CEL3B_HUMAN
ID CEL3B_HUMAN Reviewed; 270 AA.
AC P08861; B2RE44; P11423; Q5VU28; Q5VU29; Q5VU30;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 193.
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=ELA3B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=2826474; DOI=10.1016/s0021-9258(19)57291-x;
RA Tani T., Ohsumi J., Mita K., Takiguchi Y.;
RT "Identification of a novel class of elastase isozyme, human pancreatic
RT elastase III, by cDNA and genomic gene cloning.";
RL J. Biol. Chem. 263:1231-1239(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TRP-79.
RC TISSUE=Urinary bladder;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TRP-79.
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TRP-79.
RC TISSUE=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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-270.
RC TISSUE=Pancreas;
RX PubMed=3477287; DOI=10.1021/bi00386a030;
RA Shen W., Fletcher T.S., Largman C.;
RT "Primary structure of human pancreatic protease E determined by sequence
RT analysis of the cloned mRNA.";
RL Biochemistry 26:3447-3452(1987).
RN [7]
RP PROTEIN SEQUENCE OF 18-57.
RX PubMed=2675835; DOI=10.1016/0006-291x(89)91104-2;
RA Aviles F.X., Pascual R., Salva M., Bonicel J., Puigserver A.;
RT "Generation of a subunit III-like protein by autolysis of human and porcine
RT proproteinase E in a binary complex with procarboxypeptidase A.";
RL Biochem. Biophys. Res. Commun. 163:1191-1196(1989).
RN [8]
RP PROTEIN SEQUENCE OF 31-63.
RX PubMed=3178837; DOI=10.1016/s0006-291x(88)80842-8;
RA Guy-Crotte O., Barthe C., Basso D., Fournet B., Figarella C.;
RT "Characterization of two glycoproteins of human pancreatic juice: P35, a
RT truncated protease E and P19, precursor of protein X.";
RL Biochem. Biophys. Res. Commun. 156:318-322(1988).
RN [9]
RP PROTEIN SEQUENCE OF 31-50.
RC TISSUE=Pancreas;
RX PubMed=2753124; DOI=10.1016/0014-5793(89)80712-4;
RA Moulard M., Kerfelec B., Mallet B., Chapus C.;
RT "Identification of a procarboxypeptidase A-truncated protease E binary
RT complex in human pancreatic juice.";
RL FEBS Lett. 250:166-170(1989).
RN [10]
RP PROTEIN SEQUENCE OF 94-164, AND GLYCOSYLATION AT ASN-114.
RC TISSUE=Pancreas;
RX PubMed=2737288; DOI=10.1016/0014-5793(89)80640-4;
RA Wendorf P., Geyer R., Sziegoleit A., Linder D.;
RT "Localization and characterization of the glycosylation site of human
RT pancreatic elastase 1.";
RL FEBS Lett. 249:275-278(1989).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=10620133; DOI=10.1046/j.1523-1747.2000.00825.x;
RA Talas U., Dunlop J., Khalaf S., Leigh I.M., Kelsell D.P.;
RT "Human elastase 1: evidence for expression in the skin and the
RT identification of a frequent frameshift polymorphism.";
RL J. Invest. Dermatol. 114:165-170(2000).
CC -!- FUNCTION: Efficient protease with alanine specificity but only little
CC elastolytic activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Ala-|-Xaa. Does not hydrolyze elastin.;
CC EC=3.4.21.70;
CC -!- TISSUE SPECIFICITY: Pancreas. Not detectable in keratinocytes.
CC {ECO:0000269|PubMed:10620133}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- CAUTION: Was originally thought to be elastase 1.
CC {ECO:0000305|PubMed:2737288}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M16630; AAA36482.1; -; mRNA.
DR EMBL; AK315798; BAG38141.1; -; mRNA.
DR EMBL; AL590556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471134; EAW94999.1; -; Genomic_DNA.
DR EMBL; BC005216; AAH05216.1; -; mRNA.
DR EMBL; M18692; AAA58454.1; -; mRNA.
DR CCDS; CCDS219.1; -.
DR PIR; B29934; B29934.
DR RefSeq; NP_031378.1; NM_007352.3.
DR AlphaFoldDB; P08861; -.
DR SMR; P08861; -.
DR BioGRID; 117004; 15.
DR STRING; 9606.ENSP00000338369; -.
DR MEROPS; S01.205; -.
DR GlyConnect; 125; 19 N-Linked glycans (1 site).
DR GlyGen; P08861; 1 site, 40 N-linked glycans (1 site).
DR iPTMnet; P08861; -.
DR PhosphoSitePlus; P08861; -.
DR BioMuta; CELA3B; -.
DR DMDM; 317373457; -.
DR SWISS-2DPAGE; P08861; -.
DR jPOST; P08861; -.
DR MassIVE; P08861; -.
DR PaxDb; P08861; -.
DR PeptideAtlas; P08861; -.
DR PRIDE; P08861; -.
DR ProteomicsDB; 52169; -.
DR Antibodypedia; 30049; 722 antibodies from 23 providers.
DR DNASU; 23436; -.
DR Ensembl; ENST00000337107.11; ENSP00000338369.6; ENSG00000219073.8.
DR GeneID; 23436; -.
DR KEGG; hsa:23436; -.
DR MANE-Select; ENST00000337107.11; ENSP00000338369.6; NM_007352.4; NP_031378.1.
DR UCSC; uc001bfk.4; human.
DR CTD; 23436; -.
DR DisGeNET; 23436; -.
DR GeneCards; CELA3B; -.
DR HGNC; HGNC:15945; CELA3B.
DR HPA; ENSG00000219073; Tissue enriched (pancreas).
DR MIM; 618694; gene.
DR neXtProt; NX_P08861; -.
DR OpenTargets; ENSG00000219073; -.
DR PharmGKB; PA27737; -.
DR VEuPathDB; HostDB:ENSG00000219073; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234528; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; P08861; -.
DR OMA; EHCSKWN; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P08861; -.
DR TreeFam; TF330455; -.
DR PathwayCommons; P08861; -.
DR BioGRID-ORCS; 23436; 7 hits in 999 CRISPR screens.
DR GeneWiki; CELA3B; -.
DR GenomeRNAi; 23436; -.
DR Pharos; P08861; Tbio.
DR PRO; PR:P08861; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P08861; protein.
DR Bgee; ENSG00000219073; Expressed in body of pancreas and 87 other tissues.
DR ExpressionAtlas; P08861; baseline and differential.
DR Genevisible; P08861; HS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; TAS:ProtInc.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..15
FT /note="Or 16"
FT /evidence="ECO:0000255"
FT PROPEP 16..28
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027699"
FT CHAIN 29..270
FT /note="Chymotrypsin-like elastase family member 3B"
FT /id="PRO_0000027700"
FT DOMAIN 29..268
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 73
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 123
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 217
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2737288"
FT /id="CAR_000212"
FT DISULFID 58..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 117..120
FT /evidence="ECO:0000305"
FT DISULFID 157..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 188..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 213..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VARIANT 79
FT /note="R -> W (in dbSNP:rs7528405)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16710414"
FT /id="VAR_025446"
FT CONFLICT 4
FT /note="R -> G (in Ref. 5; AAA36482)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="A -> G (in Ref. 5; AAA36482)"
FT /evidence="ECO:0000305"
FT CONFLICT 129..131
FT /note="Missing (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="R -> P (in Ref. 5; AAA36482)"
FT /evidence="ECO:0000305"
SQ 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
