TMPS9_MOUSE
ID TMPS9_MOUSE Reviewed; 1065 AA.
AC P69525;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Transmembrane protease serine 9;
DE EC=3.4.21.-;
DE AltName: Full=Polyserase-I;
DE AltName: Full=Polyserine protease 1;
DE Short=Polyserase-1;
DE Contains:
DE RecName: Full=Serase-1;
DE Contains:
DE RecName: Full=Serase-2;
DE Contains:
DE RecName: Full=Serase-3;
GN Name=Tmprss9;
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;
RN [1]
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).
RN [2]
RP IDENTIFICATION.
RX PubMed=12886014; DOI=10.1073/pnas.1633392100;
RA Cal S., Quesada V., Garabaya C., Lopez-Otin C.;
RT "Polyserase-I, a human polyprotease with the ability to generate
RT independent serine protease domains from a single translation product.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9185-9190(2003).
CC -!- FUNCTION: Serase-1 and serase-2 are serine proteases that hydrolyze the
CC peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC. In
CC contrast, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Ala-Pro-Ala-AMC are not
CC significantly hydrolyzed (By similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Inhibited by serine protease inhibitors PMSF and
CC 4-(2-aminoethyl)benzenesulfonyl fluoride, but not by EDTA.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: The serine protease 1 and 2 domains are catalytically active,
CC whereas the serine protease 3 domain lacks the essential Ser residue of
CC the catalytic triad at position 1015 and is predicted to be inactive.
CC {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved to generate 3 independent serine protease
CC chains. The cleaved chains may remain attached to the membrane thanks
CC to disulfide bonds. It is unclear whether cleavage always takes place
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AC152413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC166937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P69525; -.
DR SMR; P69525; -.
DR STRING; 10090.ENSMUSP00000100970; -.
DR GlyGen; P69525; 4 sites.
DR iPTMnet; P69525; -.
DR PhosphoSitePlus; P69525; -.
DR PaxDb; P69525; -.
DR PRIDE; P69525; -.
DR ProteomicsDB; 259268; -.
DR MGI; MGI:3612246; Tmprss9.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P69525; -.
DR PhylomeDB; P69525; -.
DR ChiTaRS; Tmprss9; mouse.
DR PRO; PR:P69525; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P69525; protein.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:MGI.
DR GO; GO:0031639; P:plasminogen activation; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; IDA:MGI.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd00190; Tryp_SPc; 3.
DR Gene3D; 2.40.10.10; -; 4.
DR Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR017324; Tmprss9.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00089; Trypsin; 3.
DR PIRSF; PIRSF037931; TMPRSS9_polyserase-1; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00020; Tryp_SPc; 3.
DR SUPFAM; SSF50494; SSF50494; 3.
DR SUPFAM; SSF57424; SSF57424; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 3.
DR PROSITE; PS00134; TRYPSIN_HIS; 3.
DR PROSITE; PS00135; TRYPSIN_SER; 2.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Repeat; Serine protease; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1065
FT /note="Transmembrane protease serine 9"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027871"
FT CHAIN 205..505
FT /note="Serase-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027872"
FT CHAIN 506..833
FT /note="Serase-2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027873"
FT CHAIN 834..1065
FT /note="Serase-3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027874"
FT TOPO_DOM 3..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..1065
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 155..192
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 205..438
FT /note="Peptidase S1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DOMAIN 506..738
FT /note="Peptidase S1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DOMAIN 834..1064
FT /note="Peptidase S1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 445..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 245
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 294
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 389
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 546
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 594
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 689
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 204..205
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 505..506
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 833..834
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 792
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 156..168
FT /evidence="ECO:0000250"
FT DISULFID 163..182
FT /evidence="ECO:0000250"
FT DISULFID 176..191
FT /evidence="ECO:0000250"
FT DISULFID 230..246
FT /evidence="ECO:0000250"
FT DISULFID 328..395
FT /evidence="ECO:0000250"
FT DISULFID 360..374
FT /evidence="ECO:0000250"
FT DISULFID 385..414
FT /evidence="ECO:0000250"
FT DISULFID 531..547
FT /evidence="ECO:0000250"
FT DISULFID 628..695
FT /evidence="ECO:0000250"
FT DISULFID 660..674
FT /evidence="ECO:0000250"
FT DISULFID 685..714
FT /evidence="ECO:0000250"
FT DISULFID 860..876
FT /evidence="ECO:0000250"
FT DISULFID 955..1021
FT /evidence="ECO:0000250"
FT DISULFID 986..1000
FT /evidence="ECO:0000250"
FT DISULFID 1011..1040
FT /evidence="ECO:0000250"
SQ SEQUENCE 1065 AA; 114486 MW; B0EAD1D515D18D4F CRC64;
MEPTAPDLQL VPEVTKAVSV SAPDPGPCRT AVIAVVGISM AIVTLGVLSA FFSAQGAHVE
HIAELHGIRF TSSLQQENSD FYRLLTHALQ TLLHFLLRAL QPLSLKQEAD ILQKGIQARL
QEQGLSLAAY GTIVSVELTG RCEGPVTERD LKSGHCPGNV FSCQNGQCVS KENPECDDRV
DCSDESDEAQ CDCGWQPAWR SAGRIVGGVE AAPGEFPWQV SLRENHEHFC GATIIGARWL
VSAAHCFNEF QDPAQWAAQA GSVHLSGSEA SAVRTRVLRI AKHPAYDADT ADFDVAVLEL
ARPLPFGRYV QPACLPAATH VFPPGKKCLI SGWGYLKEDF LVKPEVLQKA TVELLDQSLC
SSLYGHSLTD RMVCAGYLDG KVDSCQGDSG GPLVCEEPSG RFFLAGIVSW GIGCAEARRP
GVYTRVTRLR DWILEVTSAA DMPVVPTATP APATPSTPWP TSPESWAPNT FAKPTAAPSP
VPLHPSTTAK PQECGARPAM DKPTRIVGGI SAVSGEVPWQ ASLKEGPRHF CGATVVGDRW
LLSAAHCFNH TKVEQVQAHL GTVSLLGVGG SPVKLGLRRV ALHPRYNPGI LDFDVALLEL
AQPLVFNKYI QPVCLPLAIH KFPVGRKCMI SGWGNMQEGN ATKPDILQKA SVGIIEQKMC
GALYNFSLTD RMLCAGFLEG RVDSCQGDSG GPLACEETPG VFYLAGIVSW GIGCAQAKKP
GVYARITRLK DWILKAMSSD PSSMARPHTS STRLIPSEPP KTTAAGLIIP EATTSRLATP
RATIRVTTRP LNTTLSARST TTRGQTAAPS APGTTIHSHL PDCGLAPPGA LTRIVGGSAA
SLGEWPWQVS LWLRRREHRC GAVLVAERWL LSAAHCFDIY GDPMQWAAFL GTPFLSSTEG
QLERVARIYR HPFYNIYTLD YDVALLELAG PVRRSRLVRP ICLPGPARPP DGARCVITGW
GSLREGGSMA RQLQKAAVRV LSEQTCRRFY PVQISSRMLC AGFPQGGVDS CSGDAGGPLA
CREPSGQWVL TGVTSWGYGC GRPHFPGVYT RVAAVLGWIG QNIQE
