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ACRO_MOUSE
ID   ACRO_MOUSE              Reviewed;         436 AA.
AC   P23578;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 181.
DE   RecName: Full=Acrosin;
DE            EC=3.4.21.10;
DE   Contains:
DE     RecName: Full=Acrosin light chain;
DE   Contains:
DE     RecName: Full=Acrosin heavy chain;
DE   Flags: Precursor;
GN   Name=Acr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2127931; DOI=10.1093/oxfordjournals.jbchem.a123281;
RA   Kashiwabara S., Baba T., Takada M., Watanabe K., Yano Y., Arai Y.;
RT   "Primary structure of mouse proacrosin deduced from the cDNA sequence and
RT   its gene expression during spermatogenesis.";
RL   J. Biochem. 108:785-791(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1939002; DOI=10.1093/oxfordjournals.jbchem.a123466;
RA   Watanabe K., Baba T., Kashiwabara S., Okamoto A., Arai Y.;
RT   "Structure and organization of the mouse acrosin gene.";
RL   J. Biochem. 109:828-833(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2111255; DOI=10.1111/j.1432-0436.1990.tb00757.x;
RA   Klemm U., Maier W.-M., Tsaousidou S., Adham I.M., Willison K., Engel W.;
RT   "Mouse preproacrosin: cDNA sequence, primary structure and postmeiotic
RT   expression in spermatogenesis.";
RL   Differentiation 42:160-166(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1783391; DOI=10.1016/0888-7543(91)90005-y;
RA   Kremling H., Keime S., Wilhelm K., Adham I.M., Hameister H., Engel W.;
RT   "Mouse proacrosin gene: nucleotide sequence, diploid expression, and
RT   chromosomal localization.";
RL   Genomics 11:828-834(1991).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Acrosin is the major protease of mammalian spermatozoa. It is
CC       a serine protease of trypsin-like cleavage specificity, it is
CC       synthesized in a zymogen form, proacrosin and stored in the acrosome.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.10;
CC   -!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
CC   -!- SUBUNIT: Heavy chain (catalytic) and a light chain linked by two
CC       disulfide bonds. Forms a heterodimer with SERPINA5 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA40124.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA00651.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA36704.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D00754; BAA00651.1; ALT_INIT; mRNA.
DR   EMBL; S66245; AAB20293.1; -; Genomic_DNA.
DR   EMBL; S64500; AAB20293.1; JOINED; Genomic_DNA.
DR   EMBL; S66243; AAB20293.1; JOINED; Genomic_DNA.
DR   EMBL; X52466; CAA36704.1; ALT_INIT; mRNA.
DR   EMBL; M85170; AAA40124.1; ALT_INIT; mRNA.
DR   EMBL; M96430; AAA37163.1; -; Genomic_DNA.
DR   EMBL; M96426; AAA37163.1; JOINED; Genomic_DNA.
DR   EMBL; M96427; AAA37163.1; JOINED; Genomic_DNA.
DR   EMBL; M96428; AAA37163.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS27755.1; -.
DR   PIR; A37344; A37344.
DR   PIR; JX0172; JX0172.
DR   RefSeq; NP_038483.1; NM_013455.3.
DR   AlphaFoldDB; P23578; -.
DR   SMR; P23578; -.
DR   BioGRID; 197930; 1.
DR   STRING; 10090.ENSMUSP00000023295; -.
DR   MEROPS; S01.223; -.
DR   GlyGen; P23578; 2 sites.
DR   PaxDb; P23578; -.
DR   PRIDE; P23578; -.
DR   ProteomicsDB; 285845; -.
DR   Antibodypedia; 53952; 210 antibodies from 27 providers.
DR   DNASU; 11434; -.
DR   Ensembl; ENSMUST00000023295; ENSMUSP00000023295; ENSMUSG00000022622.
DR   GeneID; 11434; -.
DR   KEGG; mmu:11434; -.
DR   UCSC; uc007xhc.2; mouse.
DR   CTD; 49; -.
DR   MGI; MGI:87884; Acr.
DR   VEuPathDB; HostDB:ENSMUSG00000022622; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000162430; -.
DR   HOGENOM; CLU_006842_0_4_1; -.
DR   InParanoid; P23578; -.
DR   OMA; LMCRDNV; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; P23578; -.
DR   TreeFam; TF335943; -.
DR   Reactome; R-MMU-1300645; Acrosome Reaction and Sperm:Oocyte Membrane Binding.
DR   BioGRID-ORCS; 11434; 2 hits in 73 CRISPR screens.
DR   PRO; PR:P23578; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; P23578; protein.
DR   Bgee; ENSMUSG00000022622; Expressed in seminiferous tubule of testis and 46 other tissues.
DR   ExpressionAtlas; P23578; baseline and differential.
DR   Genevisible; P23578; MM.
DR   GO; GO:0043159; C:acrosomal matrix; TAS:HGNC-UCL.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR   GO; GO:0005798; C:Golgi-associated vesicle; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0004040; F:amidase activity; ISS:UniProtKB.
DR   GO; GO:0042806; F:fucose binding; ISS:UniProtKB.
DR   GO; GO:0005537; F:mannose binding; ISS:UniProtKB.
DR   GO; GO:0008233; F:peptidase activity; IMP:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
DR   GO; GO:0002077; P:acrosome matrix dispersal; ISO:MGI.
DR   GO; GO:0007340; P:acrosome reaction; ISS:UniProtKB.
DR   GO; GO:0007190; P:activation of adenylate cyclase activity; ISS:UniProtKB.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; IGI:MGI.
DR   GO; GO:0007341; P:penetration of zona pellucida; IMP:MGI.
DR   GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR   GO; GO:0048545; P:response to steroid hormone; ISO:MGI.
DR   GO; GO:0007338; P:single fertilization; IMP:UniProtKB.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR012267; Pept_S1A_acrosin.
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   PIRSF; PIRSF001141; Acrosin; 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   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..19
FT   CHAIN           20..436
FT                   /note="Acrosin"
FT                   /id="PRO_0000027522"
FT   CHAIN           20..42
FT                   /note="Acrosin light chain"
FT                   /id="PRO_0000027523"
FT   CHAIN           43..345
FT                   /note="Acrosin heavy chain"
FT                   /id="PRO_0000027524"
FT   PROPEP          346..436
FT                   /note="Pro-rich"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027525"
FT   DOMAIN          43..291
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        89
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        143
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        241
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        22
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        25..155
FT                   /note="Interchain (between light and heavy chains)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        29..163
FT                   /note="Interchain (between light and heavy chains)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        74..90
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        178..247
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        210..226
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        237..267
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        8
FT                   /note="Missing (in Ref. 3; CAA36704/AAA40124)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        10..14
FT                   /note="VLVLA -> FWSVK (in Ref. 3; CAA36704/AAA40124)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        17..18
FT                   /note="VV -> AG (in Ref. 3; CAA36704/AAA40124)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="T -> A (in Ref. 3; CAA36704/AAA40124)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        26
FT                   /note="D -> F (in Ref. 3; CAA36704/AAA40124)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        33
FT                   /note="F -> T (in Ref. 3; CAA36704/AAA40124)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50..51
FT                   /note="QL -> HV (in Ref. 3; CAA36704/AAA40124)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="Q -> E (in Ref. 3; CAA36704/AAA40124 and 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149
FT                   /note="I -> V (in Ref. 3; CAA36704/AAA40124 and 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        173..174
FT                   /note="QI -> RNT (in Ref. 3; AAA40124)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        173
FT                   /note="Q -> RK (in Ref. 3; CAA36704)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177..183
FT                   /note="TCYVTGW -> LLRDWV (in Ref. 3; AAA40124)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        185..186
FT                   /note="YI -> IH (in Ref. 3; AAA40124)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188..189
FT                   /note="EK -> RE (in Ref. 3; CAA36704/AAA40124)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        251..253
FT                   /note="VDS -> ARQ (in Ref. 3; CAA36704/AAA40124)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        255..268
FT                   /note="FVVVGITSWGVGCA -> LCGRGDHELGGRLC (in Ref. 3;
FT                   AAA40124 and 4; AAA37163)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        299..300
FT                   /note="QP -> PA (in Ref. 3; CAA36704/AAA40124)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        320
FT                   /note="L -> F (in Ref. 3; CAA36704/AAA40124)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        405
FT                   /note="H -> Y (in Ref. 3; CAA36704/AAA40124)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        407..436
FT                   /note="SQYSGPRNYHYRFSTFEPLSNKPSEPFLHS -> PSTVDKELPLPLLHV
FT                   (in Ref. 3; CAA36704/AAA40124 and 4)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   436 AA;  48929 MW;  4CC6EAD56CB51F54 CRC64;
     MVEMLPTVAV LVLAVSVVAK DNTTCDGPCG LRFRQNSQAG TRIVSGQSAQ LGAWPWMVSL
     QIFTSHNSRR YHACGGSLLN SHWVLTAAHC FDNKKKVYDW RLVFGAQEIE YGRNKPVKEP
     QQERYVQKIV IHEKYNVVTE GNDIALLKIT PPVTCGNFIG PCCLPHFKAG PPQIPHTCYV
     TGWGYIKEKA PRPSPVLMEA RVDLIDLDLC NSTQWYNGRV TSTNVCAGYP EGKIDTCQGD
     SGGPLMCRDN VDSPFVVVGI TSWGVGCARA KRPGVYTATW DYLDWIASKI GPNALHLIQP
     ATPHPPTTRH PMVSFHPPSL RPPWYFQHLP SRPLYLRPLR PLLHRPSSTQ TSSSLMPLLS
     PPTPAQPASF TIATQHMRHR TTLSFARRLQ RLIEALKMRT YPMKHPSQYS GPRNYHYRFS
     TFEPLSNKPS EPFLHS
 
 
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