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-MAY-2013, entry version 78.
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).
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 (By similarity).
CC -!- COFACTOR: Magnesium or manganese (By similarity).
CC -!- SUBUNIT: Homooctamer and homotetramer. Interacts with PALMD (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Mitochondrion (By
CC similarity).
CC -!- PTM: Ubiquitinated by ZNRF1 (By similarity).
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
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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 OrthoDB; EOG444KKD; -.
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:EC.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA: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; Gln_synt_beta; 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 (By similarity).
FT CHAIN 2 373 Glutamine synthetase.
FT /FTId=PRO_0000153142.
FT MOD_RES 2 2 N-acetylalanine (By similarity).
FT MOD_RES 104 104 Phosphotyrosine (By similarity).
FT MOD_RES 180 180 Phosphotyrosine (By similarity).
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
//
