GenomeNet

Database: UniProt
Entry: Q9NRS4
LinkDB: Q9NRS4
Original site: Q9NRS4 
ID   TMPS4_HUMAN             Reviewed;         437 AA.
AC   Q9NRS4; A8MU84; B0YJB0; B7Z8C5; E7ERX8; Q5XKQ6; Q6UX37; Q9NZA5;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   08-MAY-2019, entry version 176.
DE   RecName: Full=Transmembrane protease serine 4;
DE            EC=3.4.21.-;
DE   AltName: Full=Channel-activating protease 2;
DE            Short=CAPH2;
DE   AltName: Full=Membrane-type serine protease 2;
DE            Short=MT-SP2;
GN   Name=TMPRSS4; Synonyms=TMPRSS3; ORFNames=UNQ776/PRO1570;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-208.
RC   TISSUE=Pancreatic carcinoma;
RX   PubMed=10825129;
RA   Wallrapp C., Haehnel S., Mueller-Pillasch F., Burghardt B.,
RA   Iwamura T., Ruthenbuerger M., Lerch M.M., Adler G., Gress T.M.;
RT   "A novel transmembrane serine protease (TMPRSS3) overexpressed in
RT   pancreatic cancer.";
RL   Cancer Res. 60:2602-2606(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-208.
RA   Smeekens S.S., Lorimer D.D., Wang E., Hou J., Linnevers C.;
RT   "MT-SP2, a novel type II membrane serine protease expressed in
RT   trachea, colon, and small intestine: identification, cloning, and
RT   chromosomal localization.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP   GLY-208.
RC   TISSUE=Colon;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
RP   GLY-208.
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP   GLY-208.
RC   TISSUE=Ovary, and Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Probable protease. Seems to be capable of activating
CC       ENaC (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8N6L0:CCDC155; NbExp=3; IntAct=EBI-10313040, EBI-749265;
CC       Q9BXN2:CLEC7A; NbExp=3; IntAct=EBI-10312990, EBI-3939278;
CC       Q8N205:SYNE4; NbExp=3; IntAct=EBI-10312990, EBI-7131783;
CC       Q9BSE2:TMEM79; NbExp=3; IntAct=EBI-10312990, EBI-8649725;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9NRS4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NRS4-2; Sequence=VSP_013117;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q9NRS4-3; Sequence=VSP_013116;
CC         Note=No experimental confirmation available.;
CC       Name=4;
CC         IsoId=Q9NRS4-4; Sequence=VSP_013116, VSP_054229;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: High levels in pancreatic, gastric, colorectal
CC       and ampullary cancer. Very weak expression in normal
CC       gastrointestinal and urogenital tract.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF31436.1; Type=Frameshift; Positions=31; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/TMPRSS4ID42594ch11q23.html";
DR   EMBL; AF179224; AAF74526.1; -; mRNA.
DR   EMBL; AF216312; AAF31436.1; ALT_FRAME; mRNA.
DR   EMBL; AK172766; BAD18749.1; -; mRNA.
DR   EMBL; AK303173; BAH13911.1; -; mRNA.
DR   EMBL; AY358530; AAQ88894.1; -; mRNA.
DR   EMBL; EF445038; ACA06088.1; -; Genomic_DNA.
DR   EMBL; AP000665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP002800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC004855; AAH04855.1; -; mRNA.
DR   EMBL; BC011703; AAH11703.1; -; mRNA.
DR   CCDS; CCDS31684.1; -. [Q9NRS4-1]
DR   CCDS; CCDS44743.1; -. [Q9NRS4-2]
DR   CCDS; CCDS53716.1; -. [Q9NRS4-3]
DR   CCDS; CCDS53717.1; -. [Q9NRS4-4]
DR   RefSeq; NP_001077416.1; NM_001083947.1.
DR   RefSeq; NP_001167023.1; NM_001173552.1.
DR   RefSeq; NP_063947.1; NM_019894.3.
DR   SMR; Q9NRS4; -.
DR   BioGrid; 121163; 5.
DR   IntAct; Q9NRS4; 13.
DR   STRING; 9606.ENSP00000477949; -.
DR   BindingDB; Q9NRS4; -.
DR   ChEMBL; CHEMBL2331048; -.
DR   MEROPS; S01.034; -.
DR   iPTMnet; Q9NRS4; -.
DR   PhosphoSitePlus; Q9NRS4; -.
DR   BioMuta; TMPRSS4; -.
DR   DMDM; 317373304; -.
DR   jPOST; Q9NRS4; -.
DR   MaxQB; Q9NRS4; -.
DR   PaxDb; Q9NRS4; -.
DR   PeptideAtlas; Q9NRS4; -.
DR   PRIDE; Q9NRS4; -.
DR   ProteomicsDB; 82418; -.
DR   ProteomicsDB; 82419; -. [Q9NRS4-2]
DR   ProteomicsDB; 82420; -. [Q9NRS4-3]
DR   DNASU; 56649; -.
DR   Ensembl; ENST00000437212; ENSP00000416037; ENSG00000137648. [Q9NRS4-1]
DR   Ensembl; ENST00000522824; ENSP00000430547; ENSG00000137648. [Q9NRS4-2]
DR   Ensembl; ENST00000523251; ENSP00000429209; ENSG00000137648. [Q9NRS4-4]
DR   Ensembl; ENST00000534111; ENSP00000435184; ENSG00000137648. [Q9NRS4-3]
DR   Ensembl; ENST00000618855; ENSP00000477949; ENSG00000137648. [Q9NRS4-1]
DR   GeneID; 56649; -.
DR   KEGG; hsa:56649; -.
DR   UCSC; uc010rxo.3; human. [Q9NRS4-1]
DR   CTD; 56649; -.
DR   DisGeNET; 56649; -.
DR   GeneCards; TMPRSS4; -.
DR   HGNC; HGNC:11878; TMPRSS4.
DR   HPA; HPA006238; -.
DR   MalaCards; TMPRSS4; -.
DR   MIM; 606565; gene.
DR   neXtProt; NX_Q9NRS4; -.
DR   OpenTargets; ENSG00000137648; -.
DR   Orphanet; 363969; Autosomal recessive cerebral atrophy.
DR   PharmGKB; PA36579; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00950000182707; -.
DR   HOGENOM; HOG000251822; -.
DR   InParanoid; Q9NRS4; -.
DR   KO; K09635; -.
DR   OMA; HCLACGE; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; Q9NRS4; -.
DR   TreeFam; TF351678; -.
DR   ChiTaRS; TMPRSS4; human.
DR   GenomeRNAi; 56649; -.
DR   PRO; PR:Q9NRS4; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; ENSG00000137648; Expressed in 129 organ(s), highest expression level in nasal cavity epithelium.
DR   ExpressionAtlas; Q9NRS4; baseline and differential.
DR   Genevisible; Q9NRS4; HS.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0030141; C:secretory granule; IDA:MGI.
DR   GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; NAS:UniProtKB.
DR   GO; GO:0045967; P:negative regulation of growth rate; IDA:MGI.
DR   GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR   GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR   CDD; cd00112; LDLa; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 3.10.250.10; -; 1.
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; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF15494; SRCR_2; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00202; SR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF56487; SSF56487; 1.
DR   SUPFAM; SSF57424; SSF57424; 1.
DR   PROSITE; PS50287; SRCR_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
KW   Hydrolase; Membrane; Polymorphism; Protease; Reference proteome;
KW   Serine protease; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN         1    437       Transmembrane protease serine 4.
FT                                /FTId=PRO_0000088692.
FT   TOPO_DOM      1     32       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     33     53       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     54    437       Extracellular. {ECO:0000255}.
FT   DOMAIN       61     93       LDL-receptor class A.
FT   DOMAIN       94    204       SRCR. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00196}.
FT   DOMAIN      205    434       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    245    245       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    290    290       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    387    387       Charge relay system. {ECO:0000250}.
FT   SITE        204    205       Cleavage. {ECO:0000255}.
FT   CARBOHYD    130    130       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    178    178       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     64     83       {ECO:0000250}.
FT   DISULFID     77     92       {ECO:0000250}.
FT   DISULFID    127    183       {ECO:0000250}.
FT   DISULFID    140    193       {ECO:0000250}.
FT   DISULFID    196    310       {ECO:0000250}.
FT   DISULFID    230    246       {ECO:0000250}.
FT   DISULFID    356    372       {ECO:0000250}.
FT   DISULFID    383    410       {ECO:0000250}.
FT   VAR_SEQ       1      3       MLQ -> M (in isoform 3 and isoform 4).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_013116.
FT   VAR_SEQ      14     53       LDVKPLRKPRIPMETFRKVGIPIIIALLSLASIIIVVVLI
FT                                -> LV (in isoform 4).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_054229.
FT   VAR_SEQ     147    151       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:12975309}.
FT                                /FTId=VSP_013117.
FT   VARIANT     177    177       R -> Q (in dbSNP:rs1894176).
FT                                /FTId=VAR_024293.
FT   VARIANT     198    198       K -> E (in dbSNP:rs12270001).
FT                                /FTId=VAR_046505.
FT   VARIANT     208    208       V -> G (in dbSNP:rs1941635).
FT                                {ECO:0000269|PubMed:10825129,
FT                                ECO:0000269|PubMed:12975309,
FT                                ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|Ref.2}.
FT                                /FTId=VAR_046506.
FT   CONFLICT      2      2       L -> V (in Ref. 2; AAF31436).
FT                                {ECO:0000305}.
SQ   SEQUENCE   437 AA;  48246 MW;  3CF55633361A2BE7 CRC64;
     MLQDPDSDQP LNSLDVKPLR KPRIPMETFR KVGIPIIIAL LSLASIIIVV VLIKVILDKY
     YFLCGQPLHF IPRKQLCDGE LDCPLGEDEE HCVKSFPEGP AVAVRLSKDR STLQVLDSAT
     GNWFSACFDN FTEALAETAC RQMGYSSKPT FRAVEIGPDQ DLDVVEITEN SQELRMRNSS
     GPCLSGSLVS LHCLACGKSL KTPRVVGVEE ASVDSWPWQV SIQYDKQHVC GGSILDPHWV
     LTAAHCFRKH TDVFNWKVRA GSDKLGSFPS LAVAKIIIIE FNPMYPKDND IALMKLQFPL
     TFSGTVRPIC LPFFDEELTP ATPLWIIGWG FTKQNGGKMS DILLQASVQV IDSTRCNADD
     AYQGEVTEKM MCAGIPEGGV DTCQGDSGGP LMYQSDQWHV VGIVSWGYGC GGPSTPGVYT
     KVSAYLNWIY NVWKAEL
//
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