CEL2B_HUMAN
ID CEL2B_HUMAN Reviewed; 269 AA.
AC P08218; Q14D16; Q6ISM5; Q96QV5;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Chymotrypsin-like elastase family member 2B;
DE EC=3.4.21.71;
DE AltName: Full=Elastase-2B;
DE Flags: Precursor;
GN Name=CELA2B; Synonyms=ELA2B;
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], AND VARIANTS ARG-79; ASN-114 AND ARG-177.
RX PubMed=3646943; DOI=10.1089/dna.1987.6.163;
RA Kawashima I., Tani T., Shimoda K., Takiguchi Y.;
RT "Characterization of pancreatic elastase II cDNAs: two elastase II mRNAs
RT are expressed in human pancreas.";
RL DNA 6:163-172(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-79; ASN-114 AND
RP ARG-177.
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).
CC -!- FUNCTION: Acts upon elastin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa.
CC Hydrolyzes elastin.; EC=3.4.21.71;
CC -!- INTERACTION:
CC P08218; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-11478642, EBI-739580;
CC P08218; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-11478642, EBI-9996449;
CC P08218; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-11478642, EBI-12837904;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Pancreas.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; M16653; AAA52381.1; -; mRNA.
DR EMBL; AL512883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471167; EAW51728.1; -; Genomic_DNA.
DR EMBL; BC069455; AAH69455.1; -; mRNA.
DR EMBL; BC113540; AAI13541.1; -; mRNA.
DR EMBL; BC113542; AAI13543.1; -; mRNA.
DR CCDS; CCDS30605.1; -.
DR PIR; C26823; C26823.
DR RefSeq; NP_056933.2; NM_015849.2.
DR AlphaFoldDB; P08218; -.
DR SMR; P08218; -.
DR BioGRID; 119238; 43.
DR IntAct; P08218; 15.
DR MINT; P08218; -.
DR STRING; 9606.ENSP00000365075; -.
DR MEROPS; S01.206; -.
DR BioMuta; CELA2B; -.
DR DMDM; 212288098; -.
DR MassIVE; P08218; -.
DR PaxDb; P08218; -.
DR PeptideAtlas; P08218; -.
DR PRIDE; P08218; -.
DR ProteomicsDB; 52087; -.
DR Antibodypedia; 53459; 8 antibodies from 7 providers.
DR DNASU; 51032; -.
DR Ensembl; ENST00000375910.8; ENSP00000365075.3; ENSG00000215704.10.
DR GeneID; 51032; -.
DR KEGG; hsa:51032; -.
DR MANE-Select; ENST00000375910.8; ENSP00000365075.3; NM_015849.3; NP_056933.3.
DR UCSC; uc001awl.3; human.
DR CTD; 51032; -.
DR DisGeNET; 51032; -.
DR GeneCards; CELA2B; -.
DR HGNC; HGNC:29995; CELA2B.
DR HPA; ENSG00000215704; Tissue enriched (pancreas).
DR MIM; 609444; gene.
DR neXtProt; NX_P08218; -.
DR OpenTargets; ENSG00000215704; -.
DR PharmGKB; PA165750841; -.
DR VEuPathDB; HostDB:ENSG00000215704; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234528; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; P08218; -.
DR OMA; NRWFLTA; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P08218; -.
DR TreeFam; TF330455; -.
DR PathwayCommons; P08218; -.
DR SignaLink; P08218; -.
DR BioGRID-ORCS; 51032; 7 hits in 1064 CRISPR screens.
DR GeneWiki; CELA2B; -.
DR GenomeRNAi; 51032; -.
DR Pharos; P08218; Tdark.
DR PRO; PR:P08218; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P08218; protein.
DR Bgee; ENSG00000215704; Expressed in body of pancreas and 94 other tissues.
DR ExpressionAtlas; P08218; baseline and differential.
DR Genevisible; P08218; HS.
DR GO; GO:0005576; C:extracellular region; TAS:ProtInc.
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; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..16
FT PROPEP 17..28
FT /note="Activation peptide"
FT /id="PRO_0000027695"
FT CHAIN 29..269
FT /note="Chymotrypsin-like elastase family member 2B"
FT /id="PRO_0000027696"
FT DOMAIN 29..267
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 121
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 58..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 155..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 186..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 212..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VARIANT 79
FT /note="G -> R (in dbSNP:rs3820071)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3646943"
FT /id="VAR_044534"
FT VARIANT 114
FT /note="D -> N (in dbSNP:rs3766160)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3646943"
FT /id="VAR_044535"
FT VARIANT 177
FT /note="Q -> R (in dbSNP:rs6429745)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3646943"
FT /id="VAR_044536"
FT VARIANT 235
FT /note="G -> S (in dbSNP:rs3737703)"
FT /id="VAR_044537"
SQ 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
