PRS46_RAT
ID PRS46_RAT Reviewed; 314 AA.
AC Q6IE63;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Serine protease 46;
DE EC=3.4.21.-;
DE AltName: Full=Testis-specific serine protease-6;
GN Name=Prss46; Synonyms=Tessp6;
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] OF 1-230.
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 [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: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; CH473984; EDL77052.1; -; Genomic_DNA.
DR EMBL; BN000330; CAE48385.1; -; mRNA.
DR RefSeq; NP_001008865.1; NM_001008865.1.
DR RefSeq; XP_006244055.1; XM_006243993.2.
DR AlphaFoldDB; Q6IE63; -.
DR SMR; Q6IE63; -.
DR STRING; 10116.ENSRNOP00000028479; -.
DR MEROPS; S01.250; -.
DR PaxDb; Q6IE63; -.
DR Ensembl; ENSRNOT00000028479; ENSRNOP00000028479; ENSRNOG00000020981.
DR GeneID; 408245; -.
DR KEGG; rno:408245; -.
DR UCSC; RGD:1302970; rat.
DR CTD; 74306; -.
DR RGD; 1302970; Prss46.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162940; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q6IE63; -.
DR OMA; EICNHRY; -.
DR OrthoDB; 1314811at2759; -.
DR PRO; PR:Q6IE63; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 5.
DR Bgee; ENSRNOG00000020981; Expressed in testis and 2 other tissues.
DR Genevisible; Q6IE63; RN.
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:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
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; Hydrolase; Membrane; Protease; Reference proteome;
KW Serine protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..314
FT /note="Serine protease 46"
FT /id="PRO_0000418334"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 44..281
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 84
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 130
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 233
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 69..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 164..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 197..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 229..257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 314 AA; 34999 MW; 722ECD51D8C930E5 CRC64;
MACGSVDPQG LLSPPLSSAR LSNVPHVEGP WFWSCGQTNI SCKVVNGKVV EVGKWPWQVS
ILFLGMYICS GSLIHHHWVL TAAHCLQRSK NPANYTVKVG VQTLPDNSSS ELLVTSIVIH
ENFINHMSHD IAILKLKYPV TWSPFIQPIC LPEVNFKPSI GTMCWVIGWG LEKAKGAPKT
PYSVQGVAVR IVNNEICNHR YQFLLLKNQK KFIGNDMLCT SPEWGLDTCQ DASGSSLVCQ
MNKTWIQMGV VSWNFGCGRR QFPSIYTSTS HFTQWIKRQI GDLKFASMAV PSFLSPFILT
GYILLVSLGS LWLL