CATG_RAT
ID CATG_RAT Reviewed; 250 AA.
AC P17977; G3V9Q7;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cathepsin G;
DE EC=3.4.21.20 {ECO:0000250|UniProtKB:P08311};
DE Flags: Precursor;
GN Name=Ctsg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000312|EMBL:EDM14312.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 21-46.
RC STRAIN=Sprague-Dawley, and Wistar;
RX PubMed=2222858; DOI=10.1515/bchm3.1990.371.2.595;
RA Bjoerk P., Ohlsson K.;
RT "Purification and N-terminal amino-acid sequence analysis of rat
RT polymorphonuclear leukocyte cathepsin G.";
RL Biol. Chem. Hoppe-Seyler 371:595-601(1990).
CC -!- FUNCTION: Serine protease with trypsin- and chymotrypsin-like
CC specificity. Also displays antibacterial activity against Gram-negative
CC and Gram-positive bacteria independent of its protease activity.
CC Prefers Phe and Tyr residues in the P1 position of substrates but also
CC cleaves efficiently after Trp and Leu. Shows a preference for
CC negatively charged amino acids in the P2' position and for aliphatic
CC amino acids both upstream and downstream of the cleavage site. Required
CC for recruitment and activation of platelets which is mediated by the
CC F2RL3/PAR4 platelet receptor. Binds reversibly to and stimulates B
CC cells and CD4(+) and CD8(+) T cells. Also binds reversibly to natural
CC killer (NK) cells and enhances NK cell cytotoxicity through its
CC protease activity. Cleaves complement C3 (By similarity). Cleaves
CC vimentin (By similarity). Cleaves thrombin receptor F2R/PAR1. Cleaves
CC the synovial mucin-type protein PRG4/lubricin. Cleaves and activates
CC IL36G which promotes expression of chemokines CXCL1 and CXLC8 in
CC keratinocytes. Cleaves IL33 into mature forms which have greater
CC activity than the unprocessed form. Cleaves coagulation factor F8 to
CC produce a partially activated form. Also cleaves and activates
CC coagulation factor F10. Cleaves leukocyte cell surface protein SPN/CD43
CC to releases its extracellular domain and trigger its intramembrane
CC proteolysis by gamma-secretase, releasing the CD43 cytoplasmic tail
CC chain (CD43-ct) which translocates to the nucleus. During apoptosis,
CC cleaves SMARCA2/BRM to produce a 160 kDa cleavage product which
CC localizes to the cytosol. Cleaves MBP in B cell lysosomes at '88-Phe-|-
CC Lys-89' and '112-Phe-|-Ser-113', degrading the major immunogenic MBP
CC epitope and preventing the activation of MBP-specific autoreactive T
CC cells. Cleaves annexin ANXA1 and antimicrobial peptide CAMP to produce
CC peptides which act on neutrophil N-formyl peptide receptors to enhance
CC the release of CXCL2. Acts as a ligand for the N-formyl peptide
CC receptor FPR1, enhancing phagocyte chemotaxis. Has antibacterial
CC activity against the Gram-negative bacteria N.gonorrhoeae and
CC P.aeruginosa. Likely to act against N.gonorrhoeae by interacting with
CC N.gonorrhoeae penA/PBP2. Exhibits potent antimicrobial activity against
CC the Gram-positive bacterium L.monocytogenes. Has antibacterial activity
CC against the Gram-positive bacterium S.aureus and degrades S.aureus
CC biofilms, allowing polymorphonuclear leukocytes to penetrate the
CC biofilm and phagocytose bacteria. Has antibacterial activity against
CC M.tuberculosis (By similarity). {ECO:0000250|UniProtKB:P08311,
CC ECO:0000250|UniProtKB:P28293}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specificity similar to chymotrypsin C.; EC=3.4.21.20;
CC Evidence={ECO:0000250|UniProtKB:P08311};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08311};
CC Peripheral membrane protein {ECO:0000305}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:P08311}. Secreted
CC {ECO:0000250|UniProtKB:P08311}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P08311}. Lysosome
CC {ECO:0000250|UniProtKB:P08311}. Nucleus {ECO:0000250|UniProtKB:P08311}.
CC Note=Secreted by activated neutrophils. Detected in synovial fluid.
CC Localizes to lysosomes in B cells where it is not endogenously
CC synthesized but is internalized from the cell membrane. Localizes to
CC the nucleus during apoptosis. {ECO:0000250|UniProtKB:P08311}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AABR07017957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474049; EDM14312.1; -; Genomic_DNA.
DR PIR; S10608; S10608.
DR RefSeq; NP_001099511.1; NM_001106041.1.
DR AlphaFoldDB; P17977; -.
DR SMR; P17977; -.
DR STRING; 10116.ENSRNOP00000056429; -.
DR MEROPS; S01.133; -.
DR PaxDb; P17977; -.
DR GeneID; 290257; -.
DR KEGG; rno:290257; -.
DR UCSC; RGD:1307681; rat.
DR CTD; 1511; -.
DR RGD; 1307681; Ctsg.
DR VEuPathDB; HostDB:ENSRNOG00000020647; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P17977; -.
DR OMA; QLDQMEI; -.
DR OrthoDB; 1076876at2759; -.
DR TreeFam; TF333630; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Proteomes; UP000234681; Chromosome 15.
DR Bgee; ENSRNOG00000020647; Expressed in thymus and 3 other tissues.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0030141; C:secretory granule; ISO:RGD.
DR GO; GO:0089720; F:caspase binding; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISO:RGD.
DR GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR GO; GO:0048018; F:receptor ligand activity; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; ISO:RGD.
DR GO; GO:0019731; P:antibacterial humoral response; ISO:RGD.
DR GO; GO:0098786; P:biofilm matrix disassembly; ISS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0050832; P:defense response to fungus; ISO:RGD.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR GO; GO:0002548; P:monocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0050868; P:negative regulation of T cell activation; ISS:UniProtKB.
DR GO; GO:0042119; P:neutrophil activation; ISS:UniProtKB.
DR GO; GO:0070946; P:neutrophil-mediated killing of gram-positive bacterium; ISO:RGD.
DR GO; GO:0030168; P:platelet activation; ISS:UniProtKB.
DR GO; GO:0050778; P:positive regulation of immune response; ISO:RGD.
DR GO; GO:1901731; P:positive regulation of platelet aggregation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0016485; P:protein processing; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
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 Antibiotic; Antimicrobial; Cell membrane; Chemotaxis; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lysosome; Membrane; Nucleus; Protease; Reference proteome; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..20
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P08311"
FT /id="PRO_0000453628"
FT CHAIN 21..250
FT /note="Cathepsin G"
FT /evidence="ECO:0000255"
FT /id="PRO_0000453629"
FT DOMAIN 21..244
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 21..25
FT /note="Important for antimicrobial activity"
FT /evidence="ECO:0000250|UniProtKB:P08311"
FT REGION 97..112
FT /note="Important for antimicrobial activity"
FT /evidence="ECO:0000250|UniProtKB:P08311"
FT ACT_SITE 64
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 109
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 143..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 173..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 250 AA; 27804 MW; CCA0F0389C5BBF75 CRC64;
MQPLLFLLIF VLFQEDEAGK IIGGREARPN SHPYMAFLLI QSPEGLSACG GFLVREDFVL
TAGHCFGSSI NVTLGAHNIR RQEGTQQHIT VLRAIRHPDY NPPPVIQNDI MLLQLRSRAR
RSRAVKPVAL PQATKRVQPG ALCTVAGWGL VSQRRGTNVL QEVKLRVQTD QTCANRFQFY
NSQTQICVGN PRERKSAFKG DSGGPLVCNN VAQGIVSYGS SSGNPPAVFT RIQSFMPWIK
RTMRRLSSRY
