ID TMPSD_MOUSE Reviewed; 543 AA.
AC Q5U405; Q8CFE0; Q91VQ8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Transmembrane protease serine 13;
DE EC=3.4.21.- {ECO:0000250|UniProtKB:Q9BYE2};
DE AltName: Full=Membrane-type mosaic serine protease;
DE Short=Mosaic serine protease;
GN Name=Tmprss13; Synonyms=Msp;
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 MRNA].
RC STRAIN=B5/EGFP, and FVB/N; TISSUE=Mammary tumor, and Trophoblast stem cell;
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).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24832573; DOI=10.1042/bj20140337;
RA Madsen D.H., Szabo R., Molinolo A.A., Bugge T.H.;
RT "TMPRSS13 deficiency impairs stratum corneum formation and epidermal
RT barrier acquisition.";
RL Biochem. J. 461:487-495(2014).
CC -!- FUNCTION: Serine protease (By similarity). Cleaves the proform of
CC PRSS8/prostasin to form the active protein (By similarity). Cleaves the
CC proform of HGF to form the active protein which promotes MAPK signaling
CC (By similarity). Promotes the formation of the stratum corneum and
CC subsequently the epidermal barrier in embryos (PubMed:24832573).
CC {ECO:0000250|UniProtKB:Q9BYE2, ECO:0000269|PubMed:24832573}.
CC -!- ACTIVITY REGULATION: Cleavage of HGF is inhibited by SPINT1/HAI-1 via
CC the BPTI/Kunitz inhibitor 1 domain. {ECO:0000250|UniProtKB:Q9BYE2}.
CC -!- SUBUNIT: Interacts with SPINT1/HAI-1; the interaction promotes the
CC phosphorylation and cell membrane localization of TMPRSS13 (By
CC similarity). Interacts with SPINT2/HAI-2; the interaction promotes the
CC phosphorylation and cell membrane localization of TMPRSS13 (By
CC similarity). {ECO:0000250|UniProtKB:Q9BYE2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BYE2};
CC Single-pass type II membrane protein {ECO:0000255}. Secreted
CC {ECO:0000250|UniProtKB:Q9BYE2}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9BYE2}. Note=The non-phosphorylated, inactive
CC full length protein localizes intracellularly (By similarity). N-
CC glycosylation and phosphorylation is required for trafficking to the
CC cell surface (By similarity). Interaction with SPINT1/HAI-1 and
CC SPINT2/HAI-2 facilitate its translocation to the cell surface (By
CC similarity). Proteolytic cleavage is required for secretion (By
CC similarity). {ECO:0000250|UniProtKB:Q9BYE2}.
CC -!- TISSUE SPECIFICITY: Expressed in the suprabasal squamous epithelium of
CC the epidermis, hair follicles, oral epithelium, cornea, upper digestive
CC tract, transitional epithelium of the bladder, prostate, heart,
CC intestine, kidney and thymus. {ECO:0000269|PubMed:24832573}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 14.5 dpc in the spinous and
CC granular/transitional layer of the epidermis of the face, developing
CC ear and limbs (PubMed:24832573). Expression is more abundant at 15.5
CC dpc and at 16.5 dpc is present in the entire developing epidermis
CC (PubMed:24832573). {ECO:0000269|PubMed:24832573}.
CC -!- PTM: The inactive zymogen is post-translationally modified and then
CC trafficked to the cell surface, whereby it undergoes autocatalytic
CC cleavage resulting in an activated form that is released
CC extracellularly. {ECO:0000250|UniProtKB:Q9BYE2}.
CC -!- PTM: Phosphorylation is required for localization at the cell surface
CC (By similarity). Phosphorylation increases following inhibition of
CC protease activity by SPINT2/HAI-2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BYE2}.
CC -!- DISRUPTION PHENOTYPE: Increases trans-epidermal fluid loss and shows
CC abnormally developed stratum corneum of the epidermis with fewer and
CC smaller intercorneocyte lacunae at birth which results in a thinner
CC epidermis, however the thickness of the living layer of the epidermis
CC shows no change (PubMed:24832573). At birth mice have 30% shorter
CC whiskers, this difference in length normalizes by adulthood
CC (PubMed:24832573). {ECO:0000269|PubMed:24832573}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; BC010843; AAH10843.1; -; mRNA.
DR EMBL; BC042878; AAH42878.1; -; mRNA.
DR EMBL; BC085323; AAH85323.1; -; mRNA.
DR AlphaFoldDB; Q5U405; -.
DR SMR; Q5U405; -.
DR STRING; 10090.ENSMUSP00000034597; -.
DR MEROPS; S01.087; -.
DR GlyCosmos; Q5U405; 4 sites, No reported glycans.
DR GlyGen; Q5U405; 4 sites.
DR iPTMnet; Q5U405; -.
DR PhosphoSitePlus; Q5U405; -.
DR PaxDb; 10090-ENSMUSP00000034597; -.
DR ProteomicsDB; 259269; -.
DR AGR; MGI:2682935; -.
DR MGI; MGI:2682935; Tmprss13.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q5U405; -.
DR PhylomeDB; Q5U405; -.
DR ChiTaRS; Tmprss13; mouse.
DR PRO; PR:Q5U405; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q5U405; Protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0061436; P:establishment of skin barrier; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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; IPR017327; Peptidase_S1A_TMPRSS13.
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 PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF14; TRANSMEMBRANE PROTEASE SERINE 3-LIKE; 1.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF037935; TMPRSS13; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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; Cytoplasm; Disulfide bond; Glycoprotein; Hydrolase;
KW Membrane; Protease; Reference proteome; Repeat; Secreted; Serine protease;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..543
FT /note="Transmembrane protease serine 13"
FT /id="PRO_0000088699"
FT TOPO_DOM 1..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..543
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REPEAT 14..17
FT /note="1-1"
FT REPEAT 18..22
FT /note="2-1"
FT REPEAT 23..27
FT /note="2-2; approximate"
FT REPEAT 28..31
FT /note="1-2; approximate"
FT REPEAT 32..36
FT /note="2-3"
FT REPEAT 37..40
FT /note="1-3"
FT REPEAT 41..45
FT /note="2-4"
FT REPEAT 46..49
FT /note="1-4"
FT REPEAT 50..54
FT /note="2-5"
FT REPEAT 55..59
FT /note="2-6; approximate"
FT REPEAT 60..64
FT /note="2-7"
FT REPEAT 65..69
FT /note="2-8"
FT DOMAIN 180..202
FT /note="LDL-receptor class A"
FT DOMAIN 199..301
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 302..535
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 14..49
FT /note="4 X 4 AA repeats of T-P-P-Q"
FT REGION 18..69
FT /note="8 X 5 AA repeats of A-S-P-A-R"
FT REGION 109..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..65
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 342
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 390
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 487
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9BYE2"
FT SITE 204..205
FT /note="Cleavage; by autolysis; required for cell surface
FT localization and secretion"
FT /evidence="ECO:0000250|UniProtKB:Q9BYE2"
FT SITE 301
FT /note="Required for autocleavage and PRSS8 cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q9BYE2"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 226..290
FT /evidence="ECO:0000250"
FT DISULFID 239..293
FT /evidence="ECO:0000250"
FT DISULFID 327..343
FT /evidence="ECO:0000250"
FT DISULFID 424..493
FT /evidence="ECO:0000250"
FT DISULFID 456..472
FT /evidence="ECO:0000250"
FT DISULFID 483..511
FT /evidence="ECO:0000250"
FT CONFLICT 281
FT /note="S -> P (in Ref. 1; AAH42878)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="D -> G (in Ref. 1; AAH85323)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="I -> T (in Ref. 1; AAH85323)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 59806 MW; 61026D04A0FCE2D5 CRC64;
MDRGSHRNSS PARTPPQASP ARTSPARAPP QASPARTPPQ ASPARTPPQA SPARAPPPQA
SPARASPARA PPSRSSSGRS SSARSASTTS SPTRVYLVRA TPVGAVPIRA SPARSAPATR
ATRESPGLSF PKFSWQETQR QLPLIGCVIL LISLVISLIL LFYFWRGHTG IKYKEPLESC
PIHAVRCDGV VDCKMKSDEL GCVRFDWDKS LLKVYSGSSG EWLPVCSSSW NDTDSKRTCQ
QLGFDSAYRT TEVAHRDITS SFLLSEYNTT IQESLYRSQC SSRRYVSLQC SHCGLRAMTG
RIVGGALTSE SKWPWQVSLH FGTTHICGGT LIDAQWVLTA AHCFFVTREK LLEGWKVYAG
TSNLHQLPEA ASISQIIING NYTDEQDDYD IALIRLSKPL TLSAHIHPAC LPMHGQTFGL
NETCWITGFG KTKETDEKTS PFLREVQVNL IDFKKCNDYL VYDSYLTPRM MCAGDLRGGR
DSCQGDSGGP LVCEQNNRWY LAGVTSWGTG CGQKNKPGVY TKVTEVLPWI YRKMESEVRF
RKS
//
