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P12815

- PDCD6_MOUSE

UniProt

P12815 - PDCD6_MOUSE

Protein

Programmed cell death protein 6

Gene

Pdcd6

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Calcium-binding protein required for T-cell receptor-, Fas-, and glucocorticoid-induced cell death. Calcium-dependent adapter necessary for the association between PDCD6IP and TSG101 By similarity. May mediate Ca2+-regulated signals along the death pathway. Interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity. May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition of VEGF-induced phosphoprylation of the Akt signaling pathway. Isoform 2 has a lower Ca2+ affinity than isoform 1. Isoform 1 and, to a lesser extend, isoform 2, can stabilize SHISA5.By similarity2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi36 – 47121Add
    BLAST
    Calcium bindingi73 – 84122PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi103 – 114123Add
    BLAST
    Calcium bindingi169 – 181134Add
    BLAST

    GO - Molecular functioni

    1. binding, bridging Source: UniProtKB
    2. calcium-dependent cysteine-type endopeptidase activity Source: RefGenome
    3. calcium-dependent protein binding Source: UniProtKB
    4. calcium ion binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein dimerization activity Source: UniProtKB
    7. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
    2. angiogenesis Source: UniProtKB-KW
    3. apoptotic process Source: MGI
    4. cellular response to heat Source: UniProtKB
    5. intracellular protein transport Source: UniProtKB
    6. negative regulation of protein kinase B signaling Source: UniProtKB
    7. negative regulation of TOR signaling Source: UniProtKB
    8. negative regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
    9. positive regulation of angiogenesis Source: UniProtKB
    10. positive regulation of endothelial cell migration Source: UniProtKB
    11. positive regulation of endothelial cell proliferation Source: UniProtKB
    12. proteolysis Source: RefGenome
    13. response to calcium ion Source: UniProtKB
    14. vascular endothelial growth factor receptor-2 signaling pathway Source: UniProtKB

    Keywords - Biological processi

    Angiogenesis, Apoptosis

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Programmed cell death protein 6
    Alternative name(s):
    ALG-257
    PMP41
    Probable calcium-binding protein ALG-2
    Gene namesi
    Name:Pdcd6
    Synonyms:Alg2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:109283. Pdcd6.

    Subcellular locationi

    Nucleus membrane By similarity; Peripheral membrane protein By similarity. Endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity. Nucleus By similarity. Endosome By similarity
    Note: Interaction with RBM22 induces relocalization from the cytoplasm to the nucleus. Translocated from the cytoplasm to the nucleus after heat shock cell treatment. Accumulates in cytoplasmic vesicle-like organelles after heat shock treatment, which may represent stress granules By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic vesicle Source: Ensembl
    3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    4. endosome Source: UniProtKB-SubCell
    5. nuclear membrane Source: UniProtKB-SubCell
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Endosome, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 191190Programmed cell death protein 6PRO_0000073730Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP12815.
    PaxDbiP12815.
    PRIDEiP12815.

    PTM databases

    PhosphoSiteiP12815.

    Expressioni

    Gene expression databases

    BgeeiP12815.
    CleanExiMM_PDCD6.
    GenevestigatoriP12815.

    Interactioni

    Subunit structurei

    Isoform 1 and isoform 2 self-associate; probably forming homodimers. Interacts with SHISA5, PEF1, RBM22, PLSCR4, ANXA7, TSG101 and DAPK1. Interacts with PDCD6IP, SEC31A, ANXA11 (via N-terminus), PLSCR3 (via N-terminus) and MCOLN1; the interactions are calcium-dependent. Seems to play a role in the regulation of the distribution and function of MCOLN1 in the endosomal pathway. Isoform 2 does not interact with SHISA5, PDCD6IP, TSG101, ANXA7 and ANXA11.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FASP254452EBI-309164,EBI-494743From a different organism.
    SHISA5Q8N1145EBI-309164,EBI-2115556From a different organism.

    Protein-protein interaction databases

    BioGridi202071. 3 interactions.
    IntActiP12815. 9 interactions.
    MINTiMINT-217398.

    Structurei

    Secondary structure

    1
    191
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi25 – 3511
    Beta strandi41 – 433
    Helixi45 – 517
    Beta strandi55 – 584
    Helixi62 – 7211
    Beta strandi75 – 806
    Helixi82 – 10221
    Beta strandi108 – 1103
    Helixi112 – 12211
    Helixi128 – 13811
    Helixi148 – 16821
    Helixi180 – 1878

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HQVX-ray2.30A1-191[»]
    ProteinModelPortaliP12815.
    SMRiP12815. Positions 20-188.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12815.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 5836EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini59 – 8931EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini90 – 12536EF-hand 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini126 – 16136EF-hand 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini162 – 19130EF-hand 5PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 5 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG249191.
    GeneTreeiENSGT00620000087734.
    HOGENOMiHOG000231984.
    HOVERGENiHBG004492.
    InParanoidiP12815.
    OMAiFLWNIFQ.
    OrthoDBiEOG7RV9FM.
    PhylomeDBiP12815.
    TreeFamiTF314682.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view]
    PfamiPF00036. EF-hand_1. 1 hit.
    PF13405. EF-hand_6. 1 hit.
    [Graphical view]
    SMARTiSM00054. EFh. 5 hits.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P12815-1) [UniParc]FASTAAdd to Basket

    Also known as: ALG-2,5

    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.

    « Hide

    MAAYSYRPGP GGGPGPAAGA ALPDQSFLWN VFQRVDKDRS GVISDNELQQ    50
    ALSNGTWTPF NPVTVRSIIS MFDRENKAGV NFSEFTGVWK YITDWQNVFR 100
    TYDRDNSGMI DKNELKQALS GFGYRLSDQF HDILIRKFDR QGRGQIAFDD 150
    FIQGCIVLQR LTDIFRRYDT DQDGWIQVSY EQYLSMVFSI V 191
    Length:191
    Mass (Da):21,867
    Last modified:November 1, 1997 - v2
    Checksum:i2704E984BF7F6F40
    GO
    Isoform 2 (identifier: P12815-2) [UniParc]FASTAAdd to Basket

    Also known as: ALG-2,1

    The sequence of this isoform differs from the canonical sequence as follows:
         121-122: Missing.

    Show »
    Length:189
    Mass (Da):21,663
    Checksum:i725B3EF5FDA06A72
    GO

    Sequence cautioni

    The sequence CAA33064.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei121 – 1222Missing in isoform 2. CuratedVSP_047715

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49112 mRNA. Translation: AAB38108.1.
    AK008610 mRNA. Translation: BAB25775.1.
    AK028223 mRNA. Translation: BAC25823.1.
    AK150335 mRNA. Translation: BAE29477.1.
    BC040079 mRNA. Translation: AAH40079.1.
    X14938 mRNA. Translation: CAA33064.1. Different initiation.
    CCDSiCCDS26642.1. [P12815-1]
    RefSeqiNP_035181.1. NM_011051.3. [P12815-1]
    XP_006517219.1. XM_006517156.1. [P12815-2]
    UniGeneiMm.24254.

    Genome annotation databases

    EnsembliENSMUST00000022060; ENSMUSP00000022060; ENSMUSG00000021576. [P12815-1]
    GeneIDi18570.
    KEGGimmu:18570.
    UCSCiuc007rey.2. mouse. [P12815-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49112 mRNA. Translation: AAB38108.1 .
    AK008610 mRNA. Translation: BAB25775.1 .
    AK028223 mRNA. Translation: BAC25823.1 .
    AK150335 mRNA. Translation: BAE29477.1 .
    BC040079 mRNA. Translation: AAH40079.1 .
    X14938 mRNA. Translation: CAA33064.1 . Different initiation.
    CCDSi CCDS26642.1. [P12815-1 ]
    RefSeqi NP_035181.1. NM_011051.3. [P12815-1 ]
    XP_006517219.1. XM_006517156.1. [P12815-2 ]
    UniGenei Mm.24254.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HQV X-ray 2.30 A 1-191 [» ]
    ProteinModelPortali P12815.
    SMRi P12815. Positions 20-188.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202071. 3 interactions.
    IntActi P12815. 9 interactions.
    MINTi MINT-217398.

    PTM databases

    PhosphoSitei P12815.

    Proteomic databases

    MaxQBi P12815.
    PaxDbi P12815.
    PRIDEi P12815.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022060 ; ENSMUSP00000022060 ; ENSMUSG00000021576 . [P12815-1 ]
    GeneIDi 18570.
    KEGGi mmu:18570.
    UCSCi uc007rey.2. mouse. [P12815-1 ]

    Organism-specific databases

    CTDi 10016.
    MGIi MGI:109283. Pdcd6.

    Phylogenomic databases

    eggNOGi NOG249191.
    GeneTreei ENSGT00620000087734.
    HOGENOMi HOG000231984.
    HOVERGENi HBG004492.
    InParanoidi P12815.
    OMAi FLWNIFQ.
    OrthoDBi EOG7RV9FM.
    PhylomeDBi P12815.
    TreeFami TF314682.

    Miscellaneous databases

    EvolutionaryTracei P12815.
    NextBioi 294404.
    PROi P12815.
    SOURCEi Search...

    Gene expression databases

    Bgeei P12815.
    CleanExi MM_PDCD6.
    Genevestigatori P12815.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view ]
    Pfami PF00036. EF-hand_1. 1 hit.
    PF13405. EF-hand_6. 1 hit.
    [Graphical view ]
    SMARTi SM00054. EFh. 5 hits.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Interfering with apoptosis: Ca(2+)-binding protein ALG-2 and Alzheimer's disease gene ALG-3."
      Vito P., Lacana E., D'Adamio L.
      Science 271:521-525(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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.
      , 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] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Bone marrow and Small intestine.
    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] (ISOFORM 1).
      Strain: FVB/N.
      Tissue: Mammary gland.
    4. "A partial cDNA for a novel protein which has a typical E-F hand structure."
      Kageyama H., Shimizu M., Hiwasa T., Sakiyama S.
      Biochim. Biophys. Acta 1008:255-257(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 44-181.
      Strain: BALB/c.
      Tissue: Fibroblast.
    5. "Alix, a novel mouse protein undergoing calcium-dependent interaction with the apoptotsis-linked-gene 2 (ALG-2) protein."
      Missotten M., Nichols A., Rieger K., Sadoul R.
      Cell Death Differ. 6:124-129(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SELF-ASSOCIATION, INTERACTION WITH PDCD6IP.
    6. "Two forms of the apoptosis-linked protein ALG-2 with different Ca(2+) affinities and target recognition."
      Tarabykina S., Moller A.L., Durussel I., Cox J., Berchtold M.W.
      J. Biol. Chem. 275:10514-10518(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION, SELF-ASSOCIATION, INTERACTION WITH PDCD6IP.
    7. "The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane."
      Draeby I., Woods Y.L., la Cour J.M., Mollerup J., Bourdon J.C., Berchtold M.W.
      Arch. Biochem. Biophys. 467:87-94(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH WITH SHISA5.
    8. "Structure of apoptosis-linked protein ALG-2: insights into Ca2+-induced changes in penta-EF-hand proteins."
      Jia J., Tarabykina S., Hansen C., Berchtold M., Cygler M.
      Structure 9:267-275(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CALCIUM, SUBUNIT, INTERACTION WITH PDCD6IP.

    Entry informationi

    Entry nameiPDCD6_MOUSE
    AccessioniPrimary (citable) accession number: P12815
    Secondary accession number(s): Q545I0, Q61145
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3