TYSD1_MOUSE
ID TYSD1_MOUSE Reviewed; 568 AA.
AC Q9DBA6; Q0VE90;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Peroxisomal leader peptide-processing protease;
DE EC=3.4.21.-;
DE AltName: Full=Trypsin domain-containing protein 1;
DE Contains:
DE RecName: Full=Peroxisomal leader peptide-processing protease, 10 kDa form;
DE Contains:
DE RecName: Full=Peroxisomal leader peptide-processing protease, 49 kDa form;
GN Name=Tysnd1;
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, and NOD; TISSUE=Liver;
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 PROTEIN SEQUENCE OF N-TERMINUS, PROTEOLYTIC CLEAVAGE AT CYS-110, FUNCTION,
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=17255948; DOI=10.1038/sj.emboj.7601525;
RA Kurochkin I.V., Mizuno Y., Konagaya A., Sakaki Y., Schoenbach C.,
RA Okazaki Y.;
RT "Novel peroxisomal protease Tysnd1 processes PTS1- and PTS2-containing
RT enzymes involved in beta-oxidation of fatty acids.";
RL EMBO J. 26:835-845(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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).
CC -!- FUNCTION: Peroxisomal protease that mediates both the removal of the
CC leader peptide from proteins containing a PTS2 target sequence and
CC processes several PTS1-containing proteins. Catalyzes the processing of
CC PTS1-proteins involved in the peroxisomal beta-oxidation of fatty acids
CC (By similarity). {ECO:0000250, ECO:0000269|PubMed:17255948}.
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide (NEM). Not affected
CC by leupeptin or trans-epoxysuccinyl-l-leucylamido-(4-gianidino) butane
CC (E64). {ECO:0000269|PubMed:17255948}.
CC -!- SUBUNIT: Homodimer. Forms a heterodimer with the C-terminal cleavage
CC product (49 kDa form). Forms a heterodimer with the N-terminal cleavage
CC product (10 kDa form). Interacts with PEX5. Interacts with LONP2.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17255948}.
CC -!- INDUCTION: By the proliferator-activated receptor alpha agonist
CC bezafibrate. {ECO:0000269|PubMed:17255948}.
CC -!- PTM: Self-cleavage gives rise to an N-terminal 10-kDa fragment and C-
CC terminal 49-kDa fragment upon import into the peroxisomes. The full-
CC lengh TYSND1 is the active the proteolytic processing of PTS1- and
CC PTS2-proteins and in self-cleavage, and intermolecular self-cleavage of
CC TYSND1 down-regulates its protease activity.
CC {ECO:0000269|PubMed:17255948}.
CC -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR EMBL; AK005069; BAB23793.1; -; mRNA.
DR EMBL; AK154513; BAE32642.1; -; mRNA.
DR EMBL; BC119320; AAI19321.2; -; mRNA.
DR CCDS; CCDS48575.1; -.
DR RefSeq; NP_001259019.1; NM_001272090.1.
DR RefSeq; NP_001259020.1; NM_001272091.1.
DR RefSeq; NP_001259021.1; NM_001272092.1.
DR RefSeq; NP_082188.1; NM_027912.1.
DR AlphaFoldDB; Q9DBA6; -.
DR SMR; Q9DBA6; -.
DR BioGRID; 214911; 2.
DR STRING; 10090.ENSMUSP00000020284; -.
DR MEROPS; S01.286; -.
DR iPTMnet; Q9DBA6; -.
DR PhosphoSitePlus; Q9DBA6; -.
DR SwissPalm; Q9DBA6; -.
DR EPD; Q9DBA6; -.
DR jPOST; Q9DBA6; -.
DR MaxQB; Q9DBA6; -.
DR PaxDb; Q9DBA6; -.
DR PeptideAtlas; Q9DBA6; -.
DR PRIDE; Q9DBA6; -.
DR ProteomicsDB; 298050; -.
DR Antibodypedia; 48786; 66 antibodies from 17 providers.
DR DNASU; 71767; -.
DR Ensembl; ENSMUST00000020284; ENSMUSP00000020284; ENSMUSG00000020087.
DR GeneID; 71767; -.
DR KEGG; mmu:71767; -.
DR UCSC; uc007fgh.2; mouse.
DR CTD; 219743; -.
DR MGI; MGI:1919017; Tysnd1.
DR VEuPathDB; HostDB:ENSMUSG00000020087; -.
DR eggNOG; KOG1320; Eukaryota.
DR GeneTree; ENSGT00390000014627; -.
DR HOGENOM; CLU_034855_1_0_1; -.
DR InParanoid; Q9DBA6; -.
DR OMA; IACGSPF; -.
DR OrthoDB; 1307240at2759; -.
DR PhylomeDB; Q9DBA6; -.
DR TreeFam; TF331254; -.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR Reactome; R-MMU-9033500; TYSND1 cleaves peroxisomal proteins.
DR BioGRID-ORCS; 71767; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9DBA6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9DBA6; protein.
DR Bgee; ENSMUSG00000020087; Expressed in right kidney and 261 other tissues.
DR ExpressionAtlas; Q9DBA6; baseline and differential.
DR Genevisible; Q9DBA6; MM.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; EXP:Reactome.
DR GO; GO:0016485; P:protein processing; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0031998; P:regulation of fatty acid beta-oxidation; ISS:UniProtKB.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR017345; Pept_S1A_Tysnd1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR039245; TYSND1/DEG15.
DR PANTHER; PTHR21004; PTHR21004; 1.
DR PIRSF; PIRSF037989; Peptidase_S1B_Tysnd1; 1.
DR SUPFAM; SSF50494; SSF50494; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Peroxisome; Protease;
KW Reference proteome; Serine protease.
FT CHAIN 1..568
FT /note="Peroxisomal leader peptide-processing protease"
FT /id="PRO_0000286127"
FT CHAIN 1..110
FT /note="Peroxisomal leader peptide-processing protease, 10
FT kDa form"
FT /id="PRO_0000286128"
FT CHAIN 111..568
FT /note="Peroxisomal leader peptide-processing protease, 49
FT kDa form"
FT /id="PRO_0000286129"
FT REGION 332..568
FT /note="Serine protease"
FT ACT_SITE 374
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 410
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 483
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 110..111
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:17255948"
SQ SEQUENCE 568 AA; 59066 MW; B7BED91B4DB50E5E CRC64;
MGRQWGPSMR VAEQAGCVVS ASRAGQPDAG SWSCSGVILS RNPGLVLCHG GIFTPFLRTG
SAALTQTGTA FLPGDSCSDD LRLHVQWGPT AASPAGRADQ ELPGLCTPQC ASLGLEPGAP
SRARARPLQP PRPAQLLLLL SCPAFRSHFA RLFGADAVDQ WHFVSSAPDD AVSEEEEEDQ
LRALGWFALL RVQRGAAAEE RRGPVVTVAP LGAVVKGAPL LACGSPFGAF CPDIFLNTLS
RGVLSNAAGP LLLTDARCLP GTEGGGVFAA RPAGALVALV AAPLCWKARE WVGLTLLCAA
APLLQVARWA LARLHPGSAS LSVLLPPPDV STPRGLPLRD LGPPWAAAAV LVECGTVWGS
GVVVAPRLVV TCRHVAPREA ARVLVHSATP KNVAIWGQVV FATQETSPYD IAVVSLEEEL
NGVPTPVPAG HFHEGEPVSV VGFGVFGQAC GPSVTSGILS AVVRVDGSPV MLQTTCAVHG
GSSGGPLFSS GSGDLLGIVA SNTRDNNTGA TYPHLNFSIP ITVLQPALKQ YSQTGDLGGL
RELDHTTEPV RVVWRLQRPL SEVPRSKL
