       This enzyme has 2 functions: it catalyzes the production of
CC       glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA),
CC       the latter in a pyridoxal phosphate-independent manner (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC       L-glutamine.
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC   -!- COFACTOR: Biotin. {ECO:0000250}.
CC   -!- COFACTOR: Magnesium or manganese. {ECO:0000250}.
CC   -!- SUBUNIT: Homooctamer and homotetramer. Interacts with PALMD (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion
CC       {ECO:0000250}.
CC   -!- PTM: Ubiquitinated by ZNRF1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; Z29636; CAA82747.1; -; mRNA.
DR   PIR; S41452; S41452.
DR   RefSeq; NP_999074.1; NM_213909.1.
DR   UniGene; Ssc.93760; -.
DR   ProteinModelPortal; P46410; -.
DR   SMR; P46410; 3-372.
DR   STRING; 9823.ENSSSCP00000016481; -.
DR   PaxDb; P46410; -.
DR   GeneID; 396944; -.
DR   KEGG; ssc:396944; -.
DR   CTD; 2752; -.
DR   eggNOG; COG0174; -.
DR   HOGENOM; HOG000061500; -.
DR   HOVERGEN; HBG005847; -.
DR   KO; K01915; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.10.20.70; -; 1.
DR   Gene3D; 3.30.590.10; -; 1.
DR   InterPro; IPR008147; Gln_synt_beta.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   InterPro; IPR027303; Gln_synth_gly_rich_site.
DR   InterPro; IPR027302; Gln_synth_N_conserv_site.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF03951; Gln-synt_N; 1.
DR   SUPFAM; SSF54368; SSF54368; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Complete proteome; Cytoplasm; Ligase; Lyase;
KW   Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    373       Glutamine synthetase.
FT                                /FTId=PRO_0000153142.
FT   MOD_RES       2      2       N-acetylalanine. {ECO:0000250}.
FT   MOD_RES     104    104       Phosphotyrosine. {ECO:0000250}.
SQ   SEQUENCE   373 AA;  42030 MW;  FB0FD3414ACA7C55 CRC64;
     MATSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE PKCIEELPEW
     NFDGSSTFQS EGSNSDMYLV PAAMFRDPFR KDPNKLVFCE VFKYNRKPAE TNLRHTCKRI
     MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADKA YGRDIVEAHY
     RACLYAGIKI GGTNAEVMPA QWEFQIGPCE GIDMGDHLWV ARFILHRVCE DFGVIATFDP
     KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNTRRL
     TGFHETSNIN DFSAGVANRG ASIRIPRTGG QEKKGYFEDR RPSANCDPFA VTEALIRTCL
     LNETGDEPFQ YKN
//
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