PRS40_RAT
ID PRS40_RAT Reviewed; 369 AA.
AC Q6AXZ6;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Serine protease 40;
DE EC=3.4.21.-;
DE AltName: Full=Testicular serine protease 2;
DE Flags: Precursor;
GN Name=Prss40; Synonyms=Tesp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
CC -!- FUNCTION: May play an important role in the sperm/egg interaction;
CC released during the acrosome reaction. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome.
CC Secreted {ECO:0000250}.
CC -!- MISCELLANEOUS: There appears to be no human ortholog of this protein.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; BC079254; AAH79254.1; -; mRNA.
DR RefSeq; NP_001013244.1; NM_001013226.1.
DR AlphaFoldDB; Q6AXZ6; -.
DR SMR; Q6AXZ6; -.
DR STRING; 10116.ENSRNOP00000038053; -.
DR MEROPS; S01.985; -.
DR PaxDb; Q6AXZ6; -.
DR Ensembl; ENSRNOT00000034214; ENSRNOP00000038053; ENSRNOG00000023858.
DR GeneID; 363215; -.
DR KEGG; rno:363215; -.
DR UCSC; RGD:1561330; rat.
DR CTD; 21755; -.
DR RGD; 1561330; Prss40.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000157345; -.
DR InParanoid; Q6AXZ6; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q6AXZ6; -.
DR TreeFam; TF351692; -.
DR PRO; PR:Q6AXZ6; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000023858; Expressed in testis and 12 other tissues.
DR ExpressionAtlas; Q6AXZ6; baseline and differential.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; 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; 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 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Disulfide bond; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..369
FT /note="Serine protease 40"
FT /id="PRO_0000344983"
FT DOMAIN 70..314
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 265
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 95..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 194..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 227..250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 261..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 369 AA; 41448 MW; F96511B4F112B919 CRC64;
MWGSRAQQSG PDRGRTCLLA VLLLSFSLFQ LHAQDYKPSQ TPPPTSDALL KPMGRVQKEI
CGKTKFQGKI YGGSIAKAER WPWQASLIFR GRHICGAVLI DKNWVASAAH CFKRSLKPSD
YRILLGYNEL SNPSNYSRQM TLSKVIVHED YNKLHSQEKD IVLIQLHLPV RYSSHIFPVC
VPDQTTKEPS DESCWISGWG MVTDDKFLQA PFPLLDSEVF LMNDQECEAF FQTPQISITE
YDAIKDDMIC AGDITNQKST CRGDSGGPLV CLLDSYWYLV GLASWSGACL EPIHSPSIFT
RVSHFSDWIE KKKADTPDVD PSLAPLEETA PSLIGWRNYS AGTTLEPRIC TTLLSSQVLL
LQSIWLRIL