ID PRS56_MOUSE Reviewed; 604 AA.
AC F2YMG0; Q9CVU9;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Serine protease 56;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=Prss56;
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 [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=21397065; DOI=10.1016/j.ajhg.2011.02.006;
RA Gal A., Rau I., El Matri L., Kreienkamp H.J., Fehr S., Baklouti K.,
RA Chouchane I., Li Y., Rehbein M., Fuchs J., Fledelius H.C., Vilhelmsen K.,
RA Schorderet D.F., Munier F.L., Ostergaard E., Thompson D.A., Rosenberg T.;
RT "Autosomal-recessive posterior microphthalmos is caused by mutations in
RT PRSS56, a gene encoding a trypsin-like serine protease.";
RL Am. J. Hum. Genet. 88:382-390(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J;
RX PubMed=21532570; DOI=10.1038/ng.813;
RA Nair K.S., Hmani-Aifa M., Ali Z., Kearney A.L., Ben Salem S.,
RA Macalinao D.G., Cosma I.M., Bouassida W., Hakim B., Benzina Z., Soto I.,
RA Soderkvist P., Howell G.R., Smith R.S., Ayadi H., John S.W.;
RT "Alteration of the serine protease PRSS56 causes angle-closure glaucoma in
RT mice and posterior microphthalmia in humans and mice.";
RL Nat. Genet. 43:579-584(2011).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 373-604.
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).
CC -!- FUNCTION: Serine protease required during eye development.
CC {ECO:0000269|PubMed:21532570}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21532570}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21532570}.
CC -!- TISSUE SPECIFICITY: Expressed in the eye: present in the retina and in
CC the optic nerve. {ECO:0000269|PubMed:21397065,
CC ECO:0000269|PubMed:21532570}.
CC -!- DEVELOPMENTAL STAGE: First detected in the eye at 17 dpc and maintained
CC into adulthood. {ECO:0000269|PubMed:21397065}.
CC -!- DISRUPTION PHENOTYPE: Mice display the glaucoma-relevant mutant 4
CC (Grm4) phenotype, with angle-closure glaucoma and eyes having short
CC axial length. High intraocular pressure (IOP) in mutant eyes increases
CC with age and the anterior chambers become enlarged in some eyes at
CC around 3 months of age. Eye's angles are not occluded with abnormal
CC tissue (synechia) and have detectable trabecular meshwork and Schlemm's
CC canal (2 important drainage structures). However, compromised aqueous
CC humor drainage (outflow) contributes to the IOP elevation. After IOP
CC elevation, mutants develop glaucomatous neurodegeneration, which is
CC characterized by retinal ganglion cell death and optic nerve atrophy.
CC {ECO:0000269|PubMed:21532570}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24587.1; Type=Frameshift; Evidence={ECO:0000305};
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; JF323950; ADZ55664.1; -; mRNA.
DR EMBL; JF698684; AED98564.1; -; mRNA.
DR EMBL; GL456086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK006434; BAB24587.1; ALT_FRAME; mRNA.
DR CCDS; CCDS59538.1; -.
DR RefSeq; NP_081360.1; NM_027084.2.
DR AlphaFoldDB; F2YMG0; -.
DR SMR; F2YMG0; -.
DR STRING; 10090.ENSMUSP00000138773; -.
DR MEROPS; S01.514; -.
DR MEROPS; S01.951; -.
DR GlyCosmos; F2YMG0; 1 site, No reported glycans.
DR GlyGen; F2YMG0; 1 site.
DR iPTMnet; F2YMG0; -.
DR PhosphoSitePlus; F2YMG0; -.
DR PaxDb; 10090-ENSMUSP00000138773; -.
DR PeptideAtlas; F2YMG0; -.
DR ProteomicsDB; 291753; -.
DR Antibodypedia; 71253; 78 antibodies from 11 providers.
DR Ensembl; ENSMUST00000044533.9; ENSMUSP00000138773.2; ENSMUSG00000036480.10.
DR GeneID; 69453; -.
DR KEGG; mmu:69453; -.
DR UCSC; uc007bwe.2; mouse.
DR AGR; MGI:1916703; -.
DR CTD; 646960; -.
DR MGI; MGI:1916703; Prss56.
DR VEuPathDB; HostDB:ENSMUSG00000036480; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000157183; -.
DR HOGENOM; CLU_034171_0_0_1; -.
DR InParanoid; F2YMG0; -.
DR OMA; VMEIQHR; -.
DR OrthoDB; 4629979at2759; -.
DR PhylomeDB; F2YMG0; -.
DR BioGRID-ORCS; 69453; 1 hit in 73 CRISPR screens.
DR PRO; PR:F2YMG0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; F2YMG0; Protein.
DR Bgee; ENSMUSG00000036480; Expressed in seminiferous tubule of testis and 21 other cell types or tissues.
DR Genevisible; F2YMG0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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 PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF10; SERINE PROTEASE 56; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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 Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW Protease; Reference proteome; Serine protease; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..604
FT /note="Serine protease 56"
FT /id="PRO_0000422245"
FT DOMAIN 109..341
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 70..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 290
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 134..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 229..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 260..275
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 286..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 604 AA; 65134 MW; 93FA872AE93BACE3 CRC64;
MPLAMLLLLL LLLSPDSQTA HGHPLYTRLS PGALQVLSAQ GTQALQAAQR SAQWAIKRVL
MEIQHRLHEC QGPGRPRPQA PLLQDPPEPV QCGERHQGVA NTTRAHGRIV GGSTAPSGAW
PWLVRLQLGG LPLCGGVLVA ASWVLTAAHC FAGASNELLW TVMLAEGPQG EQAEEVQVNR
ILPHPKFDPQ TFHNDLALVQ LWTPVSPEGP ARPICLPQGS REPPAGTPCA IAGWGALFED
GPESEAVREA RVPLLSADTC QKVLGPGLRP STMLCAGYLA GGIDSCQGDS GGPLTCSEPG
PRPREVLFGV TSWGDGCGEP GKPGVYTRVT VFKDWLQEQM SAGPSTREPS CRELLNWNAR
EEEPFTDAPG LCAFYARQCL GSESSCARLA LQQCLQRRRR CELRSLAHTL LGLLRGAQEL
LGPRPGLRRG VSAPARSAPS LQELPGHNPR EQRLYSGSRI AGTWLQKPKP ERRPETKGCP
GLEPLQQKLA AIQRAHAWIL QIPAEHLAMN FHEVLADLGS KTLTGLFRAW VRAGLGDQRV
VFSGLVGLEP STLAHSLPRL LVQALKAFRS ASLTEGEPQA PWIGADQGQR LGKERQGQLQ
PPVP
//
