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P0DJD7

- PEPA4_HUMAN

UniProt

P0DJD7 - PEPA4_HUMAN

Protein

Pepsin A-4

Gene

PGA4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 24 (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

    Protein family/group databases

    MEROPSiA01.070.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pepsin A-4 (EC:3.4.23.1)
    Alternative name(s):
    Pepsinogen-4
    Gene namesi
    Name:PGA4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:8886. PGA4.

    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_0000415757Add
    BLAST
    Chaini63 – 388326Pepsin A-4PRO_0000415758Add
    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

    PRIDEiP0DJD7.

    PTM databases

    PhosphoSiteiP0DJD7.

    Expressioni

    Gene expression databases

    BgeeiP0DJD7.
    CleanExiHS_PGA4.

    Organism-specific databases

    HPAiCAB026358.
    HPA046875.

    Interactioni

    Structurei

    Secondary structure

    1
    388
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi65 – 673
    Beta strandi69 – 713
    Turni72 – 743
    Beta strandi75 – 828
    Turni83 – 864
    Beta strandi87 – 948
    Beta strandi100 – 1023
    Helixi110 – 1134
    Helixi120 – 1223
    Beta strandi127 – 13610
    Beta strandi141 – 15313
    Beta strandi156 – 16813
    Helixi172 – 1765
    Beta strandi180 – 1845
    Helixi188 – 1903
    Helixi192 – 1943
    Helixi198 – 2047
    Beta strandi209 – 2168
    Beta strandi226 – 2294
    Helixi234 – 2363
    Beta strandi237 – 2393
    Beta strandi242 – 2454
    Turni249 – 2524
    Beta strandi253 – 2564
    Beta strandi258 – 2614
    Beta strandi264 – 2674
    Beta strandi272 – 2765
    Beta strandi282 – 2854
    Helixi287 – 29610
    Beta strandi307 – 3093
    Helixi311 – 3166
    Beta strandi320 – 3245
    Beta strandi327 – 3315
    Helixi333 – 3364
    Beta strandi337 – 3404
    Beta strandi343 – 3508
    Beta strandi361 – 3633
    Helixi365 – 3706
    Beta strandi371 – 3766
    Turni377 – 3804
    Beta strandi381 – 3877

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FLHX-ray2.45A63-388[»]
    1PSNX-ray2.20A63-388[»]
    1PSOX-ray2.00E63-388[»]
    1QRPX-ray1.96E63-388[»]
    3UTLX-ray2.61A63-388[»]
    ProteinModelPortaliP0DJD7.
    SMRiP0DJD7. Positions 17-388.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase A1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    KOiK06002.
    OMAiAYFGTIS.
    OrthoDBiEOG7HQN88.
    PhylomeDBiP0DJD7.
    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.

    P0DJD7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKWLLLLGLV ALSECIMYKV PLIRKKSLRR TLSERGLLKD FLKKHNLNPA    50
    RKYFPQWEAP 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):41,977
    Last modified:February 22, 2012 - v1
    Checksum:iC9CB89BA08F4D78B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti291 – 2911A → T in BAF84553. (PubMed:14702039)Curated
    Sequence conflicti371 – 3722YF → FY AA sequence (PubMed:4909888)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00287
    , J00279, J00280, J00281, J00282, J00283, J00284, J00285, J00286 Genomic DNA. Translation: AAA98529.1.
    AK291864 mRNA. Translation: BAF84553.1.
    AP000437 Genomic DNA. No translation available.
    AP003037 Genomic DNA. No translation available.
    BC150659 mRNA. Translation: AAI50660.1.
    BC171910 mRNA. Translation: AAI71910.1.
    BC171920 mRNA. Translation: AAI71920.1.
    CCDSiCCDS31575.1.
    PIRiA00980. PEHU.
    A30142.
    A92058.
    B30142.
    RefSeqiNP_001073276.1. NM_001079808.2.
    UniGeneiHs.432854.
    Hs.661883.

    Genome annotation databases

    EnsembliENST00000378149; ENSP00000367391; ENSG00000229183.
    GeneIDi643847.
    KEGGihsa:643847.
    UCSCiuc001nqy.3. human.

    Polymorphism databases

    DMDMi378521995.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00287
    , J00279 , J00280 , J00281 , J00282 , J00283 , J00284 , J00285 , J00286 Genomic DNA. Translation: AAA98529.1 .
    AK291864 mRNA. Translation: BAF84553.1 .
    AP000437 Genomic DNA. No translation available.
    AP003037 Genomic DNA. No translation available.
    BC150659 mRNA. Translation: AAI50660.1 .
    BC171910 mRNA. Translation: AAI71910.1 .
    BC171920 mRNA. Translation: AAI71920.1 .
    CCDSi CCDS31575.1.
    PIRi A00980. PEHU.
    A30142.
    A92058.
    B30142.
    RefSeqi NP_001073276.1. NM_001079808.2.
    UniGenei Hs.432854.
    Hs.661883.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FLH X-ray 2.45 A 63-388 [» ]
    1PSN X-ray 2.20 A 63-388 [» ]
    1PSO X-ray 2.00 E 63-388 [» ]
    1QRP X-ray 1.96 E 63-388 [» ]
    3UTL X-ray 2.61 A 63-388 [» ]
    ProteinModelPortali P0DJD7.
    SMRi P0DJD7. Positions 17-388.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P0DJD7.

    Protein family/group databases

    MEROPSi A01.070.

    PTM databases

    PhosphoSitei P0DJD7.

    Polymorphism databases

    DMDMi 378521995.

    Proteomic databases

    PRIDEi P0DJD7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000378149 ; ENSP00000367391 ; ENSG00000229183 .
    GeneIDi 643847.
    KEGGi hsa:643847.
    UCSCi uc001nqy.3. human.

    Organism-specific databases

    CTDi 643847.
    GeneCardsi GC11P060989.
    HGNCi HGNC:8886. PGA4.
    HPAi CAB026358.
    HPA046875.
    MIMi 169700. gene.
    169720. gene.
    neXtProti NX_P0DJD7.
    GenAtlasi Search...

    Phylogenomic databases

    KOi K06002.
    OMAi AYFGTIS.
    OrthoDBi EOG7HQN88.
    PhylomeDBi P0DJD7.
    TreeFami TF314990.

    Miscellaneous databases

    GenomeRNAii 643847.
    NextBioi 115463.
    PROi P0DJD7.
    SOURCEi Search...

    Gene expression databases

    Bgeei P0DJD7.
    CleanExi HS_PGA4.

    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. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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: Skeletal muscle.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Colon and Kidney.
    5. "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.
    6. "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.
    7. "Activation of human pepsinogens."
      Foltmann B.
      FEBS Lett. 241:69-72(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 16-68.
    8. "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.
    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 nameiPEPA4_HUMAN
    AccessioniPrimary (citable) accession number: P0DJD7
    Secondary accession number(s): A8K749
    , 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 24 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

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3