ARMC9_MOUSE
ID ARMC9_MOUSE Reviewed; 817 AA.
AC Q9D2I5; Q8BQQ3; Q8BR45; Q8BSX7; Q8C6A6; Q8C889; Q8CA23; Q8CBG2; Q8K112;
AC Q9CYL1; Q9D2L3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=LisH domain-containing protein ARMC9;
GN Name=Armc9 {ECO:0000312|MGI:MGI:1926045};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 8 AND
RP 9).
RC STRAIN=C57BL/6J;
RC TISSUE=Adipose tissue, Cerebellum, Corpora quadrigemina, Head, Liver,
RC Ovary, Testis, Thymus, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 7).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29459677; DOI=10.1038/s41588-018-0054-7;
RA Breslow D.K., Hoogendoorn S., Kopp A.R., Morgens D.W., Vu B.K.,
RA Kennedy M.C., Han K., Li A., Hess G.T., Bassik M.C., Chen J.K.,
RA Nachury M.V.;
RT "A CRISPR-based screen for Hedgehog signaling provides insights into
RT ciliary function and ciliopathies.";
RL Nat. Genet. 50:460-471(2018).
CC -!- FUNCTION: Involved in ciliogenesis (By similarity). It is required for
CC appropriate acetylation and polyglutamylation of ciliary microtubules,
CC and regulation of cilium length (By similarity). Acts as a positive
CC regulator of hedgehog (Hh) signaling (PubMed:29459677). May participate
CC in the trafficking and/or retention of GLI2 and GLI3 proteins at the
CC ciliary tip (PubMed:29459677). {ECO:0000250|UniProtKB:E7F187,
CC ECO:0000250|UniProtKB:Q7Z3E5, ECO:0000269|PubMed:29459677}.
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:0000269|PubMed:29459677}. 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 (PubMed:29459677). Localizes to the
CC daughter centriole of the primary cilium in RPE1 cells (By similarity).
CC {ECO:0000250|UniProtKB:Q7Z3E5, ECO:0000269|PubMed:29459677}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1;
CC IsoId=Q9D2I5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D2I5-2; Sequence=VSP_023812;
CC Name=3;
CC IsoId=Q9D2I5-3; Sequence=VSP_023815;
CC Name=4;
CC IsoId=Q9D2I5-4; Sequence=VSP_023814, VSP_023816;
CC Name=5;
CC IsoId=Q9D2I5-5; Sequence=VSP_023811;
CC Name=6;
CC IsoId=Q9D2I5-6; Sequence=VSP_023805, VSP_023814, VSP_023816;
CC Name=7;
CC IsoId=Q9D2I5-7; Sequence=VSP_023806, VSP_023809, VSP_023814,
CC VSP_023816;
CC Name=8;
CC IsoId=Q9D2I5-8; Sequence=VSP_023810, VSP_023813;
CC Name=9;
CC IsoId=Q9D2I5-9; Sequence=VSP_023807, VSP_023808;
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DR EMBL; AK017564; BAB30807.1; -; mRNA.
DR EMBL; AK019512; BAB31770.1; -; mRNA.
DR EMBL; AK019600; BAB31811.1; -; mRNA.
DR EMBL; AK030307; BAC26890.1; -; mRNA.
DR EMBL; AK036083; BAC29299.1; -; mRNA.
DR EMBL; AK039800; BAC30457.1; -; mRNA.
DR EMBL; AK046693; BAC32837.1; -; mRNA.
DR EMBL; AK045699; BAC32462.1; -; mRNA.
DR EMBL; AK048064; BAC33231.1; -; mRNA.
DR EMBL; AK076239; BAC36270.1; -; mRNA.
DR EMBL; AK161393; BAE36370.1; -; mRNA.
DR EMBL; BC028964; AAH28964.1; -; mRNA.
DR EMBL; BC043101; AAH43101.1; -; mRNA.
DR CCDS; CCDS15118.1; -. [Q9D2I5-1]
DR CCDS; CCDS48303.1; -. [Q9D2I5-2]
DR CCDS; CCDS78642.1; -. [Q9D2I5-3]
DR RefSeq; NP_001297631.1; NM_001310702.1. [Q9D2I5-3]
DR RefSeq; NP_081732.1; NM_027456.2. [Q9D2I5-2]
DR RefSeq; NP_084460.1; NM_030184.2. [Q9D2I5-1]
DR RefSeq; XP_006530019.1; XM_006529956.3. [Q9D2I5-5]
DR AlphaFoldDB; Q9D2I5; -.
DR SMR; Q9D2I5; -.
DR BioGRID; 219638; 1.
DR STRING; 10090.ENSMUSP00000108934; -.
DR iPTMnet; Q9D2I5; -.
DR PhosphoSitePlus; Q9D2I5; -.
DR MaxQB; Q9D2I5; -.
DR PaxDb; Q9D2I5; -.
DR PRIDE; Q9D2I5; -.
DR ProteomicsDB; 277295; -. [Q9D2I5-1]
DR ProteomicsDB; 277296; -. [Q9D2I5-2]
DR ProteomicsDB; 277297; -. [Q9D2I5-3]
DR ProteomicsDB; 277298; -. [Q9D2I5-4]
DR ProteomicsDB; 277299; -. [Q9D2I5-5]
DR ProteomicsDB; 277300; -. [Q9D2I5-6]
DR ProteomicsDB; 277301; -. [Q9D2I5-7]
DR ProteomicsDB; 277302; -. [Q9D2I5-8]
DR ProteomicsDB; 277303; -. [Q9D2I5-9]
DR Antibodypedia; 20202; 110 antibodies from 18 providers.
DR DNASU; 78795; -.
DR Ensembl; ENSMUST00000027434; ENSMUSP00000027434; ENSMUSG00000062590. [Q9D2I5-1]
DR Ensembl; ENSMUST00000113309; ENSMUSP00000108934; ENSMUSG00000062590. [Q9D2I5-3]
DR Ensembl; ENSMUST00000131412; ENSMUSP00000117267; ENSMUSG00000062590. [Q9D2I5-2]
DR GeneID; 78795; -.
DR KEGG; mmu:78795; -.
DR UCSC; uc007bva.1; mouse. [Q9D2I5-9]
DR UCSC; uc007bvb.1; mouse. [Q9D2I5-8]
DR UCSC; uc007bvc.1; mouse. [Q9D2I5-1]
DR UCSC; uc007bvf.1; mouse. [Q9D2I5-4]
DR UCSC; uc007bvh.1; mouse. [Q9D2I5-5]
DR UCSC; uc007bvi.1; mouse. [Q9D2I5-3]
DR CTD; 80210; -.
DR MGI; MGI:1926045; Armc9.
DR VEuPathDB; HostDB:ENSMUSG00000062590; -.
DR eggNOG; ENOG502QQ9W; Eukaryota.
DR GeneTree; ENSGT00390000018026; -.
DR HOGENOM; CLU_007962_1_0_1; -.
DR InParanoid; Q9D2I5; -.
DR OMA; ALIFKAN; -.
DR OrthoDB; 1327587at2759; -.
DR PhylomeDB; Q9D2I5; -.
DR TreeFam; TF317676; -.
DR BioGRID-ORCS; 78795; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Armc9; mouse.
DR PRO; PR:Q9D2I5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9D2I5; protein.
DR Bgee; ENSMUSG00000062590; Expressed in spermatocyte and 183 other tissues.
DR ExpressionAtlas; Q9D2I5; baseline and differential.
DR Genevisible; Q9D2I5; MM.
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; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA: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; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..817
FT /note="LisH domain-containing protein ARMC9"
FT /id="PRO_0000280596"
FT DOMAIN 7..39
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REGION 637..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 204..230
FT /evidence="ECO:0000255"
FT COMPBIAS 784..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3E5"
FT VAR_SEQ 1..559
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023805"
FT VAR_SEQ 1..235
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023806"
FT VAR_SEQ 201..205
FT /note="KENGP -> VSFMK (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023807"
FT VAR_SEQ 206..817
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023808"
FT VAR_SEQ 236
FT /note="Q -> M (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023809"
FT VAR_SEQ 295..314
FT /note="ASTMLRASLAPEKLKDVPLL -> GTEDWAEKGDHISKPKRGTR (in
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023810"
FT VAR_SEQ 315..817
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023813"
FT VAR_SEQ 574
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023811"
FT VAR_SEQ 667..817
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023812"
FT VAR_SEQ 712..731
FT /note="FMDHKPREWSPAGHQKSRLV -> CKNAVGAKPVLSSWAQESKR (in
FT isoform 4, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023814"
FT VAR_SEQ 712
FT /note="F -> SV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023815"
FT VAR_SEQ 732..817
FT /note="Missing (in isoform 4, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023816"
FT CONFLICT 36
FT /note="K -> Q (in Ref. 1; BAC26890)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="P -> T (in Ref. 1; BAC33231)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="N -> K (in Ref. 1; BAC26890)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="D -> G (in Ref. 1; BAC29299)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="L -> I (in Ref. 1; BAC32462)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 817 AA; 91922 MW; 0E1F2899F9287A23 CRC64;
MGDILAHESE LLGLVKEYLD FAEFEDTLKT FSKECKVKGK PLCKNVGGPL KKDSKSLVIQ
RDLVAAFDSG DQKAFFDLWE GHIPSSVRDT DSLAQKLEFY LHIHFAIYLL KYCRGRPDKQ
ELDKRISYFK TYLETKGAAL SQTTEFLPFY ALPFVPNPMV HPSFKELFQD SWTPELKLKL
EKFLALTFKA NNTPKLLTIY KENGPNSKEL LQQLHQQLVE AERRAMTYLK RYNKIQADYH
NLIGVTAELV DSLEATVSGK MITPEYLQSV CVRLFSNQMR QSLAHSVDFT RPGTASTMLR
ASLAPEKLKD VPLLPSLDYE KLKKDLIWGS DRLKAFLLQA LRWRLTTSHP GEQRETVLQA
YISNDLLDCH SHNQRSVLQL LHSKSEAVRQ YMARLINALA SLAEGRLYLA QNTKVLRMLE
GRLKEEDKDV ITRENVLGAL QKFSLRRPLQ TAMIRDGLIF WLIDLLKDPD CLSDYTLEYS
VALLMNLCLR SAGKNMCAKV AGLMLKVLSD LLGHENHEIQ PYVNGALYSI LSIPSIREEA
RAMGMEDILR CFIKEGNAEM IRQIEFIIKQ LNSEDLLDGV LESDDDEDED DEEDHDIMEA
DLDKDELIQP QLGELSGEKL LTTEYLGIMT NTGKARRKGP ASVQWSGDEP LRRPVTPGGH
RTGCPVLGDH LISPQNAQQA RNGCLRAMPV AHPDDYKEGK PGVTGCGTSS SFMDHKPREW
SPAGHQKSRL VPTAALGWPR EMTQDPSSGH ITREFVPAFT CKPQVPSTPE TVEQNPLKAK
ALSLAPQFSS SGPQQASRPA STASSTRGLH SSQSIRK
