TMPSD_MOUSE
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 03-AUG-2022, entry version 111.
DE RecName: Full=Transmembrane protease serine 13;
DE EC=3.4.21.-;
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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
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 GlyGen; Q5U405; 4 sites.
DR iPTMnet; Q5U405; -.
DR PhosphoSitePlus; Q5U405; -.
DR PaxDb; Q5U405; -.
DR PRIDE; Q5U405; -.
DR ProteomicsDB; 259269; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
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; 2.40.10.10; -; 1.
DR Gene3D; 3.10.250.10; -; 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 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; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56487; SSF56487; 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 Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Repeat; Serine protease; Signal-anchor; Transmembrane;
KW 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"
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
