ACRO_MELGA
ID ACRO_MELGA Reviewed; 346 AA.
AC Q2UVH8;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Acrosin {ECO:0000303|PubMed:20561916};
DE EC=3.4.21.10 {ECO:0000250|UniProtKB:P10626};
DE AltName: Full=Proacrosin {ECO:0000303|PubMed:20561916};
DE Short=Proacro1 {ECO:0000312|EMBL:CAJ45027.1};
DE Contains:
DE RecName: Full=Acrosin light chain {ECO:0000303|PubMed:20561916};
DE Contains:
DE RecName: Full=Acrosin heavy chain {ECO:0000303|PubMed:20561916};
DE Flags: Precursor;
GN Name=ACR {ECO:0000250|UniProtKB:P10323};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAJ45027.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 41-66, ACTIVITY REGULATION,
RP GLYCOSYLATION, AND MASS SPECTROMETRY.
RC TISSUE=Sperm {ECO:0000269|PubMed:20561916}, and
RC Testis {ECO:0000312|EMBL:CAJ45027.1};
RX PubMed=20561916; DOI=10.1016/j.cbpb.2010.05.011;
RA Slowinska M., Olczak M., Liszewska E., Watorek W., Ciereszko A.;
RT "Isolation, characterization and cDNA sequencing of acrosin from turkey
RT spermatozoa.";
RL Comp. Biochem. Physiol. 157:127-136(2010).
RN [2] {ECO:0000305}
RP GLYCOSYLATION.
RC TISSUE=Sperm {ECO:0000269|PubMed:3163935};
RX PubMed=3163935; DOI=10.1095/biolreprod38.3.645;
RA Richardson M.E., Bodine A.B., Froman D.P., Thurston R.J.;
RT "Turkey acrosin. I. Isolation, purification, and partial
RT characterization.";
RL Biol. Reprod. 38:645-651(1988).
RN [3] {ECO:0000305}
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Sperm {ECO:0000269|PubMed:1333593};
RX PubMed=1333593; DOI=10.3382/ps.0711789;
RA Richardson M.E., Korn N., Bodine A.B., Thurston R.J.;
RT "Research note: kinetic and inhibition studies with turkey acrosin.";
RL Poult. Sci. 71:1789-1793(1992).
RN [4] {ECO:0000305}
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Sperm {ECO:0000269|PubMed:11665890};
RX PubMed=11665890; DOI=10.1016/s0093-691x(01)00616-1;
RA Glogowski J., Jankowski J., Faruga A., Ottobre J.S., Ciereszko A.;
RT "Acrosin activity in turkey spermatozoa: assay by clinical method and
RT effect of zinc and benzamidine on the activity.";
RL Theriogenology 56:889-901(2001).
CC -!- FUNCTION: Serine protease of trypsin-like cleavage specificity.
CC Synthesized in a zymogen form, proacrosin and stored in the acrosome
CC (By similarity). {ECO:0000250|UniProtKB:P10626}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.10;
CC Evidence={ECO:0000250|UniProtKB:P10626};
CC -!- ACTIVITY REGULATION: Inhibited by aprotinin, ovomucoid, soybean trypsin
CC inhibitor, benzamidine, p-aminobenzamidine, and zinc ions. Activity
CC also inhibited by a Kazal-type proteinase inhibitor.
CC {ECO:0000269|PubMed:11665890, ECO:0000269|PubMed:1333593,
CC ECO:0000269|PubMed:20561916}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.17 mM for N-alpha-benzoyl-DL-arginine-p-nitroanilide (at 25
CC degrees Celsius) {ECO:0000269|PubMed:11665890,
CC ECO:0000269|PubMed:1333593};
CC Vmax=1.50 mmol/min/mg enzyme toward N-alpha-benzoyl-DL-arginine-p-
CC nitroanilide {ECO:0000269|PubMed:11665890,
CC ECO:0000269|PubMed:1333593};
CC pH dependence:
CC Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:11665890,
CC ECO:0000269|PubMed:1333593};
CC Temperature dependence:
CC Active between 20.0-37.0 degrees Celsius. Activity increases above 25
CC degrees Celsius. {ECO:0000269|PubMed:11665890,
CC ECO:0000269|PubMed:1333593};
CC -!- SUBUNIT: Heavy chain (catalytic) and a light chain linked by two
CC disulfide bonds. {ECO:0000250|UniProtKB:P10323}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:20561916,
CC ECO:0000269|PubMed:3163935}.
CC -!- MASS SPECTROMETRY: [Acrosin heavy chain]: Mass=30874;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:20561916};
CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 6.4.
CC {ECO:0000269|PubMed:20561916}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AM167974; CAJ45027.1; -; mRNA.
DR AlphaFoldDB; Q2UVH8; -.
DR SMR; Q2UVH8; -.
DR MEROPS; S01.223; -.
DR InParanoid; Q2UVH8; -.
DR BRENDA; 3.4.21.10; 3210.
DR SABIO-RK; Q2UVH8; -.
DR Proteomes; UP000001645; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0097180; C:serine protease inhibitor complex; IDA:AgBase.
DR GO; GO:0004040; F:amidase activity; IDA:AgBase.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
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 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; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..346
FT /note="Acrosin"
FT /evidence="ECO:0000255"
FT /id="PRO_5000077652"
FT CHAIN 20..40
FT /note="Acrosin light chain"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:20561916"
FT /id="PRO_0000415801"
FT CHAIN 41..265
FT /note="Acrosin heavy chain"
FT /evidence="ECO:0000269|PubMed:20561916"
FT /id="PRO_0000415802"
FT PROPEP 266..346
FT /evidence="ECO:0000250|UniProtKB:P10323"
FT /id="PRO_0000415803"
FT DOMAIN 41..284
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 85
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9GL10"
FT ACT_SITE 134
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9GL10"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9GL10"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..146
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000250|UniProtKB:Q9GL10,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 27..154
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000250|UniProtKB:Q9GL10,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 70..86
FT /evidence="ECO:0000250|UniProtKB:Q9GL10,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 168..240
FT /evidence="ECO:0000250|UniProtKB:Q9GL10,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 203..219
FT /evidence="ECO:0000250|UniProtKB:Q9GL10,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 230..260
FT /evidence="ECO:0000250|UniProtKB:Q9GL10,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 346 AA; 37950 MW; FC0C38468C3310E1 CRC64;
MALLLPLAVL LAACRPGHGF SGGCDTCGLR PVAYHYGGMR VVGGTEALHG SWPWIVSIQN
PRFAGTGHMC GGSLITPQWV LSAAHCFGRP NYILQSRVVI GANDLTQLGQ EVEVRSIRRA
ILHEYFNNKT MINDIALLEL DRPVHCSYYI QLACVPDPSL RVSELTDCYV SGWGHMGMRS
AAPTQTAEVL QEAKVHLLDL NLCNSSHWYD GVLHSHNLCA GYPQGGIDTC QGDSGGPLMC
RDSSADYFWL VGVTSWGRGC GRAFRPGIYT STQHFYNWIL LQVRAAAHPT SRTWSHYMST
SSYHHGPNAV PTQPSVSDSC PFPAQKLREF FTGVQNLLQS LWGSKA
