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P20142 (PEPC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gastricsin

EC=3.4.23.3
Alternative name(s):
Pepsinogen C
Gene names
Name:PGC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes a variety of proteins.

Catalytic activity

More restricted specificity than pepsin A, but shows preferential cleavage at Tyr-|-Xaa bonds. High activity on hemoglobin.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase A1 family.

Sequence caution

The sequence AAA60062.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processDigestion
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdigestion

Traceable author statement Ref.1. Source: ProtInc

proteolysis

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentextracellular space

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionaspartic-type endopeptidase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P20142-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P20142-2)

The sequence of this isoform differs from the canonical sequence as follows:
     217-388: QQGSSGGAVV...NNRVGFATAA → LVLESSGLGP...PPRSQHHSGA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.9 Ref.10
Propeptide17 – 5943Activation peptide
PRO_0000026056
Chain60 – 388329Gastricsin
PRO_0000026057

Sites

Active site911
Active site2761

Amino acid modifications

Disulfide bond104 ↔ 109
Disulfide bond267 ↔ 271
Disulfide bond310 ↔ 343

Natural variations

Alternative sequence217 – 388172QQGSS…FATAA → LVLESSGLGPLLTPSRAAPP SSTLQLPEKPLEQTWNILTP FTKTLPVSNLSRKVTSWAGV GIPVTCLPEAGSGGERRAEC GLGVPTTRGPPRSQHHSGA in isoform 2.
VSP_042312

Experimental info

Sequence conflict40 – 412GE → ED AA sequence Ref.10
Sequence conflict521W → S AA sequence Ref.10

Secondary structure

............................................................................... 388
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: F862DFDC1438BB92

FASTA38842,426
        10         20         30         40         50         60 
MKWMVVVLVC LQLLEAAVVK VPLKKFKSIR ETMKEKGLLG EFLRTHKYDP AWKYRFGDLS 

        70         80         90        100        110        120 
VTYEPMAYMD AAYFGEISIG TPPQNFLVLF DTGSSNLWVP SVYCQSQACT SHSRFNPSES 

       130        140        150        160        170        180 
STYSTNGQTF SLQYGSGSLT GFFGYDTLTV QSIQVPNQEF GLSENEPGTN FVYAQFDGIM 

       190        200        210        220        230        240 
GLAYPALSVD EATTAMQGMV QEGALTSPVF SVYLSNQQGS SGGAVVFGGV DSSLYTGQIY 

       250        260        270        280        290        300 
WAPVTQELYW QIGIEEFLIG GQASGWCSEG CQAIVDTGTS LLTVPQQYMS ALLQATGAQE 

       310        320        330        340        350        360 
DEYGQFLVNC NSIQNLPSLT FIINGVEFPL PPSSYILSNN GYCTVGVEPT YLSSQNGQPL 

       370        380 
WILGDVFLRS YYSVYDLGNN RVGFATAA 

« Hide

Isoform 2 [UniParc].

Checksum: 79BD7C79ABDF8879
Show »

FASTA31534,208

References

« Hide 'large scale' references
[1]"Primary structure of human pepsinogen C gene."
Hayano T., Sogawa K., Ichihara Y., Fujii-Kuriyama Y., Takahashi K.
J. Biol. Chem. 263:1382-1385(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Erratum
Hayano T., Sogawa K., Ichihara Y., Fujii-Kuriyama Y., Takahashi K.
J. Biol. Chem. 263:14592-14592(1988)
[3]"Human pepsinogen C (progastricsin). Isolation of cDNA clones, localization to chromosome 6, and sequence homology with pepsinogen A."
Taggart R.T., Cass L.G., Mohandas T.K., Derby P., Barr P.J., Pals G., Bell G.I.
J. Biol. Chem. 264:375-379(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Human pepsinogen C (progastricsin) polymorphism: evidence for a single locus located at 6p21.1-pter."
Pals G., Azuma T., Mohandas T.K., Bell G.I., Bacon J., Samloff I.M., Walz D.A., Barr P.J., Taggart R.T.
Genomics 4:137-148(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[5]"cDNA sequence of human gastricsin."
Wong R.N.S., Tang J.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Stomach.
[7]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORM 1).
Tissue: Liver.
[9]"A comparative study on the NH2-terminal amino acid sequences and some other properties of six isozymic forms of human pepsinogens and pepsins."
Athauda S.B.P., Tanji M., Kageyama T., Takahashi K.
J. Biochem. 106:920-927(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-101.
[10]"Human progastricsin. Analysis of intermediates during activation into gastricsin and determination of the amino acid sequence of the propart."
Foltmann B., Jensen A.L.
Eur. J. Biochem. 128:63-70(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-64.
[11]"Crystal and molecular structures of human progastricsin at 1.62-A resolution."
Moore S.A., Sielecki A.R., Chernaia M.M., Tarasova N.I., James M.N.G.
J. Mol. Biol. 247:466-485(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS).
[12]"Structural characterization of activation 'intermediate 2' on the pathway to human gastricsin."
Khan A.R., Cherney M.M., Tarasova N.I., James M.N.
Nat. Struct. Biol. 4:1010-1015(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18667 expand/collapse EMBL AC list , M18659, M18660, M18661, M18662, M18663, M18664, M18665, M18666 Genomic DNA. Translation: AAA60062.1. Different initiation.
J04443 mRNA. Translation: AAA60074.1.
M23077 expand/collapse EMBL AC list , M23069, M23070, M23071, M23072, M23073, M23074, M23075 Genomic DNA. Translation: AAA60063.1.
U75272 mRNA. Translation: AAB18273.1.
AK301298 mRNA. Translation: BAG62855.1.
AL365205 Genomic DNA. Translation: CAI13181.1.
BC073740 mRNA. Translation: AAH73740.1.
CCDSCCDS4859.1. [P20142-1]
CCDS55000.1. [P20142-2]
PIRA29937.
RefSeqNP_001159896.1. NM_001166424.1. [P20142-2]
NP_002621.1. NM_002630.3. [P20142-1]
UniGeneHs.1867.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AVFX-ray2.36A/J60-388[»]
P/Q17-42[»]
1HTRX-ray1.62B60-388[»]
P17-59[»]
ProteinModelPortalP20142.
SMRP20142. Positions 17-388.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111246. 4 interactions.
STRING9606.ENSP00000362116.

Chemistry

BindingDBP20142.
ChEMBLCHEMBL2136.

Protein family/group databases

MEROPSA01.003.

PTM databases

PhosphoSiteP20142.

Polymorphism databases

DMDM129796.

Proteomic databases

MaxQBP20142.
PaxDbP20142.
PRIDEP20142.

Protocols and materials databases

DNASU5225.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373025; ENSP00000362116; ENSG00000096088. [P20142-1]
ENST00000425343; ENSP00000405094; ENSG00000096088. [P20142-2]
GeneID5225.
KEGGhsa:5225.
UCSCuc003ora.2. human. [P20142-1]
uc021yzm.1. human. [P20142-2]

Organism-specific databases

CTD5225.
GeneCardsGC06M041704.
HGNCHGNC:8890. PGC.
HPAHPA031717.
HPA031718.
MIM169740. gene.
neXtProtNX_P20142.
PharmGKBPA33228.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG248684.
HOGENOMHOG000197681.
HOVERGENHBG000482.
InParanoidP20142.
KOK01377.
OMAASGWCSE.
OrthoDBEOG7HQN88.
PhylomeDBP20142.
TreeFamTF314990.

Gene expression databases

ArrayExpressP20142.
BgeeP20142.
CleanExHS_PGC.
GenevestigatorP20142.

Family and domain databases

Gene3D2.40.70.10. 2 hits.
InterProIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERPTHR13683. PTHR13683. 1 hit.
PfamPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. SSF50630. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPGC. human.
EvolutionaryTraceP20142.
GeneWikiGastricsin.
GenomeRNAi5225.
NextBio20200.
PMAP-CutDBP20142.
PROP20142.
SOURCESearch...

Entry information

Entry namePEPC_HUMAN
AccessionPrimary (citable) accession number: P20142
Secondary accession number(s): B4DVZ3, Q5T3D7, Q5T3D8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM