ID   ANKY2_CHICK             Reviewed;         460 AA.
AC   Q5ZMD2;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Ankyrin repeat and MYND domain-containing protein 2;
GN   Name=ANKMY2; ORFNames=RCJMB04_2i2;
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 [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: May be involved in the trafficking of signaling proteins to
CC       the cilia. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250}.
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; AJ719452; CAG31111.1; -; mRNA.
DR   RefSeq; NP_001026150.1; NM_001030979.1.
DR   AlphaFoldDB; Q5ZMD2; -.
DR   SMR; Q5ZMD2; -.
DR   STRING; 9031.ENSGALP00000017545; -.
DR   PaxDb; Q5ZMD2; -.
DR   GeneID; 420593; -.
DR   KEGG; gga:420593; -.
DR   CTD; 57037; -.
DR   VEuPathDB; HostDB:geneid_420593; -.
DR   eggNOG; KOG1710; Eukaryota.
DR   InParanoid; Q5ZMD2; -.
DR   OrthoDB; 1413951at2759; -.
DR   PhylomeDB; Q5ZMD2; -.
DR   PRO; PR:Q5ZMD2; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR002893; Znf_MYND.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SMART; SM00248; ANK; 3.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; Cell projection; Cilium; Metal-binding; Reference proteome;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..460
FT                   /note="Ankyrin repeat and MYND domain-containing protein 2"
FT                   /id="PRO_0000247168"
FT   REPEAT          45..74
FT                   /note="ANK 1"
FT   REPEAT          79..108
FT                   /note="ANK 2"
FT   REPEAT          159..188
FT                   /note="ANK 3"
FT   ZN_FING         320..357
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   REGION          371..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..438
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         320
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         332
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         335
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         341
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         345
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         357
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
SQ   SEQUENCE   460 AA;  51649 MW;  F9C722617C2F62BE CRC64;
     MAPPRKGELS PEEKDLLGVI AKGNVEEAGR LLGSKNVHVN CLDEHGMTPL MHAAYKGKVD
     MCRLLLRHGA DVNCNEHEHG YTALMFAGLS GNKEITWMML EAGAETDVVN SVGRTAAQMA
     AFVGQHDCVT IINNFFPRER LDYYTKPQGL DKEPKLPVKL AGPLHKIITT TNMHPVKIVL
     LVKENPLLAE VEALQKCYRV LDLICEKCMK QKDMNEVLAM KMHYISCIFQ KCVTFLKERE
     DKLDGFIKSL LKGRDKDGFP VYQEKLIRES IRKFPYCEAT LLQQLVRSIA PVELGSDPTA
     FSVLTQAITG QVGFVDAEFC TTCGEKGADK RCSVCKVVMY CDQNCQKTHW FTHKKVCKTL
     KEIHEKQELE AAKEKRRQEK KQKKDEAQLE EAGATSEEQS APGPDATKEA DPNLWIQTDQ
     TEETELTKEP EARAPRPDSP LESETALADI ALQKIQDSEE