ID   CTRB1_MOUSE             Reviewed;         263 AA.
AC   Q9CR35; Q9D8X8; Q9DC86;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 148.
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;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas, Spleen, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, Lung, Pancreas, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; AK003060; BAB22539.1; -; mRNA.
DR   EMBL; AK003079; BAB22553.1; -; mRNA.
DR   EMBL; AK007566; BAB25112.1; -; mRNA.
DR   EMBL; AK007765; BAB25241.1; -; mRNA.
DR   EMBL; AK007815; BAB25280.1; -; mRNA.
DR   EMBL; AK008644; BAC25226.1; -; mRNA.
DR   EMBL; AK008729; BAB25861.1; -; mRNA.
DR   EMBL; AK008888; BAB25954.1; -; mRNA.
DR   EMBL; AK008927; BAB25971.1; -; mRNA.
DR   EMBL; BC061083; AAH61083.1; -; mRNA.
DR   CCDS; CCDS22679.1; -.
DR   RefSeq; NP_079859.2; NM_025583.2.
DR   AlphaFoldDB; Q9CR35; -.
DR   SMR; Q9CR35; -.
DR   STRING; 10090.ENSMUSP00000034435; -.
DR   MEROPS; S01.152; -.
DR   iPTMnet; Q9CR35; -.
DR   PhosphoSitePlus; Q9CR35; -.
DR   jPOST; Q9CR35; -.
DR   MaxQB; Q9CR35; -.
DR   PaxDb; 10090-ENSMUSP00000034435; -.
DR   PeptideAtlas; Q9CR35; -.
DR   ProteomicsDB; 279201; -.
DR   DNASU; 66473; -.
DR   Ensembl; ENSMUST00000034435.7; ENSMUSP00000034435.6; ENSMUSG00000031957.7.
DR   GeneID; 66473; -.
DR   KEGG; mmu:66473; -.
DR   UCSC; uc009nms.2; mouse.
DR   AGR; MGI:88559; -.
DR   CTD; 1504; -.
DR   MGI; MGI:88559; Ctrb1.
DR   VEuPathDB; HostDB:ENSMUSG00000031957; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000153216; -.
DR   HOGENOM; CLU_006842_7_6_1; -.
DR   InParanoid; Q9CR35; -.
DR   OMA; WITQNIC; -.
DR   OrthoDB; 4629979at2759; -.
DR   PhylomeDB; Q9CR35; -.
DR   TreeFam; TF330455; -.
DR   Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR   BioGRID-ORCS; 66473; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Ctrb1; mouse.
DR   PRO; PR:Q9CR35; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9CR35; Protein.
DR   Bgee; ENSMUSG00000031957; Expressed in pyloric antrum and 74 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:MGI.
DR   GO; GO:0008236; F:serine-type peptidase activity; IDA:MGI.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR   GO; GO:0006508; P:proteolysis; IDA:MGI.
DR   GO; GO:0034097; P:response to cytokine; ISO:MGI.
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.
DR   Genevisible; Q9CR35; MM.
PE   1: Evidence at protein level;
KW   Digestion; Disulfide bond; Hydrolase; Phosphoprotein; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..263
FT                   /note="Chymotrypsinogen B"
FT                   /id="PRO_0000285874"
FT   CHAIN           19..31
FT                   /note="Chymotrypsin B chain A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000285875"
FT   CHAIN           34..164
FT                   /note="Chymotrypsin B chain B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000285876"
FT   CHAIN           167..263
FT                   /note="Chymotrypsin B chain C"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000285877"
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:0007744|PubMed:21183079"
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   CONFLICT        63
FT                   /note="S -> Y (in Ref. 1; BAB25112)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82
FT                   /note="D -> N (in Ref. 1; BAB22539)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   263 AA;  27822 MW;  28C4487AF1A26B27 CRC64;
     MAFLWLVSCF ALVGATFGCG VPAIQPVLTG LSRIVNGEDA IPGSWPWQVS LQDRTGFHFC
     GGSLISENWV VTAAHCGVKT TDVVVAGEFD QGSDEENVQV LKIAQVFKNP KFNSFTVRND
     ITLLKLATPA QFSETVSAVC LPTVDDDFPA GTLCATTGWG KTKYNALKTP DKLQQAALPI
     VSEAKCKESW GSKITDVMIC AGASGVSSCM GDSGGPLVCQ KDGVWTLAGI VSWGSGFCST
     STPAVYARVT ALMPWVQEIL EAN
//