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PRS43_MOUSE
ID   PRS43_MOUSE             Reviewed;         382 AA.
AC   Q76HL1;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Putative inactive serine protease 43 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=Prss43 {ECO:0000312|MGI:MGI:2684822};
GN   Synonyms=Tessp3 {ECO:0000303|PubMed:23536369};
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 {ECO:0000312|EMBL:BAD06396.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, AND TOPOLOGY.
RX   PubMed=23536369; DOI=10.1095/biolreprod.112.106328;
RA   Yoneda R., Takahashi T., Matsui H., Takano N., Hasebe Y., Ogiwara K.,
RA   Kimura A.P.;
RT   "Three testis-specific paralogous serine proteases play different roles in
RT   murine spermatogenesis and are involved in germ cell survival during
RT   meiosis.";
RL   Biol. Reprod. 88:118-118(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: Plays a role in spermatogenesis. Involved in germ cell
CC       survival during meiosis. {ECO:0000269|PubMed:23536369}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23536369};
CC       Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:23536369}.
CC   -!- TISSUE SPECIFICITY: Testis-specific (PubMed:23536369). Expressed in
CC       germ cells at the stages from late pachytene spermatocytes to
CC       spermatids (PubMed:23536369). {ECO:0000269|PubMed:23536369}.
CC   -!- DEVELOPMENTAL STAGE: In testis, expressed at all stages from the late
CC       pachytene primary spermatocyte to the secondary spermatocyte. Not
CC       detected at day 7 after birth. Expression is detected at day 14 and
CC       increases dramatically at day 21 and reach a peak at day 28 to remain
CC       high until day 56. {ECO:0000269|PubMed:23536369}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR   EMBL; AC139378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB100999; BAD06396.1; -; mRNA.
DR   CCDS; CCDS23574.1; -.
DR   RefSeq; NP_955765.1; NM_199471.1.
DR   AlphaFoldDB; Q76HL1; -.
DR   SMR; Q76HL1; -.
DR   STRING; 10090.ENSMUSP00000076752; -.
DR   MEROPS; S01.099; -.
DR   PaxDb; Q76HL1; -.
DR   PRIDE; Q76HL1; -.
DR   ProteomicsDB; 334438; -.
DR   DNASU; 272643; -.
DR   Ensembl; ENSMUST00000077549; ENSMUSP00000076752; ENSMUSG00000058398.
DR   GeneID; 272643; -.
DR   KEGG; mmu:272643; -.
DR   UCSC; uc009ruv.1; mouse.
DR   CTD; 272643; -.
DR   MGI; MGI:2684822; Prss43.
DR   VEuPathDB; HostDB:ENSMUSG00000058398; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000162829; -.
DR   HOGENOM; CLU_006842_0_4_1; -.
DR   InParanoid; Q76HL1; -.
DR   OMA; CGHRITE; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; Q76HL1; -.
DR   TreeFam; TF351676; -.
DR   BioGRID-ORCS; 272643; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Prss43; mouse.
DR   PRO; PR:Q76HL1; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q76HL1; protein.
DR   Bgee; ENSMUSG00000058398; Expressed in spermatocyte and 12 other tissues.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0007281; P:germ cell development; IDA:MGI.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:0007283; P:spermatogenesis; IDA:MGI.
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   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.
PE   1: Evidence at protein level;
KW   Cell membrane; Differentiation; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Hydrolase; Lipoprotein; Membrane; Protease; Reference proteome; Signal;
KW   Spermatogenesis; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..382
FT                   /note="Putative inactive serine protease 43"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5015098640"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          119..355
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          30..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        159
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        205
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        307
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        144..160
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        239..313
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        272..293
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        303..331
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   382 AA;  42203 MW;  A11894C74E8EEB6E CRC64;
     MGGFCGADRG GFLALLVWLQ LLQPLFSGTY KPREDSGVMH RPQRPRRPRS DPEAPAQQSR
     LKSLSISHPS GVPVSVDRTE IPGSGSPSGT TTKITLENRR SSLGGPFFTD TCGHRITEVD
     PGSLSAGRKW PWQVSLQSQN EHVCGGSLIS HRWVLTAAHC IYEQEEYMVM LGDDMLHSES
     ESVTLVPVQD IIFPSNFDIQ TMRNDIALAL LYFPVNYSSL IQPVCLPEEP FRVKNGTVCW
     VTGWGQQNEI DAGFASILLQ EVQQRILLQK HCNTLFQRQL GTSKNLVIKG MICGLQDSGQ
     SLCWGDSGNP LVCESDNTWT QVGIMSWGIN CNGVPVLSVY TDIAEYNEWV SYVLSQASRM
     DPMGVLVLYL SLVFPLALLV AL
 
 
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