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   02-SEP-2026, entry version 152.
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_001025200.4.
DR   AlphaFoldDB; Q6GPI1; -.
DR   SMR; Q6GPI1; -.
DR   BioGRID; 136533; 2.
DR   FunCoup; Q6GPI1; 260.
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; 9606-ENSP00000303963; -.
DR   PeptideAtlas; Q6GPI1; -.
DR   ProteomicsDB; 66317; -.
DR   Antibodypedia; 81624; 4 antibodies from 3 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   AGR; HGNC:2522; -.
DR   ClinPGx; PA27023; -.
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   OpenTargets; ENSG00000168928; -.
DR   VEuPathDB; HostDB:ENSG00000168928; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000153216; -.
DR   HOGENOM; CLU_006842_7_6_1; -.
DR   InParanoid; Q6GPI1; -.
DR   OMA; WGFRIAD; -.
DR   OrthoDB; 5918597at2759; -.
DR   PAN-GO; Q6GPI1; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q6GPI1; -.
DR   BRENDA; 3.4.21.1; 2681.
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   Agora; ENSG00000168928; -.
DR   BioGRID-ORCS; 440387; 8 hits in 1083 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 84 other cell types or tissues.
DR   ExpressionAtlas; Q6GPI1; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   FunFam; 2.40.10.10:FF:000118; Chymotrypsinogen A; 1.
DR   FunFam; 2.40.10.10:FF:000176; Chymotrypsinogen A; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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:SF53; CHYMOTRYPSINOGEN B2; 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.
PE   1: Evidence at protein level;
KW   Digestion; Disulfide bond; Hydrolase; Protease; Proteomics identification;
KW   Reference proteome; 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
//