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Chymotrypsin-like elastase family member 2B (EC 3.4.21.71) (Elastase-2B)

 CEL2B_HUMAN             Reviewed;         269 AA.
P08218; Q14D16; Q6ISM5; Q96QV5;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 2.
25-APR-2018, entry version 158.
RecName: Full=Chymotrypsin-like elastase family member 2B;
EC=3.4.21.71;
AltName: Full=Elastase-2B;
Flags: Precursor;
Name=CELA2B; Synonyms=ELA2B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-79; ASN-114 AND ARG-177.
PubMed=3646943; DOI=10.1089/dna.1987.6.163;
Kawashima I., Tani T., Shimoda K., Takiguchi Y.;
"Characterization of pancreatic elastase II cDNAs: two elastase II
mRNAs are expressed in human pancreas.";
DNA 6:163-172(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-79; ASN-114
AND ARG-177.
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).
-!- FUNCTION: Acts upon elastin.
-!- CATALYTIC ACTIVITY: Preferential cleavage: Leu-|-Xaa, Met-|-Xaa
and Phe-|-Xaa. Hydrolyzes elastin.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Pancreas.
-!- SIMILARITY: Belongs to the peptidase S1 family. Elastase
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; M16653; AAA52381.1; -; mRNA.
EMBL; AL512883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471167; EAW51728.1; -; Genomic_DNA.
EMBL; BC069455; AAH69455.1; -; mRNA.
EMBL; BC113540; AAI13541.1; -; mRNA.
EMBL; BC113542; AAI13543.1; -; mRNA.
CCDS; CCDS30605.1; -.
PIR; C26823; C26823.
RefSeq; NP_056933.2; NM_015849.2.
UniGene; Hs.631871; -.
ProteinModelPortal; P08218; -.
SMR; P08218; -.
BioGrid; 119238; 16.
IntAct; P08218; 3.
MINT; P08218; -.
STRING; 9606.ENSP00000365075; -.
MEROPS; S01.206; -.
BioMuta; CELA2B; -.
DMDM; 212288098; -.
PaxDb; P08218; -.
PeptideAtlas; P08218; -.
PRIDE; P08218; -.
DNASU; 51032; -.
Ensembl; ENST00000375910; ENSP00000365075; ENSG00000215704.
GeneID; 51032; -.
KEGG; hsa:51032; -.
UCSC; uc001awl.3; human.
CTD; 51032; -.
EuPathDB; HostDB:ENSG00000215704.9; -.
GeneCards; CELA2B; -.
HGNC; HGNC:29995; CELA2B.
MIM; 609444; gene.
neXtProt; NX_P08218; -.
OpenTargets; ENSG00000215704; -.
PharmGKB; PA165750841; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000119027; -.
HOGENOM; HOG000251820; -.
InParanoid; P08218; -.
KO; K01346; -.
OMA; HKDWNSD; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; P08218; -.
TreeFam; TF330455; -.
GeneWiki; CELA2B; -.
GenomeRNAi; 51032; -.
PMAP-CutDB; P08218; -.
PRO; PR:P08218; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000215704; -.
ExpressionAtlas; P08218; baseline and differential.
Genevisible; P08218; HS.
GO; GO:0005576; C:extracellular region; TAS:ProtInc.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0004252; F:serine-type endopeptidase activity; 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.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Hydrolase; Polymorphism; Protease;
Reference proteome; Secreted; Serine protease; Signal; Zymogen.
SIGNAL 1 16
PROPEP 17 28 Activation peptide.
/FTId=PRO_0000027695.
CHAIN 29 269 Chymotrypsin-like elastase family member
2B.
/FTId=PRO_0000027696.
DOMAIN 29 267 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 73 73 Charge relay system. {ECO:0000250}.
ACT_SITE 121 121 Charge relay system. {ECO:0000250}.
ACT_SITE 216 216 Charge relay system. {ECO:0000250}.
DISULFID 58 74 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 155 222 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 186 202 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 212 243 {ECO:0000255|PROSITE-ProRule:PRU00274}.
VARIANT 79 79 G -> R (in dbSNP:rs3820071).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:3646943}.
/FTId=VAR_044534.
VARIANT 114 114 D -> N (in dbSNP:rs3766160).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:3646943}.
/FTId=VAR_044535.
VARIANT 177 177 Q -> R (in dbSNP:rs6429745).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:3646943}.
/FTId=VAR_044536.
VARIANT 235 235 G -> S (in dbSNP:rs3737703).
/FTId=VAR_044537.
SEQUENCE 269 AA; 28810 MW; CC81C1D18B918B5F CRC64;
MIRTLLLSTL VAGALSCGVS TYAPDMSRML GGEEARPNSW PWQVSLQYSS NGQWYHTCGG
SLIANSWVLT AAHCISSSGI YRVMLGQHNL YVAESGSLAV SVSKIVVHKD WNSDQVSKGN
DIALLKLANP VSLTDKIQLA CLPPAGTILP NNYPCYVTGW GRLQTNGALP DDLKQGQLLV
VDYATCSSSG WWGSTVKTNM ICAGGDGVIC TCNGDSGGPL NCQASDGRWE VHGIGSLTSV
LGCNYYYKPS IFTRVSNYND WINSVIANN


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