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Protein

Antizyme inhibitor 1

Gene

Azin1

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 antizyme OAZ1, OAZ2 and OAZ3 on ODC1 activity (PubMed:16916800, PubMed:18062773, PubMed:18508777). Inhibits antizyme-dependent ODC degradation by binding to antizymes (PubMed:18062773). Releases ODC1 from its inactive complex with antizymes, leading to formation of the catalytically active ODC1.5 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Polyamine biosynthesis

Enzyme and pathway databases

ReactomeiR-MMU-350562. Regulation of ornithine decarboxylase (ODC).

Names & Taxonomyi

Protein namesi
Recommended name:
Antizyme inhibitor 1
Short name:
AZI
Alternative name(s):
Ornithine decarboxylase antizyme inhibitor
Gene namesi
Name:Azin1
Synonyms:Oazi, Oazin
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1859169. Azin1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Antizyme inhibitor 1PRO_0000149993Add
BLAST

Post-translational modificationi

Ubiquitinated, leading to its proteasomal degradation; a process that is reduced in presence of antizyme OAZ1.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei69 – 691Not modifiedCombined sources1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiO35484.
PRIDEiO35484.

PTM databases

iPTMnetiO35484.
PhosphoSiteiO35484.

Expressioni

Tissue specificityi

Expressed during testis development.2 Publications

Gene expression databases

BgeeiO35484.
CleanExiMM_AZIN1.
ExpressionAtlasiO35484. baseline and differential.
GenevisibleiO35484. MM.

Interactioni

Subunit structurei

Monomer. Interacts with OAZ1 and OAZ3; the interactions stabilize the complex by inhibiting AZIN2 ubiquitination and degradation.2 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000065544.

Structurei

Secondary structure

1
448
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 156Combined sources
Helixi21 – 3414Combined sources
Beta strandi40 – 445Combined sources
Helixi45 – 5814Combined sources
Beta strandi62 – 676Combined sources
Helixi68 – 703Combined sources
Helixi74 – 8310Combined sources
Beta strandi86 – 916Combined sources
Helixi92 – 1009Combined sources
Helixi105 – 1073Combined sources
Beta strandi108 – 1103Combined sources
Helixi117 – 12610Combined sources
Beta strandi130 – 1334Combined sources
Helixi136 – 14510Combined sources
Beta strandi150 – 1556Combined sources
Helixi174 – 18714Combined sources
Beta strandi190 – 1956Combined sources
Helixi207 – 22418Combined sources
Beta strandi231 – 2333Combined sources
Helixi242 – 25918Combined sources
Beta strandi267 – 2704Combined sources
Helixi274 – 2774Combined sources
Turni278 – 2803Combined sources
Beta strandi281 – 29212Combined sources
Beta strandi312 – 3176Combined sources
Turni320 – 3245Combined sources
Helixi325 – 3284Combined sources
Beta strandi348 – 3547Combined sources
Beta strandi363 – 3719Combined sources
Beta strandi378 – 3836Combined sources
Helixi394 – 3963Combined sources
Beta strandi402 – 4087Combined sources
Helixi409 – 4179Combined sources
Helixi420 – 4223Combined sources
Helixi424 – 4263Combined sources
Beta strandi429 – 4335Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BTNX-ray2.05A/B1-448[»]
ProteinModelPortaliO35484.
SMRiO35484. Positions 8-435.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35484.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0622. Eukaryota.
COG0019. LUCA.
GeneTreeiENSGT00390000011560.
HOGENOMiHOG000274133.
HOVERGENiHBG005456.
InParanoidiO35484.
OMAiNDKFSSG.
OrthoDBiEOG73Z2T6.
PhylomeDBiO35484.
TreeFamiTF300760.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR031178. Azin1.
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:SF7. PTHR11482:SF7. 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.

O35484-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGFIDDANY SVGLLDEGTN LGNVIDNYVY EHTLTGKNAF FVGDLGKIVK
60 70 80 90 100
KHSQWQTVVA QIKPFYTVKC NSTPAVLEIL AALGTGFACS SKNEMALVQE
110 120 130 140 150
LGVSPENIIF TSPCKQVSQI KYAAKVGVNI MTCDNEIELK KIARNHPNAK
160 170 180 190 200
VLLHIATEDN IGGEDGNMKF GTTLKNCRHL LECAKELDVQ IIGVKFHVSS
210 220 230 240 250
ACKEYQVYVH ALSDARCVFD MAGEFGFTMN MLDIGGGFTG TEIQLEEVNH
260 270 280 290 300
VISPLLDIYF PEGSGIQIIS EPGSYYVSSA FTLAVNIIAK KVVENDKFSS
310 320 330 340 350
GVEKNGSDEP AFVYYMNDGV YGSFASKLSE DLNTIPEVHK KYKEDEPLFT
360 370 380 390 400
SSLWGPSCDE LDQIVESCLL PELNVGDWLI FDNMGADSFH EPSAFNDFQR
410 420 430 440
PAIYFMMSFS DWYEMQDAGI TSDAMMKNFF FAPSCIQLSQ EDSFSTEA
Length:448
Mass (Da):49,549
Last modified:January 1, 1998 - v1
Checksum:i117F3C2C24DDCA0F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361G → E in AAH19412 (PubMed:15489334).Curated
Sequence conflicti367 – 3671S → G in BAC40151 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF032128 mRNA. Translation: AAB87464.1.
AK049680 mRNA. Translation: BAC33870.1.
AK088112 mRNA. Translation: BAC40151.1.
AK088671 mRNA. Translation: BAC40494.1.
BC019412 mRNA. Translation: AAH19412.1.
BC043722 mRNA. Translation: AAH43722.1.
CCDSiCCDS37065.1.
RefSeqiNP_001095928.1. NM_001102458.1.
NP_001288617.1. NM_001301688.1.
NP_061215.1. NM_018745.5.
UniGeneiMm.250214.

Genome annotation databases

EnsembliENSMUST00000065308; ENSMUSP00000065544; ENSMUSG00000037458.
ENSMUST00000110329; ENSMUSP00000105958; ENSMUSG00000037458.
GeneIDi54375.
KEGGimmu:54375.
UCSCiuc007vns.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF032128 mRNA. Translation: AAB87464.1.
AK049680 mRNA. Translation: BAC33870.1.
AK088112 mRNA. Translation: BAC40151.1.
AK088671 mRNA. Translation: BAC40494.1.
BC019412 mRNA. Translation: AAH19412.1.
BC043722 mRNA. Translation: AAH43722.1.
CCDSiCCDS37065.1.
RefSeqiNP_001095928.1. NM_001102458.1.
NP_001288617.1. NM_001301688.1.
NP_061215.1. NM_018745.5.
UniGeneiMm.250214.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BTNX-ray2.05A/B1-448[»]
ProteinModelPortaliO35484.
SMRiO35484. Positions 8-435.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000065544.

PTM databases

iPTMnetiO35484.
PhosphoSiteiO35484.

Proteomic databases

PaxDbiO35484.
PRIDEiO35484.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000065308; ENSMUSP00000065544; ENSMUSG00000037458.
ENSMUST00000110329; ENSMUSP00000105958; ENSMUSG00000037458.
GeneIDi54375.
KEGGimmu:54375.
UCSCiuc007vns.1. mouse.

Organism-specific databases

CTDi51582.
MGIiMGI:1859169. Azin1.

Phylogenomic databases

eggNOGiKOG0622. Eukaryota.
COG0019. LUCA.
GeneTreeiENSGT00390000011560.
HOGENOMiHOG000274133.
HOVERGENiHBG005456.
InParanoidiO35484.
OMAiNDKFSSG.
OrthoDBiEOG73Z2T6.
PhylomeDBiO35484.
TreeFamiTF300760.

Enzyme and pathway databases

ReactomeiR-MMU-350562. Regulation of ornithine decarboxylase (ODC).

Miscellaneous databases

ChiTaRSiAzin1. mouse.
EvolutionaryTraceiO35484.
PROiO35484.
SOURCEiSearch...

Gene expression databases

BgeeiO35484.
CleanExiMM_AZIN1.
ExpressionAtlasiO35484. baseline and differential.
GenevisibleiO35484. MM.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR031178. Azin1.
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:SF7. PTHR11482:SF7. 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. "Antizyme inhibitor is rapidly induced in growth-stimulated mouse fibroblasts and releases ornithine decarboxylase from antizyme suppression."
    Nilsson J., Grahn B., Heby O.
    Biochem. J. 346:699-704(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: BALB/cJ.
  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 and NOD.
    Tissue: Spinal cord and Thymus.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary gland.
  4. "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: FUNCTION.
  5. "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, INTERACTION WITH OAZ1 AND OAZ3, UBIQUITINATION.
  6. "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.
  7. "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: TISSUE SPECIFICITY.
  8. "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.
  9. "Crystallographic and biochemical studies revealing the structural basis for antizyme inhibitor function."
    Albeck S., Dym O., Unger T., Snapir Z., Bercovich Z., Kahana C.
    Protein Sci. 17:793-802(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), ABSENCE OF PYRIDOXAL PHOSPHATE BINDING, SUBUNIT, FUNCTION.

Entry informationi

Entry nameiAZIN1_MOUSE
AccessioniPrimary (citable) accession number: O35484
Secondary accession number(s): Q542G5, Q8C2R8, Q8K1E5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 117 of the entry and version 1 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.