TMPSC_MOUSE
ID TMPSC_MOUSE Reviewed; 336 AA.
AC Q3V0Q7;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Transmembrane protease serine 12;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=Tmprss12;
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=Testis;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AK132967; BAE21447.1; -; mRNA.
DR CCDS; CCDS49732.1; -.
DR RefSeq; NP_898932.2; NM_183109.3.
DR AlphaFoldDB; Q3V0Q7; -.
DR SMR; Q3V0Q7; -.
DR STRING; 10090.ENSMUSP00000093914; -.
DR MEROPS; S01.958; -.
DR GlyGen; Q3V0Q7; 3 sites.
DR PhosphoSitePlus; Q3V0Q7; -.
DR PaxDb; Q3V0Q7; -.
DR PRIDE; Q3V0Q7; -.
DR ProteomicsDB; 260712; -.
DR Antibodypedia; 2710; 75 antibodies from 15 providers.
DR DNASU; 75002; -.
DR Ensembl; ENSMUST00000096200; ENSMUSP00000093914; ENSMUSG00000045631.
DR GeneID; 75002; -.
DR KEGG; mmu:75002; -.
DR UCSC; uc007xqt.1; mouse.
DR CTD; 283471; -.
DR MGI; MGI:1922252; Tmprss12.
DR VEuPathDB; HostDB:ENSMUSG00000045631; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000161878; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q3V0Q7; -.
DR OMA; HEAEVHY; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q3V0Q7; -.
DR TreeFam; TF335943; -.
DR BioGRID-ORCS; 75002; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q3V0Q7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q3V0Q7; protein.
DR Bgee; ENSMUSG00000045631; Expressed in spermatocyte and 9 other tissues.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IMP:MGI.
DR GO; GO:0016485; P:protein processing; IMP:MGI.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 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 Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..336
FT /note="Transmembrane protease serine 12"
FT /id="PRO_0000290439"
FT TOPO_DOM 19..312
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 66..306
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 256
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 194..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 225..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 252..282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 336 AA; 36916 MW; 9398CB6A6D8EEC1B CRC64;
MASWALSAAL LCLGGAFAYS ELHSLSLREG SALGQATVPG PPEEEQPVTK DCGIAPLRGA
VEGSRIIGGS QADTGAWPWQ VSLQVQDGDI LMHVCGGALV RDRWVLTAAH CTKEARDPLK
WRAVMGTNDL TRSPYHSRNI RITDIIIPPD FIMETFVNDI ALFRLKRAVR YNDYIQPICL
PFGVFQKLDQ NTACFISGWG RTREEGNGTT ILQEAKVHFI SREVCSSDQG YSGMIPNTSF
CAGHENGTFD SCRGDSGGPL MCYLPEHSRY FVMGITSYGH GCGRRHFPGV YSNPSFFQEW
MTHYLSQGNI NRLFNMDIVL GQVLTALGSV ILLGVT
