TRYL5_CAEEL
ID TRYL5_CAEEL Reviewed; 327 AA.
AC O01887;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Trypsin-like protease try-5 {ECO:0000312|WormBase:K07B1.1};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU00274};
DE AltName: Full=Trypsin-like serine protease try-5 {ECO:0000305};
DE Flags: Precursor;
GN Name=try-5 {ECO:0000312|WormBase:K07B1.1};
GN ORFNames=K07B1.1 {ECO:0000312|WormBase:K07B1.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AEV41575.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP MET-1; CYS-29 AND 308-GLY--ALA-327.
RX PubMed=22125495; DOI=10.1371/journal.pgen.1002375;
RA Smith J.R., Stanfield G.M.;
RT "TRY-5 Is a Sperm-Activating Protease in Caenorhabditis elegans Seminal
RT Fluid.";
RL PLoS Genet. 7:E1002375-E1002375(2011).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=30470702; DOI=10.1242/dev.167734;
RA Chavez D.R., Snow A.K., Smith J.R., Stanfield G.M.;
RT "Soma-germ line interactions and a role for muscle in the regulation of C.
RT elegans sperm motility.";
RL Development 145:0-0(2018).
CC -!- FUNCTION: Serine protease which, in males, acts as a promoting signal
CC during mating to activate sperm. {ECO:0000269|PubMed:22125495}.
CC -!- ACTIVITY REGULATION: In the male gonad, probably maintained inactive by
CC swm-1. {ECO:0000269|PubMed:22125495}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22125495,
CC ECO:0000269|PubMed:30470702}. Cytoplasmic vesicle, secretory vesicle
CC lumen {ECO:0000269|PubMed:22125495, ECO:0000269|PubMed:30470702}.
CC Note=In males, partially colocalizes with swm-1 in vesicles near the
CC apical membrane of cuboidal cells (PubMed:30470702, PubMed:22125495).
CC During the spicule insertion stage of mating, secreted by the male vas
CC deferens and transferred together with sperm into hermaphrodites where
CC it spread into the uterus (PubMed:22125495).
CC {ECO:0000269|PubMed:22125495, ECO:0000269|PubMed:30470702}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the male gonad including
CC the seminal vesicle, the valve region and the vas deferens.
CC {ECO:0000269|PubMed:22125495, ECO:0000269|PubMed:30470702}.
CC -!- DEVELOPMENTAL STAGE: Expressed in male L4 larvae and adults.
CC {ECO:0000269|PubMed:22125495}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR EMBL; JN651275; AEV41575.1; -; mRNA.
DR EMBL; JN651276; AEV41576.1; -; mRNA.
DR EMBL; JN651277; AEV41577.1; -; mRNA.
DR EMBL; BX284605; CCD68623.1; -; Genomic_DNA.
DR RefSeq; NP_505421.3; NM_073020.3.
DR AlphaFoldDB; O01887; -.
DR SMR; O01887; -.
DR STRING; 6239.K07B1.1.1; -.
DR MEROPS; S01.B74; -.
DR PaxDb; O01887; -.
DR PeptideAtlas; O01887; -.
DR EnsemblMetazoa; K07B1.1.1; K07B1.1.1; WBGene00006623.
DR GeneID; 187088; -.
DR KEGG; cel:CELE_K07B1.1; -.
DR UCSC; K07B1.1; c. elegans.
DR CTD; 187088; -.
DR WormBase; K07B1.1; CE45442; WBGene00006623; try-5.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000167670; -.
DR HOGENOM; CLU_006842_7_6_1; -.
DR InParanoid; O01887; -.
DR OMA; ANYACLP; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; O01887; -.
DR PRO; PR:O01887; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00006623; Expressed in adult organism and 3 other tissues.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0099503; C:secretory vesicle; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0007286; P:spermatid development; IMP:UniProtKB.
DR Gene3D; 2.40.10.10; -; 2.
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 1: Evidence at protein level;
KW Cytoplasmic vesicle; Differentiation; Disulfide bond; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Secreted; Serine protease; Signal;
KW Spermatogenesis.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..327
FT /note="Trypsin-like protease try-5"
FT /evidence="ECO:0000255"
FT /id="PRO_5015096730"
FT DOMAIN 43..327
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 88
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 270
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 73..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 242..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 266..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT MUTAGEN 1
FT /note="M->T: In jn21; in males, suppresses premature sperm
FT activation in a swm-1 (me66) mutant background."
FT /evidence="ECO:0000269|PubMed:22125495"
FT MUTAGEN 29
FT /note="C->Y: In jn2; male and hermaphrodite fertility is
FT normal. Suppresses premature sperm activation in a swm-1
FT (me66) mutant background."
FT /evidence="ECO:0000269|PubMed:22125495"
FT MUTAGEN 308..327
FT /note="Missing: In jn13; in males, suppresses premature
FT sperm activation in a swm-1 (me66) mutant background."
FT /evidence="ECO:0000269|PubMed:22125495"
SQ SEQUENCE 327 AA; 35996 MW; FB09AA1E7A325A86 CRC64;
MRPRIIVFLF QVLVVIKGTK LKYYNDELCG RQSTYTSFML TDAAGNTGNP THLAPWAVQI
RVKARKGDFE VICGGTLITL KHVLTAAHCF QKHFGAKKEG GEENSMSGRY CESNQRFTDS
EILTRTVVTV GAMCTRLEQK YGCVNEKQNG KTLKISRFAI GDFYKTHCEQ GNDIVILELE
STIDDVEGAN YACLPFLPEV NIQSGANVTS FGWGSDPGKG FDNAAFPMIQ VLTLATETLA
TCEENWGTSI PFDSFCTAEE EDKNVCSGDS GGGLTFHQSD SAREFIIAIV SYGSDCVQLI
GGSEPRSQIN TDVRKHQKFI VNFINQA
