ID SPRM_HALRO Reviewed; 388 AA.
AC Q966V2;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Spermosin {ECO:0000303|PubMed:11856325, ECO:0000312|EMBL:BAB60896.1};
DE EC=3.4.21.99;
DE Contains:
DE RecName: Full=Spermosin L1 light chain {ECO:0000303|PubMed:11856325};
DE Contains:
DE RecName: Full=Spermosin L2 light chain {ECO:0000303|PubMed:11856325};
DE Contains:
DE RecName: Full=Spermosin heavy chain {ECO:0000303|PubMed:11856325};
DE Flags: Precursor;
OS Halocynthia roretzi (Sea squirt) (Cynthia roretzi).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC Pyuridae; Halocynthia.
OX NCBI_TaxID=7729;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB60896.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-26; 97-100 AND 130-163,
RP SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Gonad {ECO:0000269|PubMed:11856325}, and
RC Sperm {ECO:0000269|PubMed:11856325};
RX PubMed=11856325; DOI=10.1046/j.0014-2956.2001.02696.x;
RA Kodama E., Baba T., Kohno N., Satoh S., Yokosawa H., Sawada H.;
RT "Spermosin, a trypsin-like protease from ascidian sperm: cDNA cloning,
RT protein structures and functional analysis.";
RL Eur. J. Biochem. 269:657-663(2002).
RN [2] {ECO:0000305}
RP ACTIVITY REGULATION.
RX PubMed=6381175; DOI=10.1016/0012-1606(84)90281-1;
RA Sawada H., Yokosawa H., Someno T., Saino T., Ishii S.;
RT "Evidence for the participation of two sperm proteases, spermosin and
RT acrosin, in fertilization of the ascidian, Halocynthia roretzi: inhibitory
RT effects of leupeptin analogs on enzyme activities and fertilization.";
RL Dev. Biol. 105:246-249(1984).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=6365918; DOI=10.1016/s0021-9258(17)43233-9;
RA Sawada H., Yokosawa H., Ishii S.;
RT "Purification and characterization of two types of trypsin-like enzymes
RT from sperm of the ascidian (Prochordata) Halocynthia roretzi. Evidence for
RT the presence of spermosin, a novel acrosin-like enzyme.";
RL J. Biol. Chem. 259:2900-2904(1984).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=8670234; DOI=10.1006/bbrc.1996.0773;
RA Sawada H., Iwasaki K., Kihara-Negishi F., Ariga H., Yokosawa H.;
RT "Localization, expression, and the role in fertilization of spermosin, an
RT ascidian sperm trypsin-like protease.";
RL Biochem. Biophys. Res. Commun. 222:499-504(1996).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=8914083;
RX DOI=10.1002/(sici)1098-2795(199610)45:2<240::aid-mrd18>3.0.co;2-4;
RA Sawada H., Someno T.;
RT "Substrate specificity of ascidian sperm trypsin-like proteases, spermosin
RT and acrosin.";
RL Mol. Reprod. Dev. 45:240-243(1996).
CC -!- FUNCTION: Trypsin-like protease with a narrow substrate specificity.
CC Preferentially hydrolyzes substrates with Pro in the P2 position and
CC Val in the P3 position. Plays a role in fertilization.
CC {ECO:0000269|PubMed:6365918, ECO:0000269|PubMed:8670234,
CC ECO:0000269|PubMed:8914083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes arginyl bonds, preferably with Pro in the P2
CC position.; EC=3.4.21.99; Evidence={ECO:0000269|PubMed:6365918,
CC ECO:0000269|PubMed:8914083};
CC -!- ACTIVITY REGULATION: Inhibited by peptidyl-argininals with Pro in the
CC P2 position, diisopropyl fluorophosphate, phenylmethanesulfonyl
CC fluoride, leupeptin, antipain, soybean trypsin inhibitor, aprotinin,
CC ovomucoid, valyl-prolyl-arginyl-chloromethane, glycyl-valyl-arginyl-
CC chloromethane, p-aminobenzamidine, benzamidine, zinc chloride and
CC mercuric chloride. {ECO:0000269|PubMed:6365918,
CC ECO:0000269|PubMed:6381175, ECO:0000269|PubMed:8914083}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=145 uM for Boc-Val-Pro-Arg-MCA {ECO:0000269|PubMed:6365918};
CC pH dependence:
CC Optimum pH is 8.5-9.0. {ECO:0000269|PubMed:6365918};
CC -!- SUBUNIT: Heterodimer of a heavy chain and either an L1 light chain or
CC an L2 light chain linked by a disulfide bond.
CC {ECO:0000269|PubMed:11856325}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8670234}.
CC Note=Localized on the sperm head. Released into the surrounding
CC seawater in response to the sperm reaction, a large proportion remains
CC associated with the sperm cell surface. {ECO:0000269|PubMed:8670234}.
CC -!- TISSUE SPECIFICITY: Detected in sperm, but not in unfertilized eggs (at
CC protein level). Expressed in gonad, but not in hepatopancreas,
CC intestine or branchial basket. {ECO:0000269|PubMed:11856325,
CC ECO:0000269|PubMed:8670234}.
CC -!- DEVELOPMENTAL STAGE: Expression begins about half a month before the
CC start of the spawning season (early December), and continues throughout
CC the spawning season. {ECO:0000269|PubMed:8670234}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AB052776; BAB60896.1; -; mRNA.
DR AlphaFoldDB; Q966V2; -.
DR SMR; Q966V2; -.
DR MEROPS; S01.082; -.
DR KEGG; ag:BAB60896; -.
DR BRENDA; 3.4.21.99; 2564.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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 InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24264:SF54; HEPATOCYTE GROWTH FACTOR ACTIVATOR-LIKE; 1.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Protease; Secreted;
KW Serine protease; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:11856325"
FT CHAIN 23..129
FT /note="Spermosin L1 light chain"
FT /evidence="ECO:0000269|PubMed:11856325"
FT /id="PRO_0000395364"
FT CHAIN 97..127
FT /note="Spermosin L2 light chain"
FT /evidence="ECO:0000269|PubMed:11856325"
FT /id="PRO_0000395365"
FT CHAIN 130..388
FT /note="Spermosin heavy chain"
FT /evidence="ECO:0000269|PubMed:11856325"
FT /id="PRO_0000395366"
FT DOMAIN 130..372
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 29..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9CR35"
FT ACT_SITE 231
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9CR35"
FT ACT_SITE 324
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9CR35"
FT DISULFID 116..251
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:11856325"
FT DISULFID 163..179
FT /evidence="ECO:0000250|UniProtKB:Q9CR35,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 265..330
FT /evidence="ECO:0000250|UniProtKB:Q9CR35,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 295..310
FT /evidence="ECO:0000250|UniProtKB:Q9CR35,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 320..349
FT /evidence="ECO:0000250|UniProtKB:Q9CR35,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
SQ 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
//
