TM11G_RAT
ID TM11G_RAT Reviewed; 417 AA.
AC Q5QSK2; Q5NJM5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Transmembrane protease serine 11G;
DE EC=3.4.21.-;
DE AltName: Full=Serine protease DESC4;
DE Contains:
DE RecName: Full=Transmembrane protease serine 11G non-catalytic chain;
DE Contains:
DE RecName: Full=Transmembrane protease serine 11G catalytic chain;
DE Flags: Precursor;
GN Name=Tmprss11g; Synonyms=Desc4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAE84986.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Wistar {ECO:0000312|EMBL:CAE84986.1}; TISSUE=Circumvallate papilla;
RX PubMed=15558215; DOI=10.1007/s00018-004-4263-0;
RA Behrens M., Bufe B., Schmale H., Meyerhof W.;
RT "Molecular cloning and characterisation of DESC4, a new transmembrane
RT serine protease.";
RL Cell. Mol. Life Sci. 61:2866-2877(2004).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15558215}; Single-
CC pass type II membrane protein {ECO:0000269|PubMed:15558215}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15558215};
CC IsoId=Q5QSK2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15558215};
CC IsoId=Q5QSK2-2; Sequence=VSP_014182;
CC -!- TISSUE SPECIFICITY: Highest expression in lung and tongue. Also
CC expressed in brain, colon, heart and liver. Isoform 1 is the
CC predominant form in tongue whereas both isoforms are expressed in
CC similar amounts in lung. At the cellular level, expression is confined
CC to epithelial cells within the cleft of the circumvallate papillae
CC extending into the ducts of the minor salivary glands, the respiratory
CC epithelium of the nasal cavity and tear gland ducts.
CC {ECO:0000269|PubMed:15558215}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AJ617481; CAE84572.1; -; mRNA.
DR EMBL; AJ617528; CAE84986.1; -; mRNA.
DR RefSeq; NP_001008554.1; NM_001008554.1. [Q5QSK2-1]
DR AlphaFoldDB; Q5QSK2; -.
DR SMR; Q5QSK2; -.
DR STRING; 10116.ENSRNOP00000047610; -.
DR MEROPS; S01.436; -.
DR PaxDb; Q5QSK2; -.
DR PRIDE; Q5QSK2; -.
DR GeneID; 289546; -.
DR KEGG; rno:289546; -.
DR UCSC; RGD:1306446; rat. [Q5QSK2-1]
DR CTD; 320454; -.
DR RGD; 1306446; Tmprss11g.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q5QSK2; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q5QSK2; -.
DR PRO; PR:Q5QSK2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.30.70.960; -; 1.
DR InterPro; IPR017329; Pept_S1A_HAT/DESC1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF037941; TMPRSS11ABCDE; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF82671; SSF82671; 1.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zymogen.
FT CHAIN 1..185
FT /note="Transmembrane protease serine 11G non-catalytic
FT chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027839"
FT CHAIN 186..417
FT /note="Transmembrane protease serine 11G catalytic chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027840"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..417
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 46..165
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 186..416
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P10144"
FT ACT_SITE 271
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P10144"
FT ACT_SITE 367
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P10144"
FT DISULFID 211..227
FT /evidence="ECO:0000250|UniProtKB:P49863,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 336..352
FT /evidence="ECO:0000250|UniProtKB:P49863,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 363..392
FT /evidence="ECO:0000250|UniProtKB:P49863,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 160..173
FT /note="EMNAAQAEHILNSN -> D (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15558215"
FT /id="VSP_014182"
SQ SEQUENCE 417 AA; 46593 MW; 4B4380D78726FDA4 CRC64;
MYQPGILGRR KRVCKPWTVA LTTTAALLAL AVLIGLLVYF LVYEEKTHYY QASFWIPSIK
YSSDLSEEQS KLQINLKQKI NNEIDVIFQR SSLKHHYVKS QVVNFRPSND GVKADILIKF
QIPRKNADTL RSEADSILNK KLQSSQSFLK RDISLPYLRE MNAAQAEHIL NSNCGLGMEY
PRIARIADGK PAGSNSWPWQ SSLQVEGIHL CGASLIGSQW LVTSAHCFDN YKNPKLWTVS
FGRTLGNPLT TRKVESIIIH ENYAAHKHDD DIAVVKLSSP VLFSENLRTV CLPEATFQVL
PKSKVFVTGW GALKANGPFP NSLQEVEIEI ISNDVCNQVN VYGGAISSGM ICAGFLTGKL
DACEGDSGGP LVISDNRNKW YLLGIVSWGI DCGKENKPGI YTRVTHYRNW IKSKTNI
