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P63277

- AMELX_MOUSE

UniProt

P63277 - AMELX_MOUSE

Protein

Amelogenin, X isoform

Gene

Amelx

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      Previous versions | rss
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    Functioni

    Plays a role in the biomineralization of teeth. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel.

    GO - Molecular functioni

    1. growth factor activity Source: BHF-UCL
    2. hydroxyapatite binding Source: BHF-UCL
    3. identical protein binding Source: BHF-UCL
    4. protein binding Source: BHF-UCL

    GO - Biological processi

    1. cell adhesion Source: BHF-UCL
    2. cell proliferation Source: BHF-UCL
    3. odontogenesis of dentin-containing tooth Source: BHF-UCL
    4. signal transduction Source: BHF-UCL
    5. tooth mineralization Source: BHF-UCL

    Keywords - Biological processi

    Biomineralization

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Amelogenin, X isoform
    Alternative name(s):
    Leucine-rich amelogenin peptide
    Short name:
    LRAP
    Gene namesi
    Name:Amelx
    Synonyms:Amel
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:88005. Amelx.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: MGI
    2. cell surface Source: BHF-UCL

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616By similarityAdd
    BLAST
    Chaini17 – 210194Amelogenin, X isoformPRO_0000001201Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321PhosphoserineBy similarity

    Post-translational modificationi

    Several forms are produced by C-terminal processing.

    Keywords - PTMi

    Phosphoprotein

    Expressioni

    Gene expression databases

    BgeeiP63277.
    CleanExiMM_AMELX.
    GenevestigatoriP63277.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-59703N.

    Structurei

    3D structure databases

    DisProtiDP00692.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the amelogenin family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG69988.
    GeneTreeiENSGT00390000009151.
    HOGENOMiHOG000231643.
    HOVERGENiHBG016835.

    Family and domain databases

    InterProiIPR004116. Amelogenin.
    [Graphical view]
    PfamiPF02948. Amelogenin. 1 hit.
    [Graphical view]
    PRINTSiPR01757. AMELOGENIN.
    SMARTiSM00818. Amelogenin. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 4 (identifier: P63277-4) [UniParc]FASTAAdd to Basket

    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

    MGTWILFACL LGAAFAMPLP PHPGSPGYIN LSYEKSHSQA INTDRTALVL    50
    TPLKWYQSMI RQPYPSYGYE PMGGWLHHQI IPVLSQQHPP SHTLQPHHHL 100
    PVVPAQQPVA PQQPMMPVPG HHSMTPTQHH QPNIPPSAQQ PFQQPFQPQA 150
    IPPQSHQPMQ PQSPLHPMQP LAPQPPLPPL FSMQPLSPIL PELPLEAWPA 200
    TDKTKREEVD 210
    Length:210
    Mass (Da):23,483
    Last modified:October 11, 2004 - v1
    Checksum:iEB6ED5D09AA83AFA
    GO
    Isoform 1 (identifier: P63277-1) [UniParc] [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         35-48: Missing.

    Show »
    Length:196
    Mass (Da):21,959
    Checksum:i8E9DE372A13669F4
    GO
    Isoform 2 (identifier: P63277-2) [UniParc] [UniParc]FASTAAdd to Basket

    Also known as: LRAP

    The sequence of this isoform differs from the canonical sequence as follows:
         35-48: Missing.
         64-184: Missing.

    Show »
    Length:75
    Mass (Da):8,406
    Checksum:i14D8D8D2CA9DD235
    GO
    Isoform 3 (identifier: P63277-3) [UniParc] [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         35-48: Missing.
         64-87: Missing.

    Show »
    Length:172
    Mass (Da):19,176
    Checksum:i0C571EDAFACC111C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti111 – 1111P → A in AAA37218. (PubMed:4015654)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei35 – 4814Missing in isoform 1, isoform 2 and isoform 3. 1 PublicationVSP_011688Add
    BLAST
    Alternative sequencei64 – 184121Missing in isoform 2. CuratedVSP_000230Add
    BLAST
    Alternative sequencei64 – 8724Missing in isoform 3. CuratedVSP_000231Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D31768 mRNA. Translation: BAA06546.1.
    D31769 mRNA. Translation: BAA06547.1.
    D83067 Genomic DNA. Translation: BAA23665.1.
    AK029358 mRNA. Translation: BAC26415.1.
    AL805974 Genomic DNA. Translation: CAM21303.1.
    AL805974 Genomic DNA. Translation: CAM21304.1.
    M10095 mRNA. Translation: AAA37218.1.
    CCDSiCCDS41214.1. [P63277-1]
    PIRiI49486.
    PC1148.
    RefSeqiNP_001075447.1. NM_001081978.2.
    NP_001277300.1. NM_001290371.1. [P63277-3]
    NP_033796.1. NM_009666.4. [P63277-1]
    XP_006528755.1. XM_006528692.1. [P63277-4]
    UniGeneiMm.391342.

    Genome annotation databases

    EnsembliENSMUST00000112118; ENSMUSP00000107746; ENSMUSG00000031354. [P63277-1]
    ENSMUST00000112119; ENSMUSP00000107747; ENSMUSG00000031354. [P63277-4]
    ENSMUST00000112120; ENSMUSP00000107748; ENSMUSG00000031354. [P63277-3]
    GeneIDi11704.
    KEGGimmu:11704.
    UCSCiuc009uxt.2. mouse. [P63277-3]
    uc009uxu.1. mouse. [P63277-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D31768 mRNA. Translation: BAA06546.1 .
    D31769 mRNA. Translation: BAA06547.1 .
    D83067 Genomic DNA. Translation: BAA23665.1 .
    AK029358 mRNA. Translation: BAC26415.1 .
    AL805974 Genomic DNA. Translation: CAM21303.1 .
    AL805974 Genomic DNA. Translation: CAM21304.1 .
    M10095 mRNA. Translation: AAA37218.1 .
    CCDSi CCDS41214.1. [P63277-1 ]
    PIRi I49486.
    PC1148.
    RefSeqi NP_001075447.1. NM_001081978.2.
    NP_001277300.1. NM_001290371.1. [P63277-3 ]
    NP_033796.1. NM_009666.4. [P63277-1 ]
    XP_006528755.1. XM_006528692.1. [P63277-4 ]
    UniGenei Mm.391342.

    3D structure databases

    DisProti DP00692.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59703N.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000112118 ; ENSMUSP00000107746 ; ENSMUSG00000031354 . [P63277-1 ]
    ENSMUST00000112119 ; ENSMUSP00000107747 ; ENSMUSG00000031354 . [P63277-4 ]
    ENSMUST00000112120 ; ENSMUSP00000107748 ; ENSMUSG00000031354 . [P63277-3 ]
    GeneIDi 11704.
    KEGGi mmu:11704.
    UCSCi uc009uxt.2. mouse. [P63277-3 ]
    uc009uxu.1. mouse. [P63277-4 ]

    Organism-specific databases

    CTDi 265.
    MGIi MGI:88005. Amelx.

    Phylogenomic databases

    eggNOGi NOG69988.
    GeneTreei ENSGT00390000009151.
    HOGENOMi HOG000231643.
    HOVERGENi HBG016835.

    Miscellaneous databases

    NextBioi 279383.
    PROi P63277.
    SOURCEi Search...

    Gene expression databases

    Bgeei P63277.
    CleanExi MM_AMELX.
    Genevestigatori P63277.

    Family and domain databases

    InterProi IPR004116. Amelogenin.
    [Graphical view ]
    Pfami PF02948. Amelogenin. 1 hit.
    [Graphical view ]
    PRINTSi PR01757. AMELOGENIN.
    SMARTi SM00818. Amelogenin. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Alternative splicing of the mouse amelogenin primary RNA transcript contributes to amelogenin heterogeneity."
      Lau E.C., Simmer J.P., Bringas P. Jr., Hsu D.D.J., Hu C.C., Zeichner-David M., Thiemann F., Snead M.L., Slavkin H.C., Fincham A.G.
      Biochem. Biophys. Res. Commun. 188:1253-1260(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2 AND 3).
      Strain: ICR.
    2. Oida S., Iimura T., Arai N., Takeda K., Maruoka Y., Terashima T., Shimokawa H., Sasaki S.
      Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 4.
    3. "Molecular structure of the mouse amelogenin genomic DNA."
      Oida S., Miyazaki H., Iimura T., Suzuki M., Sasaki M., Shimokawa H.
      DNA Seq. 6:307-310(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 4).
    4. "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: Head.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. "DNA sequence for cloned cDNA for murine amelogenin reveal the amino acid sequence for enamel-specific protein."
      Snead M.L., Lau E.C., Zeichner-David M., Fincham A.G., Woo S.L., Slavkin H.C.
      Biochem. Biophys. Res. Commun. 129:812-818(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 57-210.

    Entry informationi

    Entry nameiAMELX_MOUSE
    AccessioniPrimary (citable) accession number: P63277
    Secondary accession number(s): A2ALX2
    , A2ALX3, P45559, P70592, Q61293
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3