ID   AZIN1_PONAB             Reviewed;         448 AA.
AC   Q5R7K3;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Antizyme inhibitor 1;
DE            Short=AZI;
DE   AltName: Full=Ornithine decarboxylase antizyme inhibitor;
GN   Name=AZIN1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Inhibits antizyme-dependent ODC
CC       degradation and releases ODC monomers from their inactive complex with
CC       antizymes, leading to formation of the catalytically active ODC
CC       homodimer and restoring polyamine production.
CC       {ECO:0000250|UniProtKB:O14977, ECO:0000250|UniProtKB:O35484}.
CC   -!- SUBUNIT: Monomer. Interacts with OAZ1 and OAZ3; this interaction
CC       disrupts the interaction between the antizyme and ODC1.
CC       {ECO:0000250|UniProtKB:O14977, ECO:0000250|UniProtKB:O35484}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- PTM: Ubiquitinated, leading to its proteasomal degradation; a process
CC       that is reduced in presence of antizyme OAZ1. {ECO:0000250}.
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; CR860112; CAH92257.1; -; mRNA.
DR   RefSeq; NP_001126321.2; NM_001132849.2.
DR   AlphaFoldDB; Q5R7K3; -.
DR   SMR; Q5R7K3; -.
DR   GeneID; 100173300; -.
DR   KEGG; pon:100173300; -.
DR   CTD; 51582; -.
DR   InParanoid; Q5R7K3; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0042978; F:ornithine decarboxylase activator activity; ISS:UniProtKB.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Nucleus; Polyamine biosynthesis; Reference proteome; Ubl conjugation.
FT   CHAIN           1..448
FT                   /note="Antizyme inhibitor 1"
FT                   /id="PRO_0000239256"
FT   SITE            69
FT                   /note="Not modified"
FT                   /evidence="ECO:0000250|UniProtKB:O35484"
SQ   SEQUENCE   448 AA;  49568 MW;  BF04CD04890E5D4E CRC64;
     MKGFIDDVDY SVGLLDEGTN LGNVIDNYVY EHTLTGKNAF FVGDLGKIVK KHSQWQNVVA
     QIKPFYTVKC NSAPAVLEIL AALGTGFACS SKNEMALVQE LGVPPENIIY ISPCKQVSQI
     KYAAKVGVNI MTCDNEIELK KIARNHPNAK VLLHIATEDN IGGEEGNMKF GTTLKNCRHL
     LECAKELDVQ IIGVKFHVSS ACKESQVYVH ALSDARCVFD MAGEIGFTMN MLDIGGGFTG
     TEFQLEEVNH VISPLLDVYF PEGSGVKIIS EPGSYYVSSA FTLAVNIIAK KVVENDKFPS
     GVEKTGSDEP AFMYYMNDGV YGSFASKLSE DLNTIPEVHK KYKEDEPLFT SSLWGPSCDE
     LDQIVESCLL PELNVGDWLI FDNMGADSFH EPSAFNDFQR PAIYYMMSFS DWYEMQDAGI
     TSDSMMKNFF FVPSCIQLSQ EDSFSAEA