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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}.
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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
 
 
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