CEL3B_MOUSE
ID CEL3B_MOUSE Reviewed; 269 AA.
AC Q9CQ52; Q7TNI0; Q9D7T9;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Chymotrypsin-like elastase family member 3B;
DE EC=3.4.21.70;
DE AltName: Full=Elastase IIIB;
DE AltName: Full=Elastase-3B;
DE AltName: Full=Protease E;
DE Flags: Precursor;
GN Name=Cela3b; Synonyms=Ela3, Ela3b;
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=Stomach, and Tongue;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, and Pancreas;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Pancreas, and Spleen;
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 -!- FUNCTION: Efficient protease with alanine specificity but only little
CC elastolytic activity. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Ala-|-Xaa. Does not hydrolyze elastin.;
CC EC=3.4.21.70;
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH56210.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK008858; BAB25932.1; -; mRNA.
DR EMBL; AK009129; BAB26092.1; -; mRNA.
DR EMBL; AK010149; BAB26734.1; -; mRNA.
DR EMBL; AL645468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056210; AAH56210.1; ALT_INIT; mRNA.
DR EMBL; BC061066; AAH61066.1; -; mRNA.
DR CCDS; CCDS18817.1; -.
DR RefSeq; NP_080695.1; NM_026419.2.
DR AlphaFoldDB; Q9CQ52; -.
DR SMR; Q9CQ52; -.
DR STRING; 10090.ENSMUSP00000099581; -.
DR MEROPS; S01.983; -.
DR PhosphoSitePlus; Q9CQ52; -.
DR MaxQB; Q9CQ52; -.
DR PaxDb; Q9CQ52; -.
DR PeptideAtlas; Q9CQ52; -.
DR PRIDE; Q9CQ52; -.
DR ProteomicsDB; 279997; -.
DR DNASU; 67868; -.
DR Ensembl; ENSMUST00000102522; ENSMUSP00000099581; ENSMUSG00000023433.
DR GeneID; 67868; -.
DR KEGG; mmu:67868; -.
DR UCSC; uc008vja.1; mouse.
DR CTD; 23436; -.
DR MGI; MGI:1915118; Cela3b.
DR VEuPathDB; HostDB:ENSMUSG00000023433; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234528; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q9CQ52; -.
DR OMA; ESFYPTC; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9CQ52; -.
DR TreeFam; TF330455; -.
DR BioGRID-ORCS; 67868; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Cela3b; mouse.
DR PRO; PR:Q9CQ52; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9CQ52; protein.
DR Bgee; ENSMUSG00000023433; Expressed in pyloric antrum and 40 other tissues.
DR Genevisible; Q9CQ52; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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; Hydrolase; Protease; Reference proteome; Serine protease;
KW Signal; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..27
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000416105"
FT CHAIN 28..269
FT /note="Chymotrypsin-like elastase family member 3B"
FT /id="PRO_0000416106"
FT DOMAIN 28..267
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 72
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 122
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 57..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 156..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 187..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 212..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 18
FT /note="G -> E (in Ref. 1; BAB25932)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 28905 MW; C543F76957B2A7CE CRC64;
MLRLLSSLLL VALASGCGQP SHNPSSRVVN GEEAVPHSWP WQVSLQYEKD GSFHHTCGGS
LITPDWVLTA GHCISTSRTY QVVLGEHERG VEEGQEQVIP INAGDLFVHP KWNSMCVSCG
NDIALVKLSR SAQLGDAVQL ACLPPAGEIL PNGAPCYISG WGRLSTNGPL PDKLQQALLP
VVDYEHCSRW NWWGLSVKTT MVCAGGDIQS GCNGDSGGPL NCPADNGTWQ VHGVTSFVSS
LGCNTLRKPT VFTRVSAFID WIEETIANN
