TM11D_RAT
ID TM11D_RAT Reviewed; 417 AA.
AC Q8VHJ4; Q9QZ74;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Transmembrane protease serine 11D;
DE EC=3.4.21.-;
DE AltName: Full=Adrenal secretory serine protease;
DE Short=AsP;
DE AltName: Full=Airway trypsin-like protease;
DE Short=AT;
DE Contains:
DE RecName: Full=Transmembrane protease serine 11D non-catalytic chain;
DE Contains:
DE RecName: Full=Transmembrane protease serine 11D catalytic chain;
DE Flags: Precursor;
GN Name=Tmprss11d; Synonyms=Rat;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=New England Deaconess Hospital;
RX PubMed=11439186; DOI=10.1016/s0092-8674(01)00403-2;
RA Bicknell A.B., Lomthaisong K., Woods R.J., Hutchinson E.G., Bennett H.P.J.,
RA Gladwell R.T., Lowry P.J.;
RT "Characterization of a serine protease that cleaves pro-gamma-melanotropin
RT at the adrenal to stimulate growth.";
RL Cell 105:903-912(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND ALTERNATIVE
RP SPLICING.
RC STRAIN=Wistar; TISSUE=Trachea;
RX PubMed=14691009; DOI=10.1210/en.2003-0930;
RA Hansen I.A., Fassnacht M., Hahner S., Hammer F., Schammann M., Meyer S.R.,
RA Bicknell A.B., Allolio B.;
RT "The adrenal secretory serine protease AsP is a short secretory isoform of
RT the transmembrane airway trypsin-like protease.";
RL Endocrinology 145:1898-1905(2004).
CC -!- FUNCTION: May play some biological role in the host defense system on
CC the mucous membrane independently of or in cooperation with other
CC substances in airway mucous or bronchial secretions. Plays a role in
CC the proteolytic processing of ACE2. Preferentially cleaves the C-
CC terminal side of arginine residues at the P1 position of certain
CC peptides (By similarity). Isoform 2 may play a key role in regulating
CC adrenal proliferation by specifically cleaving N-POMC. {ECO:0000250,
CC ECO:0000269|PubMed:11439186}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protease serine 11D catalytic
CC chain]: Secreted {ECO:0000250}. Note=Activated by cleavage and
CC secreted. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=RAT1;
CC IsoId=Q8VHJ4-1; Sequence=Displayed;
CC Name=2; Synonyms=RAT2;
CC IsoId=Q8VHJ4-2; Sequence=VSP_014521, VSP_014522;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in the
CC esophagus, tongue and trachea. Isoform 2 is also highly expressed in
CC the adrenal cortex and heart. {ECO:0000269|PubMed:11439186,
CC ECO:0000269|PubMed:14691009}.
CC -!- MISCELLANEOUS: [Isoform 2]: Secreted and retained on the cell surface
CC after secretion. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AF198087; AAF13253.1; -; mRNA.
DR EMBL; AF453776; AAL50817.1; -; mRNA.
DR RefSeq; NP_001028824.1; NM_001033652.1. [Q8VHJ4-1]
DR RefSeq; NP_072152.1; NM_022630.1.
DR AlphaFoldDB; Q8VHJ4; -.
DR SMR; Q8VHJ4; -.
DR STRING; 10116.ENSRNOP00000002748; -.
DR MEROPS; S01.047; -.
DR PaxDb; Q8VHJ4; -.
DR PRIDE; Q8VHJ4; -.
DR GeneID; 64565; -.
DR KEGG; rno:64565; -.
DR UCSC; RGD:620654; rat. [Q8VHJ4-1]
DR CTD; 9407; -.
DR RGD; 620654; Tmprss11d.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q8VHJ4; -.
DR OrthoDB; 1314811at2759; -.
DR PRO; PR:Q8VHJ4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0040008; P:regulation of growth; IMP:RGD.
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; IPR018114; TRYPSIN_HIS.
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; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Hydrolase; Membrane;
KW Protease; Reference proteome; Secreted; Serine protease; Signal-anchor;
KW Transmembrane; Transmembrane helix; Zymogen.
FT CHAIN 1..185
FT /note="Transmembrane protease serine 11D non-catalytic
FT chain"
FT /id="PRO_0000027889"
FT CHAIN 186..417
FT /note="Transmembrane protease serine 11D catalytic chain"
FT /id="PRO_0000027890"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..417
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 46..162
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"
FT ACT_SITE 271
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 367
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 172..291
FT /note="Interchain (between non-catalytic and catalytic
FT chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 211..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 336..352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 363..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 1..138
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11439186"
FT /id="VSP_014521"
FT VAR_SEQ 139..158
FT /note="LQRLSSSGNLEIAPSNGITS -> MSFSFCFVDLLLVLSFLTLA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11439186"
FT /id="VSP_014522"
FT CONFLICT 300
FT /note="M -> I (in Ref. 1; AAF13253)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="V -> A (in Ref. 1; AAF13253)"
FT /evidence="ECO:0000305"
SQ 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
