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Q9CR35 (CTRB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Chymotrypsinogen B
EC=3.4.21.1

Cleaved into the following 3 chains:

  1. Chymotrypsin B chain A
  2. Chymotrypsin B chain B
  3. Chymotrypsin B chain C
Gene names
Name:Ctrb1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.

Subcellular location

Secreted › extracellular space By similarity.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processDigestion
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdigestion

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from direct assay PubMed 1820020. Source: MGI

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptidase activity

Inferred from direct assay PubMed 1820020. Source: MGI

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 263245Chymotrypsinogen B
PRO_0000285874
Chain19 – 3113Chymotrypsin B chain A By similarity
PRO_0000285875
Chain34 – 164131Chymotrypsin B chain B By similarity
PRO_0000285876
Chain167 – 26397Chymotrypsin B chain C By similarity
PRO_0000285877

Regions

Domain34 – 261228Peptidase S1

Sites

Active site751Charge relay system By similarity
Active site1201Charge relay system By similarity
Active site2131Charge relay system By similarity

Amino acid modifications

Disulfide bond19 ↔ 140 By similarity
Disulfide bond60 ↔ 76 By similarity
Disulfide bond154 ↔ 219 By similarity
Disulfide bond186 ↔ 200 By similarity
Disulfide bond209 ↔ 238 By similarity

Experimental info

Sequence conflict631S → Y in BAB25112. Ref.1
Sequence conflict821D → N in BAB22539. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CR35 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 28C4487AF1A26B27

FASTA26327,822
        10         20         30         40         50         60 
MAFLWLVSCF ALVGATFGCG VPAIQPVLTG LSRIVNGEDA IPGSWPWQVS LQDRTGFHFC 

        70         80         90        100        110        120 
GGSLISENWV VTAAHCGVKT TDVVVAGEFD QGSDEENVQV LKIAQVFKNP KFNSFTVRND 

       130        140        150        160        170        180 
ITLLKLATPA QFSETVSAVC LPTVDDDFPA GTLCATTGWG KTKYNALKTP DKLQQAALPI 

       190        200        210        220        230        240 
VSEAKCKESW GSKITDVMIC AGASGVSSCM GDSGGPLVCQ KDGVWTLAGI VSWGSGFCST 

       250        260 
STPAVYARVT ALMPWVQEIL EAN

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Pancreas, Spleen and Stomach.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK003060 mRNA. Translation: BAB22539.1.
AK003079 mRNA. Translation: BAB22553.1.
AK007566 mRNA. Translation: BAB25112.1.
AK007765 mRNA. Translation: BAB25241.1.
AK007815 mRNA. Translation: BAB25280.1.
AK008644 mRNA. Translation: BAC25226.1.
AK008729 mRNA. Translation: BAB25861.1.
AK008888 mRNA. Translation: BAB25954.1.
AK008927 mRNA. Translation: BAB25971.1.
BC061083 mRNA. Translation: AAH61083.1.
IPIIPI00315696.
RefSeqNP_079859.2. NM_025583.2.
UniGeneMm.34374.

3D structure databases

HSSPHSSP built from PDB template 1GCT based on UniProtKB P00766.
ProteinModelPortalQ9CR35.
SMRQ9CR35. Positions 19-263.
ModBaseSearch...

Protein family/group databases

MEROPSS01.152.

PTM databases

PhosphoSiteQ9CR35.

Proteomic databases

PaxDbQ9CR35.
PRIDEQ9CR35.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034435; ENSMUSP00000034435; ENSMUSG00000031957.
GeneID66473.
KEGGmmu:66473.
UCSCuc009nms.2. mouse.

Organism-specific databases

CTD1504.
MGIMGI:88559. Ctrb1.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00640000091333.
HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidQ9CR35.
KOK01310.
OMAEAKCKES.
OrthoDBEOG4VMFG1.

Gene expression databases

BgeeQ9CR35.
CleanExMM_CTRB1.
GenevestigatorQ9CR35.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTRB1. mouse.
NextBio321790.
SOURCESearch...

Entry information

Entry nameCTRB1_MOUSE
AccessionPrimary (citable) accession number: Q9CR35
Secondary accession number(s): Q9D8X8, Q9DC86
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: June 1, 2001
Last modified: April 3, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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