PRS45_RAT
ID PRS45_RAT Reviewed; 330 AA.
AC Q6IE62;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Inactive serine protease 45;
DE AltName: Full=Inactive testis serine protease 5;
DE Flags: Precursor;
GN Name=Prss45; Synonyms=Tessp5;
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: In contrast to other members of the family, lacks the
CC conserved Ser at position 243 which is replaced by a Pro residue,
CC suggesting it is inactive. {ECO:0000305}.
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DR EMBL; AABR03062292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000331; CAE48386.1; -; mRNA.
DR RefSeq; NP_001008864.1; NM_001008864.1.
DR AlphaFoldDB; Q6IE62; -.
DR SMR; Q6IE62; -.
DR STRING; 10116.ENSRNOP00000040152; -.
DR MEROPS; S01.968; -.
DR GlyGen; Q6IE62; 1 site.
DR PaxDb; Q6IE62; -.
DR PRIDE; Q6IE62; -.
DR Ensembl; ENSRNOT00000043249; ENSRNOP00000040152; ENSRNOG00000029649.
DR GeneID; 408244; -.
DR KEGG; rno:408244; -.
DR UCSC; RGD:1303021; rat.
DR CTD; 260408; -.
DR RGD; 1303021; Prss45.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000161932; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q6IE62; -.
DR OMA; PWEVSLQ; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q6IE62; -.
DR TreeFam; TF351676; -.
DR PRO; PR:Q6IE62; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000029649; Expressed in testis.
DR Genevisible; Q6IE62; RN.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..330
FT /note="Inactive serine protease 45"
FT /id="PRO_5000095982"
FT DOMAIN 45..291
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 172..249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 207..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 239..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 330 AA; 37303 MW; 13F672DDE29FD61A CRC64;
MATSLRLLDA GPGSLRRWIP TCFAALLLLP PRPNLGYNED HAEPVCGAPW WSDSLEERHH
WPWEVSLQIE NEHVCGGALI DQSWVVSAAH CIQGNKEYLV MLGSSTLQPS GSPWALKIPV
GDIIMHPKYW GQNFIRSDIA LLCLETPVTF NKYIQPICLP EHNFNLKVGM KCWVTGWGQA
KQHPSAKLTR SLELWEAEVS IVDNKNCDRV FHKKTFYPQV IPLIRKNMIC TTNHRENPCY
GDPGGPLACE VHGRWILAGI FSWEKACTKA PNLSVYTRID KYTGWIKEQV SRGARSGRCR
TSCLLFLPWL LQLPVSPGPP HPFLFLLCLC
