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

 CEL3B_HUMAN             Reviewed;         270 AA.
P08861; B2RE44; P11423; Q5VU28; Q5VU29; Q5VU30;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
20-JUN-2018, entry version 171.
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=ELA3B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreas;
PubMed=2826474;
Tani T., Ohsumi J., Mita K., Takiguchi Y.;
"Identification of a novel class of elastase isozyme, human pancreatic
elastase III, by cDNA and genomic gene cloning.";
J. Biol. Chem. 263:1231-1239(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TRP-79.
TISSUE=Urinary bladder;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TRP-79.
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).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TRP-79.
TISSUE=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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-270.
TISSUE=Pancreas;
PubMed=3477287; DOI=10.1021/bi00386a030;
Shen W., Fletcher T.S., Largman C.;
"Primary structure of human pancreatic protease E determined by
sequence analysis of the cloned mRNA.";
Biochemistry 26:3447-3452(1987).
[7]
PROTEIN SEQUENCE OF 18-57.
PubMed=2675835; DOI=10.1016/0006-291X(89)91104-2;
Aviles F.X., Pascual R., Salva M., Bonicel J., Puigserver A.;
"Generation of a subunit III-like protein by autolysis of human and
porcine proproteinase E in a binary complex with procarboxypeptidase
A.";
Biochem. Biophys. Res. Commun. 163:1191-1196(1989).
[8]
PROTEIN SEQUENCE OF 31-63.
PubMed=3178837; DOI=10.1016/S0006-291X(88)80842-8;
Guy-Crotte O., Barthe C., Basso D., Fournet B., Figarella C.;
"Characterization of two glycoproteins of human pancreatic juice: P35,
a truncated protease E and P19, precursor of protein X.";
Biochem. Biophys. Res. Commun. 156:318-322(1988).
[9]
PROTEIN SEQUENCE OF 31-50.
TISSUE=Pancreas;
PubMed=2753124; DOI=10.1016/0014-5793(89)80712-4;
Moulard M., Kerfelec B., Mallet B., Chapus C.;
"Identification of a procarboxypeptidase A-truncated protease E binary
complex in human pancreatic juice.";
FEBS Lett. 250:166-170(1989).
[10]
PROTEIN SEQUENCE OF 94-164, AND GLYCOSYLATION AT ASN-114.
TISSUE=Pancreas;
PubMed=2737288; DOI=10.1016/0014-5793(89)80640-4;
Wendorf P., Geyer R., Sziegoleit A., Linder D.;
"Localization and characterization of the glycosylation site of human
pancreatic elastase 1.";
FEBS Lett. 249:275-278(1989).
[11]
TISSUE SPECIFICITY.
PubMed=10620133; DOI=10.1046/j.1523-1747.2000.00825.x;
Talas U., Dunlop J., Khalaf S., Leigh I.M., Kelsell D.P.;
"Human elastase 1: evidence for expression in the skin and the
identification of a frequent frameshift polymorphism.";
J. Invest. Dermatol. 114:165-170(2000).
-!- FUNCTION: Efficient protease with alanine specificity but only
little elastolytic activity.
-!- CATALYTIC ACTIVITY: Preferential cleavage: Ala-|-Xaa. Does not
hydrolyze elastin.
-!- TISSUE SPECIFICITY: Pancreas. Not detectable in keratinocytes.
{ECO:0000269|PubMed:10620133}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Elastase
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- CAUTION: Was originally thought to be elastase 1.
{ECO:0000305|PubMed:2737288}.
-!- SEQUENCE CAUTION:
Sequence=CAH71872.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH71873.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; M16630; AAA36482.1; -; mRNA.
EMBL; AK315798; BAG38141.1; -; mRNA.
EMBL; AL590556; CAH71871.1; -; Genomic_DNA.
EMBL; AL590556; CAH71872.1; ALT_SEQ; Genomic_DNA.
EMBL; AL590556; CAH71873.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471134; EAW94999.1; -; Genomic_DNA.
EMBL; BC005216; AAH05216.1; -; mRNA.
EMBL; M18692; AAA58454.1; -; mRNA.
CCDS; CCDS219.1; -.
PIR; B29934; B29934.
RefSeq; NP_031378.1; NM_007352.3.
UniGene; Hs.728752; -.
ProteinModelPortal; P08861; -.
SMR; P08861; -.
BioGrid; 117004; 9.
STRING; 9606.ENSP00000338369; -.
MEROPS; S01.205; -.
GlyConnect; 125; -.
iPTMnet; P08861; -.
PhosphoSitePlus; P08861; -.
UniCarbKB; P08861; -.
BioMuta; CELA3B; -.
DMDM; 317373457; -.
SWISS-2DPAGE; P08861; -.
PaxDb; P08861; -.
PeptideAtlas; P08861; -.
PRIDE; P08861; -.
ProteomicsDB; 52169; -.
Ensembl; ENST00000337107; ENSP00000338369; ENSG00000219073.
GeneID; 23436; -.
KEGG; hsa:23436; -.
UCSC; uc001bfk.4; human.
CTD; 23436; -.
DisGeNET; 23436; -.
EuPathDB; HostDB:ENSG00000219073.7; -.
GeneCards; CELA3B; -.
HGNC; HGNC:15945; CELA3B.
HPA; HPA028086; -.
HPA; HPA045650; -.
neXtProt; NX_P08861; -.
OpenTargets; ENSG00000219073; -.
PharmGKB; PA27737; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000119027; -.
HOGENOM; HOG000251820; -.
InParanoid; P08861; -.
KO; K01345; -.
OMA; VDHEHCS; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; P08861; -.
TreeFam; TF330455; -.
GeneWiki; CELA3B; -.
GenomeRNAi; 23436; -.
PRO; PR:P08861; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000219073; -.
CleanEx; HS_ELA3B; -.
ExpressionAtlas; P08861; baseline and differential.
Genevisible; P08861; HS.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0008233; F:peptidase activity; TAS:ProtInc.
GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
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; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hydrolase; Polymorphism; Protease; Reference proteome;
Serine protease; Signal; Zymogen.
SIGNAL 1 15 Or 16. {ECO:0000255}.
PROPEP 16 28 Activation peptide. {ECO:0000255}.
/FTId=PRO_0000027699.
CHAIN 29 270 Chymotrypsin-like elastase family member
3B.
/FTId=PRO_0000027700.
DOMAIN 29 268 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 73 73 Charge relay system. {ECO:0000250}.
ACT_SITE 123 123 Charge relay system. {ECO:0000250}.
ACT_SITE 217 217 Charge relay system. {ECO:0000250}.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2737288}.
/FTId=CAR_000212.
DISULFID 58 74 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 117 120 {ECO:0000305}.
DISULFID 157 223 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 188 204 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 213 244 {ECO:0000255|PROSITE-ProRule:PRU00274}.
VARIANT 79 79 R -> W (in dbSNP:rs7528405).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16710414}.
/FTId=VAR_025446.
CONFLICT 4 4 R -> G (in Ref. 5; AAA36482).
{ECO:0000305}.
CONFLICT 64 64 A -> G (in Ref. 5; AAA36482).
{ECO:0000305}.
CONFLICT 129 131 Missing (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 164 164 R -> P (in Ref. 5; AAA36482).
{ECO:0000305}.
SEQUENCE 270 AA; 29263 MW; F738C5F8F5195D8C CRC64;
MMLRLLSSLL LVAVASGYGP PSSRPSSRVV NGEDAVPYSW PWQVSLQYEK SGSFYHTCGG
SLIAPDWVVT AGHCISSSRT YQVVLGEYDR AVKEGPEQVI PINSGDLFVH PLWNRSCVAC
GNDIALIKLS RSAQLGDAVQ LASLPPAGDI LPNETPCYIT GWGRLYTNGP LPDKLQEALL
PVVDYEHCSR WNWWGSSVKK TMVCAGGDIR SGCNGDSGGP LNCPTEDGGW QVHGVTSFVS
AFGCNTRRKP TVFTRVSAFI DWIEETIASH


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