PSMA8_MOUSE
ID PSMA8_MOUSE Reviewed; 250 AA.
AC Q9CWH6; Q14A44;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Proteasome subunit alpha type-8 {ECO:0000303|PubMed:31358751};
DE AltName: Full=Proteasome alpha 4 subunit {ECO:0000303|PubMed:23706739};
DE Short=Alpha4s {ECO:0000303|PubMed:23706739};
DE AltName: Full=Proteasome subunit alpha-type 7-like;
GN Name=Psma8 {ECO:0000303|PubMed:23706739, ECO:0000312|MGI:MGI:1920927};
GN Synonyms=Psma7l;
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=Embryonic stem cell;
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 TISSUE=Brain;
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=Testis;
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 DEVELOPMENTAL STAGE.
RX PubMed=23706739; DOI=10.1016/j.cell.2013.04.032;
RA Qian M.X., Pang Y., Liu C.H., Haratake K., Du B.Y., Ji D.Y., Wang G.F.,
RA Zhu Q.Q., Song W., Yu Y., Zhang X.X., Huang H.T., Miao S., Chen L.B.,
RA Zhang Z.H., Liang Y.N., Liu S., Cha H., Yang D., Zhai Y., Komatsu T.,
RA Tsuruta F., Li H., Cao C., Li W., Li G.H., Cheng Y., Chiba T., Wang L.,
RA Goldberg A.L., Shen Y., Qiu X.B.;
RT "Acetylation-mediated proteasomal degradation of core histones during DNA
RT repair and spermatogenesis.";
RL Cell 153:1012-1024(2013).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=31358751; DOI=10.1038/s41467-019-11346-y;
RA Zhang Q., Ji S.Y., Busayavalasa K., Shao J., Yu C.;
RT "Meiosis I progression in spermatogenesis requires a type of testis-
RT specific 20S core proteasome.";
RL Nat. Commun. 10:3387-3387(2019).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND INTERACTION WITH PSME3; PSME4; CCT6B; CCT2; TRIP12; NEDD4; TRIM36;
RP RAD18; USP9X; USP34; USP5; USP47; CDK1; TRIP13; SIX6OS1 AND SYCE3.
RX PubMed=31437213; DOI=10.1371/journal.pgen.1008316;
RA Gomez-H L., Felipe-Medina N., Condezo Y.B., Garcia-Valiente R., Ramos I.,
RA Suja J.A., Barbero J.L., Roig I., Sanchez-Martin M., de Rooij D.G.,
RA Llano E., Pendas A.M.;
RT "The PSMA8 subunit of the spermatoproteasome is essential for proper
RT meiotic exit and mouse fertility.";
RL PLoS Genet. 15:E1008316-E1008316(2019).
CC -!- FUNCTION: Component of the spermatoproteasome, a proteasome
CC specifically found in testis that promotes acetylation-dependent
CC degradation of histones, thereby participating actively to the exchange
CC of histones during spermatogenesis (PubMed:23706739, PubMed:31358751,
CC PubMed:31437213). The proteasome is a protein complex that degrades
CC unneeded or damaged proteins by proteolysis, a chemical reaction that
CC breaks peptide bonds (Probable). Required for 20S core proteasome
CC assembly, essential for the degradation of meiotic proteins RAD51 and
CC RPA1 at late prophase I and the progression of meiosis I during
CC spermatogenesis (PubMed:31358751). Localizes to the synaptonemal
CC complex, a 'zipper'-like structure that holds homologous chromosome
CC pairs in synapsis during meiotic prophase I (PubMed:31437213).
CC {ECO:0000269|PubMed:23706739, ECO:0000269|PubMed:31358751,
CC ECO:0000269|PubMed:31437213, ECO:0000305}.
CC -!- SUBUNIT: Component of the outer alpha-ring of the 20S proteasome core
CC which is composed of 28 subunits that are arranged in four stacked
CC rings, resulting in a barrel-shaped structure (PubMed:23706739,
CC PubMed:31358751). The catalytic chamber with the active sites is on the
CC inside of the barrel (Probable). Interacts with canonical subunits of
CC the spermatoproteasome, including proteasome activators PSME4 (also
CC called PA200) and PSME3 (also called PA28-gamma) (PubMed:31437213).
CC Interacts with proteasome-interacting proteins chaperones including
CC CCT6B and CCT2, ubiquitin ligases (TRIP12, NEDD4, TRIM36 and RAD18),
CC and ubiquitin specific proteases such as USP9X, USP34, USP5 and USP47
CC (PubMed:31437213). Interacts with meiotic proteins cyclin dependent
CC kinase CDK1 and the ATPase TRIP13 as well as proteins of the
CC synaptonemal complex SIX6OS1 and SYCE3 (PubMed:31437213).
CC {ECO:0000269|PubMed:23706739, ECO:0000269|PubMed:31358751,
CC ECO:0000269|PubMed:31437213, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31437213}.
CC Note=Localizes to the central region of the synaptonemal complex.
CC {ECO:0000269|PubMed:31437213}.
CC -!- DEVELOPMENTAL STAGE: In testes, expressed in spermatocytes at the
CC pachytene stage (weakly in early pachynema and strongly in late
CC pachynema), and its expression persisted thereafter throughout
CC spermatogenesis. {ECO:0000269|PubMed:23706739,
CC ECO:0000269|PubMed:31358751, ECO:0000269|PubMed:31437213}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice were obtained according to the
CC expected Mendelian ratios and showed no obvious phenotypes with respect
CC to viability and development; however males show infertility
CC (PubMed:31358751, PubMed:31437213). PSMA8-null spermatocytes exhibit
CC delayed M-phase entry and are finally arrested at this stage, resulting
CC in male infertility (PubMed:31358751, PubMed:31437213).
CC {ECO:0000269|PubMed:31358751, ECO:0000269|PubMed:31437213}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
CC -!- CAUTION: Predicted to have endopeptidase activity (By similarity).
CC However, as it is located in the outer alpha-ring, it is suggested to
CC lack catalytic activity and preferentially interact with regulatory
CC complexes such as PSME4/PA200. {ECO:0000255,
CC ECO:0000305|PubMed:23706739}.
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DR EMBL; AK010717; BAB27139.1; -; mRNA.
DR EMBL; BC116990; AAI16991.1; -; mRNA.
DR EMBL; BC116992; AAI16993.1; -; mRNA.
DR CCDS; CCDS50226.1; -.
DR RefSeq; NP_001157081.1; NM_001163609.1.
DR AlphaFoldDB; Q9CWH6; -.
DR SMR; Q9CWH6; -.
DR BioGRID; 216184; 3.
DR IntAct; Q9CWH6; 1.
DR STRING; 10090.ENSMUSP00000042590; -.
DR MEROPS; T01.978; -.
DR iPTMnet; Q9CWH6; -.
DR PhosphoSitePlus; Q9CWH6; -.
DR jPOST; Q9CWH6; -.
DR MaxQB; Q9CWH6; -.
DR PaxDb; Q9CWH6; -.
DR PeptideAtlas; Q9CWH6; -.
DR PRIDE; Q9CWH6; -.
DR ProteomicsDB; 291654; -.
DR Antibodypedia; 22107; 75 antibodies from 23 providers.
DR DNASU; 73677; -.
DR Ensembl; ENSMUST00000040860; ENSMUSP00000042590; ENSMUSG00000036743.
DR GeneID; 73677; -.
DR KEGG; mmu:73677; -.
DR UCSC; uc008edj.2; mouse.
DR CTD; 143471; -.
DR MGI; MGI:1920927; Psma8.
DR VEuPathDB; HostDB:ENSMUSG00000036743; -.
DR eggNOG; KOG0183; Eukaryota.
DR GeneTree; ENSGT00940000160354; -.
DR HOGENOM; CLU_035750_4_0_1; -.
DR InParanoid; Q9CWH6; -.
DR OMA; RLFHTEP; -.
DR OrthoDB; 1222564at2759; -.
DR PhylomeDB; Q9CWH6; -.
DR TreeFam; TF106212; -.
DR BRENDA; 3.4.25.1; 3474.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69481; G2/M Checkpoints.
DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-MMU-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 73677; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Psma8; mouse.
DR PRO; PR:Q9CWH6; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9CWH6; protein.
DR Bgee; ENSMUSG00000036743; Expressed in spermatocyte and 69 other tissues.
DR ExpressionAtlas; Q9CWH6; baseline and differential.
DR Genevisible; Q9CWH6; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR GO; GO:1990111; C:spermatoproteasome complex; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:0060631; P:regulation of meiosis I; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 1: Evidence at protein level;
KW Differentiation; Nucleus; Proteasome; Reference proteome; Spermatogenesis.
FT CHAIN 1..250
FT /note="Proteasome subunit alpha type-8"
FT /id="PRO_0000124150"
SQ SEQUENCE 250 AA; 27866 MW; 86258DBE01B0C0E6 CRC64;
MASRYDRAIT VFSPDGHLFQ VEYAQEAVKK GSTAVGIRGT NIVVLGVEKK SVAKLQDERT
VRKICALDDH VCMAFAGLTA DARVVISRAR VECQSHKLTV EDPVTVEYIT RFIATLKQKY
TQSNGRRPFG ISALIVGFDD DGIPRLYQTD PSGTYHAWKA NAIGRSAKTV REFLEKNYTE
DAISNDKEAI KLAIKALLEV VQSGGKNIEL AIIRRDQPLK MFSAKEIELE VSEIEREKDE
AEKTKSKKST
