AZIN1_HUMAN
ID AZIN1_HUMAN Reviewed; 448 AA.
AC O14977; A6NCD5; Q6IBQ7; Q96D20;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Antizyme inhibitor 1;
DE Short=AZI;
DE Short=AZI1;
DE AltName: Full=Ornithine decarboxylase antizyme inhibitor;
GN Name=AZIN1; Synonyms=OAZI, OAZIN;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=9349715; DOI=10.1016/s0167-4781(97)00106-1;
RA Koguchi K., Kobayashi S., Hayashi T., Matsufuji S., Murakami Y.,
RA Hayashi S.;
RT "Cloning and sequencing of a human cDNA encoding ornithine decarboxylase
RT antizyme inhibitor.";
RL Biochim. Biophys. Acta 1353:209-216(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 273-448.
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, 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 X-RAY CRYSTALLOGRAPHY (5.81 ANGSTROMS) OF 2-437 IN COMPLEX WITH OAZ1, AND
RP FUNCTION.
RX PubMed=26305948; DOI=10.1073/pnas.1508187112;
RA Wu H.Y., Chen S.F., Hsieh J.Y., Chou F., Wang Y.H., Lin W.T., Lee P.Y.,
RA Yu Y.J., Lin L.Y., Lin T.S., Lin C.L., Liu G.Y., Tzeng S.R., Hung H.C.,
RA Chan N.L.;
RT "Structural basis of antizyme-mediated regulation of polyamine
RT homeostasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11229-11234(2015).
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, PubMed:26305948).
CC Inhibits antizyme-dependent ODC degradation and releases ODC monomers
CC from their inactive complex with antizymes, leading to formation of the
CC catalytically active ODC homodimer and restoring polyamine production
CC (PubMed:17900240). {ECO:0000269|PubMed:17900240,
CC ECO:0000269|PubMed:26305948}.
CC -!- SUBUNIT: Monomer (PubMed:26305948). Interacts with OAZ1 and OAZ3; this
CC interaction disrupts the interaction between the antizyme and ODC1
CC (Probable). {ECO:0000269|PubMed:26305948, ECO:0000305|PubMed:26305948}.
CC -!- INTERACTION:
CC O14977; O00327-8: ARNTL; NbExp=3; IntAct=EBI-1054824, EBI-11991546;
CC O14977; Q9UMX2: OAZ3; NbExp=5; IntAct=EBI-1054824, EBI-10281601;
CC O14977; Q9UMX2-2: OAZ3; NbExp=3; IntAct=EBI-1054824, EBI-12049527;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O35484}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:9349715}.
CC -!- PTM: Ubiquitinated, leading to its proteasomal degradation; a process
CC that is reduced in presence of antizyme OAZ1.
CC {ECO:0000269|PubMed:17900240}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC ODC antizyme inhibitor subfamily. {ECO:0000305}.
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DR EMBL; D88674; BAA23593.1; -; mRNA.
DR EMBL; BT006858; AAP35504.1; -; mRNA.
DR EMBL; CR456745; CAG33026.1; -; mRNA.
DR EMBL; AP003354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471060; EAW91851.1; -; Genomic_DNA.
DR EMBL; BC013420; AAH13420.1; -; mRNA.
DR EMBL; BC019279; AAH19279.1; -; mRNA.
DR EMBL; AF070634; AAC25391.1; -; mRNA.
DR CCDS; CCDS6295.1; -.
DR RefSeq; NP_056962.2; NM_015878.5.
DR RefSeq; NP_680479.1; NM_148174.3.
DR RefSeq; XP_011515428.1; XM_011517126.1.
DR RefSeq; XP_011515429.1; XM_011517127.1.
DR PDB; 4ZGZ; X-ray; 5.81 A; A/C=2-437.
DR PDBsum; 4ZGZ; -.
DR AlphaFoldDB; O14977; -.
DR SMR; O14977; -.
DR BioGRID; 119621; 35.
DR IntAct; O14977; 15.
DR MINT; O14977; -.
DR STRING; 9606.ENSP00000337180; -.
DR iPTMnet; O14977; -.
DR PhosphoSitePlus; O14977; -.
DR BioMuta; AZIN1; -.
DR MassIVE; O14977; -.
DR MaxQB; O14977; -.
DR PaxDb; O14977; -.
DR PeptideAtlas; O14977; -.
DR PRIDE; O14977; -.
DR ProteomicsDB; 48351; -.
DR Antibodypedia; 26333; 194 antibodies from 23 providers.
DR DNASU; 51582; -.
DR Ensembl; ENST00000337198.10; ENSP00000337180.5; ENSG00000155096.15.
DR Ensembl; ENST00000347770.8; ENSP00000321507.4; ENSG00000155096.15.
DR Ensembl; ENST00000681985.1; ENSP00000506898.1; ENSG00000155096.15.
DR Ensembl; ENST00000682725.1; ENSP00000507451.1; ENSG00000155096.15.
DR Ensembl; ENST00000684566.1; ENSP00000506895.1; ENSG00000155096.15.
DR GeneID; 51582; -.
DR KEGG; hsa:51582; -.
DR MANE-Select; ENST00000337198.10; ENSP00000337180.5; NM_148174.4; NP_680479.1.
DR UCSC; uc003ykx.4; human.
DR CTD; 51582; -.
DR DisGeNET; 51582; -.
DR GeneCards; AZIN1; -.
DR HGNC; HGNC:16432; AZIN1.
DR HPA; ENSG00000155096; Low tissue specificity.
DR MIM; 607909; gene.
DR neXtProt; NX_O14977; -.
DR OpenTargets; ENSG00000155096; -.
DR PharmGKB; PA31887; -.
DR VEuPathDB; HostDB:ENSG00000155096; -.
DR eggNOG; KOG0622; Eukaryota.
DR GeneTree; ENSGT00950000182995; -.
DR HOGENOM; CLU_026444_1_1_1; -.
DR InParanoid; O14977; -.
DR OMA; FNGLYEM; -.
DR OrthoDB; 725914at2759; -.
DR PhylomeDB; O14977; -.
DR TreeFam; TF300760; -.
DR PathwayCommons; O14977; -.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR SignaLink; O14977; -.
DR BioGRID-ORCS; 51582; 47 hits in 1077 CRISPR screens.
DR ChiTaRS; AZIN1; human.
DR GeneWiki; AZIN1; -.
DR GenomeRNAi; 51582; -.
DR Pharos; O14977; Tbio.
DR PRO; PR:O14977; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O14977; protein.
DR Bgee; ENSG00000155096; Expressed in bronchial epithelial cell and 212 other tissues.
DR ExpressionAtlas; O14977; baseline and differential.
DR Genevisible; O14977; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042978; F:ornithine decarboxylase activator activity; IDA:UniProtKB.
DR GO; GO:0004586; F:ornithine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:1902269; P:positive regulation of polyamine transmembrane transport; IDA:UniProtKB.
DR GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IBA:GO_Central.
DR DisProt; DP02675; -.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR031178; Azin1.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022657; De-COase2_CS.
DR InterPro; IPR022644; De-COase2_N.
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:SF7; PTHR11482:SF7; 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; PS00879; ODR_DC_2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Polyamine biosynthesis; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..448
FT /note="Antizyme inhibitor 1"
FT /id="PRO_0000149992"
FT SITE 69
FT /note="Not modified"
FT /evidence="ECO:0000250|UniProtKB:O35484"
FT CONFLICT 20
FT /note="N -> D (in Ref. 1; BAA23593)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 448 AA; 49535 MW; DD26B22A993318E4 CRC64;
MKGFIDDANY SVGLLDEGTN LGNVIDNYVY EHTLTGKNAF FVGDLGKIVK KHSQWQNVVA
QIKPFYTVKC NSAPAVLEIL AALGTGFACS SKNEMALVQE LGVPPENIIY ISPCKQVSQI
KYAAKVGVNI LTCDNEIELK KIARNHPNAK VLLHIATEDN IGGEEGNMKF GTTLKNCRHL
LECAKELDVQ IIGVKFHVSS ACKESQVYVH ALSDARCVFD MAGEIGFTMN MLDIGGGFTG
TEFQLEEVNH VISPLLDIYF PEGSGVKIIS EPGSYYVSSA FTLAVNIIAK KVVENDKFPS
GVEKTGSDEP AFMYYMNDGV YGSFASKLSE DLNTIPEVHK KYKEDEPLFT SSLWGPSCDE
LDQIVESCLL PELNVGDWLI FDNMGADSFH EPSAFNDFQR PAIYYMMSFS DWYEMQDAGI
TSDSMMKNFF FVPSCIQLSQ EDSFSAEA
