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Protein

Pepsin A-3

Gene

PGA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.

Catalytic activityi

Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei94 – 941PROSITE-ProRule annotation1 Publication
Active sitei277 – 2771PROSITE-ProRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Keywords - Biological processi

Digestion

Names & Taxonomyi

Protein namesi
Recommended name:
Pepsin A-3 (EC:3.4.23.1)
Alternative name(s):
Pepsinogen-3
Gene namesi
Name:PGA3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:8885. PGA3.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Polymorphism and mutation databases

BioMutaiPGA3.
DMDMi378521956.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 15152 PublicationsAdd
BLAST
Propeptidei16 – 6247Activation peptidePRO_0000026013Add
BLAST
Chaini63 – 388326Pepsin A-3PRO_0000026014Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi107 ↔ 1121 Publication
Disulfide bondi268 ↔ 2721 Publication
Disulfide bondi311 ↔ 3441 Publication

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PRIDEiP0DJD8.

PTM databases

PhosphoSiteiP0DJD8.

Expressioni

Gene expression databases

BgeeiP0DJD8.
CleanExiHS_PGA3.
ExpressionAtlasiP0DJD8. baseline.
GenevisibleiP0DJD8. HS.

Organism-specific databases

HPAiCAB026358.
HPA046875.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000322192.

Structurei

3D structure databases

ProteinModelPortaliP0DJD8.
SMRiP0DJD8. Positions 17-388.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG248684.
GeneTreeiENSGT00760000118929.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP0DJD8.
KOiK06002.
OMAiXNDESGS.
OrthoDBiEOG7HQN88.
PhylomeDBiP0DJD8.
TreeFamiTF314990.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0DJD8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKWLLLLGLV ALSECIMYKV PLIRKKSLRR TLSERGLLKD FLKKHNLNPA
60 70 80 90 100
RKYFPQWKAP TLVDEQPLEN YLDMEYFGTI GIGTPAQDFT VVFDTGSSNL
110 120 130 140 150
WVPSVYCSSL ACTNHNRFNP EDSSTYQSTS ETVSITYGTG SMTGILGYDT
160 170 180 190 200
VQVGGISDTN QIFGLSETEP GSFLYYAPFD GILGLAYPSI SSSGATPVFD
210 220 230 240 250
NIWNQGLVSQ DLFSVYLSAD DQSGSVVIFG GIDSSYYTGS LNWVPVTVEG
260 270 280 290 300
YWQITVDSIT MNGEAIACAE GCQAIVDTGT SLLTGPTSPI ANIQSDIGAS
310 320 330 340 350
ENSDGDMVVS CSAISSLPDI VFTINGVQYP VPPSAYILQS EGSCISGFQG
360 370 380
MNLPTESGEL WILGDVFIRQ YFTVFDRANN QVGLAPVA
Length:388
Mass (Da):41,976
Last modified:February 22, 2012 - v1
Checksum:i5DA16E41FE198582
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921V → L in BAG35783 (PubMed:14702039).Curated
Sequence conflicti92 – 921V → L in BAG54225 (PubMed:14702039).Curated
Sequence conflicti92 – 921V → L in AAI71815 (PubMed:15489334).Curated
Sequence conflicti371 – 3722YF → FY AA sequence (PubMed:4909888).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK312941 mRNA. Translation: BAG35783.1.
AK125628 mRNA. Translation: BAG54225.1.
AP000437 Genomic DNA. No translation available.
BC171815 mRNA. Translation: AAI71815.1.
CCDSiCCDS31574.1.
PIRiA00980. PEHU.
A30142.
A92058.
B30142.
RefSeqiNP_001073275.1. NM_001079807.2.
UniGeneiHs.601055.
Hs.661883.

Genome annotation databases

EnsembliENST00000325558; ENSP00000322192; ENSG00000229859.
GeneIDi643834.
KEGGihsa:643834.
UCSCiuc001nqx.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK312941 mRNA. Translation: BAG35783.1.
AK125628 mRNA. Translation: BAG54225.1.
AP000437 Genomic DNA. No translation available.
BC171815 mRNA. Translation: AAI71815.1.
CCDSiCCDS31574.1.
PIRiA00980. PEHU.
A30142.
A92058.
B30142.
RefSeqiNP_001073275.1. NM_001079807.2.
UniGeneiHs.601055.
Hs.661883.

3D structure databases

ProteinModelPortaliP0DJD8.
SMRiP0DJD8. Positions 17-388.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000322192.

PTM databases

PhosphoSiteiP0DJD8.

Polymorphism and mutation databases

BioMutaiPGA3.
DMDMi378521956.

Proteomic databases

PRIDEiP0DJD8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000325558; ENSP00000322192; ENSG00000229859.
GeneIDi643834.
KEGGihsa:643834.
UCSCiuc001nqx.3. human.

Organism-specific databases

CTDi643834.
GeneCardsiGC11P060970.
HGNCiHGNC:8885. PGA3.
HPAiCAB026358.
HPA046875.
MIMi169700. gene.
169710. gene.
neXtProtiNX_P0DJD8.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG248684.
GeneTreeiENSGT00760000118929.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP0DJD8.
KOiK06002.
OMAiXNDESGS.
OrthoDBiEOG7HQN88.
PhylomeDBiP0DJD8.
TreeFamiTF314990.

Miscellaneous databases

ChiTaRSiPGA3. human.
NextBioi115445.
PROiP0DJD8.
SOURCEiSearch...

Gene expression databases

BgeeiP0DJD8.
CleanExiHS_PGA3.
ExpressionAtlasiP0DJD8. baseline.
GenevisibleiP0DJD8. HS.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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].
    Tissue: Stomach.
  2. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Isolation of human, swine, and rat prepepsinogens and calf preprochymosin, and determination of the primary structures of their NH2-terminal signal sequences."
    Ichihara Y., Sogawa K., Takahashi K.
    J. Biochem. 98:483-492(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE OF 1-28.
  5. "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 16-100.
  6. "Activation of human pepsinogens."
    Foltmann B.
    FEBS Lett. 241:69-72(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 16-68.
  7. "Carboxyl-terminal sequence of human gastricsin and pepsin."
    Huang W.-Y., Tang J.
    J. Biol. Chem. 245:2189-2193(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 362-388.
  8. "Primary structure of human pepsinogen gene."
    Sogawa K., Fujii-Kuriyama Y., Mizukami Y., Ichihara Y., Takahashi K.
    J. Biol. Chem. 258:5306-5311(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  9. "Nucleotide sequence comparison of five human pepsinogen A (PGA) genes: evolution of the PGA multigene family."
    Evers M.P.J., Zelle B., Bebelman J.-P., van Beusechem V., Kraakman L., Hoffer M.J.V., Pronk J.C., Mager W.H., Planta R.J., Eriksson A.W., Frants R.R.
    Genomics 4:232-239(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
    Tissue: Placenta.
  10. "Crystal structure of human pepsin and its complex with pepstatin."
    Fujinaga M., Chernaia M.M., Tarasova N.I., Mosimann S.C., James M.N.G.
    Protein Sci. 4:960-972(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 63-388, ACTIVE SITES, DISULFIDE BONDS.

Entry informationi

Entry nameiPEPA3_HUMAN
AccessioniPrimary (citable) accession number: P0DJD8
Secondary accession number(s): A8K749
, B2R7D6, B7ZW75, P00790, Q7M4R0, Q8N1E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: February 22, 2012
Last modified: July 22, 2015
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.