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Transmembrane protease serine 11D (EC 3.4.21.-) (Adrenal secretory serine protease) (AsP) (Airway trypsin-like protease) (AT) [Cleaved into: Transmembrane protease serine 11D non-catalytic chain; Transmembrane protease serine 11D catalytic chain]

 TM11D_RAT               Reviewed;         417 AA.
Q8VHJ4; Q9QZ74;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
22-NOV-2017, entry version 106.
RecName: Full=Transmembrane protease serine 11D;
EC=3.4.21.-;
AltName: Full=Adrenal secretory serine protease;
Short=AsP;
AltName: Full=Airway trypsin-like protease;
Short=AT;
Contains:
RecName: Full=Transmembrane protease serine 11D non-catalytic chain;
Contains:
RecName: Full=Transmembrane protease serine 11D catalytic chain;
Flags: Precursor;
Name=Tmprss11d; Synonyms=Rat;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE
SPECIFICITY.
STRAIN=New England Deaconess Hospital;
PubMed=11439186; DOI=10.1016/S0092-8674(01)00403-2;
Bicknell A.B., Lomthaisong K., Woods R.J., Hutchinson E.G.,
Bennett H.P.J., Gladwell R.T., Lowry P.J.;
"Characterization of a serine protease that cleaves pro-gamma-
melanotropin at the adrenal to stimulate growth.";
Cell 105:903-912(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
ALTERNATIVE SPLICING.
STRAIN=Wistar; TISSUE=Trachea;
PubMed=14691009; DOI=10.1210/en.2003-0930;
Hansen I.A., Fassnacht M., Hahner S., Hammer F., Schammann M.,
Meyer S.R., Bicknell A.B., Allolio B.;
"The adrenal secretory serine protease AsP is a short secretory
isoform of the transmembrane airway trypsin-like protease.";
Endocrinology 145:1898-1905(2004).
-!- FUNCTION: May play some biological role in the host defense system
on the mucous membrane independently of or in cooperation with
other substances in airway mucous or bronchial secretions. Plays a
role in the proteolytic processing of ACE2. Preferentially cleaves
the C-terminal side of arginine residues at the P1 position of
certain peptides (By similarity). Isoform 2 may play a key role in
regulating adrenal proliferation by specifically cleaving N-POMC.
{ECO:0000250, ECO:0000269|PubMed:11439186}.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type II membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Transmembrane protease serine 11D catalytic
chain: Secreted {ECO:0000250}. Note=Activated by cleavage and
secreted. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=RAT1;
IsoId=Q8VHJ4-1; Sequence=Displayed;
Name=2; Synonyms=RAT2;
IsoId=Q8VHJ4-2; Sequence=VSP_014521, VSP_014522;
Note=Secreted and retained on the cell surface after secretion.;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in the
esophagus, tongue and trachea. Isoform 2 is also highly expressed
in the adrenal cortex and heart. {ECO:0000269|PubMed:11439186,
ECO:0000269|PubMed:14691009}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; AF198087; AAF13253.1; -; mRNA.
EMBL; AF453776; AAL50817.1; -; mRNA.
RefSeq; NP_001028824.1; NM_001033652.1. [Q8VHJ4-1]
RefSeq; NP_072152.1; NM_022630.1.
UniGene; Rn.48747; -.
ProteinModelPortal; Q8VHJ4; -.
STRING; 10116.ENSRNOP00000002748; -.
MEROPS; S01.047; -.
PaxDb; Q8VHJ4; -.
PRIDE; Q8VHJ4; -.
GeneID; 64565; -.
KEGG; rno:64565; -.
UCSC; RGD:620654; rat. [Q8VHJ4-1]
CTD; 9407; -.
RGD; 620654; Tmprss11d.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
HOGENOM; HOG000251823; -.
HOVERGEN; HBG013304; -.
InParanoid; Q8VHJ4; -.
KO; K09641; -.
PRO; PR:Q8VHJ4; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0008236; F:serine-type peptidase activity; IDA:RGD.
GO; GO:0006508; P:proteolysis; ISO:RGD.
GO; GO:0040008; P:regulation of growth; IMP:RGD.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 3.30.70.960; -; 1.
InterPro; IPR017329; Pept_S1A_HAT/DESC1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR000082; SEA_dom.
InterPro; IPR036364; SEA_dom_sf.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF01390; SEA; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF037941; TMPRSS11ABCDE; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF82671; SSF82671; 1.
PROSITE; PS50024; SEA; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
2: Evidence at transcript level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Hydrolase; Membrane; Protease; Reference proteome;
Secreted; Serine protease; Signal-anchor; Transmembrane;
Transmembrane helix; Zymogen.
CHAIN 1 185 Transmembrane protease serine 11D non-
catalytic chain.
/FTId=PRO_0000027889.
CHAIN 186 417 Transmembrane protease serine 11D
catalytic chain.
/FTId=PRO_0000027890.
TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}.
TRANSMEM 18 38 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 39 417 Extracellular. {ECO:0000255}.
DOMAIN 46 162 SEA. {ECO:0000255|PROSITE-
ProRule:PRU00188}.
DOMAIN 186 416 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 226 226 Charge relay system. {ECO:0000250}.
ACT_SITE 271 271 Charge relay system. {ECO:0000250}.
ACT_SITE 367 367 Charge relay system. {ECO:0000250}.
DISULFID 172 291 Interchain (between non-catalytic and
catalytic chains). {ECO:0000255|PROSITE-
ProRule:PRU00274}.
DISULFID 211 227 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 336 352 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 363 392 {ECO:0000255|PROSITE-ProRule:PRU00274}.
VAR_SEQ 1 138 Missing (in isoform 2).
{ECO:0000303|PubMed:11439186}.
/FTId=VSP_014521.
VAR_SEQ 139 158 LQRLSSSGNLEIAPSNGITS -> MSFSFCFVDLLLVLSFL
TLA (in isoform 2).
{ECO:0000303|PubMed:11439186}.
/FTId=VSP_014522.
CONFLICT 300 300 M -> I (in Ref. 1; AAF13253).
{ECO:0000305}.
CONFLICT 307 307 V -> A (in Ref. 1; AAF13253).
{ECO:0000305}.
SEQUENCE 417 AA; 46288 MW; DB9504158B018E21 CRC64;
MYRPRSMVSP SRFFNPFMVA LIVIITVGLL AMTAGLLIHF LAFDKRAYFY HSNFHILNVD
YTEALNSPAT HEYRTLSERI ESMITDAFRE SNLRSEFIRT HVVKLRKEGS GVVADVVMKF
RSSKRNNKKA IKTRIQSVLQ RLSSSGNLEI APSNGITSLT DQDTENVLTQ ECGARPDLIT
LSEERIIGGT QAETGDWPWQ VSLQLNNVHH CGGTLISNLW VLTAAHCFRS YSNPQQWTAT
FGVSTISPRL RVRVRAILAH AEYNSITRDN DIAVVQLDRP VTFTRNIHRV CLPAATQNIM
PDSVAYVTGW GSLTYGGNTV TNLQQGEVRI VSSEVCNEPA GYGGSVLPGM LCAGVRSGAV
DACQGDSGGP LVQEDTRRLW FVVGIVSWGY QCGLPNKPGV YTRVTAYRNW IRQQTGI


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