PRS37_MOUSE
ID PRS37_MOUSE Reviewed; 237 AA.
AC Q9DAA4; Q9CUH3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Probable inactive serine protease 37 {ECO:0000305};
DE AltName: Full=Probable inactive trypsin-X2;
DE Flags: Precursor;
GN Name=Prss37 {ECO:0000312|MGI:MGI:1914940}; Synonyms=Tryx2;
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=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 [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, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23553430; DOI=10.1095/biolreprod.112.107086;
RA Shen C., Kuang Y., Liu J., Feng J., Chen X., Wu W., Chi J., Tang L.,
RA Wang Y., Fei J., Wang Z.;
RT "Prss37 is required for male fertility in the mouse.";
RL Biol. Reprod. 88:123-123(2013).
CC -!- FUNCTION: Plays a role in male fertility (PubMed:23553430). May have a
CC role in sperm migration or binding to zona-intact eggs
CC (PubMed:23553430). Involved in the activation of the proacrosin/acrosin
CC system (By similarity). {ECO:0000250|UniProtKB:A4D1T9,
CC ECO:0000269|PubMed:23553430}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000250|UniProtKB:A4D1T9}. Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Testis-specific (PubMed:23553430). Expressed in
CC spermatids (PubMed:23553430). Weakly expressed in mature sperm (at
CC protein level) (PubMed:23553430). {ECO:0000269|PubMed:23553430}.
CC -!- DEVELOPMENTAL STAGE: Expressed exclusively in the spermatids at steps
CC 9-14 of spermiogenesis (PubMed:23553430).
CC {ECO:0000269|PubMed:23553430}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit male infertility, but their mating
CC behavior, spermatogenesis, sperm morphology and motility remain
CC unaffected (PubMed:23553430). Male sperm migration from uterus into
CC oviduct and zona-intact oocyte binding are impaired; however, sperm is
CC still able to fertilize cumulus-intact oocytes (PubMed:23553430). Male
CC show an absence of mature ADAM3 in sperm (PubMed:23553430).
CC {ECO:0000269|PubMed:23553430}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: Although related to peptidase S1 family, lacks the conserved
CC active Ser residue in position 192 which is replaced by an Ala,
CC suggesting that it has no protease activity. Lacks also metal binding
CC sites Glu in position 67 which is replaced by Asn and Asn in position
CC 69 which is replaced by Lys. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK006028; BAB24373.1; -; mRNA.
DR EMBL; AK016088; BAB30109.1; -; mRNA.
DR EMBL; AK029780; BAC26613.1; -; mRNA.
DR EMBL; BC125467; AAI25468.1; -; mRNA.
DR EMBL; BC125493; AAI25494.1; -; mRNA.
DR CCDS; CCDS20033.1; -.
DR RefSeq; NP_080593.1; NM_026317.2.
DR RefSeq; XP_006506588.1; XM_006506525.3.
DR AlphaFoldDB; Q9DAA4; -.
DR SMR; Q9DAA4; -.
DR STRING; 10090.ENSMUSP00000031967; -.
DR MEROPS; S01.989; -.
DR PaxDb; Q9DAA4; -.
DR PRIDE; Q9DAA4; -.
DR ProteomicsDB; 291675; -.
DR Antibodypedia; 18320; 27 antibodies from 11 providers.
DR DNASU; 67690; -.
DR Ensembl; ENSMUST00000031967; ENSMUSP00000031967; ENSMUSG00000029909.
DR GeneID; 67690; -.
DR KEGG; mmu:67690; -.
DR UCSC; uc009bmx.1; mouse.
DR CTD; 136242; -.
DR MGI; MGI:1914940; Prss37.
DR VEuPathDB; HostDB:ENSMUSG00000029909; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000161483; -.
DR HOGENOM; CLU_006842_1_6_1; -.
DR InParanoid; Q9DAA4; -.
DR OMA; DKDCQKT; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9DAA4; -.
DR TreeFam; TF331065; -.
DR BioGRID-ORCS; 67690; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q9DAA4; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9DAA4; protein.
DR Bgee; ENSMUSG00000029909; Expressed in seminiferous tubule of testis and 18 other tissues.
DR Genevisible; Q9DAA4; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IMP:MGI.
DR GO; GO:0008354; P:germ cell migration; IMP:MGI.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; ISS:UniProtKB.
DR GO; GO:1905516; P:positive regulation of fertilization; IMP:UniProtKB.
DR GO; GO:0051604; P:protein maturation; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0070613; P:regulation of protein processing; ISS:UniProtKB.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001254; Trypsin_dom.
DR Pfam; PF00089; Trypsin; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Disulfide bond; Fertilization; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..237
FT /note="Probable inactive serine protease 37"
FT /id="PRO_0000326072"
FT DOMAIN 20..233
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 40..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 131..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 163..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 112
FT /note="N -> R (in Ref. 1; BAB30109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 26698 MW; EF91396566B0394A CRC64;
MKLIIYLTIL AGTALVTHSS VQKEDHAPYL AYLKSNFNPC VGVLIKASWV LAPSHCYLPN
LRVMLGNFKS RVRDGTEQTI YPIQIIRYWN YSHTAPQDDL MLIKLAKPAT FNHKVQVLPI
ATTNVRPGTV CTLSGLDWSQ ENNGRHPDLR QNLEAPVMTD KDCQKTQQGS SHRNSLCVRF
VKVFSRIFGE VAVATVICKN KLQGIEVGHF MGGDVGIYTN IYSYVPWIEK TTKEKMT
