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TM11G_MOUSE
ID   TM11G_MOUSE             Reviewed;         417 AA.
AC   Q8BZ10; Q8BZ04;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
DT   03-AUG-2022, entry version 140.
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   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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
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).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC29676.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK036981; BAC29657.1; -; mRNA.
DR   EMBL; AK037029; BAC29676.1; ALT_INIT; mRNA.
DR   EMBL; AC103930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS51532.1; -.
DR   RefSeq; NP_796136.2; NM_177162.4.
DR   AlphaFoldDB; Q8BZ10; -.
DR   SMR; Q8BZ10; -.
DR   STRING; 10090.ENSMUSP00000122709; -.
DR   MEROPS; S01.436; -.
DR   GlyGen; Q8BZ10; 1 site.
DR   PaxDb; Q8BZ10; -.
DR   PRIDE; Q8BZ10; -.
DR   ProteomicsDB; 259217; -.
DR   DNASU; 320454; -.
DR   Ensembl; ENSMUST00000134179; ENSMUSP00000122709; ENSMUSG00000079451.
DR   GeneID; 320454; -.
DR   KEGG; mmu:320454; -.
DR   UCSC; uc008xxr.2; mouse.
DR   CTD; 320454; -.
DR   MGI; MGI:2444058; Tmprss11g.
DR   VEuPathDB; HostDB:ENSMUSG00000079451; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000163094; -.
DR   InParanoid; Q8BZ10; -.
DR   OMA; LQMDGIH; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; Q8BZ10; -.
DR   TreeFam; TF351684; -.
DR   BioGRID-ORCS; 320454; 2 hits in 74 CRISPR screens.
DR   PRO; PR:Q8BZ10; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q8BZ10; protein.
DR   Bgee; ENSMUSG00000079451; Expressed in esophagus and 23 other tissues.
DR   ExpressionAtlas; Q8BZ10; baseline and differential.
DR   Genevisible; Q8BZ10; MM.
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; ISO:MGI.
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   Disulfide bond; Glycoprotein; 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_0000027837"
FT   CHAIN           186..417
FT                   /note="Transmembrane protease serine 11G catalytic chain"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027838"
FT   TOPO_DOM        1..21
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        22..42
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        43..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   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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   CONFLICT        52
FT                   /note="A -> V (in Ref. 1; BAC29657)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   417 AA;  46614 MW;  CD3D36219EA5A8D5 CRC64;
     MYQPGILVRR KRVWKPWTVA LITVALLLAL AVLIGLLVYF LVYDEKTHYY QASFWIPSIN
     YSSDLSKEQS KFRTGLKQKI SNEIDVIFQR SSLKHHYVKS QVVNFRPSND GVKADVLIKF
     QIPRKNAGTL KRQADNILQE KLQSSQSILK RDASLPYLRE MNAAQAEHIL NSDCGSGMEY
     PPIARIADGK PADKASWPWQ SSLQVEGIHL CGASLIGSQW LVTSAHCFDN YKNPKLWTVS
     FGRTLSSPLT TRKVESIIVH ENYASHKHDD DIAVVKLSSP VLFSENLHRV CLPDATFQVL
     PKSKVFVTGW GALKANGPFP NSLQEVEIEI ISNDVCNQVN VYGGAISSGM ICAGFLTGKL
     DACEGDSGGP LVISDNRNKW YLLGIVSWGI DCGKENKPGI YTRVTHYRDW IKSKTSI
 
 
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