ID CTRB1_RAT Reviewed; 263 AA. AC P07338; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 27-MAR-2024, entry version 160. 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; Synonyms=Ctrb; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6209274; DOI=10.1016/s0021-9258(18)89887-8; RA Bell G.I., Quinto C., Quiroga M., Valenzuela P., Craik C.S., Rutter W.J.; RT "Isolation and sequence of a rat chymotrypsin B gene."; RL J. Biol. Chem. 259:14265-14270(1984). 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 --------------------------------------------------------------------------- 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; K02298; AAA98732.1; -; Genomic_DNA. DR PIR; A22658; KYRTB. DR RefSeq; NP_036668.1; NM_012536.1. DR PDB; 1KDQ; X-ray; 2.55 A; A=34-164, B=165-263. DR PDB; 2JET; X-ray; 2.20 A; A=19-28, B=37-164, C=165-263. DR PDBsum; 1KDQ; -. DR PDBsum; 2JET; -. DR AlphaFoldDB; P07338; -. DR SMR; P07338; -. DR STRING; 10116.ENSRNOP00000026017; -. DR MEROPS; S01.152; -. DR iPTMnet; P07338; -. DR PhosphoSitePlus; P07338; -. DR PaxDb; 10116-ENSRNOP00000026017; -. DR GeneID; 24291; -. DR KEGG; rno:24291; -. DR UCSC; RGD:2444; rat. DR AGR; RGD:2444; -. DR CTD; 1504; -. DR RGD; 2444; Ctrb1. DR eggNOG; KOG3627; Eukaryota. DR InParanoid; P07338; -. DR OrthoDB; 4629979at2759; -. DR PhylomeDB; P07338; -. DR BRENDA; 3.4.21.1; 5301. DR Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases. DR EvolutionaryTrace; P07338; -. DR PRO; PR:P07338; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0008233; F:peptidase activity; ISO:RGD. DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:RGD. DR GO; GO:0008236; F:serine-type peptidase activity; ISO:RGD. DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD. DR GO; GO:0030163; P:protein catabolic process; IDA:RGD. DR GO; GO:0006508; P:proteolysis; ISO:RGD. DR GO; GO:0034097; P:response to cytokine; IDA:RGD. DR GO; GO:0032094; P:response to food; IEP:RGD. DR GO; GO:0007584; P:response to nutrient; IEP:RGD. DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD. DR GO; GO:0009636; P:response to toxic substance; IEP:RGD. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3. 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 1: Evidence at protein level; KW 3D-structure; Digestion; Disulfide bond; Hydrolase; Phosphoprotein; KW Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen. FT SIGNAL 1..18 FT CHAIN 19..263 FT /note="Chymotrypsinogen B" FT /id="PRO_0000027642" FT CHAIN 19..31 FT /note="Chymotrypsin B chain A" FT /id="PRO_0000027643" FT CHAIN 34..164 FT /note="Chymotrypsin B chain B" FT /id="PRO_0000027644" FT CHAIN 167..263 FT /note="Chymotrypsin B chain C" FT /id="PRO_0000027645" 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 DISULFID 154..219 FT DISULFID 186..200 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 209..238 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT STRAND 48..52 FT /evidence="ECO:0007829|PDB:2JET" FT STRAND 58..72 FT /evidence="ECO:0007829|PDB:2JET" FT STRAND 83..87 FT /evidence="ECO:0007829|PDB:2JET" FT STRAND 90..93 FT /evidence="ECO:0007829|PDB:1KDQ" FT STRAND 99..108 FT /evidence="ECO:0007829|PDB:2JET" FT TURN 114..116 FT /evidence="ECO:0007829|PDB:2JET" FT STRAND 122..128 FT /evidence="ECO:0007829|PDB:2JET" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:2JET" FT STRAND 153..158 FT /evidence="ECO:0007829|PDB:2JET" FT STRAND 174..181 FT /evidence="ECO:0007829|PDB:2JET" FT HELIX 183..189 FT /evidence="ECO:0007829|PDB:2JET" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:2JET" FT STRAND 204..207 FT /evidence="ECO:0007829|PDB:2JET" FT HELIX 208..210 FT /evidence="ECO:0007829|PDB:2JET" FT STRAND 216..234 FT /evidence="ECO:0007829|PDB:2JET" FT STRAND 239..242 FT /evidence="ECO:0007829|PDB:1KDQ" FT STRAND 244..248 FT /evidence="ECO:0007829|PDB:2JET" FT HELIX 249..260 FT /evidence="ECO:0007829|PDB:2JET" SQ SEQUENCE 263 AA; 27849 MW; ACAFDBACF8C4DA6D CRC64; MAFLWLVSCF ALVGATFGCG VPTIQPVLTG LSRIVNGEDA IPGSWPWQVS LQDKTGFHFC GGSLISEDWV VTAAHCGVKT SDVVVAGEFD QGSDEENIQV LKIAQVFKNP KFNMFTVRND ITLLKLATPA QFSETVSAVC LPNVDDDFPP GTVCATTGWG KTKYNALKTP EKLQQAALPI VSEADCKKSW GSKITDVMTC AGASGVSSCM GDSGGPLVCQ KDGVWTLAGI VSWGSGVCST STPAVYSRVT ALMPWVQQIL EAN //