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Q8HZM5

- GLNA_CANFA

UniProt

Q8HZM5 - GLNA_CANFA

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Protein

Glutamine synthetase

Gene

GLUL

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Essential for proliferation of fetal skin fibroblasts. This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner (By similarity).By similarity

Catalytic activityi

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.
L-glutamate = 4-aminobutanoate + CO2.

Cofactori

Protein has several cofactor binding sites:
  • biotinBy similarityNote: Biotin.By similarity
  • Mg2+By similarity, Mn2+By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate-ammonia ligase activity Source: UniProtKB-EC
  3. glutamate decarboxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. glutamine biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Lyase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_254787. Amino acid synthesis and interconversion (transamination).
REACT_260379. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
SABIO-RKQ8HZM5.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase (EC:6.3.1.2)
Short name:
GS
Alternative name(s):
Glutamate decarboxylase (EC:4.1.1.15)
Glutamate--ammonia ligase
Gene namesi
Name:GLUL
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Chromosome 7

Subcellular locationi

Cytoplasm By similarity. Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 373372Glutamine synthetasePRO_0000153137Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei104 – 1041PhosphotyrosineBy similarity

Post-translational modificationi

Ubiquitinated by ZNRF1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ8HZM5.

Interactioni

Subunit structurei

Homooctamer and homotetramer. Interacts with PALMD (By similarity).By similarity

Structurei

Secondary structure

1
373
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Helixi11 – 188Combined sources
Beta strandi26 – 338Combined sources
Beta strandi40 – 4910Combined sources
Helixi54 – 563Combined sources
Beta strandi60 – 634Combined sources
Helixi64 – 674Combined sources
Beta strandi76 – 8611Combined sources
Turni88 – 903Combined sources
Beta strandi95 – 1028Combined sources
Helixi114 – 1229Combined sources
Helixi123 – 1275Combined sources
Beta strandi130 – 14011Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi158 – 1603Combined sources
Turni167 – 1693Combined sources
Helixi173 – 18614Combined sources
Beta strandi190 – 1956Combined sources
Beta strandi201 – 21010Combined sources
Helixi213 – 23220Combined sources
Beta strandi235 – 2373Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi251 – 2577Combined sources
Helixi259 – 2624Combined sources
Turni264 – 2663Combined sources
Helixi267 – 27812Combined sources
Helixi281 – 2877Combined sources
Turni290 – 2956Combined sources
Helixi296 – 2983Combined sources
Turni303 – 3053Combined sources
Beta strandi314 – 3163Combined sources
Beta strandi321 – 3255Combined sources
Helixi327 – 3326Combined sources
Beta strandi337 – 3393Combined sources
Helixi348 – 35912Combined sources
Beta strandi365 – 3673Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2UU7X-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-373[»]
ProteinModelPortaliQ8HZM5.
SMRiQ8HZM5. Positions 3-372.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8HZM5.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0174.
GeneTreeiENSGT00390000010047.
HOGENOMiHOG000061500.
HOVERGENiHBG005847.
InParanoidiQ8HZM5.
OrthoDBiEOG7CZK5G.

Family and domain databases

Gene3Di3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8HZM5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE
60 70 80 90 100
PKGVEELPEW NFDGSSTFQS EGSNSDMYLV PAAMFRDPFR KDPNKLVFCE
110 120 130 140 150
VFKYNRKPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP
160 170 180 190 200
SNGFPGPQGP YYCGVGADKA YGRDIVEAHY RACLYAGIKI AGTNAEVMPA
210 220 230 240 250
QWEFQIGPCE GIDMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA
260 270 280 290 300
GCHTNFSTKA MREENGLKYI EESIEKLSKR HQYHIRAYDP KGGLDNARRL
310 320 330 340 350
TGFHETSNIN DFSAGVANRG ASIRIPRTVG QEKKGYFEDR RPSANCDPFS
360 370
VTEALIRTCL LNETGDEPFQ YKN
Length:373
Mass (Da):42,028
Last modified:January 23, 2007 - v3
Checksum:iE5AD18AEED3F0C52
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF544242 mRNA. Translation: AAN41001.1.
AF544243 Genomic DNA. Translation: AAN41002.1.
RefSeqiNP_001002965.2. NM_001002965.2.
NP_001280153.1. NM_001293224.1.
UniGeneiCfa.1407.

Genome annotation databases

EnsembliENSCAFT00000020795; ENSCAFP00000019307; ENSCAFG00000013102.
GeneIDi403443.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF544242 mRNA. Translation: AAN41001.1 .
AF544243 Genomic DNA. Translation: AAN41002.1 .
RefSeqi NP_001002965.2. NM_001002965.2.
NP_001280153.1. NM_001293224.1.
UniGenei Cfa.1407.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2UU7 X-ray 3.00 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O 2-373 [» ]
ProteinModelPortali Q8HZM5.
SMRi Q8HZM5. Positions 3-372.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q8HZM5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSCAFT00000020795 ; ENSCAFP00000019307 ; ENSCAFG00000013102 .
GeneIDi 403443.

Organism-specific databases

CTDi 2752.

Phylogenomic databases

eggNOGi COG0174.
GeneTreei ENSGT00390000010047.
HOGENOMi HOG000061500.
HOVERGENi HBG005847.
InParanoidi Q8HZM5.
OrthoDBi EOG7CZK5G.

Enzyme and pathway databases

Reactomei REACT_254787. Amino acid synthesis and interconversion (transamination).
REACT_260379. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
SABIO-RK Q8HZM5.

Miscellaneous databases

EvolutionaryTracei Q8HZM5.
NextBioi 20816961.

Family and domain databases

Gene3Di 3.30.590.10. 1 hit.
InterProi IPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view ]
Pfami PF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view ]
SUPFAMi SSF54368. SSF54368. 1 hit.
PROSITEi PS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "A splice variant acquiring an extra transcript leader region decreases the translation of glutamine synthetase gene."
    Shin D., Park S., Park C.
    Biochem. J. 374:175-184(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].

Entry informationi

Entry nameiGLNA_CANFA
AccessioniPrimary (citable) accession number: Q8HZM5
Secondary accession number(s): Q8HZM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 79 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3