TMPS9_RAT
ID TMPS9_RAT Reviewed; 1061 AA.
AC P69526;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
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 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.
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 1011 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; AABR03056045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001040565.2; NM_001047100.2.
DR AlphaFoldDB; P69526; -.
DR SMR; P69526; -.
DR STRING; 10116.ENSRNOP00000041782; -.
DR MEROPS; S01.969; -.
DR GlyGen; P69526; 5 sites.
DR PaxDb; P69526; -.
DR GeneID; 314636; -.
DR KEGG; rno:314636; -.
DR UCSC; RGD:1309581; rat.
DR CTD; 360200; -.
DR RGD; 1309581; Tmprss9.
DR VEuPathDB; HostDB:ENSRNOG00000032429; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_004497_2_0_1; -.
DR InParanoid; P69526; -.
DR OMA; HCFNHTR; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P69526; -.
DR PRO; PR:P69526; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000032429; Expressed in testis and 10 other tissues.
DR ExpressionAtlas; P69526; baseline and differential.
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; ISO:RGD.
DR GO; GO:0031639; P:plasminogen activation; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
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; Cleavage on pair of basic residues; Disulfide bond;
KW Glycoprotein; Hydrolase; Membrane; Protease; Reference proteome; Repeat;
KW Serine protease; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..1061
FT /note="Transmembrane protease serine 9"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027875"
FT CHAIN 205..505
FT /note="Serase-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027876"
FT CHAIN 506..829
FT /note="Serase-2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027877"
FT CHAIN 804..1061
FT /note="Serase-3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027878"
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..1061
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 830..1060
FT /note="Peptidase S1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 443..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..810
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 740..768
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 829..830
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
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 791
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 856..872
FT /evidence="ECO:0000250"
FT DISULFID 951..1017
FT /evidence="ECO:0000250"
FT DISULFID 982..996
FT /evidence="ECO:0000250"
FT DISULFID 1007..1036
FT /evidence="ECO:0000250"
SQ SEQUENCE 1061 AA; 113890 MW; 3319B65E62FF4CAD CRC64;
MEPAAPDLQP VPEVTKGVPV PTPDSGCCRA AVTTVVAISV ASLTLGVLSA FLSAQGVQVE
HTAQLHGVRF TSLLQQENSD FYRLLTPALQ TLLHFLLRAL QPLSLDQEAD ILQKGIQARL
QGQGLSLAAY GTITSVELTG RCEGPVTERD LKSGHCPGNA FSCQNSQCVS KENPECDDRV
DCSDGSDEAQ CDCGWQPAWR SAGRIVGGAE AAPGEFPWQV SLRENHEHFC GATIIGARWL
VSAAHCFNEF QDPAQWAAQA GSVHLSGSEA SAVRARVLRI AKHPAYNADT ADFDVAVLEL
ARPLPFGRYV QPACLPAATH VFPPRKKCLI SGWGYLKEDF LVKPEVLQKA TVELLDQNLC
SSLYGHSLTD RMVCAGYLDG KVDSCQGDSG GPLVCEEPSG RFFLAGVVSW GIGCAEARRP
GVYTRVTRLR DWILEVTSSA DTPVVPTEAP APITPSTPWP TSPESRVPNT TAKPTVAPTP
APLHPSTAAK PQECGARPAM DKPTRIVGGI SAVSGEVPWQ ASLKEGSRHF CGATVVGDRW
LLSAAHCFNH TKLEQVQAHL GTVSLLGVGG SPVKLGLRSV ALHPRYNPGI LDFDVALLEL
AQPLVFNKYI QPVCLPLAIH KFPVGRKCMI SGWGNMQEGN ATKPDILQKA SVGIIEQKMC
GALYNFSLTD RMLCAGFLEG RVDSCQGDSG GPLACEETPG VFYLAGIVSW GIGCAQAKKP
GVYARITRLK DWILKAMSSD PSSTAHPHTS STRLIPSQPP TTTAAGLIPE ASTGRPATLR
ATIRVTTRPL NTTLSARSTT TRRQTPAPGT TVFSHLPDCG LAPPGALTRI VGGSAASLGE
WPWQVSLWLR RREHRCGAVL VAERWLLSAA HCFDVYGDPM QWAAFLGTPF LSSTEGQLER
VARIYRHPFY NIYTLDYDVA LLELAGPVRR SRLVRPICLP GPTRPPEGAR CVITGWGSLR
EGGSMARQLQ KAAVRVLSEQ TCRRFYPVQI SSRMLCAGFP QGGVDSCSGD AGGPLACREP
SGQWVLTGVT SWGYGCGRPH FPGVYTRVAA VLGWIGQNIR E
