PRS57_RAT
ID PRS57_RAT Reviewed; 278 AA.
AC Q6IE59;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Serine protease 57;
DE EC=3.4.21.- {ECO:0000250|UniProtKB:Q6UWY2};
DE AltName: Full=Complement factor D-like protein;
DE AltName: Full=Neutrophil serine protease 4 {ECO:0000250|UniProtKB:Q6UWY2};
DE Short=NSP4 {ECO:0000250|UniProtKB:Q6UWY2};
DE AltName: Full=Serine protease 1-like protein 1;
DE Flags: Precursor;
GN Name=Prss57; Synonyms=Df2, Prssl1;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
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]
RP IDENTIFICATION.
RC STRAIN=Sprague-Dawley;
RX PubMed=15060002; DOI=10.1101/gr.1946304;
RA Puente X.S., Lopez-Otin C.;
RT "A genomic analysis of rat proteases and protease inhibitors.";
RL Genome Res. 14:609-622(2004).
CC -!- FUNCTION: Serine protease that cleaves preferentially after Arg
CC residues. Can also cleave after citrulline (deimidated arginine) and
CC methylarginine residues. {ECO:0000250|UniProtKB:Q6UWY2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule lumen
CC {ECO:0000250|UniProtKB:Q6UWY2}. Secreted
CC {ECO:0000250|UniProtKB:Q6UWY2}. Note=Stored in cytoplasmic granules and
CC secreted as active enzyme in response to stimulation of neutrophils.
CC {ECO:0000250|UniProtKB:Q6UWY2}.
CC -!- PTM: After cleavage of the signal peptide, the N-terminus is probably
CC further processed by CTSC. Processing by CTSC is probably required for
CC accumulation in cytoplasmic granules; in the absence of CTSC the
CC protein does not accumulate. {ECO:0000250|UniProtKB:Q6UWY2}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6UWY2}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AABR03056948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000334; CAE48389.1; -; mRNA.
DR RefSeq; NP_001003956.1; NM_001003956.1.
DR RefSeq; XP_006241041.1; XM_006240979.3.
DR AlphaFoldDB; Q6IE59; -.
DR SMR; Q6IE59; -.
DR STRING; 10116.ENSRNOP00000031690; -.
DR MEROPS; S01.368; -.
DR GlyGen; Q6IE59; 1 site.
DR PaxDb; Q6IE59; -.
DR GeneID; 408241; -.
DR KEGG; rno:408241; -.
DR UCSC; RGD:1303330; rat.
DR CTD; 400668; -.
DR RGD; 1303330; Prss57.
DR VEuPathDB; HostDB:ENSRNOG00000025293; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; Q6IE59; -.
DR OMA; VCNSSWR; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q6IE59; -.
DR TreeFam; TF333630; -.
DR PRO; PR:Q6IE59; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000025293; Expressed in thymus.
DR Genevisible; Q6IE59; RN.
DR GO; GO:0035578; C:azurophil granule lumen; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Heparin-binding; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..278
FT /note="Serine protease 57"
FT /id="PRO_0000295855"
FT DOMAIN 34..263
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 74
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6UWY2"
FT ACT_SITE 122
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6UWY2"
FT ACT_SITE 218
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6UWY2"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 157..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 188..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 214..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 278 AA; 29518 MW; 0965724CD44BE967 CRC64;
MVPGTGGGRD CLTLVVATAL TQLLWLPGCC GSHIVGGHEV KPHARPYMAS VNFEGHHHCG
GFLFHAHWVL SAAHCFSDRD PSTGLVVLGA HALLTPEPTQ QVFGIAAVVS HPDFEPTTQA
NDICLLRLNG SAVLGPAVRL LRLPRRGAKP PVAGTRCRVS GWGSVSDFEE PPPGLMEVEV
RILDLSVCNS SWQGQLSPAM LCTHSGDRRR RGFCSADSGG PLVCGNRAHG LVSFSGLWCG
DPKTPDVYTQ VSAFVSWIWD VVRASPTPGS MGCSLRAV
