SWM1_CAEEL
ID SWM1_CAEEL Reviewed; 135 AA.
AC Q18158;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Serine protease inhibitor swm-1 {ECO:0000305};
DE AltName: Full=Sperm activation without mating protein 1 {ECO:0000312|WormBase:C25E10.9};
DE Flags: Precursor;
GN Name=swm-1 {ECO:0000312|WormBase:C25E10.9};
GN ORFNames=C25E10.9 {ECO:0000312|WormBase:C25E10.9};
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|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 [2] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLY-38 AND CYS-80.
RX PubMed=16461278; DOI=10.1016/j.cub.2005.12.041;
RA Stanfield G.M., Villeneuve A.M.;
RT "Regulation of sperm activation by SWM-1 is required for reproductive
RT success of C. elegans males.";
RL Curr. Biol. 16:252-263(2006).
RN [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLY-38 AND CYS-80.
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 [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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 inhibitor (Probable) (PubMed:22125495).
CC Probably by inhibiting serine protease tyr-5 in males, prevents the
CC maturation of spermatids into mature motile spermatozoa until their
CC transfer into a hermaphrodite (PubMed:16461278, PubMed:22125495,
CC PubMed:30470702). Also required for efficient sperm transfer and thus
CC for male fertility (PubMed:16461278). {ECO:0000269|PubMed:16461278,
CC ECO:0000269|PubMed:22125495, ECO:0000269|PubMed:30470702,
CC ECO:0000305|PubMed:16461278}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30470702}.
CC Cytoplasmic vesicle, secretory vesicle lumen
CC {ECO:0000269|PubMed:30470702}. Note=In males, partially colocalizes
CC with tyr-5 in vesicles near the apical membrane of cuboidal cells.
CC Secreted predominantly by muscles into the pseudocoelom where it enters
CC the seminal vesicle in males and the spermatheca in hermaphrodites.
CC Localizes around the spermatocytes at the late stages of meiosis.
CC During mating, transferred together with sperm into hermaphrodites
CC where it spread into the uterus. Also, is uptaken by coelomocytes.
CC {ECO:0000269|PubMed:30470702}.
CC -!- TISSUE SPECIFICITY: In male, expressed in the vas deferens cuboidal
CC cells and, in posterior body wall and male-specific diagonal muscles
CC (PubMed:30470702). In hermaphrodites, expressed in posterior body wall
CC muscles and spermatheca (PubMed:30470702).
CC {ECO:0000269|PubMed:30470702}.
CC -!- DEVELOPMENTAL STAGE: In males, expression begins at late larval stage
CC and continues in adults. {ECO:0000269|PubMed:30470702}.
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DR EMBL; BX284605; CCD65654.1; -; Genomic_DNA.
DR PIR; T15610; T15610.
DR RefSeq; NP_505346.1; NM_072945.1.
DR AlphaFoldDB; Q18158; -.
DR STRING; 6239.C25E10.9a; -.
DR EPD; Q18158; -.
DR PaxDb; Q18158; -.
DR PeptideAtlas; Q18158; -.
DR EnsemblMetazoa; C25E10.9.1; C25E10.9.1; WBGene00023417.
DR GeneID; 182893; -.
DR KEGG; cel:CELE_C25E10.9; -.
DR UCSC; C25E10.9b.1; c. elegans.
DR CTD; 182893; -.
DR WormBase; C25E10.9; CE06871; WBGene00023417; swm-1.
DR eggNOG; ENOG502SEN9; Eukaryota.
DR GeneTree; ENSGT00970000195908; -.
DR HOGENOM; CLU_092192_1_0_1; -.
DR InParanoid; Q18158; -.
DR OMA; ACHNTCE; -.
DR OrthoDB; 1625853at2759; -.
DR PhylomeDB; Q18158; -.
DR PRO; PR:Q18158; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00023417; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0099503; C:secretory vesicle; IDA:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0007286; P:spermatid development; IMP:UniProtKB.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR Pfam; PF01826; TIL; 2.
DR SUPFAM; SSF57567; SSF57567; 2.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Differentiation; Disulfide bond; Glycoprotein;
KW Protease inhibitor; Reference proteome; Repeat; Secreted;
KW Serine protease inhibitor; Signal; Spermatogenesis.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..135
FT /note="Serine protease inhibitor swm-1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004186764"
FT DOMAIN 20..73
FT /note="TIL 1"
FT /evidence="ECO:0000255"
FT DOMAIN 80..133
FT /note="TIL 2"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 20..53
FT /evidence="ECO:0000250|UniProtKB:P83516"
FT DISULFID 29..48
FT /evidence="ECO:0000250|UniProtKB:P83516"
FT DISULFID 33..44
FT /evidence="ECO:0000250|UniProtKB:P83516"
FT DISULFID 37..73
FT /evidence="ECO:0000250|UniProtKB:P83516"
FT DISULFID 55..67
FT /evidence="ECO:0000250|UniProtKB:P83516"
FT DISULFID 80..114
FT /evidence="ECO:0000250|UniProtKB:P83516"
FT DISULFID 89..109
FT /evidence="ECO:0000250|UniProtKB:P83516"
FT DISULFID 93..105
FT /evidence="ECO:0000250|UniProtKB:P83516"
FT DISULFID 97..133
FT /evidence="ECO:0000250|UniProtKB:P83516"
FT DISULFID 116..127
FT /evidence="ECO:0000250|UniProtKB:P83516"
FT MUTAGEN 38
FT /note="G->E: In me86; severe reduction in male fertility
FT caused by a premature activation of spermatids and impaired
FT sperm transfer into the hermaphrodite. Seminal fluid
FT transfer and trans-activation of hermaphrodite sperm are
FT normal. Does not affect hermaphrodite self-fertility. In a
FT tyr-5(jn21) mutant background, suppresses premature sperm
FT activation in males."
FT /evidence="ECO:0000269|PubMed:16461278"
FT MUTAGEN 80
FT /note="C->Y: In me66; severe reduction in male fertility
FT caused by a premature activation of spermatids and impaired
FT sperm transfer into the hermaphrodite. Seminal fluid
FT transfer and trans-activation of hermaphrodite sperm are
FT normal. In a tyr-5(jn21) mutant background, suppresses
FT premature sperm activation in males."
FT /evidence="ECO:0000269|PubMed:16461278,
FT ECO:0000269|PubMed:22125495"
SQ SEQUENCE 135 AA; 14737 MW; C8FCFC7464903255 CRC64;
MRILVIITCI VAVATATKTC EANEELVSCH NTCEPQCGYT PKACTEQCIM NTCDCKDGFV
RNSLGKCVEV SECTKETTKC PENETFFGCG TACEATCEKP NPTVCTKQCI VNVCQCSKGF
VRHGLRCIDK KDCPK
