CTRB2_HUMAN
ID CTRB2_HUMAN Reviewed; 263 AA.
AC Q6GPI1; A8K707;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Chymotrypsinogen B2;
DE EC=3.4.21.1;
DE Contains:
DE RecName: Full=Chymotrypsin B2 chain A;
DE Contains:
DE RecName: Full=Chymotrypsin B2 chain B;
DE Contains:
DE RecName: Full=Chymotrypsin B2 chain C;
DE Flags: Precursor;
GN Name=CTRB2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-250.
RC TISSUE=Pancreas;
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).
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 -!- WEB RESOURCE: Name=Wikipedia; Note=Chymotrypsin entry;
CC URL="https://en.wikipedia.org/wiki/Chymotrypsin";
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DR EMBL; AK291822; BAF84511.1; -; mRNA.
DR EMBL; AC009078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC073145; AAH73145.1; -; mRNA.
DR CCDS; CCDS32489.1; -.
DR RefSeq; NP_001020371.3; NM_001025200.3.
DR AlphaFoldDB; Q6GPI1; -.
DR SMR; Q6GPI1; -.
DR BioGRID; 136533; 1.
DR IntAct; Q6GPI1; 1.
DR STRING; 9606.ENSP00000303963; -.
DR BindingDB; Q6GPI1; -.
DR ChEMBL; CHEMBL4523987; -.
DR MEROPS; S01.152; -.
DR iPTMnet; Q6GPI1; -.
DR PhosphoSitePlus; Q6GPI1; -.
DR BioMuta; CTRB2; -.
DR DMDM; 290457638; -.
DR MassIVE; Q6GPI1; -.
DR PaxDb; Q6GPI1; -.
DR PeptideAtlas; Q6GPI1; -.
DR PRIDE; Q6GPI1; -.
DR ProteomicsDB; 66317; -.
DR Antibodypedia; 81624; 1 antibodies from 1 providers.
DR DNASU; 440387; -.
DR Ensembl; ENST00000303037.13; ENSP00000303963.8; ENSG00000168928.13.
DR GeneID; 440387; -.
DR KEGG; hsa:440387; -.
DR MANE-Select; ENST00000303037.13; ENSP00000303963.8; NM_001025200.4; NP_001020371.3.
DR UCSC; uc002fdr.4; human.
DR CTD; 440387; -.
DR DisGeNET; 440387; -.
DR GeneCards; CTRB2; -.
DR HGNC; HGNC:2522; CTRB2.
DR HPA; ENSG00000168928; Tissue enriched (pancreas).
DR MIM; 619620; gene.
DR neXtProt; NX_Q6GPI1; -.
DR OpenTargets; ENSG00000168928; -.
DR PharmGKB; PA27023; -.
DR VEuPathDB; HostDB:ENSG00000168928; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000153216; -.
DR HOGENOM; CLU_006842_7_6_1; -.
DR InParanoid; Q6GPI1; -.
DR OMA; YWGANIT; -.
DR OrthoDB; 1522379at2759; -.
DR PhylomeDB; Q6GPI1; -.
DR TreeFam; TF330455; -.
DR PathwayCommons; Q6GPI1; -.
DR Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-HSA-9758881; Uptake of dietary cobalamins into enterocytes.
DR SignaLink; Q6GPI1; -.
DR BioGRID-ORCS; 440387; 8 hits in 1011 CRISPR screens.
DR GenomeRNAi; 440387; -.
DR Pharos; Q6GPI1; Tdark.
DR PRO; PR:Q6GPI1; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6GPI1; protein.
DR Bgee; ENSG00000168928; Expressed in body of pancreas and 83 other tissues.
DR ExpressionAtlas; Q6GPI1; baseline and differential.
DR Genevisible; Q6GPI1; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
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 2: Evidence at transcript level;
KW Digestion; Disulfide bond; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..263
FT /note="Chymotrypsinogen B2"
FT /id="PRO_0000285870"
FT CHAIN 19..31
FT /note="Chymotrypsin B2 chain A"
FT /id="PRO_0000285871"
FT CHAIN 34..164
FT /note="Chymotrypsin B2 chain B"
FT /id="PRO_0000285872"
FT CHAIN 167..263
FT /note="Chymotrypsin B2 chain C"
FT /id="PRO_0000285873"
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 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 VARIANT 250
FT /note="A -> T (in dbSNP:rs4737)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_062766"
FT CONFLICT 3
FT /note="F -> S (in Ref. 3; AAH73145)"
FT /evidence="ECO:0000305"
FT CONFLICT 10..16
FT /note="WALLGTT -> FSLVGAA (in Ref. 3; AAH73145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 27923 MW; 3B1C0549F3488351 CRC64;
MAFLWLLSCW ALLGTTFGCG VPAIHPVLSG LSRIVNGEDA VPGSWPWQVS LQDKTGFHFC
GGSLISEDWV VTAAHCGVRT SDVVVAGEFD QGSDEENIQV LKIAKVFKNP KFSILTVNND
ITLLKLATPA RFSQTVSAVC LPSADDDFPA GTLCATTGWG KTKYNANKTP DKLQQAALPL
LSNAECKKSW GRRITDVMIC AGASGVSSCM GDSGGPLVCQ KDGAWTLVGI VSWGSRTCST
TTPAVYARVA KLIPWVQKIL AAN
