TM11C_MOUSE
ID TM11C_MOUSE Reviewed; 431 AA.
AC Q1JRP2;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Transmembrane protease serine 11C {ECO:0000312|MGI:MGI:3521861};
DE EC=3.4.21.- {ECO:0000255|PIRNR:PIRNR037941, ECO:0000269|PubMed:18215125};
DE AltName: Full=Neurobin {ECO:0000303|PubMed:18215125};
DE Contains:
DE RecName: Full=Transmembrane protease serine 11C non-catalytic chain {ECO:0000305};
DE Contains:
DE RecName: Full=Transmembrane protease serine 11C catalytic chain {ECO:0000305};
DE Flags: Precursor;
GN Name=Tmprss11c {ECO:0000312|MGI:MGI:3521861};
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] {ECO:0000312|EMBL:CAK18220.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PROTEOLYTIC
RP CLEAVAGE, AND MUTAGENESIS OF 190-ARG-ARG-191; ARG-196; LYS-199 AND SER-381.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:CAK18220.1};
RC TISSUE=Spinal cord {ECO:0000312|EMBL:CAK18220.1};
RX PubMed=18215125; DOI=10.1042/bj20071432;
RA Stallmach R., Gloor S.M.;
RT "Neurobin/TMPRSS11c, a novel type II transmembrane serine protease that
RT cleaves fibroblast growth factor-2 in vitro.";
RL Biochem. J. 412:81-91(2008).
RN [2] {ECO:0000312|Proteomes:UP000000589}
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).
RN [3] {ECO:0000312|EMBL:AAI47158.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Serine protease which has a preference for Arg or Lys in
CC position P1 and uncharged residues in positions P2 and P3. Shows
CC specificity towards FGF2 in vitro. {ECO:0000269|PubMed:18215125}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:18215125};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18215125};
CC Single-pass type II membrane protein {ECO:0000305}. Cell projection,
CC dendrite {ECO:0000269|PubMed:18215125}. Perikaryon
CC {ECO:0000269|PubMed:18215125}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in Purkinje neurons of the
CC cerebellum (at protein level). Also detected in spinal cord.
CC {ECO:0000269|PubMed:18215125}.
CC -!- PTM: Proteolytically cleaved via an autocatalytic mechanism.
CC {ECO:0000269|PubMed:18215125}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AM260217; CAK18220.1; -; mRNA.
DR EMBL; AC100746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC147157; AAI47158.1; -; mRNA.
DR EMBL; BC147158; AAI47159.1; -; mRNA.
DR CCDS; CCDS19380.1; -.
DR RefSeq; NP_001025468.1; NM_001030297.2.
DR AlphaFoldDB; Q1JRP2; -.
DR SMR; Q1JRP2; -.
DR STRING; 10090.ENSMUSP00000062915; -.
DR MEROPS; S01.294; -.
DR GlyGen; Q1JRP2; 3 sites.
DR iPTMnet; Q1JRP2; -.
DR PhosphoSitePlus; Q1JRP2; -.
DR PaxDb; Q1JRP2; -.
DR PeptideAtlas; Q1JRP2; -.
DR PRIDE; Q1JRP2; -.
DR ProteomicsDB; 259213; -.
DR DNASU; 435845; -.
DR Ensembl; ENSMUST00000059424; ENSMUSP00000062915; ENSMUSG00000061184.
DR GeneID; 435845; -.
DR KEGG; mmu:435845; -.
DR UCSC; uc008xxn.1; mouse.
DR CTD; 435845; -.
DR MGI; MGI:3521861; Tmprss11c.
DR VEuPathDB; HostDB:ENSMUSG00000061184; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000163237; -.
DR InParanoid; Q1JRP2; -.
DR OMA; GCGQRTI; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q1JRP2; -.
DR TreeFam; TF351684; -.
DR BioGRID-ORCS; 435845; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q1JRP2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q1JRP2; protein.
DR Bgee; ENSMUSG00000061184; Expressed in lip and 1 other tissue.
DR ExpressionAtlas; Q1JRP2; differential.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0097264; P:self proteolysis; IDA:UniProtKB.
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; SM00200; SEA; 1.
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 1: Evidence at protein level;
KW Autocatalytic cleavage; Cell membrane; Cell projection; Disulfide bond;
KW Glycoprotein; Hydrolase; Membrane; Protease; Reference proteome;
KW Serine protease; Signal-anchor; Transmembrane; Transmembrane helix;
KW Zymogen.
FT CHAIN 1..199
FT /note="Transmembrane protease serine 11C non-catalytic
FT chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436381"
FT CHAIN 200..431
FT /note="Transmembrane protease serine 11C catalytic chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436382"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 34..54
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..431
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 60..177
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 200..430
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 240
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 285
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 381
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000305|PubMed:18215125"
FT SITE 199..200
FT /note="Cleavage"
FT /evidence="ECO:0000305|PubMed:18215125"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 225..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 350..366
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 377..406
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT MUTAGEN 190..191
FT /note="RR->AA: Strongly reduced autocatalytic cleavage;
FT when associated with A-196 and A-199. Slightly reduced
FT autocatalytic cleavage; when associated with A-196."
FT /evidence="ECO:0000269|PubMed:18215125"
FT MUTAGEN 196
FT /note="R->A: Strongly reduced autocatalytic cleavage; when
FT associated with A-199. Strongly reduced autocatalytic
FT cleavage; when associated with A-199 and 190-A-A-191.
FT Slightly reduced autocatalytic cleavage; when associated
FT with 190-A-A-191."
FT /evidence="ECO:0000269|PubMed:18215125"
FT MUTAGEN 199
FT /note="K->A: Reduced autocatalytic cleavage. Strongly
FT reduced autocatalytic cleavage; when associated with A-196.
FT Strongly reduced autocatalytic cleavage; when associated
FT with A-196 and 190-A-A-191."
FT /evidence="ECO:0000269|PubMed:18215125"
FT MUTAGEN 381
FT /note="S->A: Abolishes autocatalytic cleavage."
FT /evidence="ECO:0000269|PubMed:18215125"
SQ SEQUENCE 431 AA; 48073 MW; 86A84D5B54E046D0 CRC64;
MARGQPRRSE EQWTALQNRT ECKTKIKLTR CGKITLGILT AVLAAVLIGL IAYFAACGKD
SFYYHVSFKV NNIDYDSKFA KPYSQEYMDL NKRIVSLMNE TFHESKLRKQ YVKAHTVQVS
KAKGKVVIHA VLKFKACYRN NVEKYWESVE TTLYQKLKGQ TGLLIDSSSF KFSDIAMPIA
EDLLNTCCGR RTIIHRGHKV AGGQDAEEGE WPWQASLQQN SVHRCGATLI SNYWLITAAH
CFIRAANPKD WKVSFGFLLS KPQAPRAVKN IIIHENYSYP AHDNDIAVVR LSSPVLYESN
IRRACLPEAT QKFPPNSDVV VTGWGTLKSD GDSPNILQKG KVKIIDNKTC NSGKAYGGMI
TPGMMCAGFL KGRVDACQGD SGGPLVSEDS KGIWFLAGIV SWGDECALPN KPGVYTRVTY
YRDWITSKTG L
