ID   AZIN1_RAT               Reviewed;         448 AA.
AC   Q63764;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=Antizyme inhibitor 1;
DE            Short=AZI;
DE   AltName: Full=Ornithine decarboxylase antizyme inhibitor;
GN   Name=Azin1; Synonyms=Oazi, Oazin;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Heart;
RX   PubMed=8631929; DOI=10.1074/jbc.271.7.3340;
RA   Murakami Y., Ichiba T., Matsufuji S., Hayashi S.;
RT   "Cloning of antizyme inhibitor, a highly homologous protein to ornithine
RT   decarboxylase.";
RL   J. Biol. Chem. 271:3340-3342(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar;
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   [3]
RP   SUBUNIT.
RX   PubMed=2713421; DOI=10.1016/0304-4165(89)90026-3;
RA   Kitani T., Fujisawa H.;
RT   "Purification and characterization of antizyme inhibitor of ornithine
RT   decarboxylase from rat liver.";
RL   Biochim. Biophys. Acta 991:44-49(1989).
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 (PubMed:2713421). Interacts with OAZ1 and OAZ3; this
CC       interaction disrupts the interaction between the antizyme and ODC1 (By
CC       similarity). {ECO:0000250|UniProtKB:O14977,
CC       ECO:0000250|UniProtKB:O35484, ECO:0000269|PubMed:2713421}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in various tissues including liver, heart
CC       and kidney.
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; D50734; BAA09365.1; -; mRNA.
DR   EMBL; D89983; BAA23594.1; -; mRNA.
DR   AlphaFoldDB; Q63764; -.
DR   SMR; Q63764; -.
DR   STRING; 10116.ENSRNOP00000007999; -.
DR   PaxDb; Q63764; -.
DR   UCSC; RGD:61934; rat.
DR   RGD; 61934; Azin1.
DR   eggNOG; KOG0622; Eukaryota.
DR   InParanoid; Q63764; -.
DR   PhylomeDB; Q63764; -.
DR   Reactome; R-RNO-350562; Regulation of ornithine decarboxylase (ODC).
DR   PRO; PR:Q63764; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0042978; F:ornithine decarboxylase activator activity; ISS:UniProtKB.
DR   GO; GO:0004586; F:ornithine decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0044849; P:estrous cycle; IEP:RGD.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:RGD.
DR   GO; GO:0010825; P:positive regulation of centrosome duplication; IMP:RGD.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:RGD.
DR   GO; GO:1902269; P:positive regulation of polyamine transmembrane transport; ISO:RGD.
DR   GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IBA:GO_Central.
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   Nucleus; Polyamine biosynthesis; Reference proteome; Ubl conjugation.
FT   CHAIN           1..448
FT                   /note="Antizyme inhibitor 1"
FT                   /id="PRO_0000149994"
FT   SITE            69
FT                   /note="Not modified"
FT                   /evidence="ECO:0000250|UniProtKB:O35484"
SQ   SEQUENCE   448 AA;  49333 MW;  B9A630098ECBA5DB CRC64;
     MKGFIDDANY SVGLLDEGTN LGNVIDNYVY EHTLTGKNAF FVGDLGKIVK KHSQWQNVVA
     QIKPFYMVKC NSTPAVLEIL AALGTGFACS TKNEMALVQE LGVSPENIIY TSPCKQASQI
     KYAAKVGVNI MTCDNEVELK KIARNHPNAK VLLHIATEDN IGGEDGNMKF GTTLKNCRHL
     LECAKELDVQ IIGVKFHISS ACKEYQVYVH ALSDARCVFD MAGEFGFTMN MLDIGGGFTG
     TEIQLEEVNH VISPLLDIYF PEGSGIQIIS EPGSYYVSSA FTLAVNIIAK KVVENDKLSS
     GVEKNGSDEP AFVYYMNDGV YGSFASKLSE DLNTVPEVHK KYKEDEPLFT SSLWGPSCDE
     LDQIVESCLL PELSVGDWLI FDNMGADSLH GPSAFSDTQR PAIYFMMSLS DWYEMQDAGI
     TSDAMMKNFF FAPSCIQLSQ EDNFSTEA