ID   MIM1_CHICK              Reviewed;         326 AA.
AC   P08940;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Myeloid protein 1;
DE   AltName: Full=p33;
DE   Flags: Precursor;
GN   Name=MIM1; Synonyms=MIM-1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND
RP   INDUCTION BY THE MYB ONCOGENE.
RX   PubMed=2688896; DOI=10.1016/0092-8674(89)90767-8;
RA   Ness S.A., Marknell A., Graf T.;
RT   "The v-myb oncogene product binds to and activates the promyelocyte-
RT   specific mim-1 gene.";
RL   Cell 59:1115-1125(1989).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, NUCLEOTIDE SEQUENCE [MRNA] OF 295-299, AND PTM.
RC   STRAIN=White leghorn;
RX   PubMed=1397316; DOI=10.1016/0014-5793(92)81102-r;
RA   Yamada K., Tsuchiya M., Mishima K., Shimoyama M.;
RT   "p33, an endogenous target protein for arginine-specific ADP-
RT   ribosyltransferase in chicken polymorphonuclear leukocytes, is highly
RT   homologous to mim-1 protein (myb-induced myeloid protein-1).";
RL   FEBS Lett. 311:203-205(1992).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:2688896}.
CC       Note=Granules of promyelocytes. {ECO:0000269|PubMed:2688896}.
CC   -!- INDUCTION: By the Myb oncogene. {ECO:0000269|PubMed:2688896}.
CC   -!- PTM: Substrate for arginine-specific ADP-ribosyltransferase.
CC       {ECO:0000269|PubMed:1397316}.
CC   -!- SIMILARITY: Belongs to the LECT2/MIM-1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M29448; AAA48954.1; -; Genomic_DNA.
DR   EMBL; M29449; AAA48958.1; -; mRNA.
DR   PIR; A33755; A33755.
DR   AlphaFoldDB; P08940; -.
DR   SMR; P08940; -.
DR   STRING; 9031.ENSGALP00000010210; -.
DR   PaxDb; P08940; -.
DR   VEuPathDB; HostDB:geneid_396471; -.
DR   eggNOG; ENOG502S16D; Eukaryota.
DR   InParanoid; P08940; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0044194; C:cytolytic granule; IDA:AgBase.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030851; P:granulocyte differentiation; IEP:AgBase.
DR   GO; GO:0046677; P:response to antibiotic; IDA:AgBase.
DR   Gene3D; 2.70.70.10; -; 2.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR008663; LECT2.
DR   PANTHER; PTHR11329; PTHR11329; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Metal-binding;
KW   Reference proteome; Repeat; Signal; Zinc.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250|UniProtKB:O62644"
FT   CHAIN           19..326
FT                   /note="Myeloid protein 1"
FT                   /id="PRO_0000017366"
FT   REPEAT          28..162
FT                   /note="1"
FT                   /evidence="ECO:0000305"
FT   REPEAT          177..312
FT                   /note="2"
FT                   /evidence="ECO:0000305"
FT   REGION          307..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O14960"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O14960"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O14960"
FT   DISULFID        37..74
FT                   /evidence="ECO:0000250|UniProtKB:O14960"
FT   DISULFID        48..53
FT                   /evidence="ECO:0000250|UniProtKB:O14960"
FT   DISULFID        113..156
FT                   /evidence="ECO:0000250|UniProtKB:O14960"
FT   CONFLICT        297
FT                   /note="I -> Y (in Ref. 1; AAA48954/AAA48958)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   326 AA;  35637 MW;  B8C4742EF0D3BAD3 CRC64;
     MPALSLIALL SLVSTAFARQ WEVHPPQQQG RHWAQICSGN PFNRIRGCDR YGCGNYGASR
     QGKGEKHKGV DVICTDGSIV YAPFSGQLSG PIRFFHNGNA IDDGVQISGS GYCVKLVCIH
     PIRYHGQIQK GQQLGRMLPM QKVFPGIVSH IHVENCDQSD PTHLLRPIPD ISPPFPQQDA
     HWAVVCAGNP TNEIRGCDKY GCGYFGAPRR NGKGEKHKGV DVICADGATV YAPFSGELSG
     PVKFFHNGNA IDDGVQIRGS GFCVKLLCIH PIRYNGRISK GQVLGRMLPM QRVFPGIISH
     IHVENCDRSD PTSNLERGKG ESEMEV