ID CTRB1_HUMAN Reviewed; 263 AA.
AC P17538;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 27-MAR-2024, entry version 196.
DE RecName: Full=Chymotrypsinogen B;
DE EC=3.4.21.1;
DE Contains:
DE RecName: Full=Chymotrypsin B chain A;
DE Contains:
DE RecName: Full=Chymotrypsin B chain B;
DE Contains:
DE RecName: Full=Chymotrypsin B chain C;
DE Flags: Precursor;
GN Name=CTRB1 {ECO:0000312|HGNC:HGNC:2521};
GN Synonyms=CTRB {ECO:0000312|HGNC:HGNC:2521};
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=2917002; DOI=10.1016/s0006-291x(89)80087-7;
RA Tomita N., Izumoto Y., Horii A., Doi S., Yokouchi H., Ogawa M., Mori T.,
RA Matsubara K.;
RT "Molecular cloning and nucleotide sequence of human pancreatic
RT prechymotrypsinogen cDNA.";
RL Biochem. Biophys. Res. Commun. 158:569-575(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-
CC Xaa.; EC=3.4.21.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10078,
CC ECO:0000255|PROSITE-ProRule:PRU10079};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Chymotrypsin entry;
CC URL="https://en.wikipedia.org/wiki/Chymotrypsin";
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DR EMBL; M24400; AAA52128.1; -; mRNA.
DR EMBL; BT007356; AAP36020.1; -; mRNA.
DR EMBL; AC009078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005385; AAH05385.1; -; mRNA.
DR CCDS; CCDS32490.1; -.
DR PIR; A31299; A31299.
DR RefSeq; NP_001316119.1; NM_001329190.1.
DR RefSeq; NP_001897.4; NM_001906.5.
DR AlphaFoldDB; P17538; -.
DR SMR; P17538; -.
DR IntAct; P17538; 2.
DR STRING; 9606.ENSP00000354294; -.
DR BindingDB; P17538; -.
DR ChEMBL; CHEMBL4796; -.
DR DrugBank; DB07899; (2S) N-acetyl-L-alanyl-AlphaL-phenylalanyl-chloroethylketone.
DR DrugBank; DB08119; 1,1,1-TRIFLUORO-3-((N-ACETYL)-L-LEUCYLAMIDO)-4-PHENYL-BUTAN-2-ONE(N-ACETYL-L-LEUCYL-L-PHENYLALANYL TRIFLUOROMETHYL KETONE).
DR DrugBank; DB07380; 1,1,1-TRIFLUORO-3-ACETAMIDO-4-PHENYL BUTAN-2-ONE(N-ACETYL-L-PHENYLALANYL TRIFLUOROMETHYL KETONE).
DR DrugBank; DB01704; 2,4-Dihydroxy-Trans Cinnamic Acid.
DR DrugBank; DB07749; 2-ACETYLAMINO-4-METHYL-PENTANOIC ACID (1-FORMYL-2-PHENYL-ETHYL)-AMIDE.
DR DrugBank; DB07668; alpha-Methyl-2-hydroxy-4-diethylaminocinnamic acid.
DR DrugBank; DB06692; Aprotinin.
DR DrugBank; DB08692; D-1-(4-chlorophenyl)-2-(acetamido)ethane boronic acid.
DR DrugBank; DB08566; D-1-naphthyl-2-acetamido-ethane boronic acid.
DR DrugBank; DB08693; L-1-(4-chlorophenyl)-2-(acetamido)ethane boronic acid.
DR DrugBank; DB08565; L-1-naphthyl-2-acetamido-ethane boronic acid.
DR DrugBank; DB07383; N-(1-BENZYL-3,3,3-TRIFLUORO-2,2-DIHYDROXY-PROPYL)-ACETAMIDE.
DR DrugBank; DB08374; Phenylalanylmethylchloride.
DR DrugBank; DB01963; Phenylethane Boronic Acid.
DR DrugBank; DB03976; Phosphorylisopropane.
DR DrugBank; DB01662; Trans-O-Hydroxy-Alpha-Methyl Cinnamate.
DR DrugCentral; P17538; -.
DR MEROPS; S01.152; -.
DR iPTMnet; P17538; -.
DR PhosphoSitePlus; P17538; -.
DR BioMuta; CTRB1; -.
DR DMDM; 117617; -.
DR MassIVE; P17538; -.
DR PaxDb; 9606-ENSP00000354294; -.
DR PeptideAtlas; P17538; -.
DR Antibodypedia; 30302; 221 antibodies from 20 providers.
DR DNASU; 1504; -.
DR Ensembl; ENST00000361017.9; ENSP00000354294.4; ENSG00000168925.12.
DR GeneID; 1504; -.
DR KEGG; hsa:1504; -.
DR MANE-Select; ENST00000361017.9; ENSP00000354294.4; NM_001906.6; NP_001897.4.
DR UCSC; uc002fds.4; human.
DR AGR; HGNC:2521; -.
DR CTD; 1504; -.
DR DisGeNET; 1504; -.
DR GeneCards; CTRB1; -.
DR HGNC; HGNC:2521; CTRB1.
DR HPA; ENSG00000168925; Tissue enriched (pancreas).
DR MIM; 118890; gene.
DR neXtProt; NX_P17538; -.
DR OpenTargets; ENSG00000168925; -.
DR VEuPathDB; HostDB:ENSG00000168925; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000153216; -.
DR HOGENOM; CLU_006842_7_6_1; -.
DR InParanoid; P17538; -.
DR OMA; MICAGAR; -.
DR OrthoDB; 4629979at2759; -.
DR PhylomeDB; P17538; -.
DR TreeFam; TF330455; -.
DR PathwayCommons; P17538; -.
DR Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-HSA-9758881; Uptake of dietary cobalamins into enterocytes.
DR SignaLink; P17538; -.
DR BioGRID-ORCS; 1504; 13 hits in 771 CRISPR screens.
DR GenomeRNAi; 1504; -.
DR Pharos; P17538; Tchem.
DR PRO; PR:P17538; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P17538; Protein.
DR Bgee; ENSG00000168925; Expressed in body of pancreas and 85 other cell types or tissues.
DR ExpressionAtlas; P17538; baseline and differential.
DR Genevisible; P17538; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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 PANTHER; PTHR24250; CHYMOTRYPSIN-RELATED; 1.
DR PANTHER; PTHR24250:SF60; CHYMOTRYPSINOGEN B; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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 Digestion; Disulfide bond; Hydrolase; Phosphoprotein; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT CHAIN 19..263
FT /note="Chymotrypsinogen B"
FT /id="PRO_0000027638"
FT CHAIN 19..31
FT /note="Chymotrypsin B chain A"
FT /id="PRO_0000027639"
FT CHAIN 34..164
FT /note="Chymotrypsin B chain B"
FT /id="PRO_0000027640"
FT CHAIN 167..263
FT /note="Chymotrypsin B chain C"
FT /id="PRO_0000027641"
FT DOMAIN 34..261
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 75
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 120
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 213
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CR35"
FT DISULFID 19..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 60..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 154..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 186..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 209..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VARIANT 222
FT /note="D -> H (in dbSNP:rs8061550)"
FT /id="VAR_057158"
FT VARIANT 250
FT /note="T -> A (in dbSNP:rs4737)"
FT /id="VAR_014566"
FT CONFLICT 3
FT /note="S -> F (in Ref. 1; AAA52128, 2; AAP36020 and 4;
FT AAH05385)"
FT /evidence="ECO:0000305"
FT CONFLICT 10..16
FT /note="FSLVGAA -> WALLGTT (in Ref. 1; AAA52128, 2; AAP36020
FT and 4; AAH05385)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 27713 MW; EDA816A133D42DE7 CRC64;
MASLWLLSCF SLVGAAFGCG VPAIHPVLSG LSRIVNGEDA VPGSWPWQVS LQDKTGFHFC
GGSLISEDWV VTAAHCGVRT SDVVVAGEFD QGSDEENIQV LKIAKVFKNP KFSILTVNND
ITLLKLATPA RFSQTVSAVC LPSADDDFPA GTLCATTGWG KTKYNANKTP DKLQQAALPL
LSNAECKKSW GRRITDVMIC AGASGVSSCM GDSGGPLVCQ KDGAWTLVGI VSWGSDTCST
SSPGVYARVT KLIPWVQKIL AAN
//
