ID   ELA2B_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   26-MAY-2009, entry version 86.
DE   RecName: Full=Elastase-2B;
DE            EC=3.4.21.71;
DE   Flags: Precursor;
GN   Name=ELA2B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-79; ASN-114 AND ARG-177.
RX   MEDLINE=87217962; PubMed=3646943;
RA   Kawashima I., Tani T., Shimoda K., Takiguchi Y.;
RT   "Characterization of pancreatic elastase II cDNAs: two elastase II
RT   mRNAs 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.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   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.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   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.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RP   AND 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Acts upon elastin.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Leu-|-Xaa, Met-|-Xaa
CC       and Phe-|-Xaa. Hydrolyzes elastin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Pancreas.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
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DR   EMBL; M16653; AAA52381.1; -; mRNA.
DR   EMBL; AL512883; CAC42422.1; -; 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   IPI; IPI00027723; -.
DR   PIR; C26823; C26823.
DR   UniGene; Hs.631871; -.
DR   HSSP; P08419; 1BRU.
DR   SMR; P08218; 29-269.
DR   MEROPS; S01.206; -.
DR   Ensembl; ENSG00000215704; Homo sapiens.
DR   GeneCards; GC01P015675; -.
DR   MIM; 609444; gene.
DR   HOVERGEN; P08218; -.
DR   BRENDA; 3.4.21.71; 247.
DR   PMAP-CutDB; P08218; -.
DR   ArrayExpress; P08218; -.
DR   Bgee; P08218; -.
DR   GermOnline; ENSG00000142615; Homo sapiens.
DR   GO; GO:0005576; C:extracellular region; TAS:ProtInc.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; TAS:ProtInc.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hydrolase; Polymorphism; Protease; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL        1     16
FT   PROPEP       17     28       Activation peptide.
FT                                /FTId=PRO_0000027695.
FT   CHAIN        29    269       Elastase-2B.
FT                                /FTId=PRO_0000027696.
FT   DOMAIN       29    267       Peptidase S1.
FT   ACT_SITE     73     73       Charge relay system (By similarity).
FT   ACT_SITE    121    121       Charge relay system (By similarity).
FT   ACT_SITE    216    216       Charge relay system (By similarity).
FT   DISULFID     58     74       By similarity.
FT   DISULFID    155    222       By similarity.
FT   DISULFID    186    202       By similarity.
FT   DISULFID    212    243       By similarity.
FT   VARIANT      79     79       G -> R (in dbSNP:rs3820071).
FT                                /FTId=VAR_044534.
FT   VARIANT     114    114       D -> N (in dbSNP:rs3766160).
FT                                /FTId=VAR_044535.
FT   VARIANT     177    177       Q -> R (in dbSNP:rs6429745).
FT                                /FTId=VAR_044536.
FT   VARIANT     235    235       G -> S (in dbSNP:rs3737703).
FT                                /FTId=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
//