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GLNA_BOVIN
ID   GLNA_BOVIN              Reviewed;         373 AA.
AC   P15103; O02850; Q3ZBU6; Q866Q7;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:9321487};
DE            Short=GS {ECO:0000303|PubMed:9321487};
DE            EC=6.3.1.2 {ECO:0000250|UniProtKB:P15104};
DE   AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE   AltName: Full=Palmitoyltransferase GLUL {ECO:0000305};
DE            EC=2.3.1.225 {ECO:0000250|UniProtKB:P15104};
GN   Name=GLUL {ECO:0000303|PubMed:9321487};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-267.
RX   PubMed=9321487; DOI=10.1007/s003359900577;
RA   Masabanda J., Wigger G., Eggen A., Stranzinger G., Fries R.;
RT   "The bovine glutamine synthase gene (GLUL) maps to 10q33 and a pseudogene
RT   (GLULP) to 16q21.";
RL   Mamm. Genome 8:794-795(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 258-352.
RC   TISSUE=Kidney;
RA   Matthews J.C., Etienne N.M.P.;
RT   "The pattern of EAAC1 and GLT-1 glutamate transporter expression by
RT   skeletal and adipose tissues of fattening cattle differs from that of
RT   glutamine synthetase.";
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 267-373.
RC   TISSUE=Liver;
RX   PubMed=2893372; DOI=10.1073/pnas.85.1.160;
RA   Smith D.D. Jr., Campbell J.W.;
RT   "Distribution of glutamine synthetase and carbamoyl-phosphate synthetase I
RT   in vertebrate liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:160-164(1988).
CC   -!- FUNCTION: Glutamine synthetase that catalyzes the ATP-dependent
CC       conversion of glutamate and ammonia to glutamine (By similarity). Its
CC       role depends on tissue localization: in the brain, it regulates the
CC       levels of toxic ammonia and converts neurotoxic glutamate to harmless
CC       glutamine, whereas in the liver, it is one of the enzymes responsible
CC       for the removal of ammonia (By similarity). Essential for proliferation
CC       of fetal skin fibroblasts. Independently of its glutamine synthetase
CC       activity, required for endothelial cell migration during vascular
CC       development: acts by regulating membrane localization and activation of
CC       the GTPase RHOJ, possibly by promoting RHOJ palmitoylation. May act as
CC       a palmitoyltransferase for RHOJ: able to autopalmitoylate and then
CC       transfer the palmitoyl group to RHOJ (By similarity). Plays a role in
CC       ribosomal 40S subunit biogenesis (By similarity).
CC       {ECO:0000250|UniProtKB:P15104, ECO:0000250|UniProtKB:P15105}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC         phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC         Evidence={ECO:0000250|UniProtKB:P15104};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC         hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC         COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC         EC=2.3.1.225; Evidence={ECO:0000250|UniProtKB:P15104};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P09606};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P15104};
CC   -!- ACTIVITY REGULATION: Glutamine synthetase activity is inhibited by
CC       methionine sulfoximine (MSO). {ECO:0000250|UniProtKB:P15104}.
CC   -!- SUBUNIT: Decamer; composed of two pentamers (By similarity). Interacts
CC       with PALMD (By similarity). Interacts with RHOJ (By similarity).
CC       {ECO:0000250|UniProtKB:P15104, ECO:0000250|UniProtKB:P15105}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P15104}. Microsome
CC       {ECO:0000250|UniProtKB:P09606}. Mitochondrion
CC       {ECO:0000250|UniProtKB:P09606}. Cell membrane
CC       {ECO:0000250|UniProtKB:P15104}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P15104}. Note=Mainly localizes in the cytosol,
CC       with a fraction associated with the cell membrane.
CC       {ECO:0000250|UniProtKB:P15104}.
CC   -!- PTM: Palmitoylated; undergoes autopalmitoylation.
CC       {ECO:0000250|UniProtKB:P15104}.
CC   -!- PTM: Ubiquitinated by ZNRF1. {ECO:0000250|UniProtKB:P15105}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; BC103099; AAI03100.1; -; mRNA.
DR   EMBL; Y10347; CAA71373.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY186585; AAO27470.1; -; mRNA.
DR   EMBL; J03604; AAA87357.1; -; mRNA.
DR   PIR; A34006; A34006.
DR   RefSeq; NP_001035564.1; NM_001040474.2.
DR   RefSeq; XP_005217320.1; XM_005217263.3.
DR   AlphaFoldDB; P15103; -.
DR   SMR; P15103; -.
DR   STRING; 9913.ENSBTAP00000038301; -.
DR   PaxDb; P15103; -.
DR   Ensembl; ENSBTAT00000038488; ENSBTAP00000038301; ENSBTAG00000013631.
DR   Ensembl; ENSBTAT00000074216; ENSBTAP00000057244; ENSBTAG00000013631.
DR   GeneID; 281199; -.
DR   KEGG; bta:281199; -.
DR   CTD; 2752; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013631; -.
DR   VGNC; VGNC:29426; GLUL.
DR   eggNOG; KOG0683; Eukaryota.
DR   GeneTree; ENSGT00390000010047; -.
DR   HOGENOM; CLU_036762_1_1_1; -.
DR   InParanoid; P15103; -.
DR   OMA; DRRPNAN; -.
DR   OrthoDB; 784869at2759; -.
DR   TreeFam; TF300491; -.
DR   Reactome; R-BTA-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
DR   Reactome; R-BTA-8964539; Glutamate and glutamine metabolism.
DR   Proteomes; UP000009136; Chromosome 16.
DR   Bgee; ENSBTAG00000013631; Expressed in prefrontal cortex and 104 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamate-ammonia ligase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0018345; P:protein palmitoylation; ISS:UniProtKB.
DR   GO; GO:0010594; P:regulation of endothelial cell migration; ISS:UniProtKB.
DR   GO; GO:1903670; P:regulation of sprouting angiogenesis; ISS:UniProtKB.
DR   Gene3D; 3.10.20.70; -; 1.
DR   InterPro; IPR008147; Gln_synt_b-grasp.
DR   InterPro; IPR036651; Gln_synt_N.
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   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF54368; SSF54368; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
DR   PROSITE; PS51986; GS_BETA_GRASP; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Angiogenesis; ATP-binding; Cell membrane; Cytoplasm;
KW   Endoplasmic reticulum; Ligase; Lipoprotein; Magnesium; Manganese; Membrane;
KW   Metal-binding; Microsome; Mitochondrion; Nucleotide-binding; Palmitate;
KW   Phosphoprotein; Reference proteome; Transferase; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P15105"
FT   CHAIN           2..373
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153136"
FT   DOMAIN          26..106
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          113..373
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   BINDING         134
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P15104"
FT   BINDING         134
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P15104"
FT   BINDING         136
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P15104"
FT   BINDING         196
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P15104"
FT   BINDING         203..208
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P15104"
FT   BINDING         203
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P15104"
FT   BINDING         246..247
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         253
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P15104"
FT   BINDING         255..257
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P15104"
FT   BINDING         319
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P15104"
FT   BINDING         319
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         324
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P15104"
FT   BINDING         336..338
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P15104"
FT   BINDING         338
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P15104"
FT   BINDING         340
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P15105"
FT   MOD_RES         104
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P15105"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P15104"
SQ   SEQUENCE   373 AA;  42031 MW;  BBCC6A953FD7DAD5 CRC64;
     MATSASSHLN KGIKQVYMAL PQGDKVQAMY IWIDGTGEGL RCKTRTLDSE PKCIEELPEW
     NFDGSSTFQS EGSNSDMYLV PAAMFRDPFR KDPNKLVFCE VFKYNRKPAE TNLRHTCKRI
     MDMVSNQRPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADKA YGRDIVEAHY
     RACLYAGIKI GGTNAEVMPA QWEFQIGPCE GIDMGDHLWV ARFILHRVCE DFGVIATFDP
     KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL
     TGFHETSNIN DFSAGVANRG ASIRIPRTVG QEKKGYFEDR RPSANCDPFA VTEALIRTCL
     LNETGDEPFQ YKN
 
 
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