ANKR9_MOUSE
ID ANKR9_MOUSE Reviewed; 326 AA.
AC Q8BH83; Q3TA09; Q8BHR3;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ankyrin repeat domain-containing protein 9;
GN Name=Ankrd9;
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].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spleen;
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].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: Substrate receptor subunit of a cullin-RING superfamily E3
CC ligase complex (CUL5-based E3 ubiquitin ligase complex) which mediates
CC the ubiquitination and subsequent proteasomal degradation of target
CC proteins. Depending of the metabolic state of the cell, promotes the
CC proteasomal degradation of IMPDH2, the rate-limiting enzyme in GTP
CC biosynthesis or protects IMPDH2 by stabilizing IMPDH2 filaments
CC assembly. Implicated in different cellular processes, like copper
CC homeostasis and cell proliferation. {ECO:0000250|UniProtKB:Q96BM1}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q96BM1}.
CC -!- SUBUNIT: Part of an E3 ubiquitin-protein ligase complex with Elongin BC
CC (ELOB and ELOC), CUL5 and ANKRD9. Interacts with IMPDH2; leading to
CC ubiquitination of IMPDH2 and its subsequent proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q96BM1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q96BM1}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q96BM1}. Note=Detected in long filamentous
CC cytosolic structures where it colocalizes with IMPDH2. Under basal
CC conditions ANKRD9 is mainly in vesicle-like structures, upon nutrient
CC limitation (guanine nucleotides deficiency) ANKRD9 loses its vesicular
CC pattern and assembles with IMPDH2 into rodlike filaments.
CC {ECO:0000250|UniProtKB:Q96BM1}.
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; AK032641; BAC27966.1; -; mRNA.
DR EMBL; AK172167; BAE42861.1; -; mRNA.
DR EMBL; BC023687; AAH23687.1; -; mRNA.
DR CCDS; CCDS26174.1; -.
DR RefSeq; NP_780416.2; NM_175207.4.
DR RefSeq; XP_006516357.1; XM_006516294.3.
DR RefSeq; XP_006516358.1; XM_006516295.2.
DR AlphaFoldDB; Q8BH83; -.
DR SMR; Q8BH83; -.
DR STRING; 10090.ENSMUSP00000120816; -.
DR iPTMnet; Q8BH83; -.
DR PhosphoSitePlus; Q8BH83; -.
DR EPD; Q8BH83; -.
DR PaxDb; Q8BH83; -.
DR PRIDE; Q8BH83; -.
DR ProteomicsDB; 281985; -.
DR Antibodypedia; 27869; 75 antibodies from 17 providers.
DR Ensembl; ENSMUST00000043459; ENSMUSP00000048823; ENSMUSG00000037904.
DR Ensembl; ENSMUST00000128353; ENSMUSP00000120816; ENSMUSG00000037904.
DR Ensembl; ENSMUST00000135131; ENSMUSP00000119339; ENSMUSG00000037904.
DR Ensembl; ENSMUST00000140788; ENSMUSP00000121279; ENSMUSG00000037904.
DR Ensembl; ENSMUST00000148765; ENSMUSP00000123239; ENSMUSG00000037904.
DR GeneID; 74251; -.
DR KEGG; mmu:74251; -.
DR UCSC; uc007pci.1; mouse.
DR CTD; 122416; -.
DR MGI; MGI:1921501; Ankrd9.
DR VEuPathDB; HostDB:ENSMUSG00000037904; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00390000018116; -.
DR HOGENOM; CLU_066027_0_0_1; -.
DR InParanoid; Q8BH83; -.
DR OMA; MPWSVRW; -.
DR OrthoDB; 1244686at2759; -.
DR PhylomeDB; Q8BH83; -.
DR TreeFam; TF331214; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 74251; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8BH83; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BH83; protein.
DR Bgee; ENSMUSG00000037904; Expressed in hindlimb stylopod muscle and 76 other tissues.
DR ExpressionAtlas; Q8BH83; baseline and differential.
DR Genevisible; Q8BH83; MM.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR GO; GO:0006878; P:cellular copper ion homeostasis; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Cytoplasm; Cytoplasmic vesicle; Hydrolase; Reference proteome;
KW Repeat; Ubl conjugation pathway.
FT CHAIN 1..326
FT /note="Ankyrin repeat domain-containing protein 9"
FT /id="PRO_0000066904"
FT REPEAT 70..99
FT /note="ANK 1"
FT REPEAT 111..140
FT /note="ANK 2"
FT REPEAT 157..186
FT /note="ANK 3"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 108..109
FT /note="Important role in both nutrient sensing and
FT binding/regulation of IMPDH2"
FT /evidence="ECO:0000250|UniProtKB:Q96BM1"
SQ SEQUENCE 326 AA; 35513 MW; 43041E5BCB205288 CRC64;
MPWDTRPGRS ANGGPEGPGA ARLRVQKQCR KSSFAFYLAV RDQLPVWLLE DIRASEAFHC
DERGRAAAYS PSEALLYALV HDHQAYAHYL LATFPRCALA PPSAGFRCCT APGPHVALAV
RYNRVGILRR ILRTVQDFPV EERVRLLDRR GCSRVEGGGT SLHVACELAR PECLFLLLGH
GASPGLRDGS GFTPLELLLR QLNQDASSAP TKAEAASATV NAATANTTSS EEVCQRRLLL
LDLLVLYTPG GVVGPARCEL LGDQLRWQRL LGEDKFQWLA GLAPPSLFVR AMQVLVTTIS
PGRFPEALDE LPLPSFLQPL DLTGKG
