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Spermosin (EC 3.4.21.99) [Cleaved into: Spermosin L1 light chain; Spermosin L2 light chain; Spermosin heavy chain]

 SPRM_HALRO              Reviewed;         388 AA.
Q966V2;
13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 65.
RecName: Full=Spermosin {ECO:0000303|PubMed:11856325, ECO:0000312|EMBL:BAB60896.1};
EC=3.4.21.99;
Contains:
RecName: Full=Spermosin L1 light chain {ECO:0000303|PubMed:11856325};
Contains:
RecName: Full=Spermosin L2 light chain {ECO:0000303|PubMed:11856325};
Contains:
RecName: Full=Spermosin heavy chain {ECO:0000303|PubMed:11856325};
Flags: Precursor;
Halocynthia roretzi (Sea squirt) (Cynthia roretzi).
Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
Pyuridae; Halocynthia.
NCBI_TaxID=7729;
[1] {ECO:0000305, ECO:0000312|EMBL:BAB60896.1}
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-26; 97-100 AND
130-163, SUBUNIT, AND TISSUE SPECIFICITY.
TISSUE=Gonad {ECO:0000269|PubMed:11856325}, and
Sperm {ECO:0000269|PubMed:11856325};
PubMed=11856325; DOI=10.1046/j.0014-2956.2001.02696.x;
Kodama E., Baba T., Kohno N., Satoh S., Yokosawa H., Sawada H.;
"Spermosin, a trypsin-like protease from ascidian sperm: cDNA cloning,
protein structures and functional analysis.";
Eur. J. Biochem. 269:657-663(2002).
[2] {ECO:0000305}
ENZYME REGULATION.
PubMed=6381175; DOI=10.1016/0012-1606(84)90281-1;
Sawada H., Yokosawa H., Someno T., Saino T., Ishii S.;
"Evidence for the participation of two sperm proteases, spermosin and
acrosin, in fertilization of the ascidian, Halocynthia roretzi:
inhibitory effects of leupeptin analogs on enzyme activities and
fertilization.";
Dev. Biol. 105:246-249(1984).
[3] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=6365918;
Sawada H., Yokosawa H., Ishii S.;
"Purification and characterization of two types of trypsin-like
enzymes from sperm of the ascidian (Prochordata) Halocynthia roretzi.
Evidence for the presence of spermosin, a novel acrosin-like enzyme.";
J. Biol. Chem. 259:2900-2904(1984).
[4] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=8670234; DOI=10.1006/bbrc.1996.0773;
Sawada H., Iwasaki K., Kihara-Negishi F., Ariga H., Yokosawa H.;
"Localization, expression, and the role in fertilization of spermosin,
an ascidian sperm trypsin-like protease.";
Biochem. Biophys. Res. Commun. 222:499-504(1996).
[5] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=8914083;
DOI=10.1002/(SICI)1098-2795(199610)45:2<240::AID-MRD18>3.0.CO;2-4;
Sawada H., Someno T.;
"Substrate specificity of ascidian sperm trypsin-like proteases,
spermosin and acrosin.";
Mol. Reprod. Dev. 45:240-243(1996).
-!- FUNCTION: Trypsin-like protease with a narrow substrate
specificity. Preferentially hydrolyzes substrates with Pro in the
P2 position and Val in the P3 position. Plays a role in
fertilization. {ECO:0000269|PubMed:6365918,
ECO:0000269|PubMed:8670234, ECO:0000269|PubMed:8914083}.
-!- CATALYTIC ACTIVITY: Hydrolyzes arginyl bonds, preferably with Pro
in the P2 position. {ECO:0000269|PubMed:6365918,
ECO:0000269|PubMed:8914083}.
-!- ENZYME REGULATION: Inhibited by peptidyl-argininals wth Pro in the
P2 position, diisopropyl fluorophosphate, phenylmethanesulfonyl
fluoride, leupeptin, antipain, soybean trypsin inhibitor,
aprotinin, ovomucoid, valyl-prolyl-arginyl-chloromethane, glycyl-
valyl-arginyl-chloromethane, p-aminobenzamidine, benzamidine, zinc
chloride and mercuric chloride. {ECO:0000269|PubMed:6365918,
ECO:0000269|PubMed:6381175, ECO:0000269|PubMed:8914083}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=145 uM for Boc-Val-Pro-Arg-MCA {ECO:0000269|PubMed:6365918};
pH dependence:
Optimum pH is 8.5-9.0. {ECO:0000269|PubMed:6365918};
-!- SUBUNIT: Heterodimer of a heavy chain and either an L1 light chain
or an L2 light chain linked by a disulfide bond.
{ECO:0000269|PubMed:11856325}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8670234}.
Note=Localized on the sperm head. Released into the surrounding
seawater in response to the sperm reaction, a large proportion
remains associated with the sperm cell surface.
{ECO:0000269|PubMed:8670234}.
-!- TISSUE SPECIFICITY: Detected in sperm, but not in unfertilized
eggs (at protein level). Expressed in gonad, but not in
hepatopancreas, intestine or branchial basket.
{ECO:0000269|PubMed:11856325, ECO:0000269|PubMed:8670234}.
-!- DEVELOPMENTAL STAGE: Expression begins about half a month before
the start of the spawning season (early December), and continues
throughout the spawning season. {ECO:0000269|PubMed:8670234}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; AB052776; BAB60896.1; -; mRNA.
ProteinModelPortal; Q966V2; -.
MEROPS; S01.082; -.
KEGG; ag:BAB60896; -.
KO; K20751; -.
BRENDA; 3.4.21.99; 2564.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
Secreted; Serine protease; Signal.
SIGNAL 1 22 {ECO:0000269|PubMed:11856325}.
CHAIN 23 129 Spermosin L1 light chain.
{ECO:0000269|PubMed:11856325}.
/FTId=PRO_0000395364.
CHAIN 97 127 Spermosin L2 light chain.
{ECO:0000269|PubMed:11856325}.
/FTId=PRO_0000395365.
CHAIN 130 388 Spermosin heavy chain.
{ECO:0000269|PubMed:11856325}.
/FTId=PRO_0000395366.
DOMAIN 130 372 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
COMPBIAS 28 88 Pro-rich. {ECO:0000255}.
ACT_SITE 178 178 Charge relay system.
{ECO:0000250|UniProtKB:Q9CR35}.
ACT_SITE 231 231 Charge relay system.
{ECO:0000250|UniProtKB:Q9CR35}.
ACT_SITE 324 324 Charge relay system.
{ECO:0000250|UniProtKB:Q9CR35}.
DISULFID 116 251 Interchain (between light and heavy
chains). {ECO:0000255|PROSITE-
ProRule:PRU00274,
ECO:0000269|PubMed:11856325}.
DISULFID 163 179 {ECO:0000250|UniProtKB:Q9CR35,
ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 265 330 {ECO:0000250|UniProtKB:Q9CR35,
ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 295 310 {ECO:0000250|UniProtKB:Q9CR35,
ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 320 349 {ECO:0000250|UniProtKB:Q9CR35,
ECO:0000255|PROSITE-ProRule:PRU00274}.
SEQUENCE 388 AA; 42145 MW; 5F61BDE7588AD96C CRC64;
MAAINVIFIS GAIALFALTG SCSESTNPFT NKPYATQNPY SPPQTNQPTK RPYQPGPAPT
PAPYIPQKTN PPTKRPLNPT PSPTAKPPSE NSESENSEGP VLIEEDHFTV DANFKCGIPP
VEPDLKKGKI VGGAEAVPNS WPYAAAFGTY DISGGKLEVS QMCGSTIITP RHALTAAHCF
MMDPDIDQTY YIFMGLHDET TYKGVRPNKI VGVRYHPKTN VFTDDPWLVY DFAILTLRKK
VIANFAWNYA CLPQPKKIPP EGTICWSVGW GVTQNTGGDN VLKQVAIDLV SEKRCKEEYR
STITSKSTIC GGTTPGQDTC QGDSGGPLFC KEDGKWYLQG IVSYGPSVCG SGPMAAYAAV
AYNLEWLCCY MPNLPSCEDI ECDESGEN


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