ARG1

ARG1
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1WVA, 1WVB, 2AEB, 2PHA, 2PHO, 2PLL, 2ZAV, 3DJ8, 3E6K, 3E6V, 3F80, 3GMZ, 3GN0, 3KV2, 3LP4, 3LP7, 3MFV, 3MFW, 3MJL, 3SJT, 3SKK, 3TF3, 3TH7, 3THE, 3THH, 3THJ, 4FCI, 4FCK, 4GSM, 4GSV, 4GSZ, 4GWC, 4GWD, 4HWW, 4HXQ, 4IE1
Identifikatori
Aliasi	ARG1
Vanjski ID-jevi	OMIM: 608313 MGI: 88070 HomoloGene: 29 GeneCards: ARG1
Lokacija gena (čovjek)
Hrom.	Hromosom 6 (čovjek)
Kraj	131,584,332 bp
Lokacija gena (miš)
Hrom.	Hromosom 10 (miš)
Kraj	24,803,382 bp
Ontologija gena
Molekularna funkcija	• arginase activity; • manganese ion binding; • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; • vezivanje iona metala; • hydrolase activity; • GO:0001948, GO:0016582 vezivanje za proteine;
Ćelijska komponenta	• citoplazma; • citosol; • mitochondrial outer membrane; • soma; • neuron projection; • Egzosom; • jedro; • extracellular region; • azurophil granule lumen; • specific granule lumen; • Vanćelijsko;
Biološki proces	• cellular response to interleukin-4; • cellular response to transforming growth factor beta stimulus; • response to selenium ion; • response to amino acid; • response to cadmium ion; • positive regulation of endothelial cell proliferation; • maternal process involved in female pregnancy; • lung development; • Ciklus ureje; • female pregnancy; • response to steroid hormone; • cellular response to glucagon stimulus; • GO:0010260 starenje; • response to peptide hormone; • response to zinc ion; • arginine catabolic process; • arginine metabolic process; • response to vitamin E; • protein homotrimerization; • cellular response to dexamethasone stimulus; • response to vitamin A; • arginine catabolic process to ornithine; • response to lipopolysaccharide; • response to manganese ion; • response to wounding; • response to axon injury; • collagen biosynthetic process; • response to amine; • liver development; • response to methylmercury; • cellular response to lipopolysaccharide; • response to herbicide; • cellular response to hydrogen peroxide; • mammary gland involution; • neutrophil degranulation; • negative regulation of T cell proliferation; • defense response to protozoan; • negative regulation of activated T cell proliferation; • negative regulation of interferon-gamma-mediated signaling pathway; • positive regulation of neutrophil mediated killing of fungus; • negative regulation of T-helper 2 cell cytokine production; • adaptive immune response; • immune system process; • Urođeni imunski sistem;
	Izvori:Amigo / QuickGO
Ortolozi
	383
	11846
	ENSG00000118520
	ENSMUSG00000019987
	P05089
	Q61176
	NM_000045; NM_001244438; NM_001369020
	NM_007482
	NP_000036; NP_001231367; NP_001355949
	NP_031508
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Ljudski ARG1 jest ljudski gen koji kodira protein arginaza.^[5]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 322 aminokiseline, а molekulska težina 34.735 Da.^[6]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MSAKSRTIGI	IGAPFSKGQP	RGGVEEGPTV	LRKAGLLEKL	KEQECDVKDY
GDLPFADIPN	DSPFQIVKNP	RSVGKASEQL	AGKVAEVKKN	GRISLVLGGD
HSLAIGSISG	HARVHPDLGV	IWVDAHTDIN	TPLTTTSGNL	HGQPVSFLLK
ELKGKIPDVP	GFSWVTPCIS	AKDIVYIGLR	DVDPGEHYIL	KTLGIKYFSM
TEVDRLGIGK	VMEETLSYLL	GRKKRPIHLS	FDVDGLDPSF	TPATGTPVVG
GLTYREGLYI	TEEIYKTGLL	SGLDIMEVNP	SLGKTPEEVT	RTVNTAVAIT
LACFGLAREG	NHKPIDYLNP	PK

Funkcija

Arginaza katalizira hidrolizu arginina do ornitina i ureje. Najmanje dvije izoforme sisarske arginaze postoje (tipovi I i II) koje se razlikuju po tkivnoj distribuciji subćelijske lokalizacije, imunskoj unakrsnoj reaktivnosti i fiziološkoj funkciji. Izoforma tipa I kodirana ovim genom je citosolni enzim i eksprimira se pretežno u jetri, kao komponenta ciklusa ureje. Nasljedni nedostatak ovog enzima rezultira argininemijom, autosomno recesivnim poremećajem koju karakterizira hiperamonemija. Za ovaj gen su pronađene dvije varijante transkripta koje kodiraju različite izoforme.^[7]

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000118520 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000019987 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: Arginase, liver".
^ "UniProt, P05089" (jezik: engleski). Pristupljeno 6. 10. 2021.
^ Prema RefSeq, Sep 2011]

Dopunska literatura

Morris CR, Kato GJ, Poljakovic M, Wang X, Blackwelder WC, Sachdev V, Hazen SL, Vichinsky EP, Morris SM, Gladwin MT (juli 2005). "Dysregulated arginine metabolism, hemolysis-associated pulmonary hypertension, and mortality in sickle cell disease". JAMA. 294 (1): 81–90. doi:10.1001/jama.294.1.81. PMC 2065861. PMID 15998894.
Jiang M, Ding Y, Su Y, Hu X, Li J, Zhang Z (decembar 2006). "Arginase-flotillin interaction brings arginase to red blood cell membrane". FEBS Letters. 580 (28–29): 6561–4. doi:10.1016/j.febslet.2006.11.003. PMID 17113085. S2CID 20180459.
Morris SM (juli 2009). "Recent advances in arginine metabolism: roles and regulation of the arginases". British Journal of Pharmacology. 157 (6): 922–30. doi:10.1111/j.1476-5381.2009.00278.x. PMC 2737650. PMID 19508396.
Rotondo R, Bertolotto M, Barisione G, Astigiano S, Mandruzzato S, Ottonello L, Dallegri F, Bronte V, Ferrini S, Barbieri O (maj 2011). "Exocytosis of azurophil and arginase 1-containing granules by activated polymorphonuclear neutrophils is required to inhibit T lymphocyte proliferation". Journal of Leukocyte Biology. 89 (5): 721–7. doi:10.1189/jlb.1109737. PMID 21330347. S2CID 25335372.
Shapiro MB, Senapathy P (septembar 1987). "RNA splice junctions of different classes of eukaryotes: sequence statistics and functional implications in gene expression". Nucleic Acids Research. 15 (17): 7155–74. doi:10.1093/nar/15.17.7155. PMC 306199. PMID 3658675.
Rotondo R, Barisione G, Mastracci L, Grossi F, Orengo AM, Costa R, Truini M, Fabbi M, Ferrini S, Barbieri O (august 2009). "IL-8 induces exocytosis of arginase 1 by neutrophil polymorphonuclears in nonsmall cell lung cancer". International Journal of Cancer. 125 (4): 887–93. doi:10.1002/ijc.24448. PMID 19431148. S2CID 205937936.
Salam MT, Bastain TM, Rappaport EB, Islam T, Berhane K, Gauderman WJ, Gilliland FD (mart 2011). "Genetic variations in nitric oxide synthase and arginase influence exhaled nitric oxide levels in children". Allergy. 66 (3): 412–9. doi:10.1111/j.1398-9995.2010.02492.x. PMC 3058253. PMID 21039601.
Gannon PO, Godin-Ethier J, Hassler M, Delvoye N, Aversa M, Poisson AO, Péant B, Alam Fahmy M, Saad F, Lapointe R, Mes-Masson AM (august 2010). Creighton C (ured.). "Androgen-regulated expression of arginase 1, arginase 2 and interleukin-8 in human prostate cancer". PLOS ONE. 5 (8): e12107. Bibcode:2010PLoSO...512107G. doi:10.1371/journal.pone.0012107. PMC 2920336. PMID 20711410.
Ishikawa T, Harada T, Koi H, Kubota T, Azuma H, Aso T (2007). "Identification of arginase in human placental villi". Placenta. 28 (2–3): 133–8. doi:10.1016/j.placenta.2006.03.015. PMID 16720041.

Vanjski linkovi

Lokacija ljudskog genoma ARG1 i stranica sa detaljima o genu ARG1 u UCSC Genome Browseru.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000118520 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000019987 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: Arginase, liver".

[UniProt-6] "UniProt, P05089" (jezik: engleski). Pristupljeno 6. 10. 2021.

[7] Prema RefSeq, Sep 2011]

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