TMPS4_MOUSE
ID TMPS4_MOUSE Reviewed; 435 AA.
AC Q8VCA5;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Transmembrane protease serine 4 {ECO:0000305};
DE EC=3.4.21.-;
DE AltName: Full=Channel-activating protease 4 {ECO:0000303|PubMed:12149280};
DE Short=mCAP2 {ECO:0000303|PubMed:12149280};
DE Contains:
DE RecName: Full=Transmembrane protease serine 4 catalytic chain {ECO:0000250|UniProtKB:Q9NRS4};
GN Name=Tmprss4 {ECO:0000312|MGI:MGI:2384877};
GN Synonyms=Cap2 {ECO:0000303|PubMed:12149280};
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 [MRNA], AND FUNCTION.
RX PubMed=12149280; DOI=10.1085/jgp.20028598;
RA Vuagniaux G., Vallet V., Jaeger N.F., Hummler E., Rossier B.C.;
RT "Synergistic activation of ENaC by three membrane-bound channel-activating
RT serine proteases (mCAP1, mCAP2, and mCAP3) and serum- and glucocorticoid-
RT regulated kinase (Sgk1) in Xenopus oocytes.";
RL J. Gen. Physiol. 120:191-201(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Plasma membrane-anchored serine protease that directly
CC induces processing of pro-uPA/PLAU into the active form through
CC proteolytic activity (By similarity). Seems to be capable of activating
CC ENaC (PubMed:12149280). {ECO:0000250|UniProtKB:Q9NRS4,
CC ECO:0000269|PubMed:12149280}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NRS4};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9NRS4}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protease serine 4 catalytic
CC chain]: Secreted {ECO:0000250|UniProtKB:Q9NRS4}. Note=Activated by
CC cleavage and secreted. {ECO:0000250|UniProtKB:Q9NRS4}.
CC -!- PTM: Proteolytically processed; probably by an autocatalytic mechanism.
CC {ECO:0000250|UniProtKB:Q9NRS4}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AY043240; AAK85307.1; -; mRNA.
DR EMBL; BC021368; AAH21368.1; -; mRNA.
DR CCDS; CCDS40607.1; -.
DR RefSeq; NP_663378.1; NM_145403.2.
DR AlphaFoldDB; Q8VCA5; -.
DR SMR; Q8VCA5; -.
DR BioGRID; 229534; 7.
DR STRING; 10090.ENSMUSP00000034599; -.
DR MEROPS; S01.034; -.
DR GlyGen; Q8VCA5; 2 sites.
DR iPTMnet; Q8VCA5; -.
DR PhosphoSitePlus; Q8VCA5; -.
DR MaxQB; Q8VCA5; -.
DR PaxDb; Q8VCA5; -.
DR PRIDE; Q8VCA5; -.
DR ProteomicsDB; 259045; -.
DR Antibodypedia; 1732; 295 antibodies from 32 providers.
DR DNASU; 214523; -.
DR Ensembl; ENSMUST00000034599; ENSMUSP00000034599; ENSMUSG00000032091.
DR GeneID; 214523; -.
DR KEGG; mmu:214523; -.
DR UCSC; uc009pfi.1; mouse.
DR CTD; 56649; -.
DR MGI; MGI:2384877; Tmprss4.
DR VEuPathDB; HostDB:ENSMUSG00000032091; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_19_2_1; -.
DR InParanoid; Q8VCA5; -.
DR OMA; GNWASAC; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q8VCA5; -.
DR TreeFam; TF351678; -.
DR BioGRID-ORCS; 214523; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Tmprss4; mouse.
DR PRO; PR:Q8VCA5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8VCA5; protein.
DR Bgee; ENSMUSG00000032091; Expressed in right colon and 90 other tissues.
DR ExpressionAtlas; Q8VCA5; baseline and differential.
DR Genevisible; Q8VCA5; MM.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0045967; P:negative regulation of growth rate; ISO:MGI.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; ISS:UniProtKB.
DR GO; GO:0016485; P:protein processing; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:0009611; P:response to wounding; IMP:MGI.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
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; IPR043504; Peptidase_S1_PA_chymotrypsin.
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; 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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Secreted; Serine protease; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..435
FT /note="Transmembrane protease serine 4"
FT /id="PRO_0000088693"
FT CHAIN ?..435
FT /note="Transmembrane protease serine 4 catalytic chain"
FT /id="PRO_0000451628"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..435
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 59..101
FT /note="LDL-receptor class A"
FT DOMAIN 102..202
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 203..432
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 288
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 385
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 202..203
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..81
FT /evidence="ECO:0000250"
FT DISULFID 75..90
FT /evidence="ECO:0000250"
FT DISULFID 125..181
FT /evidence="ECO:0000250"
FT DISULFID 138..191
FT /evidence="ECO:0000250"
FT DISULFID 194..308
FT /evidence="ECO:0000250"
FT DISULFID 228..244
FT /evidence="ECO:0000250"
FT DISULFID 354..370
FT /evidence="ECO:0000250"
FT DISULFID 381..408
FT /evidence="ECO:0000250"
SQ SEQUENCE 435 AA; 47496 MW; DC52E45A43E01369 CRC64;
MESDSGQPLN NRDIVPFRKP RRPQETFKKV GIPIIAVLLS LIALVIVALL IKVILDKYYF
ICGSPLTFIQ RGQLCDGHLD CASGEDEEHC VKDFPEKPGV AVRLSKDRST LQVLDAATGT
WASVCFDNFT EALAKTACRQ MGYDSQPAFR AVEIRPDQNL PVAQVTGNSQ ELQVQNGSRS
CLSGSLVSLR CLDCGKSLKT PRVVGGVEAP VDSWPWQVSI QYNKQHVCGG SILDPHWILT
AAHCFRKYLD VSSWKVRAGS NILGNSPSLP VAKIFIAEPN PLYPKEKDIA LVKLQMPLTF
SGSVRPICLP FSDEVLVPAT PVWVIGWGFT EENGGKMSDM LLQASVQVID STRCNAEDAY
EGEVTAEMLC AGTPQGGKDT CQGDSGGPLM YHSDKWQVVG IVSWGHGCGG PSTPGVYTKV
TAYLNWIYNV RKSEM
