ID   ARMC9_XENTR             Reviewed;         808 AA.
AC   A0JMA8;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=LisH domain-containing protein ARMC9;
GN   Name=armc9;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=N6; TISSUE=Oviduct;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-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).
CC       {ECO:0000250|UniProtKB:E7F187, ECO:0000250|UniProtKB:Q7Z3E5,
CC       ECO:0000250|UniProtKB:Q9D2I5}.
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}.
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DR   EMBL; BC125807; AAI25808.1; -; mRNA.
DR   RefSeq; NP_001090642.1; NM_001097173.1.
DR   AlphaFoldDB; A0JMA8; -.
DR   SMR; A0JMA8; -.
DR   STRING; 8364.ENSXETP00000021038; -.
DR   PaxDb; A0JMA8; -.
DR   GeneID; 100036614; -.
DR   KEGG; xtr:100036614; -.
DR   CTD; 80210; -.
DR   Xenbase; XB-GENE-990021; armc9.
DR   eggNOG; ENOG502QQ9W; Eukaryota.
DR   HOGENOM; CLU_007962_1_0_1; -.
DR   InParanoid; A0JMA8; -.
DR   OMA; ALIFKAN; -.
DR   OrthoDB; 1327587at2759; -.
DR   TreeFam; TF317676; -.
DR   Proteomes; UP000008143; Chromosome 5.
DR   Proteomes; UP000790000; 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   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; Reference proteome.
FT   CHAIN           1..808
FT                   /note="LisH domain-containing protein ARMC9"
FT                   /id="PRO_0000280600"
FT   DOMAIN          7..39
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   REGION          576..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          650..709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          742..808
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          196..230
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        577..599
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..709
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..808
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   808 AA;  91819 MW;  558B640F2510D262 CRC64;
     MGDILAYEAD LLGLVKEFLN FGEFQETLET FTKECKTKGK QLPKTSGLAL RESKTLLIQK
     DLITAFEDGD IKEFFALWQE HIPVETQNTN PVAQKLEFYL QIHFAIFPLK HNQGRIDRTD
     CEERISHFKT YLETSGAALS QTTEFLPFYA LPFVPHPAAH PSFKEIFQES WEAELRMRLE
     KFLSVILKAT STPRLITLYK ESLHNNQELL QQLQQQLMET EHKARTYKKC FNRMQSDYHN
     LIGVTADLVD SLEATINGKL ITPEYLQSVC TRLFSTQMKQ SSAQSIDFTR PGTASSMLRA
     SIAPLKQQEV PLFPSLDYEK LKKDLVFGND RLKALILQAL RWRLTRSQPG EQRNTVLQAY
     ISNDLLDCHH NEQKNVLMLL RSPSEVVRQY TALLIDVFSS LAYGRVYISQ NPRLLHSLVE
     TWKAEEKESV IRETVLGILQ KLSLRRSMQS AMIKDDLIFW LVQELEDTDH LSDYALQYTI
     ALFMNLCLRS AGRKMCSRDA DHVLKVLSDL LGHENHEIRS YVNGALYSIL AVPSIREEAR
     SMGMEEILRW YIREGNTDMN CHIEFIIKQL NSEDKFDESI ESDDEEEEKD DEEDEDALEA
     DLDKDEIIYA QSGELAGEKL LTTDYLGIMT NSFKVKKRMF GGVLQSADEP LQRPVTPSTH
     RVMNTVRKTS GPPSPPTNTF KTSQANMSVV SSRPPTRSGS RASTSDYCVT SDSIDSEASR
     LFSPSSQADQ RGASSPRILD LGMEKHNGQN SSKAWLPRSP EVLSATSRKA RTPTIAPQFS
     QSGPQQTSYS SSAGSSTRSR QSTQSYRK