AZIN1_MOUSE
ID AZIN1_MOUSE Reviewed; 448 AA.
AC O35484; Q542G5; Q8C2R8; Q8K1E5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Antizyme inhibitor 1;
DE Short=AZI;
DE AltName: Full=Ornithine decarboxylase antizyme inhibitor;
GN Name=Azin1; Synonyms=Oazi, Oazin;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=BALB/cJ;
RX PubMed=10698696; DOI=10.1042/bj3460699;
RA Nilsson J., Grahn B., Heby O.;
RT "Antizyme inhibitor is rapidly induced in growth-stimulated mouse
RT fibroblasts and releases ornithine decarboxylase from antizyme
RT suppression.";
RL Biochem. J. 346:699-704(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spinal cord, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP FUNCTION.
RX PubMed=16916800; DOI=10.1074/jbc.m602840200;
RA Lopez-Contreras A.J., Lopez-Garcia C., Jimenez-Cervantes C., Cremades A.,
RA Penafiel R.;
RT "Mouse ornithine decarboxylase-like gene encodes an antizyme inhibitor
RT devoid of ornithine and arginine decarboxylating activity.";
RL J. Biol. Chem. 281:30896-30906(2006).
RN [5]
RP FUNCTION, INTERACTION WITH OAZ1 AND OAZ3, AND UBIQUITINATION.
RX PubMed=18062773; DOI=10.1042/bj20071423;
RA Snapir Z., Keren-Paz A., Bercovich Z., Kahana C.;
RT "ODCp, a brain- and testis-specific ornithine decarboxylase paralogue,
RT functions as an antizyme inhibitor, although less efficiently than AzI1.";
RL Biochem. J. 410:613-619(2008).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18508777; DOI=10.1074/jbc.m801024200;
RA Lopez-Contreras A.J., Ramos-Molina B., Cremades A., Penafiel R.;
RT "Antizyme inhibitor 2 (AZIN2/ODCp) stimulates polyamine uptake in mammalian
RT cells.";
RL J. Biol. Chem. 283:20761-20769(2008).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=18973822; DOI=10.1016/j.biocel.2008.09.029;
RA Lopez-Contreras A.J., Ramos-Molina B., Martinez-de-la-Torre M.,
RA Penafiel-Verdu C., Puelles L., Cremades A., Penafiel R.;
RT "Expression of antizyme inhibitor 2 in male haploid germinal cells suggests
RT a role in spermiogenesis.";
RL Int. J. Biochem. Cell Biol. 41:1070-1078(2009).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=19449338; DOI=10.1002/jcb.22168;
RA Lopez-Contreras A.J., Sanchez-Laorden B.L., Ramos-Molina B.,
RA de la Morena M.E., Cremades A., Penafiel R.;
RT "Subcellular localization of antizyme inhibitor 2 in mammalian cells:
RT Influence of intrinsic sequences and interaction with antizymes.";
RL J. Cell. Biochem. 107:732-740(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), LACK OF PYRIDOXAL PHOSPHATE
RP BINDING, SUBUNIT, AND FUNCTION.
RX PubMed=18369191; DOI=10.1110/ps.073427208;
RA Albeck S., Dym O., Unger T., Snapir Z., Bercovich Z., Kahana C.;
RT "Crystallographic and biochemical studies revealing the structural basis
RT for antizyme inhibitor function.";
RL Protein Sci. 17:793-802(2008).
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:16916800, PubMed:18062773,
CC PubMed:18508777). Inhibits antizyme-dependent ODC degradation and
CC releases ODC monomers from their inactive complex with antizymes,
CC leading to formation of the catalytically active ODC homodimer and
CC restoring polyamine production (PubMed:10698696, PubMed:18062773,
CC PubMed:18369191). {ECO:0000269|PubMed:10698696,
CC ECO:0000269|PubMed:16916800, ECO:0000269|PubMed:18062773,
CC ECO:0000269|PubMed:18369191, ECO:0000269|PubMed:18508777}.
CC -!- SUBUNIT: Monomer (PubMed:18369191). Interacts with OAZ1 and OAZ3; this
CC interaction disrupts the interaction between the antizyme and ODC1
CC (PubMed:18062773, PubMed:18369191). {ECO:0000269|PubMed:18062773,
CC ECO:0000269|PubMed:18369191}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19449338}.
CC -!- TISSUE SPECIFICITY: Expressed during testis development.
CC {ECO:0000269|PubMed:18508777, ECO:0000269|PubMed:18973822}.
CC -!- PTM: Ubiquitinated, leading to its proteasomal degradation; a process
CC that is reduced in presence of antizyme OAZ1.
CC {ECO:0000269|PubMed:18062773}.
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; AF032128; AAB87464.1; -; mRNA.
DR EMBL; AK049680; BAC33870.1; -; mRNA.
DR EMBL; AK088112; BAC40151.1; -; mRNA.
DR EMBL; AK088671; BAC40494.1; -; mRNA.
DR EMBL; BC019412; AAH19412.1; -; mRNA.
DR EMBL; BC043722; AAH43722.1; -; mRNA.
DR CCDS; CCDS37065.1; -.
DR RefSeq; NP_001095928.1; NM_001102458.1.
DR RefSeq; NP_001288617.1; NM_001301688.1.
DR RefSeq; NP_061215.1; NM_018745.5.
DR PDB; 3BTN; X-ray; 2.05 A; A/B=1-448.
DR PDBsum; 3BTN; -.
DR AlphaFoldDB; O35484; -.
DR SMR; O35484; -.
DR STRING; 10090.ENSMUSP00000065544; -.
DR iPTMnet; O35484; -.
DR PhosphoSitePlus; O35484; -.
DR PaxDb; O35484; -.
DR PRIDE; O35484; -.
DR ProteomicsDB; 273643; -.
DR Antibodypedia; 26333; 194 antibodies from 23 providers.
DR DNASU; 54375; -.
DR Ensembl; ENSMUST00000065308; ENSMUSP00000065544; ENSMUSG00000037458.
DR Ensembl; ENSMUST00000110329; ENSMUSP00000105958; ENSMUSG00000037458.
DR GeneID; 54375; -.
DR KEGG; mmu:54375; -.
DR UCSC; uc007vns.1; mouse.
DR CTD; 51582; -.
DR MGI; MGI:1859169; Azin1.
DR VEuPathDB; HostDB:ENSMUSG00000037458; -.
DR eggNOG; KOG0622; Eukaryota.
DR GeneTree; ENSGT00950000182995; -.
DR InParanoid; O35484; -.
DR OMA; FNGLYEM; -.
DR OrthoDB; 725914at2759; -.
DR PhylomeDB; O35484; -.
DR TreeFam; TF300760; -.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR BioGRID-ORCS; 54375; 12 hits in 72 CRISPR screens.
DR ChiTaRS; Azin1; mouse.
DR EvolutionaryTrace; O35484; -.
DR PRO; PR:O35484; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; O35484; protein.
DR Bgee; ENSMUSG00000037458; Expressed in fetal liver hematopoietic progenitor cell and 251 other tissues.
DR ExpressionAtlas; O35484; baseline and differential.
DR Genevisible; O35484; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042978; F:ornithine decarboxylase activator activity; IGI:MGI.
DR GO; GO:0004586; F:ornithine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0006595; P:polyamine metabolic process; TAS:MGI.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; ISO:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
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; DP02672; -.
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_0000149993"
FT SITE 69
FT /note="Not modified"
FT /evidence="ECO:0000269|PubMed:18369191,
FT ECO:0007744|PDB:3BTN"
FT CONFLICT 36
FT /note="G -> E (in Ref. 3; AAH19412)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="S -> G (in Ref. 2; BAC40151)"
FT /evidence="ECO:0000305"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:3BTN"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:3BTN"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:3BTN"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:3BTN"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:3BTN"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:3BTN"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:3BTN"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 207..224
FT /evidence="ECO:0007829|PDB:3BTN"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 242..259
FT /evidence="ECO:0007829|PDB:3BTN"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:3BTN"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:3BTN"
FT STRAND 281..292
FT /evidence="ECO:0007829|PDB:3BTN"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:3BTN"
FT TURN 320..324
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:3BTN"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:3BTN"
FT STRAND 363..371
FT /evidence="ECO:0007829|PDB:3BTN"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:3BTN"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 409..417
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:3BTN"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:3BTN"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:3BTN"
SQ SEQUENCE 448 AA; 49549 MW; 117F3C2C24DDCA0F CRC64;
MKGFIDDANY SVGLLDEGTN LGNVIDNYVY EHTLTGKNAF FVGDLGKIVK KHSQWQTVVA
QIKPFYTVKC NSTPAVLEIL AALGTGFACS SKNEMALVQE LGVSPENIIF TSPCKQVSQI
KYAAKVGVNI MTCDNEIELK KIARNHPNAK VLLHIATEDN IGGEDGNMKF GTTLKNCRHL
LECAKELDVQ IIGVKFHVSS ACKEYQVYVH ALSDARCVFD MAGEFGFTMN MLDIGGGFTG
TEIQLEEVNH VISPLLDIYF PEGSGIQIIS EPGSYYVSSA FTLAVNIIAK KVVENDKFSS
GVEKNGSDEP AFVYYMNDGV YGSFASKLSE DLNTIPEVHK KYKEDEPLFT SSLWGPSCDE
LDQIVESCLL PELNVGDWLI FDNMGADSFH EPSAFNDFQR PAIYFMMSFS DWYEMQDAGI
TSDAMMKNFF FAPSCIQLSQ EDSFSTEA
