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Chymotrypsin-like elastase family member 3B (EC 3.4.21.70) (Elastase IIIB) (Elastase-3B) (Protease E)

 CEL3B_MOUSE             Reviewed;         269 AA.
Q9CQ52; Q7TNI0; Q9D7T9;
21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
12-SEP-2018, entry version 119.
RecName: Full=Chymotrypsin-like elastase family member 3B;
EC=3.4.21.70;
AltName: Full=Elastase IIIB;
AltName: Full=Elastase-3B;
AltName: Full=Protease E;
Flags: Precursor;
Name=Cela3b; Synonyms=Ela3, Ela3b;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Stomach, and Tongue;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver, Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Efficient protease with alanine specificity but only
little elastolytic activity. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Preferential cleavage: Ala-|-Xaa. Does not
hydrolyze elastin.
-!- SIMILARITY: Belongs to the peptidase S1 family. Elastase
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- SEQUENCE CAUTION:
Sequence=AAH56210.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AK008858; BAB25932.1; -; mRNA.
EMBL; AK009129; BAB26092.1; -; mRNA.
EMBL; AK010149; BAB26734.1; -; mRNA.
EMBL; AL645468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC056210; AAH56210.1; ALT_INIT; mRNA.
EMBL; BC061066; AAH61066.1; -; mRNA.
CCDS; CCDS18817.1; -.
RefSeq; NP_080695.1; NM_026419.2.
UniGene; Mm.297477; -.
ProteinModelPortal; Q9CQ52; -.
SMR; Q9CQ52; -.
STRING; 10090.ENSMUSP00000099581; -.
MEROPS; S01.983; -.
PhosphoSitePlus; Q9CQ52; -.
MaxQB; Q9CQ52; -.
PaxDb; Q9CQ52; -.
PeptideAtlas; Q9CQ52; -.
PRIDE; Q9CQ52; -.
Ensembl; ENSMUST00000102522; ENSMUSP00000099581; ENSMUSG00000023433.
GeneID; 67868; -.
KEGG; mmu:67868; -.
UCSC; uc008vja.1; mouse.
CTD; 23436; -.
MGI; MGI:1915118; Cela3b.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000119027; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; Q9CQ52; -.
KO; K01345; -.
OMA; VDHEHCS; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; Q9CQ52; -.
TreeFam; TF330455; -.
ChiTaRS; Cela3b; mouse.
PRO; PR:Q9CQ52; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000023433; Expressed in 93 organ(s), highest expression level in stomach.
Genevisible; Q9CQ52; MM.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0008203; P:cholesterol metabolic process; IBA:GO_Central.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Hydrolase; Protease;
Reference proteome; Serine protease; Signal; Zymogen.
SIGNAL 1 16 {ECO:0000255}.
PROPEP 17 27 Activation peptide. {ECO:0000255}.
/FTId=PRO_0000416105.
CHAIN 28 269 Chymotrypsin-like elastase family member
3B.
/FTId=PRO_0000416106.
DOMAIN 28 267 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 72 72 Charge relay system. {ECO:0000250}.
ACT_SITE 122 122 Charge relay system. {ECO:0000250}.
ACT_SITE 216 216 Charge relay system. {ECO:0000250}.
DISULFID 57 73 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 156 222 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 187 203 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 212 243 {ECO:0000255|PROSITE-ProRule:PRU00274}.
CONFLICT 18 18 G -> E (in Ref. 1; BAB25932).
{ECO:0000305}.
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


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