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   27-MAR-2024, entry version 124.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF198087; AAF13253.1; -; mRNA.
DR   EMBL; AF453776; AAL50817.1; -; mRNA.
DR   RefSeq; NP_001028824.1; NM_001033652.1.
DR   RefSeq; NP_072152.1; NM_022630.1.
DR   AlphaFoldDB; Q8VHJ4; -.
DR   SMR; Q8VHJ4; -.
DR   STRING; 10116.ENSRNOP00000073795; -.
DR   MEROPS; S01.047; -.
DR   PaxDb; 10116-ENSRNOP00000002748; -.
DR   GeneID; 64565; -.
DR   KEGG; rno:64565; -.
DR   UCSC; RGD:620654; rat. [Q8VHJ4-1]
DR   AGR; RGD:620654; -.
DR   CTD; 9407; -.
DR   RGD; 620654; Tmprss11d.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; Q8VHJ4; -.
DR   OrthoDB; 4629979at2759; -.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 3.30.70.960; SEA domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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   PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR   PANTHER; PTHR24252:SF13; TRANSMEMBRANE SERINE PROTEASE 12; 1.
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; SSF82671; SEA domain; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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
//