TMPS5_MOUSE
ID TMPS5_MOUSE Reviewed; 455 AA.
AC Q9ER04; E9Q2A5; Q9ER02; Q9ER03;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Transmembrane protease serine 5;
DE EC=3.4.21.-;
DE AltName: Full=Spinesin;
GN Name=Tmprss5;
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] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain;
RA Mitsui S., Yamaguchi N.;
RT "cDNA cloning of mouse spinesin.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RA Mitsui S., Yamaguchi N.;
RT "Molecular cloning of mouse type 4 spinesin.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: May play a role in hearing. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=4;
CC IsoId=Q9ER04-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9ER04-2; Sequence=VSP_005397, VSP_005398;
CC Name=2;
CC IsoId=Q9ER04-3; Sequence=VSP_005395;
CC Name=3;
CC IsoId=Q9ER04-4; Sequence=VSP_005396;
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AB016229; BAB20276.1; -; mRNA.
DR EMBL; AB016230; BAB20277.1; -; mRNA.
DR EMBL; AB016423; BAB20278.1; -; mRNA.
DR EMBL; AB041037; BAB40328.1; -; mRNA.
DR EMBL; AC159825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC160137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS52789.1; -. [Q9ER04-4]
DR CCDS; CCDS90560.1; -. [Q9ER04-1]
DR RefSeq; NP_109634.2; NM_030709.2. [Q9ER04-4]
DR RefSeq; XP_006510770.1; XM_006510707.3.
DR AlphaFoldDB; Q9ER04; -.
DR SMR; Q9ER04; -.
DR STRING; 10090.ENSMUSP00000064527; -.
DR MEROPS; S01.313; -.
DR GlyGen; Q9ER04; 4 sites.
DR PhosphoSitePlus; Q9ER04; -.
DR PaxDb; Q9ER04; -.
DR PRIDE; Q9ER04; -.
DR ProteomicsDB; 259046; -. [Q9ER04-1]
DR ProteomicsDB; 259047; -. [Q9ER04-2]
DR ProteomicsDB; 259048; -. [Q9ER04-3]
DR ProteomicsDB; 259049; -. [Q9ER04-4]
DR Antibodypedia; 2582; 326 antibodies from 31 providers.
DR DNASU; 80893; -.
DR Ensembl; ENSMUST00000070390; ENSMUSP00000064527; ENSMUSG00000032268. [Q9ER04-4]
DR Ensembl; ENSMUST00000165088; ENSMUSP00000132181; ENSMUSG00000032268. [Q9ER04-1]
DR GeneID; 80893; -.
DR KEGG; mmu:80893; -.
DR UCSC; uc009piw.3; mouse. [Q9ER04-1]
DR CTD; 80975; -.
DR MGI; MGI:1933407; Tmprss5.
DR VEuPathDB; HostDB:ENSMUSG00000032268; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000159163; -.
DR InParanoid; Q9ER04; -.
DR OMA; CSERWNS; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9ER04; -.
DR TreeFam; TF351678; -.
DR BioGRID-ORCS; 80893; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Tmprss5; mouse.
DR PRO; PR:Q9ER04; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9ER04; protein.
DR Bgee; ENSMUSG00000032268; Expressed in lens of camera-type eye and 51 other tissues.
DR ExpressionAtlas; Q9ER04; baseline and differential.
DR Genevisible; Q9ER04; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; ISO: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:0006508; P:proteolysis; ISO:MGI.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 3.10.250.10; -; 1.
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; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR PROSITE; PS00420; SRCR_1; 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 Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Protease; Reference proteome; Serine protease;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..455
FT /note="Transmembrane protease serine 5"
FT /id="PRO_0000088695"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..455
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 112..207
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 218..453
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 258
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 308
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 405
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 217..218
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 135..196
FT /evidence="ECO:0000250"
FT DISULFID 148..206
FT /evidence="ECO:0000250"
FT DISULFID 209..328
FT /evidence="ECO:0000250"
FT DISULFID 243..259
FT /evidence="ECO:0000250"
FT DISULFID 342..411
FT /evidence="ECO:0000250"
FT DISULFID 374..390
FT /evidence="ECO:0000250"
FT DISULFID 401..429
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..182
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_005397"
FT VAR_SEQ 1..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_005395"
FT VAR_SEQ 1..10
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_005396"
FT VAR_SEQ 183..192
FT /note="GGLVEESWKP -> MEAQVGLLWV (in isoform 1)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_005398"
FT CONFLICT 98
FT /note="R -> C (in Ref. 1; BAB20277 and 2; BAB40328)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="S -> A (in Ref. 1; BAB20276/BAB20277 and 2;
FT BAB40328)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="G -> D (in Ref. 1; BAB20276/BAB20277/BAB20278 and 2;
FT BAB40328)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="H -> Y (in Ref. 1; BAB20276/BAB20277 and 2;
FT BAB40328)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="Y -> H (in Ref. 1; BAB20276/BAB20277/BAB20278 and 2;
FT BAB40328)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 455 AA; 49644 MW; B8FE925707CABCFB CRC64;
MSPTLDDQSP MEIRCTEEGA GPGIFRMELG DQRQSISQSQ RWCCLQRGCV ILGVLGLLAG
AGIASWLLVL YLWPAASPSI SGTLQEEEMT LNCPGVSREE ELLPSLPKTV SFRINGEDLL
LQVQVRARPD WLLVCHEGWS PALGMHICKS LGHIRLTQHK AVNLSDIKLN RSQEFAQLSA
RPGGLVEESW KPSANCPSGR IVSLKCSECG ARPLASRIVG GQAVASGRWP WQASVMLGSR
HTCGASVLAP HWVVTAAHCM YSFRLSRLSS WRVHAGLVSH GAVRQHQGTM VEKIIPHPLY
SAQNHDYDVA LLQLRTPINF SDTVGAVCLP AKEQHFPWGS QCWVSGWGHT DPSHTHSSDT
LQDTMVPLLS TYLCNSSCMY SGALTHRMLC AGYLDGRADA CQGDSGGPLV CPSGDTWHLV
GVVSWGRGCA EPNRPGVYAK VAEFLDWIHD TVQVR
