CTRB1_MOUSE
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 03-AUG-2022, entry version 140.
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}.
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; 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; Q9CR35; -.
DR PeptideAtlas; Q9CR35; -.
DR PRIDE; Q9CR35; -.
DR ProteomicsDB; 279201; -.
DR DNASU; 66473; -.
DR Ensembl; ENSMUST00000034435; ENSMUSP00000034435; ENSMUSG00000031957.
DR GeneID; 66473; -.
DR KEGG; mmu:66473; -.
DR UCSC; uc009nms.2; mouse.
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; FPWLLSC; -.
DR OrthoDB; 1522379at2759; -.
DR PhylomeDB; Q9CR35; -.
DR TreeFam; TF330455; -.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 66473; 2 hits in 73 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 72 other tissues.
DR Genevisible; Q9CR35; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO: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; -; 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 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
