ID   ARMC9_BOVIN             Reviewed;         665 AA.
AC   Q2KI89;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=LisH domain-containing protein ARMC9;
GN   Name=ARMC9;
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=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in ciliogenesis. It is required for appropriate
CC       acetylation and polyglutamylation of ciliary microtubules, and
CC       regulation of cilium length (By similarity). Acts as a positive
CC       regulator of hedgehog (Hh)signaling (By similarity). May participate in
CC       the trafficking and/or retention of GLI2 and GLI3 proteins at the
CC       ciliary tip (By similarity). {ECO:0000250|UniProtKB:E7F187,
CC       ECO:0000250|UniProtKB:Q7Z3E5, ECO:0000250|UniProtKB:Q9D2I5}.
CC   -!- SUBUNIT: Interacts with TOGARAM1, CCDC66, CEP104, CSPP1 and CEP290.
CC       {ECO:0000250|UniProtKB:Q7Z3E5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000250|UniProtKB:Q7Z3E5}. Cell projection, cilium
CC       {ECO:0000250|UniProtKB:Q9D2I5}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriole
CC       {ECO:0000250|UniProtKB:Q7Z3E5}. Note=Localized to the proximal region
CC       in cilia. Stimulation of Hh signaling leads to redistribution of ARMC9
CC       toward the ciliary tip within 6 hours, follow by a gradual return to
CC       its original proximal location (By similarity). Localizes to the
CC       daughter centriole of the primary cilium in RPE1 cells (By similarity).
CC       {ECO:0000250|UniProtKB:Q7Z3E5, ECO:0000250|UniProtKB:Q9D2I5}.
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; BC112726; AAI12727.1; -; mRNA.
DR   RefSeq; NP_001039883.1; NM_001046418.2.
DR   AlphaFoldDB; Q2KI89; -.
DR   SMR; Q2KI89; -.
DR   STRING; 9913.ENSBTAP00000024631; -.
DR   PaxDb; Q2KI89; -.
DR   PRIDE; Q2KI89; -.
DR   GeneID; 536462; -.
DR   KEGG; bta:536462; -.
DR   CTD; 80210; -.
DR   eggNOG; ENOG502QQ9W; Eukaryota.
DR   HOGENOM; CLU_007962_1_0_1; -.
DR   InParanoid; Q2KI89; -.
DR   OrthoDB; 1327587at2759; -.
DR   TreeFam; TF317676; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR   GO; GO:0097542; C:ciliary tip; ISS:UniProtKB.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR040369; ARMC9.
DR   InterPro; IPR006594; LisH.
DR   PANTHER; PTHR14881; PTHR14881; 1.
DR   SMART; SM00667; LisH; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS50896; LISH; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Phosphoprotein; Reference proteome.
FT   CHAIN           1..665
FT                   /note="LisH domain-containing protein ARMC9"
FT                   /id="PRO_0000280594"
FT   DOMAIN          7..39
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   REGION          582..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          204..235
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        582..599
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         582
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3E5"
SQ   SEQUENCE   665 AA;  75764 MW;  8082A9E98B4A0EE2 CRC64;
     MVDVLAHESE LLGLVKEYLD FAEFEDTLKT FLKECKIKGK PLSKSTCGSL RDPKSLKFQR
     DLLAAFDSGD QKVFFRLWEE HIPRPIRDGD SLAQKLEFYL HIHFAIYLLK HSAGRPDKED
     LDERISYFKT FLETKGAALS QTTEFLPFYA LPFVPNPMAH PSFKELFQDS WTSELKLKLE
     KFLALMFKAS NTPKLLTLYK ENGQSNKDVL QQLHQQLVEA ERRSMTYLKR YNRIQADYHN
     LIGVTAELVD SLEATVSGKM ITPEYLQSVC VRLFSNQMRQ SLAHSVDFTR PGTASTMLRA
     SLAPVKLKDV PLLPSLDYEK LKKDLILGSD RLKAFLLQAL RWRLTTSHPG EQRETVLQAY
     ISNDLLDCHS HSQRSVLQLL QSKSEVVRQY TARLINAFAS LAEGRRYLAQ STKVLRMLEE
     RLKEEDKDVI TRENVLGALQ KFSLRRPLQT AMIQDGLIFW LIDILKEPDC LSDYTLEYSV
     ALLMNLCLRS AGKNMCAKVA GLVLKVLSDL LGHENHEIQP YVNGALYSIL SIPSIREEAR
     AMGMEDILRC FIKEGNAEMI RQIEFIIKQL NAEELLDGVL ESDDDEDEDD EEDHDTMEAD
     LDKDELIQPQ LGELSGEKLL TTEYLGIMTN TGKARRRGTA GVQWGGPEPL RRPVTPGGHR
     TGYPA