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P0DJD8

- PEPA3_HUMAN

UniProt

P0DJD8 - PEPA3_HUMAN

Protein

Pepsin A-3

Gene

PGA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 23 (01 Oct 2014)
      Sequence version 1 (22 Feb 2012)
      Previous versions | rss
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    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 – 9411 PublicationPROSITE-ProRule annotation
    Active sitei277 – 27711 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. digestion Source: UniProtKB-KW

    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: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:8885. PGA3.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    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.

    Organism-specific databases

    HPAiCAB026358.
    HPA046875.

    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.
    HOGENOMiHOG000197681.
    HOVERGENiHBG000482.
    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

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    MKWLLLLGLV ALSECIMYKV PLIRKKSLRR TLSERGLLKD FLKKHNLNPA    50
    RKYFPQWKAP TLVDEQPLEN YLDMEYFGTI GIGTPAQDFT VVFDTGSSNL 100
    WVPSVYCSSL ACTNHNRFNP EDSSTYQSTS ETVSITYGTG SMTGILGYDT 150
    VQVGGISDTN QIFGLSETEP GSFLYYAPFD GILGLAYPSI SSSGATPVFD 200
    NIWNQGLVSQ DLFSVYLSAD DQSGSVVIFG GIDSSYYTGS LNWVPVTVEG 250
    YWQITVDSIT MNGEAIACAE GCQAIVDTGT SLLTGPTSPI ANIQSDIGAS 300
    ENSDGDMVVS CSAISSLPDI VFTINGVQYP VPPSAYILQS EGSCISGFQG 350
    MNLPTESGEL WILGDVFIRQ YFTVFDRANN QVGLAPVA 388
    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:
    EMBL
    GenBank
    DDBJ
    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.
    XP_005276461.1. XM_005276404.1.
    UniGeneiHs.601055.
    Hs.661883.

    Genome annotation databases

    EnsembliENST00000325558; ENSP00000322192; ENSG00000229859.
    GeneIDi101929842.
    643834.
    KEGGihsa:101929842.
    hsa:643834.
    UCSCiuc001nqx.3. human.

    Polymorphism databases

    DMDMi378521956.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK312941 mRNA. Translation: BAG35783.1 .
    AK125628 mRNA. Translation: BAG54225.1 .
    AP000437 Genomic DNA. No translation available.
    BC171815 mRNA. Translation: AAI71815.1 .
    CCDSi CCDS31574.1.
    PIRi A00980. PEHU.
    A30142.
    A92058.
    B30142.
    RefSeqi NP_001073275.1. NM_001079807.2.
    XP_005276461.1. XM_005276404.1.
    UniGenei Hs.601055.
    Hs.661883.

    3D structure databases

    ProteinModelPortali P0DJD8.
    SMRi P0DJD8. Positions 17-388.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei P0DJD8.

    Polymorphism databases

    DMDMi 378521956.

    Proteomic databases

    PRIDEi P0DJD8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000325558 ; ENSP00000322192 ; ENSG00000229859 .
    GeneIDi 101929842.
    643834.
    KEGGi hsa:101929842.
    hsa:643834.
    UCSCi uc001nqx.3. human.

    Organism-specific databases

    CTDi 643834.
    GeneCardsi GC11P060970.
    HGNCi HGNC:8885. PGA3.
    HPAi CAB026358.
    HPA046875.
    MIMi 169700. gene.
    169710. gene.
    neXtProti NX_P0DJD8.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG248684.
    HOGENOMi HOG000197681.
    HOVERGENi HBG000482.
    KOi K06002.
    OMAi XNDESGS.
    OrthoDBi EOG7HQN88.
    PhylomeDBi P0DJD8.
    TreeFami TF314990.

    Miscellaneous databases

    ChiTaRSi PGA3. human.
    NextBioi 115445.
    PROi P0DJD8.
    SOURCEi Search...

    Gene expression databases

    Bgeei P0DJD8.
    CleanExi HS_PGA3.

    Family and domain databases

    Gene3Di 2.40.70.10. 2 hits.
    InterProi IPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR012848. Aspartic_peptidase_N.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view ]
    PANTHERi PTHR13683. PTHR13683. 1 hit.
    Pfami PF07966. A1_Propeptide. 1 hit.
    PF00026. Asp. 1 hit.
    [Graphical view ]
    PRINTSi PR00792. PEPSIN.
    SUPFAMi SSF50630. SSF50630. 1 hit.
    PROSITEi PS00141. ASP_PROTEASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 23 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