GenomeNet

Database: UniProt/SWISS-PROT
Entry: TMPS9_RAT
LinkDB: TMPS9_RAT
Original site: 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   20-JUN-2018, entry version 104.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   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.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   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.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian 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
RT   product.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9185-9190(2003).
CC   -!- FUNCTION: Serase-1 and serase-2 are serine proteases that
CC       hydrolyze the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln-
CC       Gly-Arg-AMC. In contrast, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Ala-
CC       Pro-Ala-AMC are not significantly hydrolyzed (By similarity).
CC       {ECO:0000250}.
CC   -!- ENZYME REGULATION: Inhibited by serine protease inhibitors PMSF
CC       and 4-(2-aminoethyl)benzenesulfonyl fluoride, but not by EDTA.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
CC       type II membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The serine protease 1 and 2 domains are catalytically
CC       active, whereas the serine protease 3 domain lacks the essential
CC       Ser residue of the catalytic triad at position 1011 and is
CC       predicted to be inactive. {ECO:0000250}.
CC   -!- PTM: Proteolytically cleaved to generate 3 independent serine
CC       protease chains. The cleaved chains may remain attached to the
CC       membrane thanks to disulfide bonds. It is unclear whether cleavage
CC       always takes place (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; AABR03056045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001040565.2; NM_001047100.2.
DR   UniGene; Rn.123548; -.
DR   ProteinModelPortal; P69526; -.
DR   SMR; P69526; -.
DR   STRING; 10116.ENSRNOP00000041782; -.
DR   MEROPS; S01.969; -.
DR   PaxDb; P69526; -.
DR   PRIDE; P69526; -.
DR   Ensembl; ENSRNOT00000049221; ENSRNOP00000041782; ENSRNOG00000032429.
DR   GeneID; 314636; -.
DR   KEGG; rno:314636; -.
DR   UCSC; RGD:1309581; rat.
DR   CTD; 360200; -.
DR   RGD; 1309581; Tmprss9.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00760000118962; -.
DR   HOGENOM; HOG000154654; -.
DR   HOVERGEN; HBG079270; -.
DR   InParanoid; P69526; -.
DR   KO; K09640; -.
DR   OMA; PDCGLAP; -.
DR   OrthoDB; EOG091G0DF7; -.
DR   PhylomeDB; P69526; -.
DR   PRO; PR:P69526; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000032429; -.
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   CDD; cd00112; LDLa; 1.
DR   CDD; cd00190; Tryp_SPc; 3.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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; Complete proteome;
KW   Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW   Reference proteome; Repeat; Serine protease; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1   1061       Transmembrane protease serine 9.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000027875.
FT   CHAIN       205    505       Serase-1. {ECO:0000255}.
FT                                /FTId=PRO_0000027876.
FT   CHAIN       506    829       Serase-2. {ECO:0000255}.
FT                                /FTId=PRO_0000027877.
FT   CHAIN       804   1061       Serase-3. {ECO:0000255}.
FT                                /FTId=PRO_0000027878.
FT   TOPO_DOM      3     31       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     32     52       Helical. {ECO:0000255}.
FT   TOPO_DOM     53   1061       Extracellular. {ECO:0000255}.
FT   DOMAIN      155    192       LDL-receptor class A.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      205    438       Peptidase S1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   DOMAIN      506    738       Peptidase S1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   DOMAIN      830   1060       Peptidase S1 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    245    245       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    294    294       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    389    389       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    546    546       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    594    594       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    689    689       Charge relay system. {ECO:0000250}.
FT   SITE        204    205       Cleavage. {ECO:0000255}.
FT   SITE        505    506       Cleavage. {ECO:0000255}.
FT   SITE        829    830       Cleavage. {ECO:0000255}.
FT   CARBOHYD    469    469       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    549    549       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    640    640       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    665    665       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    791    791       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    156    168       {ECO:0000250}.
FT   DISULFID    163    182       {ECO:0000250}.
FT   DISULFID    176    191       {ECO:0000250}.
FT   DISULFID    230    246       {ECO:0000250}.
FT   DISULFID    328    395       {ECO:0000250}.
FT   DISULFID    360    374       {ECO:0000250}.
FT   DISULFID    385    414       {ECO:0000250}.
FT   DISULFID    531    547       {ECO:0000250}.
FT   DISULFID    628    695       {ECO:0000250}.
FT   DISULFID    660    674       {ECO:0000250}.
FT   DISULFID    685    714       {ECO:0000250}.
FT   DISULFID    856    872       {ECO:0000250}.
FT   DISULFID    951   1017       {ECO:0000250}.
FT   DISULFID    982    996       {ECO:0000250}.
FT   DISULFID   1007   1036       {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
//
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