Reviewed, UniProtKB/Swiss-Prot Q99895 (CTRC_HUMAN)

Names and origin

Protein names

Recommended name:
    Chymotrypsin-C
    EC=3.4.21.2
Alternative name(s):
    Caldecrin

Gene names

Name:	CTRC
Synonyms:	CLCR

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	268 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has chymotrypsin-type protease activity and hypocalcemic activity.
Catalytic activity	Preferential cleavage: Leu-|-Xaa, Tyr-|-Xaa, Phe-|-Xaa, Met-|-Xaa, Trp-|-Xaa, Gln-|-Xaa, Asn-|-Xaa.
Tissue specificity	Pancreas.
Involvement in disease	Variations in CTRC influence susceptibility to chronic pancreatitis [MIM:167800]. Chronic pancreatitis is a persistent inflammatory disorder characterized by permanent destruction of the pancreatic parenchyma.
Sequence similarities	Belongs to the peptidase S1 family. Elastase subfamily. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Gene Ontology (GO)
Biological process	proteolysis Ref.1 Traceable author statement. Source: ProtInc
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	Potential
	Propeptide	17 – 29	13	Activation peptide		PRO_0000027713
	Chain	30 – 268	239	Chymotrypsin-C		PRO_0000027714
Regions
	Domain	30 – 267	238	Peptidase S1
Sites
	Active site	74	1	Charge relay system By similarity
	Active site	121	1	Charge relay system By similarity
	Active site	216	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	25	1	N-linked (GlcNAc...) Potential
	Glycosylation	52	1	N-linked (GlcNAc...) Potential
	Glycosylation	226	1	N-linked (GlcNAc...) Potential
	Disulfide bond	17 ↔ 141		By similarity
	Disulfide bond	59 ↔ 75		By similarity
	Disulfide bond	155 ↔ 222		By similarity
	Disulfide bond	186 ↔ 202		By similarity
	Disulfide bond	212 ↔ 243		By similarity
Natural variations
	Natural variant	35	1	D → H Ref.6		VAR_043516
	Natural variant	35	1	D → N Ref.6		VAR_043517
	Natural variant	37	1	R → Q Normal secretion and activity. Ref.6		VAR_043518
	Natural variant	48	1	Q → R Reduced secretion and activity. Ref.6		VAR_043519
	Natural variant	73	1	A → T Reduced secretion; abolishes activity. Ref.6		VAR_043520
	Natural variant	80	1	R → W Ref.1		VAR_010928
	Natural variant	172	1	K → E: dbSNP rs34949635. Ref.6		VAR_043521
	Natural variant	217	1	G → R Ref.6		VAR_043522
	Natural variant	217	1	G → S Reduced secretion and activity. Ref.6		VAR_043523
	Natural variant	218	1	G → S Ref.6		VAR_043524
	Natural variant	220	1	L → R Ref.6		VAR_043525
	Natural variant	225	1	E → A Ref.6		VAR_043526
	Natural variant	235	1	V → I Slightly reduced secretion and activity. Ref.6		VAR_043527
	Natural variant	249	1	P → L Ref.6		VAR_043528
	Natural variant	254	1	R → W Reduced secretion; normal activity. Ref.6		VAR_043529
	Natural variant	260	1	D → N Ref.6		VAR_043530
Experimental info
	Sequence conflict	16	1	S → T in AAB47104. Ref.1
	Sequence conflict	52	1	N → D in CAA74031. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q99895-1 [UniParc]. Last modified June 1, 2001. Version 2. Checksum: 460BF33B4A96516F	FASTA	268	29,484
	10 20 30 40 50 60 MLGITVLAAL LACASSCGVP SFPPNLSARV VGGEDARPHS WPWQISLQYL KNDTWRHTCG 70 80 90 100 110 120 GTLIASNFVL TAAHCISNTR TYRVAVGKNN LEVEDEEGSL FVGVDTIHVH KRWNALLLRN 130 140 150 160 170 180 DIALIKLAEH VELSDTIQVA CLPEKDSLLP KDYPCYVTGW GRLWTNGPIA DKLQQGLQPV 190 200 210 220 230 240 VDHATCSRID WWGFRVKKTM VCAGGDGVIS ACNGDSGGPL NCQLENGSWE VFGIVSFGSR 250 260 RGCNTRKKPV VYTRVSAYID WINEKMQL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of human caldecrin." Tomomura A., Akiyama M., Itoh H., Yoshino I., Tomomura M., Nishii Y., Noikura T., Saheki T. FEBS Lett. 386:26-28(1996) [PubMed: 8635596] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TRP-80. Tissue: Pancreas.
[2]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas.
[4]	"A human pancreatic chymotrypsin: biochemical and molecular characterization." Sziegoleit A. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-268. Tissue: Pancreas.
[5]	"Caldecrin is a novel-type serine protease expressed in pancreas, but its homologue, elastase IV, is an artifact during cloning derived from caldecrin gene." Yoshino-Yasuda I., Kobayashi K., Akiyama M., Itoh H., Tomomura A., Saheki T. J. Biochem. 123:546-554(1998) [PubMed: 9538241] [Abstract] Cited for: CHARACTERIZATION.
[6]	"Chymotrypsin C (CTRC) variants that diminish activity or secretion are associated with chronic pancreatitis." Rosendahl J., Witt H., Szmola R., Bhatia E., Ozsvari B., Landt O., Schulz H.-U., Gress T.M., Pfuetzer R., Loehr M., Kovacs P., Blueher M., Stumvoll M., Choudhuri G., Hegyi P., te Morsche R.H.M., Drenth J.P.H., Truninger K. , Macek M. Jr., Puhl G., Witt U., Schmidt H., Buening C., Ockenga J., Kage A., Groneberg D.A., Nickel R., Berg T., Wiedenmann B., Boedeker H., Keim V., Moessner J., Teich N., Sahin-Toth M. Nat. Genet. 40:78-82(2008) [PubMed: 18059268] [Abstract] Cited for: VARIANTS HIS-35; ASN-35; GLN-37; ARG-48; THR-73; GLU-172; SER-217; ARG-217; SER-218; ARG-220; ALA-225; ILE-235; LEU-249; TRP-254 AND ASN-260, CHARACTERIZATION OF VARIANTS GLN-37; ARG-48; THR-73; SER-217; ILE-235 AND TRP-254, INVOLVEMENT IN CHRONIC PANCREATITIS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	S82198 mRNA. Translation: AAB47104.2. Sequence problems. AL031283 Genomic DNA. Translation: CAB77355.1. BC015118 mRNA. Translation: AAH15118.1. Y13697 mRNA. Translation: CAA74031.1.
IPI	IPI00018553.
PIR	S68825. S68826.
RefSeq	NP_009203.2.
UniGene	Hs.631869
3D structure databases
HSSP	HSSP built from PDB template 1PYT based on UniProtKB P05805.
SMR	Q99895. Positions 17-268.
ModBase	Search...
Protein family/group databases
MEROPS	S01.157.
Genome annotation databases
Ensembl	ENSG00000162438. Homo sapiens. [Contig view]
GeneID	11330.
KEGG	hsa:11330.
NMPDR	fig|9606.3.peg.354.
Organism-specific databases
GeneCards	GC01P015637.
H-InvDB	HIX0000151.
HGNC	HGNC:2523. CTRC.
MIM	167800. phenotype. 601405. gene.
Orphanet	676. Pancreatitis, hereditary.
PharmGKB	PA27024.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q99895.
HOVERGEN	Q99895.
OMA	Q99895. CISNTRT.
Enzyme and pathway databases
BRENDA	3.4.21.2. 247.
Gene expression databases
ArrayExpress	Q99895.
Bgee	Q99895.
CleanEx	HS_CTRC.
GermOnline	ENSG00000162438. Homo sapiens.
Family and domain databases
InterPro	IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	43039.
SOURCE	Search...

Entry information

Entry name

CTRC_HUMAN

Accession

Primary (citable) accession number: Q99895
Secondary accession number(s): O00765, Q9NUH5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)