PRS55_MOUSE
ID PRS55_MOUSE Reviewed; 321 AA.
AC Q14BX2; G3X9K6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Serine protease 55;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=Prss55;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, FUNCTION,
RP AND GPI-ANCHOR.
RX PubMed=30032357; DOI=10.1007/s00018-018-2878-9;
RA Shang X., Shen C., Liu J., Tang L., Zhang H., Wang Y., Wu W., Chi J.,
RA Zhuang H., Fei J., Wang Z.;
RT "Serine protease PRSS55 is crucial for male mouse fertility via affecting
RT sperm migration and sperm-egg binding.";
RL Cell. Mol. Life Sci. 75:4371-4384(2018).
CC -!- FUNCTION: Probable serine protease, which plays a crucial role in the
CC fertility of male mice including sperm migration and sperm-egg
CC interaction (PubMed:30032357). {ECO:0000269|PubMed:30032357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30032357};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:30032357}. Cytoplasmic
CC vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:30032357}.
CC Note=Mainly observed in the luminal side of seminiferous tubules and
CC sperm acrosome. {ECO:0000269|PubMed:30032357}.
CC -!- TISSUE SPECIFICITY: Expressed in adult mouse testis.
CC {ECO:0000269|PubMed:30032357}.
CC -!- DISRUPTION PHENOTYPE: Deficient male display infertility with impaired
CC sperm migration from uterus into oviduct and defective sperm-zona and
CC sperm-egg recognition/binding. However, the mating activity, sperm
CC production, sperm morphology, sperm motility, inducibility of AR,
CC activity of acrosomal enzymes and in vitro sperm fertility are almost
CC normal. Male show an absence of mature ADAM3 in sperm.
CC {ECO:0000269|PubMed:30032357}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: Controversial data exist concerning the topology of PRS55. One
CC study in mouse shows that PRSS55 is a GPI-anchored protein
CC (PubMed:30032357). An other study does not confirm the GPI-anchor
CC status of PRSS55 (By similarity). However, as a GPI-anchor motif is
CC detected, the possibility of a GPI-anchor instead of a single-pass type
CC I membrane protein is probable. {ECO:0000250|UniProtKB:Q6UWB4,
CC ECO:0000269|PubMed:30032357, ECO:0000305}.
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DR EMBL; AC166997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115562; AAI15563.1; -; mRNA.
DR CCDS; CCDS36952.1; -.
DR RefSeq; NP_001074532.1; NM_001081063.1.
DR AlphaFoldDB; Q14BX2; -.
DR SMR; Q14BX2; -.
DR STRING; 10090.ENSMUSP00000086752; -.
DR MEROPS; S01.415; -.
DR GlyGen; Q14BX2; 1 site.
DR PaxDb; Q14BX2; -.
DR PRIDE; Q14BX2; -.
DR ProteomicsDB; 291909; -.
DR ProteomicsDB; 337358; -.
DR Antibodypedia; 8438; 83 antibodies from 13 providers.
DR DNASU; 71037; -.
DR Ensembl; ENSMUST00000089338; ENSMUSP00000086752; ENSMUSG00000034623.
DR GeneID; 71037; -.
DR KEGG; mmu:71037; -.
DR CTD; 203074; -.
DR MGI; MGI:1918287; Prss55.
DR VEuPathDB; HostDB:ENSMUSG00000034623; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000156020; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q14BX2; -.
DR OMA; HEEFNRT; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q14BX2; -.
DR TreeFam; TF338267; -.
DR BioGRID-ORCS; 71037; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Prss55; mouse.
DR PRO; PR:Q14BX2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q14BX2; protein.
DR Bgee; ENSMUSG00000034623; Expressed in seminiferous tubule of testis and 50 other tissues.
DR ExpressionAtlas; Q14BX2; baseline and differential.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IDA:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IDA:UniProtKB.
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; 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; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Protease; Reference proteome;
KW Serine protease; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..294
FT /note="Serine protease 55"
FT /evidence="ECO:0000255"
FT /id="PRO_0000328816"
FT PROPEP 295..321
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000449399"
FT DOMAIN 35..266
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 272..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 75
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 122
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT LIPID 294
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 155..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 188..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 212..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 133
FT /note="T -> A (in Ref. 2; AAI15563)"
SQ SEQUENCE 321 AA; 36087 MW; E797567966E44CA6 CRC64;
MILPSILLLV AHTLEANVEC GVRPLYDSRI QYSRIIEGQE AELGEFPWQV SIQESDHHFC
GGSILSEWWI LTVAHCFYAQ ELSPTDLRVR VGTNDLTTSP VELEVTTIIR HKGFKRLNMD
NDIALLLLAK PLTFNELTVP ICLPLWPAPP SWHECWVAGW GVTNSTDKES MSTDLMKVPM
RIIEWEECLQ MFPSLTTNML CASYGNESYD ACQGDSGGPL VCTTDPGSRW YQVGIISWGK
SCGKKGFPGI YTVLAKYTLW IEKIAQTEGK PLDFRGQSSS NKKKNRQNNQ LSKSPALNCP
QSWLLPCLLS FALLRALSNW K
