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Q9D7R7 (PEPC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Synonyms:Upg1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 BAB25952.1 differs from that shown. Reason: Frameshift at position 378.

Ontologies

Keywords
   Biological processDigestion
   Cellular componentSecreted
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMDisulfide bond
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdigestion

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Propeptide17 – 6246Activation peptide By similarity
PRO_0000026063
Chain63 – 392330Gastricsin
PRO_0000026064

Sites

Active site941 By similarity
Active site2801 By similarity

Amino acid modifications

Disulfide bond107 ↔ 112 By similarity
Disulfide bond270 ↔ 275 By similarity
Disulfide bond314 ↔ 347 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9D7R7 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 0D19D87E4683C848

FASTA39242,849
        10         20         30         40         50         60 
MKWMVVALLC LPLLEAALIR VPLKKMKSIR ETMKEQGVLK DFLKNHKYDP GQKYHFGKFG 

        70         80         90        100        110        120 
DYSVLYEPMA YMDASYYGEI SIGTPPQNFL VLFDTGSSNL WVSSVYCQSE ACTTHTRYNP 

       130        140        150        160        170        180 
SKSSTYYTQG QTFSLQYGTG SLTGFFGYDT LRVQSIQVPN QEFGLSENEP GTNFVYAQFD 

       190        200        210        220        230        240 
GIMGLAYPGL SSGGATTALQ GMLGEGALSQ PLFGVYLGSQ QGSNGGQIVF GGVDENLYTG 

       250        260        270        280        290        300 
ELTWIPVTQE LYWQITIDDF LIGNQASGWC SSSGCQGIVD TGTSLLVMPA QYLNELLQTI 

       310        320        330        340        350        360 
GAQEGEYGQY FVSCDSVSSL PTLTFVLNGV QFPLSPSSYI IQEEGSCMVG LESLSLNAES 

       370        380        390 
GQPLWILGDV FLRSYYAVFD MGNNRVGLAP SV 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Stomach.
[2]"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].
Tissue: Placenta.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK008959 mRNA. Translation: BAB25990.1.
AK008886 mRNA. Translation: BAB25952.1. Frameshift.
BC099409 mRNA. Translation: AAH99409.1.
CCDSCCDS28855.1.
RefSeqNP_080249.2. NM_025973.3.
UniGeneMm.22957.

3D structure databases

ProteinModelPortalQ9D7R7.
SMRQ9D7R7. Positions 17-57, 63-391.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000024782.

Protein family/group databases

MEROPSA01.003.

PTM databases

PhosphoSiteQ9D7R7.

Proteomic databases

PRIDEQ9D7R7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024782; ENSMUSP00000024782; ENSMUSG00000023987.
GeneID109820.
KEGGmmu:109820.
UCSCuc008cwb.1. mouse.

Organism-specific databases

CTD5225.
MGIMGI:98909. Pgc.

Phylogenomic databases

eggNOGNOG248684.
GeneTreeENSGT00670000097830.
HOGENOMHOG000197681.
HOVERGENHBG000482.
InParanoidQ9D7R7.
KOK01377.
OMAASGWCSE.
OrthoDBEOG7HQN88.
PhylomeDBQ9D7R7.
TreeFamTF314990.

Gene expression databases

BgeeQ9D7R7.
CleanExMM_PGC.
GenevestigatorQ9D7R7.

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. mouse.
NextBio362821.
PROQ9D7R7.
SOURCESearch...

Entry information

Entry namePEPC_MOUSE
AccessionPrimary (citable) accession number: Q9D7R7
Secondary accession number(s): Q9D7T2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot