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   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.
DR   Genevisible; P17538; HS.
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
//