CTRB1_RAT
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 03-AUG-2022, entry version 154.
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}.
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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; P07338; -.
DR PRIDE; P07338; -.
DR GeneID; 24291; -.
DR KEGG; rno:24291; -.
DR UCSC; RGD:2444; rat.
DR CTD; 1504; -.
DR RGD; 2444; Ctrb1.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P07338; -.
DR OrthoDB; 1522379at2759; -.
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:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
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; -; 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 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 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
