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 10-FEB-2021, entry version 166. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; Q96A70; -. DR BioGRID; 125246; 14. DR IntAct; Q96A70; 10. DR STRING; 9606.ENSP00000294517; -. DR DrugBank; DB00125; Arginine. 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 ProteomicsDB; 75928; -. [Q96A70-5] DR Antibodypedia; 31397; 77 antibodies. DR DNASU; 113451; -. DR Ensembl; ENST00000294517; ENSP00000294517; ENSG00000142920. [Q96A70-1] DR Ensembl; ENST00000373441; ENSP00000362540; ENSG00000142920. [Q96A70-2] DR Ensembl; ENST00000373443; ENSP00000362542; ENSG00000142920. [Q96A70-1] DR GeneID; 113451; -. DR KEGG; hsa:113451; -. 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 (brain, testis). DR MIM; 608353; gene. DR neXtProt; NX_Q96A70; -. DR OpenTargets; ENSG00000142920; -. DR PharmGKB; PA142672642; -. DR VEuPathDB; HostDB:ENSG00000142920.16; -. DR eggNOG; KOG0622; Eukaryota. DR GeneTree; ENSGT00950000182995; -. DR HOGENOM; CLU_026444_1_1_1; -. DR InParanoid; Q96A70; -. DR OMA; CGWEIAD; -. DR OrthoDB; 725914at2759; -. DR PhylomeDB; Q96A70; -. DR TreeFam; TF300760; -. DR BioCyc; MetaCyc:HS06971-MONOMER; -. DR BRENDA; 4.1.1.17; 2681. DR BRENDA; 4.1.1.19; 2681. DR PathwayCommons; Q96A70; -. DR Reactome; R-HSA-351143; Agmatine biosynthesis. DR BioGRID-ORCS; 113451; 1 hit in 865 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 testis and 177 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 //