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Database: UniProt
Entry: M3X894_FELCA
LinkDB: M3X894_FELCA
Original site: M3X894_FELCA 
ID   M3X894_FELCA            Unreviewed;       457 AA.
AC   M3X894;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Antizyme inhibitor 2 {ECO:0008006|Google:ProtNLM};
GN   Name=LOC101101148 {ECO:0000313|Ensembl:ENSFCAP00000022846.2};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000022846.2, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000022846.2, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000022846.2,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000022846.2, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000022846.2,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000022846.2}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000022846.2};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR600183-50};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       {ECO:0000256|RuleBase:RU003737}.
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DR   EMBL; AANG04003369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M3X894; -.
DR   STRING; 9685.ENSFCAP00000022846; -.
DR   PaxDb; 9685-ENSFCAP00000022846; -.
DR   Ensembl; ENSFCAT00000031674.3; ENSFCAP00000022846.2; ENSFCAG00000025357.3.
DR   eggNOG; KOG0622; Eukaryota.
DR   GeneTree; ENSGT00950000182995; -.
DR   HOGENOM; CLU_026444_1_2_1; -.
DR   InParanoid; M3X894; -.
DR   OMA; MNVIMEK; -.
DR   Proteomes; UP000011712; Chromosome C1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004586; F:ornithine decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IBA:GO_Central.
DR   CDD; cd00622; PLPDE_III_ODC; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
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; ARGININE/DIAMINOPIMELATE/ORNITHINE DECARBOXYLASE; 1.
DR   PANTHER; PTHR11482:SF57; GENE MODEL 853, (NCBI); 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; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011712}.
FT   DOMAIN          69..302
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          303..404
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        376
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         90
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   457 AA;  49671 MW;  DA1F800826D464CA CRC64;
     MEGSVEGSGT STPLGKPKES QGPPGSVWPK ELIALEPGES AWQVALKKIQ ELSDSDHRDP
     FMVADLGVLA SRHRAFCQAL PRVSPFYAVK CSSSVWVLRV LDTLGTGFDC ASQVEMDQVL
     GLGVAPSRII YANPCKPVSH IQYAARHGVR LLTFDSEEEL TKVAQHHPGA RLVLRLLTED
     SESIFPLSAK FGASLESCER LLKSARDLGL AVVGTSFHVG SNCRTPHSFR QAIADCRRVF
     EMGRAFGHDM SLLDIGGGFP GEAGCEPQFE EMARVINAAL AQDFPEGSGV EIIAEPGRFY
     AASVCMAAVN IIAKKAVLES GVWARGRRKL LYYLNDGHYG IFRLFLREPA PSMPIVVKEL
     CSDPPLFPCT LYGPTCDAFD KLFREEVQLP ELDVGDWLVF PSMGAYTSSM SSTFNGFPPA
     STYYAMEPEL RCLEGEGRDR PLRGSPQGLS SARGACG
//
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