CTRC_BOVIN
ID CTRC_BOVIN Reviewed; 268 AA.
AC Q7M3E1; A5PJB3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Chymotrypsin-C;
DE EC=3.4.21.2;
DE AltName: Full=bPTLP;
DE Flags: Precursor;
GN Name=CTRC;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pancreas;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-268.
RX PubMed=11282978; DOI=10.1101/gr.170101;
RA Smith T.P.L., Grosse W.M., Freking B.A., Roberts A.J., Stone R.T.,
RA Casas E., Wray J.E., White J., Cho J., Fahrenkrug S.C., Bennett G.L.,
RA Heaton M.P., Laegreid W.W., Rohrer G.A., Chitko-McKown C.G., Pertea G.,
RA Holt I., Karamycheva S., Liang F., Quackenbush J., Keele J.W.;
RT "Sequence evaluation of four pooled-tissue normalized bovine cDNA libraries
RT and construction of a gene index for cattle.";
RL Genome Res. 11:626-630(2001).
RN [3]
RP PROTEIN SEQUENCE OF 30-52.
RC TISSUE=Pancreas;
RX PubMed=8907182; DOI=10.1093/oxfordjournals.jbchem.a021193;
RA Tsuji A., Edazawa K., Sakiyama K., Nagata K., Sasaki Y., Nagamune H.,
RA Matsuda Y.;
RT "Purification and characterization of a novel serine proteinase from the
RT microsomal fraction of bovine pancreas.";
RL J. Biochem. 119:100-105(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 17-268 OF COMPLEX WITH CPA1 AND
RP PPE, DISULFIDE BONDS, AND TISSUE SPECIFICITY.
RX PubMed=7556081; DOI=10.1002/j.1460-2075.1995.tb00117.x;
RA Gomis-Rueth F.-X., Gomez M., Bode W., Huber R., Aviles F.X.;
RT "The three-dimensional structure of the native ternary complex of bovine
RT pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen
RT C.";
RL EMBO J. 14:4387-4394(1995).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 17-268 OF COMPLEX WITH CPA1 AND
RP PPE, DISULFIDE BONDS, AND TISSUE SPECIFICITY.
RX PubMed=9223647; DOI=10.1006/jmbi.1997.1040;
RA Gomis-Ruth F.-X., Gomez-Ortiz M., Vendrell J., Ventura S., Bode W.,
RA Huber R., Aviles F.X.;
RT "Crystal structure of an oligomer of proteolytic zymogens: detailed
RT conformational analysis of the bovine ternary complex and implications for
RT their activation.";
RL J. Mol. Biol. 269:861-880(1997).
CC -!- FUNCTION: Has chymotrypsin-type protease activity and hypocalcemic
CC activity. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Leu-|-Xaa, Tyr-|-Xaa, Phe-|-Xaa, Met-|-
CC Xaa, Trp-|-Xaa, Gln-|-Xaa, Asn-|-Xaa.; EC=3.4.21.2;
CC -!- SUBUNIT: Monomer. The zymogen is secreted as a ternary complex composed
CC of procarboxypeptidase A, chymotrypsinogen C and proproteinase E.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Pancreas. {ECO:0000269|PubMed:7556081,
CC ECO:0000269|PubMed:9223647}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; BC134798; AAI34799.1; -; mRNA.
DR EMBL; BC142035; AAI42036.1; -; mRNA.
DR EMBL; CK771392; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; PU0036; PU0036.
DR RefSeq; NP_001092435.1; NM_001098965.1.
DR PDB; 1PYT; X-ray; 2.35 A; D=17-268.
DR PDBsum; 1PYT; -.
DR AlphaFoldDB; Q7M3E1; -.
DR SMR; Q7M3E1; -.
DR STRING; 9913.ENSBTAP00000033942; -.
DR MEROPS; S01.157; -.
DR PaxDb; Q7M3E1; -.
DR PRIDE; Q7M3E1; -.
DR GeneID; 514047; -.
DR KEGG; bta:514047; -.
DR CTD; 11330; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q7M3E1; -.
DR OrthoDB; 1314811at2759; -.
DR TreeFam; TF330455; -.
DR EvolutionaryTrace; Q7M3E1; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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 Gene3D; 2.40.10.10; -; 2.
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 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Secreted; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..16
FT PROPEP 17..29
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:8907182"
FT /id="PRO_0000288614"
FT CHAIN 30..268
FT /note="Chymotrypsin-C"
FT /id="PRO_0000288615"
FT DOMAIN 30..268
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 74
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 121
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 17..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 59..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 155..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 186..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 212..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1PYT"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:1PYT"
FT STRAND 54..65
FT /evidence="ECO:0007829|PDB:1PYT"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1PYT"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1PYT"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1PYT"
FT STRAND 100..109
FT /evidence="ECO:0007829|PDB:1PYT"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:1PYT"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:1PYT"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:1PYT"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1PYT"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:1PYT"
FT TURN 189..195
FT /evidence="ECO:0007829|PDB:1PYT"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:1PYT"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:1PYT"
FT STRAND 227..237
FT /evidence="ECO:0007829|PDB:1PYT"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:1PYT"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:1PYT"
FT HELIX 259..265
FT /evidence="ECO:0007829|PDB:1PYT"
SQ SEQUENCE 268 AA; 29255 MW; 7B006994F91A04D8 CRC64;
MLGITVFTTF LAYASSCGAP IFQPNLSARV VGGEDAIPHS WPWQISLQYL RDNTWRHTCG
GTLITPNHVL TAAHCISNTL TYRVALGKNN LEVEDEAGSL YVGVDTIFVH EKWNSFLVRN
DIALIKLAET VELSDTIQVA CLPEEGSLLP QDYPCFVTGW GRLYTNGPIA AELQQGLQPV
VDYATCSQRD WWGTTVKETM VCAGGDGVIS ACNGDSGGPL NCQAENGNWD VRGIVSFGSG
LSCNTFKKPT VFTRVSAYID WINQKLQL
