GRAD_MOUSE
ID GRAD_MOUSE Reviewed; 252 AA.
AC P11033; P97387; Q3V2P1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 4.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Granzyme D;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=Gzmd;
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].
RX PubMed=3260382; DOI=10.1073/pnas.85.13.4814;
RA Jenne D.E., Rey C., Haefliger J.-A., Qiao B.-Y., Groscurth P., Tschopp J.;
RT "Identification and sequencing of cDNA clones encoding the granule-
RT associated serine proteases granzymes D, E, and F of cytolytic T
RT lymphocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4814-4818(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=8917549; DOI=10.1073/pnas.93.23.13090;
RA Pham C.T.N., MacIvor D.M., Hug B.A., Heusel J.W., Ley T.J.;
RT "Long-range disruption of gene expression by a selectable marker
RT cassette.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13090-13095(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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).
RN [6]
RP PROTEIN SEQUENCE OF 21-40.
RX PubMed=3555842; DOI=10.1016/0092-8674(87)90544-7;
RA Masson D., Tschopp J.;
RT "A family of serine esterases in lytic granules of cytolytic T
RT lymphocytes.";
RL Cell 49:679-685(1987).
CC -!- FUNCTION: This enzyme is probably necessary for target cell lysis in
CC cell-mediated immune responses.
CC -!- SUBCELLULAR LOCATION: Cytolytic granule.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB19190.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; J03255; AAA37736.1; -; mRNA.
DR EMBL; U66472; AAB19190.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK131671; BAE20756.1; -; mRNA.
DR EMBL; AC091783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC141122; AAI41123.1; -; mRNA.
DR CCDS; CCDS49502.1; -.
DR PIR; A36172; A36172.
DR RefSeq; NP_034502.2; NM_010372.2.
DR AlphaFoldDB; P11033; -.
DR SMR; P11033; -.
DR BioGRID; 200137; 1.
DR STRING; 10090.ENSMUSP00000080742; -.
DR MEROPS; S01.398; -.
DR GlyGen; P11033; 5 sites.
DR EPD; P11033; -.
DR PaxDb; P11033; -.
DR PeptideAtlas; P11033; -.
DR PRIDE; P11033; -.
DR DNASU; 14941; -.
DR Ensembl; ENSMUST00000082093; ENSMUSP00000080742; ENSMUSG00000059256.
DR GeneID; 14941; -.
DR KEGG; mmu:14941; -.
DR UCSC; uc007ubp.1; mouse.
DR CTD; 14941; -.
DR MGI; MGI:109255; Gzmd.
DR VEuPathDB; HostDB:ENSMUSG00000059256; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234551; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P11033; -.
DR OMA; GAHNIDK; -.
DR OrthoDB; 1076876at2759; -.
DR PhylomeDB; P11033; -.
DR TreeFam; TF333630; -.
DR BioGRID-ORCS; 14941; 1 hit in 68 CRISPR screens.
DR PRO; PR:P11033; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P11033; protein.
DR Bgee; ENSMUSG00000059256; Expressed in gastrula and 14 other tissues.
DR Genevisible; P11033; MM.
DR GO; GO:0044194; C:cytolytic granule; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0140507; P:granzyme-mediated programmed cell death signaling pathway; ISO:MGI.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:MGI.
DR GO; GO:0070269; P:pyroptosis; ISO: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 Cytolysis; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lysosome; Protease; Reference proteome; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..18
FT PROPEP 19..20
FT /evidence="ECO:0000269|PubMed:3555842"
FT /id="PRO_0000027405"
FT CHAIN 21..252
FT /note="Granzyme D"
FT /id="PRO_0000027406"
FT DOMAIN 21..250
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 113
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 147..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 179..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 215
FT /note="D -> H (in Ref. 1; AAA37736 and 2; AAB19190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 252 AA; 27955 MW; 0A6DDF6459410142 CRC64;
MPPILILLTL LLPLRAGAEE IIGGHVVKPH SRPYMAFVMS VDIKGNRIYC GGFLIQDDFV
LTAAHCKNSS VQSSMTVTLG AHNITAKEET QQIIPVAKDI PHPDYNATIF YSDIMLLKLE
SKAKRTKAVR PLKLPRSNAR VKPGDVCSVA GWGSRSINDT KASARLREVQ LVIQEDEECK
KRFRYYTETT EICAGDLKKI KTPFKGDSGG PLVCDNQAYG LFAYAKNGTI SSGIFTKVVH
FLPWISWNMK LL
