PRS41_MOUSE
ID PRS41_MOUSE Reviewed; 322 AA.
AC Q920S2; Q8BX01;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Serine protease 41 {ECO:0000305};
DE EC=3.4.21.-;
DE AltName: Full=Testis serine protease 1;
DE Short=TESSP-1;
DE Flags: Precursor;
GN Name=Prss41 {ECO:0000312|MGI:MGI:1918253};
GN Synonyms=Tessp1 {ECO:0000303|PubMed:23536369};
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, ALTERNATIVE
RP SPLICING, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=15515062; DOI=10.1002/mrd.20184;
RA Takano N., Matsui H., Takahashi T.;
RT "TESSP-1: a novel serine protease gene expressed in the spermatogonia and
RT spermatocytes of adult mouse testes.";
RL Mol. Reprod. Dev. 70:1-10(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=23536369; DOI=10.1095/biolreprod.112.106328;
RA Yoneda R., Takahashi T., Matsui H., Takano N., Hasebe Y., Ogiwara K.,
RA Kimura A.P.;
RT "Three testis-specific paralogous serine proteases play different roles in
RT murine spermatogenesis and are involved in germ cell survival during
RT meiosis.";
RL Biol. Reprod. 88:118-118(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19798924; DOI=10.2108/zsj.26.294;
RA Takano N., Kimura A., Takahashi T.;
RT "Two distinct localization patterns of testis-specific serine protease 1
RT (TESSP1) in the seminiferous tubules of the mouse testis.";
RL Zool. Sci. 26:294-300(2009).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15515062,
CC ECO:0000269|PubMed:19798924}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:15515062, ECO:0000269|PubMed:19798924}.
CC Note=Localized in the plasma membrane of spermatogonia. Localized in
CC intracellular compartment in spermatocytes, probably in the Golgi
CC apparatus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q920S2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q920S2-2; Sequence=VSP_034949, VSP_034950;
CC -!- TISSUE SPECIFICITY: Testis-specific. Expressed in spermatogonia and
CC spermatocytes. Expressed in Leydig and Sertoli cells (at protein
CC level). Expressed 2 weeks after birth and remains highly expressed in
CC the sexually mature testis. Expressed in the seminiferous tubules but
CC not in the interstitial tissues. Expressed in type B spermatogonia and
CC spermatocytes at stages between preleptotene and pachytene during the
CC spermatogenesis cycle. {ECO:0000269|PubMed:15515062,
CC ECO:0000269|PubMed:19798924}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15515062}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AB049453; BAB68561.1; -; mRNA.
DR EMBL; AK049297; BAC33665.1; -; mRNA.
DR CCDS; CCDS28466.1; -. [Q920S2-1]
DR RefSeq; NP_081920.1; NM_027644.1. [Q920S2-1]
DR AlphaFoldDB; Q920S2; -.
DR SMR; Q920S2; -.
DR STRING; 10090.ENSMUSP00000024926; -.
DR MEROPS; S01.417; -.
DR GlyGen; Q920S2; 1 site.
DR PhosphoSitePlus; Q920S2; -.
DR PaxDb; Q920S2; -.
DR PRIDE; Q920S2; -.
DR ProteomicsDB; 291905; -. [Q920S2-1]
DR ProteomicsDB; 291906; -. [Q920S2-2]
DR DNASU; 71003; -.
DR Ensembl; ENSMUST00000024926; ENSMUSP00000024926; ENSMUSG00000024114. [Q920S2-1]
DR Ensembl; ENSMUST00000151797; ENSMUSP00000122453; ENSMUSG00000024114. [Q920S2-2]
DR GeneID; 71003; -.
DR KEGG; mmu:71003; -.
DR UCSC; uc008atv.1; mouse. [Q920S2-1]
DR UCSC; uc008atw.1; mouse. [Q920S2-2]
DR CTD; 360226; -.
DR MGI; MGI:1918253; Prss41.
DR VEuPathDB; HostDB:ENSMUSG00000024114; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000155138; -.
DR HOGENOM; CLU_1111092_0_0_1; -.
DR InParanoid; Q920S2; -.
DR OMA; QDSMFCA; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q920S2; -.
DR TreeFam; TF351676; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 71003; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Prss41; mouse.
DR PRO; PR:Q920S2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q920S2; protein.
DR Bgee; ENSMUSG00000024114; Expressed in lumbar subsegment of spinal cord and 56 other tissues.
DR Genevisible; Q920S2; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0017080; F:sodium channel regulator activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
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 Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Protease; Reference proteome;
KW Serine protease; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..52
FT /evidence="ECO:0000255"
FT /id="PRO_0000345422"
FT CHAIN 53..296
FT /note="Serine protease 41"
FT /id="PRO_0000345423"
FT PROPEP 297..322
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000345424"
FT DOMAIN 53..294
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 93
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 144
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 246
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT LIPID 296
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 178..252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 212..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 242..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 191..250
FT /note="KPLPPPYHLREVQVSILNNSRCQELFEIFSLHHLITKDVFCAGAEDGSADTC
FT SGDSGGPL -> SEISNAGWACGCAICPLFQPQQALKPFSGSGAPRASCLPAQPPPPLL
FT PTCMELPSVLEQG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034949"
FT VAR_SEQ 251..322
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034950"
FT CONFLICT 83
FT /note="L -> P (in Ref. 3; BAC33665)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 36218 MW; ED55F9A199A3E491 CRC64;
MGIQGPVLLL LLLCVMLGKP GSREESQAAD LKSTDIKLLS MPCGRRNDTR SRIVGGIESM
QGRWPWQASL RLKKSHRCGG SLLSRRWVLT AAHCFRKYLD PEKWTVQLGQ LTSKPSYWNR
KAYSGRYRVK DIIVNSEDKL KSHDLALLRL ASSVTYNKDI QPVCVQPSTF TSQHQPRCWV
TGWGVLQEDL KPLPPPYHLR EVQVSILNNS RCQELFEIFS LHHLITKDVF CAGAEDGSAD
TCSGDSGGPL VCNMDGLWYQ IGIVSWGIGC GRPNLPGIYT NVSHYYNWIE TMMILNGAVR
RDLALPLLSI TLLQAPWLLR PT
