AZIN2_XENLA
ID AZIN2_XENLA Reviewed; 456 AA.
AC Q9I8S4;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Antizyme inhibitor 2;
DE Short=AzI2;
DE AltName: Full=Ornithine decarboxylase 2;
DE Short=ODC 2;
DE Short=xODC2;
DE AltName: Full=Ornithine decarboxylase-like protein;
DE Short=ODC-like protein;
DE AltName: Full=ornithine decarboxylase paralog;
DE Short=ODC-p;
GN Name=azin2; Synonyms=azi2, odc1-b, odc2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=11287202; DOI=10.1016/s0925-4773(01)00295-7;
RA Cao Y., Zhao H., Hollemann T., Chen Y., Grunz H.;
RT "Tissue-specific expression of an ornithine decarboxylase paralogue, XODC2,
RT in Xenopus laevis.";
RL Mech. Dev. 102:243-246(2001).
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 antizyme (AZ) on ODC activity by competing with ODC for
CC antizyme-binding. 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. Participates in the morphological
CC integrity of the trans-Golgi network (TGN) and functions as a regulator
CC of intracellular secretory vesicle trafficking.
CC {ECO:0000250|UniProtKB:Q8BVM4, ECO:0000250|UniProtKB:Q96A70}.
CC -!- SUBUNIT: Monomer. Interacts with OAZ1; this interaction disrupts the
CC interaction between the antizyme and ODC1. Does not form a heterodimer
CC with ODC1. {ECO:0000250|UniProtKB:Q8BVM4,
CC ECO:0000250|UniProtKB:Q96A70}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:D4A693}. Cytoplasm
CC {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Membrane
CC {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Endoplasmic
CC reticulum-Golgi intermediate compartment {ECO:0000250}. Golgi
CC apparatus, cis-Golgi network {ECO:0000250}. Golgi apparatus, trans-
CC Golgi network {ECO:0000250}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:D4A693}. Cell projection, axon {ECO:0000250}.
CC Cell projection, dendrite {ECO:0000250}. Perikaryon {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected at the animal pole at
CC stage 9. During neurula stages it is found both in the extreme anterior
CC and posterior part of the dorsal body axis. In tailbud stages the
CC expression is further shifted to both the tail and head areas and
CC gradually restricted to distinct tissues: forebrain, inner layer of
CC epidermis of the head area, stomodeal-hypophyseal anlage, frontal
CC gland, ear vesicle, branchial arches, the front tip of neural tube and
CC proctodeum. {ECO:0000269|PubMed:11287202}.
CC -!- DOMAIN: The N-terminus domain is necessary for its localization to the
CC ER-Golgi intermediate compartment (ERGIC).
CC {ECO:0000250|UniProtKB:Q8BVM4}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC ODC antizyme inhibitor subfamily. {ECO:0000305}.
CC -!- CAUTION: Human ortholog was initially reported to have ornithine
CC decarboxylase or arginine decarboxylase activities, but it was later
CC found that the mouse ortholog does not possess either of them.
CC {ECO:0000305}.
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DR EMBL; AF217544; AAF27628.2; -; mRNA.
DR RefSeq; NP_001079692.1; NM_001086223.1.
DR AlphaFoldDB; Q9I8S4; -.
DR SMR; Q9I8S4; -.
DR DNASU; 379379; -.
DR GeneID; 379379; -.
DR KEGG; xla:379379; -.
DR CTD; 379379; -.
DR Xenbase; XB-GENE-6493979; azin2.S.
DR OrthoDB; 725914at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 379379; Expressed in testis and 19 other tissues.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; ISS:UniProtKB.
DR GO; GO:1990005; C:granular vesicle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; ISS:UniProtKB.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0042978; F:ornithine decarboxylase activator activity; ISS:UniProtKB.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
DR GO; GO:1902269; P:positive regulation of polyamine transmembrane transport; ISS:UniProtKB.
DR GO; GO:0098629; P:trans-Golgi network membrane organization; ISS:UniProtKB.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR031173; Azin2.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022657; De-COase2_CS.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR022653; De-COase2_pyr-phos_BS.
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:SF4; PTHR11482:SF4; 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; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cytoplasm; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW Nucleus; Polyamine biosynthesis; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..456
FT /note="Antizyme inhibitor 2"
FT /id="PRO_0000149897"
FT ACT_SITE 357
FT /note="Proton donor; shared with dimeric partner"
FT /evidence="ECO:0000250"
FT SITE 68
FT /note="Not modified"
FT /evidence="ECO:0000250|UniProtKB:O35484"
SQ SEQUENCE 456 AA; 50637 MW; 78A0BFBC6FED27FE CRC64;
MQGYIQESDF NLVEEGFLAR DLMEEIINEV SQTEDRDAFF VADLGDVVRK HLRFLKALPR
VKPFYAVKCN SSKGVVKILA ELGAGFDCAS KTEIELVQDV GVAPERIIYA NPCKQISQIK
YAAKNGVQMM TFDNEVELSK VSRSHPNARM VLRIATDDSK SSARLSVKFG APLKSCRRLL
EMAKNLSVDV IGVSFHVGSG CTDSKAYTQA ISDARLVFEM ASEFGYKMWL LDIGGGFPGT
EDSKIRFEEI AGVINPALDM YFPESSDVQI IAEPGRYYVA SAFSLAVNVI AKKEVEHSVS
DDEENESSKS IMYYVNDGVY GSFNCLVFDH AHPKPILHKK PSPDQPLYTS SLWGPTCDGL
DQIAERVQLP ELHVGDWLLF ENMGAYTIAA SSNFNGFQQS PVHYAMPRAA WKAVQLLQRG
LQQTEEKENV CTPMSCGWEI SDSLCFTRTF AATSII
