ID   ANKY2_BOVIN             Reviewed;         442 AA.
AC   Q0VCS9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Ankyrin repeat and MYND domain-containing protein 2;
GN   Name=ANKMY2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the trafficking of signaling proteins to
CC       the cilia. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the retinal-specific guanylyl cyclase GC1.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250}.
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DR   EMBL; BC120022; AAI20023.1; -; mRNA.
DR   RefSeq; NP_001068852.1; NM_001075384.2.
DR   RefSeq; XP_005205233.1; XM_005205176.3.
DR   AlphaFoldDB; Q0VCS9; -.
DR   SMR; Q0VCS9; -.
DR   STRING; 9913.ENSBTAP00000014576; -.
DR   PaxDb; Q0VCS9; -.
DR   PRIDE; Q0VCS9; -.
DR   Ensembl; ENSBTAT00000014576; ENSBTAP00000014576; ENSBTAG00000010980.
DR   GeneID; 509032; -.
DR   KEGG; bta:509032; -.
DR   CTD; 57037; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010980; -.
DR   VGNC; VGNC:25906; ANKMY2.
DR   eggNOG; KOG1710; Eukaryota.
DR   GeneTree; ENSGT00390000016820; -.
DR   HOGENOM; CLU_048951_0_0_1; -.
DR   InParanoid; Q0VCS9; -.
DR   OMA; AFKYHYL; -.
DR   OrthoDB; 1413951at2759; -.
DR   TreeFam; TF351374; -.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000010980; Expressed in prostate gland and 106 other tissues.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
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..442
FT                   /note="Ankyrin repeat and MYND domain-containing protein 2"
FT                   /id="PRO_0000263083"
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          401..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..422
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   442 AA;  49408 MW;  F4F35CD99A55A967 CRC64;
     MVHIKKGELT QEEKELLEVI GKGTVQEAGT LLGSKNVRVN CLDENGMTPL MHAAYKGKLD
     MCKLLLRHGA DVNCHQHEHG YTALMFAALS GNKDITWVML EAGAETDVVN SVGRTAAQMA
     AFVGQHDCVT IINNFFPREK LDYYTKPQGL DKEPKLPPKL AGPLHKIITT TNLHPVKIVM
     LINENPLLAE EAALNKCYKV MDLICEKCMK QRDMNEVLAM KMHYISCIFQ KCINFLKDRE
     NKLDTLIKSL LKGRASDGFP VYQEKIIRES IRKFPYCEAT LLQQLVRSIA PVEIGSDPTA
     FSVLTQAITG QVGFVDVEFC TTCGEKGASK RCSVCKMVIY CDQTCQKTHW FAHKKICKNL
     KDIYEKQQLE AAKAKSEEEN NSKLDVNSNC VGEERLEEAE TRICQKNDNP KDSEEGEKES
     LQSDAGLEGL QEAAVGPQVS EE