TEST_MOUSE
ID TEST_MOUSE Reviewed; 324 AA.
AC Q9JHJ7; Q9DA14;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Testisin;
DE EC=3.4.21.-;
DE AltName: Full=Serine protease 21;
DE AltName: Full=Tryptase 4;
DE Flags: Precursor;
GN Name=Prss21;
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv;
RX PubMed=11231276; DOI=10.1046/j.1432-1327.2001.01986.x;
RA Scarman A.L., Hooper J.D., Boucaut K.J., Sit M.-L., Webb G.C.,
RA Normyle J.F., Antalis T.M.;
RT "Organization and chromosomal localization of the murine Testisin gene
RT encoding a serine protease temporally expressed during spermatogenesis.";
RL Eur. J. Biochem. 268:1250-1258(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=11259427; DOI=10.1074/jbc.m010422200;
RA Wong G.W., Li L., Madhusudhan M.S., Krilis S.A., Gurish M.F.,
RA Rothenberg M.E., Sali A., Stevens R.L.;
RT "Tryptase 4, a new member of the chromosome 17 family of mouse serine
RT proteases.";
RL J. Biol. Chem. 276:20648-20658(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-324.
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [4]
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).
CC -!- FUNCTION: Could regulate proteolytic events associated with testicular
CC germ cell maturation.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Testis.
CC -!- DEVELOPMENTAL STAGE: Expressed in post-meiotic testicular germ cells.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK006271; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF304012; AAK29360.1; -; Genomic_DNA.
DR EMBL; AY005145; AAG02255.1; -; mRNA.
DR EMBL; AF176209; AAF64407.2; -; mRNA.
DR EMBL; AF226710; AAF64428.2; -; Genomic_DNA.
DR EMBL; AK006271; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS28468.1; -.
DR RefSeq; NP_065233.2; NM_020487.4.
DR AlphaFoldDB; Q9JHJ7; -.
DR SMR; Q9JHJ7; -.
DR STRING; 10090.ENSMUSP00000024928; -.
DR MEROPS; S01.011; -.
DR GlyGen; Q9JHJ7; 4 sites.
DR PhosphoSitePlus; Q9JHJ7; -.
DR PaxDb; Q9JHJ7; -.
DR PRIDE; Q9JHJ7; -.
DR ProteomicsDB; 263280; -.
DR Antibodypedia; 1701; 60 antibodies from 16 providers.
DR DNASU; 57256; -.
DR Ensembl; ENSMUST00000024928; ENSMUSP00000024928; ENSMUSG00000024116.
DR GeneID; 57256; -.
DR KEGG; mmu:57256; -.
DR UCSC; uc008aty.2; mouse.
DR CTD; 10942; -.
DR MGI; MGI:1916698; Prss21.
DR VEuPathDB; HostDB:ENSMUSG00000024116; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000155138; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q9JHJ7; -.
DR OMA; GPCGHRT; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9JHJ7; -.
DR TreeFam; TF351676; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 57256; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q9JHJ7; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9JHJ7; protein.
DR Bgee; ENSMUSG00000024116; Expressed in spermatid and 11 other tissues.
DR ExpressionAtlas; Q9JHJ7; baseline and differential.
DR Genevisible; Q9JHJ7; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:MGI.
DR GO; GO:0008236; F:serine-type peptidase activity; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IBA:GO_Central.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR034380; Testisin.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24256:SF173; PTHR24256:SF173; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Protease; Reference proteome; Serine protease;
KW Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..54
FT /evidence="ECO:0000255"
FT /id="PRO_0000027852"
FT CHAIN 55..298
FT /note="Testisin"
FT /id="PRO_0000027853"
FT PROPEP 299..324
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027854"
FT DOMAIN 55..296
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 95
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 248
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT LIPID 298
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 80..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 181..254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 214..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 244..272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 275
FT /note="P -> H (in Ref. 3; AK006271)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 36175 MW; 56DC59E84F3C3CD4 CRC64;
MGARGKTLVP LLVVVATAAM ALQSTYLQVD PEKPELQEPD LLSGPCGHRT IPSRIVGGDD
AELGRWPWQG SLRVWGNHLC GATLLNRRWV LTAAHCFQKD NDPFDWTVQF GELTSRPSLW
NLQAYSNRYQ IEDIFLSPKY SEQYPNDIAL LKLSSPVTYN NFIQPICLLN STYKFENRTD
CWVTGWGAIG EDESLPSPNT LQEVQVAIIN NSMCNHMYKK PDFRTNIWGD MVCAGTPEGG
KDACFGDSGG PLACDQDTVW YQVGVVSWGI GCGRPNRPGV YTNISHHYNW IQSTMIRNGL
LRPDPVPLLL FLTLAWASSL LRPA
