PRS42_HUMAN
ID PRS42_HUMAN Reviewed; 293 AA.
AC Q7Z5A4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Putative serine protease 42 {ECO:0000305};
DE EC=3.4.21.-;
DE AltName: Full=Serine protease 42, pseudogene {ECO:0000312|HGNC:HGNC:30716};
DE AltName: Full=Testis serine protease 2;
DE Flags: Precursor;
GN Name=PRSS42P {ECO:0000312|HGNC:HGNC:30716};
GN Synonyms=PRSS42 {ECO:0000312|HGNC:HGNC:30716},
GN TESSP2 {ECO:0000312|HGNC:HGNC:30716};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12838346; DOI=10.1038/nrg1111;
RA Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C.;
RT "Human and mouse proteases: a comparative genomic approach.";
RL Nat. Rev. Genet. 4:544-558(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in spermatogenesis. Involved in germ cell
CC survival during meiosis. {ECO:0000250|UniProtKB:Q8VIF2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8VIF2}. Cell
CC membrane {ECO:0000250|UniProtKB:Q8VIF2}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:Q8VIF2}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; AJ544583; CAD67566.1; -; mRNA.
DR EMBL; CH471055; EAW64788.1; -; Genomic_DNA.
DR RefSeq; NP_874361.1; NM_182702.1.
DR AlphaFoldDB; Q7Z5A4; -.
DR SMR; Q7Z5A4; -.
DR BioGRID; 130963; 191.
DR STRING; 9606.ENSP00000401701; -.
DR MEROPS; S01.362; -.
DR GlyGen; Q7Z5A4; 3 sites.
DR iPTMnet; Q7Z5A4; -.
DR PhosphoSitePlus; Q7Z5A4; -.
DR BioMuta; PRSS42; -.
DR DMDM; 74759189; -.
DR MassIVE; Q7Z5A4; -.
DR PaxDb; Q7Z5A4; -.
DR PRIDE; Q7Z5A4; -.
DR ProteomicsDB; 69274; -.
DR DNASU; 339906; -.
DR UCSC; uc011bap.2; human.
DR GeneCards; PRSS42P; -.
DR HGNC; HGNC:30716; PRSS42P.
DR neXtProt; NX_Q7Z5A4; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q7Z5A4; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q7Z5A4; -.
DR TreeFam; TF351676; -.
DR PathwayCommons; Q7Z5A4; -.
DR SignaLink; Q7Z5A4; -.
DR BioGRID-ORCS; 339906; 7 hits in 1066 CRISPR screens.
DR GenomeRNAi; 339906; -.
DR Pharos; Q7Z5A4; Tdark.
DR PRO; PR:Q7Z5A4; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q7Z5A4; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; 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 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.
PE 5: Uncertain;
KW Cell membrane; Cytoplasm; Differentiation; Disulfide bond; Glycoprotein;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Protease; Reference proteome;
KW Serine protease; Signal; Spermatogenesis.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..293
FT /note="Putative serine protease 42"
FT /id="PRO_5000070584"
FT DOMAIN 80..293
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 33..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 166
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 267
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 141
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 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 200..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 232..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 263..291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 293 AA; 32006 MW; E49251407381B489 CRC64;
MSSGGGSRGL LAWLLLLQPW PGQNWAGMAA PRLPSPLLSE EGGENPEASP APGPEAGPPL
NLFTSFPGDS LLCGRTPLRI VGGVDAEEGR WPWQVSVRTK GRHICGGTLV TATWVLTAGH
CISSRFHYSV KMGDRSVYNE NTSVVVSVQR AFVHPKFSTV TTIRNDLALL QLQHPVNFTS
NIQPICIPQE NFQVEGRTRC WVTGWGKTPE REKLASEILQ DVDQYIMCYE ECNKIIQKAL
SSTKDVIIKG MVCGYKEQGK DSCQGDSGGR LACEYNDTWV QVGIVSWGIG CGR
