AZIN2_HUMAN
ID AZIN2_HUMAN Reviewed; 460 AA.
AC Q96A70; B2RDU5; D3DPQ9; Q5TIF4; Q5TIF5; Q5TIF6; Q8TF56; Q96L54; Q96L55;
AC Q96L56; Q96L57; Q96MD9;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Antizyme inhibitor 2;
DE Short=AzI2;
DE AltName: Full=Arginine decarboxylase;
DE Short=ADC;
DE Short=ARGDC;
DE AltName: Full=Ornithine decarboxylase-like protein;
DE Short=ODC-like protein;
DE AltName: Full=ornithine decarboxylase paralog;
DE Short=ODC-p;
GN Name=AZIN2; Synonyms=ADC, KIAA1945, ODCP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 6), AND TISSUE
RP SPECIFICITY.
RX PubMed=11587527; DOI=10.1006/bbrc.2001.5703;
RA Pitkaenen L.T., Heiskala M., Andersson L.C.;
RT "Expression of a novel human ornithine decarboxylase-like protein in the
RT central nervous system and testes.";
RL Biochem. Biophys. Res. Commun. 287:1051-1057(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14738999; DOI=10.1016/j.bbagen.2003.11.006;
RA Zhu M.-Y., Iyo A., Piletz J.E., Regunathan S.;
RT "Expression of human arginine decarboxylase, the biosynthetic enzyme for
RT agmatine.";
RL Biochim. Biophys. Acta 1670:156-164(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Substantia nigra, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION, INTERACTION WITH OAZ1; OAZ2 AND OAZ3, AND UBIQUITINATION.
RX PubMed=17900240; DOI=10.1042/bj20071004;
RA Kanerva K., Makitie L.T., Pelander A., Heiskala M., Andersson L.C.;
RT "Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor
RT but not an arginine decarboxylase.";
RL Biochem. J. 409:187-192(2008).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19756694; DOI=10.1007/s00418-009-0636-7;
RA Makitie L.T., Kanerva K., Sankila A., Andersson L.C.;
RT "High expression of antizyme inhibitor 2, an activator of ornithine
RT decarboxylase in steroidogenic cells of human gonads.";
RL Histochem. Cell Biol. 132:633-638(2009).
RN [10]
RP SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=19718454; DOI=10.1371/journal.pone.0006858;
RA Kanerva K., Lappalainen J., Makitie L.T., Virolainen S., Kovanen P.T.,
RA Andersson L.C.;
RT "Expression of antizyme inhibitor 2 in mast cells and role of polyamines as
RT selective regulators of serotonin secretion.";
RL PLoS ONE 4:E6858-E6858(2009).
RN [11]
RP REVIEW, AND CHARACTERIZATION.
RX PubMed=19956990; DOI=10.1007/s00726-009-0419-4;
RA Lopez-Contreras A.J., Ramos-Molina B., Cremades A., Penafiel R.;
RT "Antizyme inhibitor 2: molecular, cellular and physiological aspects.";
RL Amino Acids 38:603-611(2010).
RN [12]
RP ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19832840; DOI=10.1111/j.1750-3639.2009.00334.x;
RA Makitie L.T., Kanerva K., Polvikoski T., Paetau A., Andersson L.C.;
RT "Brain neurons express ornithine decarboxylase-activating antizyme
RT inhibitor 2 with accumulation in Alzheimer's disease.";
RL Brain Pathol. 20:571-580(2010).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20188728; DOI=10.1016/j.yexcr.2010.02.021;
RA Kanerva K., Makitie L.T., Back N., Andersson L.C.;
RT "Ornithine decarboxylase antizyme inhibitor 2 regulates intracellular
RT vesicle trafficking.";
RL Exp. Cell Res. 316:1896-1906(2010).
CC -!- FUNCTION: Antizyme inhibitor (AZI) protein that positively regulates
CC ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an
CC enzymatically inactive ODC homolog that counteracts the negative effect
CC of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing
CC with ODC for antizyme-binding (PubMed:17900240). Inhibits antizyme-
CC dependent ODC degradation and releases ODC monomers from their inactive
CC complex with antizymes, leading to formation of the catalytically
CC active ODC homodimer and restoring polyamine production
CC (PubMed:17900240). Participates in the morphological integrity of the
CC trans-Golgi network (TGN) and functions as a regulator of intracellular
CC secretory vesicle trafficking (PubMed:20188728).
CC {ECO:0000269|PubMed:17900240, ECO:0000269|PubMed:20188728}.
CC -!- SUBUNIT: Monomer. Interacts with OAZ1, OAZ2 and OAZ3; this interaction
CC disrupts the interaction between the antizyme and ODC1. Does not form a
CC heterodimer with ODC1. {ECO:0000269|PubMed:17900240}.
CC -!- INTERACTION:
CC Q96A70; Q9UMX2: OAZ3; NbExp=5; IntAct=EBI-10281609, EBI-10281601;
CC Q96A70; Q9UMX2-2: OAZ3; NbExp=3; IntAct=EBI-10281609, EBI-12049527;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Cytoplasm,
CC perinuclear region. Membrane {ECO:0000250}. Cytoplasmic vesicle.
CC Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}.
CC Golgi apparatus, cis-Golgi network {ECO:0000250}. Golgi apparatus,
CC trans-Golgi network. Cytoplasmic granule. Cell projection, axon. Cell
CC projection, dendrite. Perikaryon. Note=Colocalizes with KDEL receptors
CC in ER-Golgi intermediate compartment (ERGIC). Translocates from the
CC ERGIC structure to the cytoplasm in an antizyme-dependent manner.
CC Localizes with vesicle-associated membrane protein VAMP8 in the
CC vicinity of the plasma membrane within serotonin-containing secretory
CC granules (By similarity). Detected as vesicle-like pattern in neurite
CC outgrowths. Localizes to the vesicular compartments of the secretory
CC pathway, predominantly in the trans-Golgi network (TGN). Localizes with
CC vesicle-associated membrane protein VAMP8 in the vicinity of the plasma
CC membrane within serotonin-containing secretory granules. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q96A70-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96A70-2; Sequence=VSP_003756;
CC Name=3;
CC IsoId=Q96A70-3; Sequence=VSP_003757, VSP_003758;
CC Name=4;
CC IsoId=Q96A70-4; Sequence=VSP_003755, VSP_003757, VSP_003758;
CC Name=6;
CC IsoId=Q96A70-5; Sequence=VSP_003754, VSP_003757, VSP_003758;
CC -!- TISSUE SPECIFICITY: Expressed in the neocortex, thalamus, hippocampus,
CC cerebellum, medulla oblongata, gray and white matter. Expressed in
CC neurons, oligodendrocytes, basket, Purkinje and pyramidal cells.
CC Expressed in spermatocytes and Leydig cells of the testis. Expressed in
CC luteal theca cells lining corpus luteum cysts and in hilus cells of the
CC ovary. Expressed in primary and neoplastic mast cells (MC) (at protein
CC level). Highly expressed in brain. Also expressed in testis.
CC {ECO:0000269|PubMed:11587527, ECO:0000269|PubMed:14738999,
CC ECO:0000269|PubMed:19718454, ECO:0000269|PubMed:19756694,
CC ECO:0000269|PubMed:19832840}.
CC -!- DOMAIN: The N-terminus domain is necessary for its localization to the
CC ER-Golgi intermediate compartment (ERGIC). {ECO:0000250}.
CC -!- PTM: Ubiquitinated, leading to its proteasomal degradation; a process
CC that is reduced in presence of antizymes. May also be degraded through
CC the lysosomal degradative pathway in a proteasomal-independent manner.
CC {ECO:0000269|PubMed:17900240}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC ODC antizyme inhibitor subfamily. {ECO:0000305}.
CC -!- CAUTION: Was initially reported to have ornithine decarboxylase
CC (PubMed:11587527) or arginine decarboxylase (PubMed:14738999)
CC activities, but it was later found that the mouse ortholog does not
CC possess either of them. {ECO:0000305|PubMed:11587527,
CC ECO:0000305|PubMed:14738999}.
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DR EMBL; AY050634; AAL08049.1; -; mRNA.
DR EMBL; AY050635; AAL08050.1; -; mRNA.
DR EMBL; AY050636; AAL08051.1; -; mRNA.
DR EMBL; AY050637; AAL08052.1; -; mRNA.
DR EMBL; AY050638; AAL08053.1; -; mRNA.
DR EMBL; AY325129; AAQ62560.1; -; mRNA.
DR EMBL; AB075825; BAB85531.1; -; mRNA.
DR EMBL; AK057051; BAB71356.1; -; mRNA.
DR EMBL; AK095127; BAC04489.1; -; mRNA.
DR EMBL; AK315677; BAG38042.1; -; mRNA.
DR EMBL; AL020995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07472.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07481.1; -; Genomic_DNA.
DR EMBL; BC010449; AAH10449.1; -; mRNA.
DR EMBL; BC028128; AAH28128.1; -; mRNA.
DR CCDS; CCDS375.1; -. [Q96A70-1]
DR CCDS; CCDS76138.1; -. [Q96A70-2]
DR RefSeq; NP_001280491.1; NM_001293562.1. [Q96A70-1]
DR RefSeq; NP_001288752.1; NM_001301823.1.
DR RefSeq; NP_001288753.1; NM_001301824.1.
DR RefSeq; NP_001288754.1; NM_001301825.1. [Q96A70-2]
DR RefSeq; NP_001288755.1; NM_001301826.1. [Q96A70-3]
DR RefSeq; NP_443724.1; NM_052998.3. [Q96A70-1]
DR RefSeq; XP_005270461.1; XM_005270404.2.
DR RefSeq; XP_005270464.1; XM_005270407.1.
DR RefSeq; XP_011538865.1; XM_011540563.1. [Q96A70-3]
DR RefSeq; XP_016855657.1; XM_017000168.1.
DR RefSeq; XP_016855658.1; XM_017000169.1.
DR RefSeq; XP_016855659.1; XM_017000170.1.
DR RefSeq; XP_016855660.1; XM_017000171.1.
DR RefSeq; XP_016855661.1; XM_017000172.1.
DR RefSeq; XP_016855662.1; XM_017000173.1.
DR RefSeq; XP_016855664.1; XM_017000175.1.
DR AlphaFoldDB; Q96A70; -.
DR SMR; Q96A70; -.
DR BioGRID; 125246; 32.
DR IntAct; Q96A70; 10.
DR STRING; 9606.ENSP00000294517; -.
DR DrugBank; DB00125; Arginine.
DR DrugBank; DB09096; Benzoyl peroxide.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR iPTMnet; Q96A70; -.
DR PhosphoSitePlus; Q96A70; -.
DR BioMuta; AZIN2; -.
DR DMDM; 24636807; -.
DR jPOST; Q96A70; -.
DR MassIVE; Q96A70; -.
DR MaxQB; Q96A70; -.
DR PaxDb; Q96A70; -.
DR PeptideAtlas; Q96A70; -.
DR PRIDE; Q96A70; -.
DR ProteomicsDB; 75924; -. [Q96A70-1]
DR ProteomicsDB; 75925; -. [Q96A70-2]
DR ProteomicsDB; 75926; -. [Q96A70-3]
DR ProteomicsDB; 75927; -. [Q96A70-4]
DR Antibodypedia; 31397; 81 antibodies from 20 providers.
DR DNASU; 113451; -.
DR Ensembl; ENST00000294517.11; ENSP00000294517.6; ENSG00000142920.17. [Q96A70-1]
DR Ensembl; ENST00000373441.1; ENSP00000362540.1; ENSG00000142920.17. [Q96A70-2]
DR Ensembl; ENST00000373443.7; ENSP00000362542.3; ENSG00000142920.17. [Q96A70-1]
DR GeneID; 113451; -.
DR KEGG; hsa:113451; -.
DR MANE-Select; ENST00000294517.11; ENSP00000294517.6; NM_052998.4; NP_443724.1.
DR UCSC; uc001bwr.3; human. [Q96A70-1]
DR CTD; 113451; -.
DR DisGeNET; 113451; -.
DR GeneCards; AZIN2; -.
DR HGNC; HGNC:29957; AZIN2.
DR HPA; ENSG00000142920; Tissue enhanced (testis).
DR MIM; 608353; gene.
DR neXtProt; NX_Q96A70; -.
DR OpenTargets; ENSG00000142920; -.
DR PharmGKB; PA142672642; -.
DR VEuPathDB; HostDB:ENSG00000142920; -.
DR eggNOG; KOG0622; Eukaryota.
DR GeneTree; ENSGT00950000182995; -.
DR HOGENOM; CLU_026444_1_1_1; -.
DR InParanoid; Q96A70; -.
DR OMA; CPEQPWH; -.
DR OrthoDB; 725914at2759; -.
DR PhylomeDB; Q96A70; -.
DR TreeFam; TF300760; -.
DR BioCyc; MetaCyc:HS06971-MON; -.
DR BRENDA; 4.1.1.19; 2681.
DR PathwayCommons; Q96A70; -.
DR Reactome; R-HSA-351143; Agmatine biosynthesis.
DR SignaLink; Q96A70; -.
DR BioGRID-ORCS; 113451; 6 hits in 1063 CRISPR screens.
DR GeneWiki; ADC_(gene); -.
DR GenomeRNAi; 113451; -.
DR Pharos; Q96A70; Tbio.
DR PRO; PR:Q96A70; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96A70; protein.
DR Bgee; ENSG00000142920; Expressed in right testis and 146 other tissues.
DR ExpressionAtlas; Q96A70; baseline and differential.
DR Genevisible; Q96A70; HS.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; ISS:UniProtKB.
DR GO; GO:1990005; C:granular vesicle; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IMP:UniProtKB.
DR GO; GO:0008792; F:arginine decarboxylase activity; TAS:Reactome.
DR GO; GO:0042978; F:ornithine decarboxylase activator activity; IDA:UniProtKB.
DR GO; GO:0097055; P:agmatine biosynthetic process; TAS:Reactome.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
DR GO; GO:1902269; P:positive regulation of polyamine transmembrane transport; ISS:UniProtKB.
DR GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; NAS:UniProtKB.
DR GO; GO:0098629; P:trans-Golgi network membrane organization; IMP:UniProtKB.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR031173; Azin2.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022657; De-COase2_CS.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR002433; Orn_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR11482; PTHR11482; 1.
DR PANTHER; PTHR11482:SF4; PTHR11482:SF4; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR PRINTS; PR01179; ODADCRBXLASE.
DR PRINTS; PR01182; ORNDCRBXLASE.
DR SUPFAM; SSF50621; SSF50621; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasm; Cytoplasmic vesicle;
KW Golgi apparatus; Membrane; Nucleus; Polyamine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..460
FT /note="Antizyme inhibitor 2"
FT /id="PRO_0000149944"
FT REGION 117..140
FT /note="Necessary for polyamine uptake stimulation"
FT /evidence="ECO:0000250"
FT SITE 70
FT /note="Not modified"
FT /evidence="ECO:0000250|UniProtKB:O35484"
FT VAR_SEQ 94..251
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:11587527"
FT /id="VSP_003754"
FT VAR_SEQ 151
FT /note="K -> KFVQQRGTACLIR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11587527"
FT /id="VSP_003755"
FT VAR_SEQ 305
FT /note="E -> EAPLPPPHIATCAASEPSPPA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11587527"
FT /id="VSP_003756"
FT VAR_SEQ 344..362
FT /note="KPSTEQPLYSSSLWGPAVD -> SKNHSPCYMSLESIHFIAV (in
FT isoform 3, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:11587527"
FT /id="VSP_003757"
FT VAR_SEQ 363..460
FT /note="Missing (in isoform 3, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:11587527"
FT /id="VSP_003758"
FT VARIANT 288
FT /note="A -> S (in dbSNP:rs16835244)"
FT /id="VAR_050611"
FT CONFLICT 1..35
FT /note="MAGYLSESDFVMVEEGFSTRDLLKELTLGASQATT -> QQGSSVASTEPGS
FT GTWKDHGWHAQGASWMGSHIHPLLVIQ (in Ref. 3; BAB85531)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 49980 MW; 0E00667CA4BB0B56 CRC64;
MAGYLSESDF VMVEEGFSTR DLLKELTLGA SQATTDEVAA FFVADLGAIV RKHFCFLKCL
PRVRPFYAVK CNSSPGVLKV LAQLGLGFSC ANKAEMELVQ HIGIPASKII CANPCKQIAQ
IKYAAKHGIQ LLSFDNEMEL AKVVKSHPSA KMVLCIATDD SHSLSCLSLK FGVSLKSCRH
LLENAKKHHV EVVGVSFHIG SGCPDPQAYA QSIADARLVF EMGTELGHKM HVLDLGGGFP
GTEGAKVRFE EIASVINSAL DLYFPEGCGV DIFAELGRYY VTSAFTVAVS IIAKKEVLLD
QPGREEENGS TSKTIVYHLD EGVYGIFNSV LFDNICPTPI LQKKPSTEQP LYSSSLWGPA
VDGCDCVAEG LWLPQLHVGD WLVFDNMGAY TVGMGSPFWG TQACHITYAM SRVAWEALRR
QLMAAEQEDD VEGVCKPLSC GWEITDTLCV GPVFTPASIM
