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Protein

Antizyme inhibitor 2

Gene

Azin2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Antizyme inhibitor protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake by counteracting the negative effect of antizymes OAZ1, OAZ2 and OAZ3 on ODC1 activity (PubMed:18508777, PubMed:18062773, PubMed:18973822). Inhibits antizyme-dependent ODC1 degradation by binding to antizymes (PubMed:16916800). Releases ODC1 from its inactive complex with antizymes, leading to formation of the catalytically active ODC1 (PubMed:24967154). Participates in the morphological integrity of the trans-Golgi network (TGN) and functions as a regulator of intracellular secretory vesicle trafficking.5 Publications

GO - Molecular functioni

  • catalytic activity Source: InterPro
  • ornithine decarboxylase activator activity Source: UniProtKB
  • putrescine transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  • negative regulation of protein catabolic process Source: UniProtKB
  • ornithine metabolic process Source: MGI
  • polyamine biosynthetic process Source: UniProtKB-KW
  • positive regulation of catalytic activity Source: UniProtKB
  • positive regulation of polyamine transmembrane transport Source: UniProtKB
  • putrescine transport Source: UniProtKB
  • trans-Golgi network membrane organization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Polyamine biosynthesis, Transport

Enzyme and pathway databases

ReactomeiR-MMU-351143. Agmatine biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Antizyme inhibitor 2
Short name:
AzI2
Alternative name(s):
Arginine decarboxylase-like protein
Short name:
ADC
Short name:
ARGDC
Ornithine decarboxylase-like protein
Short name:
ODC-like protein
ornithine decarboxylase paralog
Short name:
ODC-p
Gene namesi
Name:Azin2
Synonyms:Adc, Odcp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2442093. Azin2.

Subcellular locationi

GO - Cellular componenti

  • axon Source: UniProtKB
  • cis-Golgi network Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB
  • dendrite Source: UniProtKB
  • endoplasmic reticulum-Golgi intermediate compartment membrane Source: UniProtKB
  • granular vesicle Source: UniProtKB
  • mitochondrion Source: MGI
  • nucleus Source: UniProtKB
  • perikaryon Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • trans-Golgi network Source: UniProtKB
  • transport vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi116 – 1161K → A: Does not inhibit interaction with OAZ1. Reduces interaction with OAZ1; when associated with A-142. 1 Publication
Mutagenesisi124 – 1241A → S: Does not inhibit interaction with OAZ1. 1 Publication
Mutagenesisi139 – 1391E → A: Strongly reduces interaction with OAZ1 and unable to abrogate both the inhibitory effect of OAZ1 on ornithine decarboxylase (ODC) activity and polyamine uptake; when associated with A-140 and A-142. 1 Publication
Mutagenesisi140 – 1401L → A: Strongly reduces interaction with OAZ1 and unable to abrogate both the inhibitory effect of OAZ1 on ornithine decarboxylase (ODC) activity and polyamine uptake; when associated with A-139 and A-142. 1 Publication
Mutagenesisi142 – 1421K → A: Does not inhibit interaction with OAZ1. Reduces interaction with OAZ1; when associated with A-116. Strongly reduces interaction with OAZ1 and unable to abrogate the inhibitory effect of OAZ1 on ornithine decarboxylase (ODC) activity and polyamine uptake; when associated with A-139 and A-140. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Antizyme inhibitor 2PRO_0000149945Add
BLAST

Post-translational modificationi

Ubiquitinated, leading to its proteosomal degradation; a process that is reduced in presence of antizymes. May also be degraded through the lysosomal degradative pathway in a proteosomal-independent manner.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ8BVM4.
PaxDbiQ8BVM4.
PRIDEiQ8BVM4.

PTM databases

PhosphoSiteiQ8BVM4.

Expressioni

Tissue specificityi

Expressed in the medulla and chromaffin cells of the adrenal gland. Expressed in the Langerhans islets of the pancreas. Expressed in the inner part of the seminiferous tubules and in spermatozoa located in the lumen of the epididymis of the testis. Expressed in the cortex, hippocampus and cerebellum of the brain. Expressed in normal and neoplastic mast cells (MC) (at protein level). Expressed in testis, pancreas and brain. Expressed throughout the differentiation process from spermatids to spermatozoa in the inner part of the seminiferous tubules. Expressed in the kidney: expressed in the superficial (Cs) and the deep layer (Cd) of the cortex region and in the outer stripe (OS), inner stripe (IS) and the inner medulla papilla (IM) of the medulla region.5 Publications

Gene expression databases

BgeeiQ8BVM4.
CleanExiMM_ADC.
ExpressionAtlasiQ8BVM4. baseline and differential.
GenevisibleiQ8BVM4. MM.

Interactioni

Subunit structurei

Interaction with OAZ1, OAZ2 and OAZ3; the interactions lead to increased ornithine decarboxylase (ODC) activity and decreased rate of ODC1 degradation (By similarity). Monomer. Interacts with OAZ1, OAZ2 and OAZ3; the interactions stabilize the complex by inhibiting AZIN2 ubiquitination and degradation. Does not form a heterodimer with ODC1.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Oaz3Q9R1092EBI-9656869,EBI-4370103

Protein-protein interaction databases

IntActiQ8BVM4. 3 interactions.
STRINGi10090.ENSMUSP00000030581.

Structurei

3D structure databases

ProteinModelPortaliQ8BVM4.
SMRiQ8BVM4. Positions 7-418.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni117 – 14024Necessary for polyamine uptake stimulationAdd
BLAST

Domaini

The N-terminus domain is necessary for its localization to the ER-Golgi intermediate compartment (ERGIC).

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0622. Eukaryota.
COG0019. LUCA.
GeneTreeiENSGT00390000011560.
HOGENOMiHOG000274133.
HOVERGENiHBG005456.
InParanoidiQ8BVM4.
KOiK01583.
OMAiSHMEVVG.
PhylomeDBiQ8BVM4.
TreeFamiTF300760.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR031173. Azin2.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR000183. Orn/DAP/Arg_de-COase.
IPR002433. Orn_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
PANTHERiPTHR11482:SF4. PTHR11482:SF4. 1 hit.
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEiPS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BVM4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGYLSESDF VMVEEGFSTR DLLEELTLGA SQATSGKVAA FFVADLGAVV
60 70 80 90 100
RKHFCFLKHL PRVRPFYAVG CNSSLGVLKV LAELGLGFSC ANKAEMELVQ
110 120 130 140 150
HIGVPASKII CANPCKQVAQ IKYAAKHGVR LLSFDNEVEL AKVVKSHPSA
160 170 180 190 200
KMVLCIATQD SHSLNHLSLR FGASLKSCRH LLENAKKSHV EVVGVSFHIG
210 220 230 240 250
SGCPDPQAYA QSIADARLVF QMGEELGHTM NILDLGGGFP GLEGAKVRFE
260 270 280 290 300
EMASVINSAL DLYFPEGCGV DILAELGRYY VTSAFTVAVS IVAKREVLDQ
310 320 330 340 350
ASREEQTGAA PKSIVYYLDE GVYGVFNSVL FDNTCPTPAL QKKPSADQPL
360 370 380 390 400
YSSSLWGPAV EGCDCVAEGL WLPQLQVGDW LVFDNMGAYT VDTKSLLGGT
410 420 430 440 450
QARRVTYAMS RLAWEALRGQ LLPAEEDQDA EGVCKPLSCG WEITDTLCVG

PVFTPASIM
Length:459
Mass (Da):49,503
Last modified:March 1, 2003 - v1
Checksum:i4C8D3994B89ABAC5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti317 – 3171Y → H no nucleotide entry (PubMed:16916800).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK077201 mRNA. Translation: BAC36679.1.
AL607086 Genomic DNA. Translation: CAM19110.1.
CCDSiCCDS18678.1.
RefSeqiNP_766463.1. NM_172875.4.
UniGeneiMm.215814.

Genome annotation databases

EnsembliENSMUST00000030581; ENSMUSP00000030581; ENSMUSG00000028789.
ENSMUST00000106068; ENSMUSP00000101683; ENSMUSG00000028789.
GeneIDi242669.
KEGGimmu:242669.
UCSCiuc008uvq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK077201 mRNA. Translation: BAC36679.1.
AL607086 Genomic DNA. Translation: CAM19110.1.
CCDSiCCDS18678.1.
RefSeqiNP_766463.1. NM_172875.4.
UniGeneiMm.215814.

3D structure databases

ProteinModelPortaliQ8BVM4.
SMRiQ8BVM4. Positions 7-418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BVM4. 3 interactions.
STRINGi10090.ENSMUSP00000030581.

PTM databases

PhosphoSiteiQ8BVM4.

Proteomic databases

MaxQBiQ8BVM4.
PaxDbiQ8BVM4.
PRIDEiQ8BVM4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030581; ENSMUSP00000030581; ENSMUSG00000028789.
ENSMUST00000106068; ENSMUSP00000101683; ENSMUSG00000028789.
GeneIDi242669.
KEGGimmu:242669.
UCSCiuc008uvq.2. mouse.

Organism-specific databases

CTDi113451.
MGIiMGI:2442093. Azin2.

Phylogenomic databases

eggNOGiKOG0622. Eukaryota.
COG0019. LUCA.
GeneTreeiENSGT00390000011560.
HOGENOMiHOG000274133.
HOVERGENiHBG005456.
InParanoidiQ8BVM4.
KOiK01583.
OMAiSHMEVVG.
PhylomeDBiQ8BVM4.
TreeFamiTF300760.

Enzyme and pathway databases

ReactomeiR-MMU-351143. Agmatine biosynthesis.

Miscellaneous databases

PROiQ8BVM4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BVM4.
CleanExiMM_ADC.
ExpressionAtlasiQ8BVM4. baseline and differential.
GenevisibleiQ8BVM4. MM.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR031173. Azin2.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR000183. Orn/DAP/Arg_de-COase.
IPR002433. Orn_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
PANTHERiPTHR11482:SF4. PTHR11482:SF4. 1 hit.
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEiPS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse ornithine decarboxylase-like gene encodes an antizyme inhibitor devoid of ornithine and arginine decarboxylating activity."
    Lopez-Contreras A.J., Lopez-Garcia C., Jimenez-Cervantes C., Cremades A., Penafiel R.
    J. Biol. Chem. 281:30896-30906(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH OAZ1; OAZ2 AND OAZ3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "ODCp, a brain- and testis-specific ornithine decarboxylase paralogue, functions as an antizyme inhibitor, although less efficiently than AzI1."
    Snapir Z., Keren-Paz A., Bercovich Z., Kahana C.
    Biochem. J. 410:613-619(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH OAZ1 AND OAZ3.
  5. "Antizyme inhibitor 2 (AZIN2/ODCp) stimulates polyamine uptake in mammalian cells."
    Lopez-Contreras A.J., Ramos-Molina B., Cremades A., Penafiel R.
    J. Biol. Chem. 283:20761-20769(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  6. "Expression of antizyme inhibitor 2 in male haploid germinal cells suggests a role in spermiogenesis."
    Lopez-Contreras A.J., Ramos-Molina B., Martinez-de-la-Torre M., Penafiel-Verdu C., Puelles L., Cremades A., Penafiel R.
    Int. J. Biochem. Cell Biol. 41:1070-1078(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH OAZ3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "Subcellular localization of antizyme inhibitor 2 in mammalian cells: Influence of intrinsic sequences and interaction with antizymes."
    Lopez-Contreras A.J., Sanchez-Laorden B.L., Ramos-Molina B., de la Morena M.E., Cremades A., Penafiel R.
    J. Cell. Biochem. 107:732-740(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Expression and distribution of genes encoding for polyamine-metabolizing enzymes in the different zones of male and female mouse kidneys."
    Levillain O., Ramos-Molina B., Forcheron F., Penafiel R.
    Amino Acids 43:2153-2163(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "Antizyme inhibitor 2: molecular, cellular and physiological aspects."
    Lopez-Contreras A.J., Ramos-Molina B., Cremades A., Penafiel R.
    Amino Acids 38:603-611(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, CHARACTERIZATION.
  10. "Antizyme inhibitor 2 hypomorphic mice. New patterns of expression in pancreas and adrenal glands suggest a role in secretory processes."
    Lopez-Garcia C., Ramos-Molina B., Lambertos A., Lopez-Contreras A.J., Cremades A., Penafiel R.
    PLoS ONE 8:E69188-E69188(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "Structural and degradative aspects of ornithine decarboxylase antizyme inhibitor 2."
    Ramos-Molina B., Lambertos A., Lopez-Contreras A.J., Kasprzak J.M., Czerwoniec A., Bujnicki J.M., Cremades A., Penafiel R.
    FEBS Open Bio 4:510-521(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH OAZ1, SUBUNIT, MUTAGENESIS OF LYS-116; ALA-124; GLU-139; LEU-140 AND LYS-142.

Entry informationi

Entry nameiAZIN2_MOUSE
AccessioniPrimary (citable) accession number: Q8BVM4
Secondary accession number(s): A2A823
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Gly-70 is present instead of the conserved Lys which would otherwise be the covalent pyridoxal phosphate binding site.Curated

Caution

The human ortholog was initially reported to have ornithine or arginine decarboxylase activities, but it was later found to possess neither of them.1 Publication
Previously reported to be localized in the mitochondrion (PubMed:16916800). However, it was not confirmed by later reports (PubMed:18062773).2 Publications

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.