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P27482

- CALL3_HUMAN

UniProt

P27482 - CALL3_HUMAN

Protein

Calmodulin-like protein 3

Gene

CALML3

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

    May function as a specific light chain of unconventional myosin-10 (MYO10), also enhances MYO10 translation, possibly by acting as a chaperone for the emerging MYO10 heavy chain protein. May compete with calmodulin by binding, with different affinities, to cellular substrates.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi21 – 32121Add
    BLAST
    Calcium bindingi57 – 68122Add
    BLAST
    Calcium bindingi94 – 105123Add
    BLAST
    Calcium bindingi130 – 141124Add
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: ProtInc
    2. protein binding Source: IntAct

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calmodulin-like protein 3
    Alternative name(s):
    CaM-like protein
    Short name:
    CLP
    Calmodulin-related protein NB-1
    Gene namesi
    Name:CALML3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Organism-specific databases

    HGNCiHGNC:1452. CALML3.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26044.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 149149Calmodulin-like protein 3PRO_0000073547Add
    BLAST

    Proteomic databases

    MaxQBiP27482.
    PaxDbiP27482.
    PeptideAtlasiP27482.
    PRIDEiP27482.

    PTM databases

    PhosphoSiteiP27482.

    Expressioni

    Tissue specificityi

    Expressed in normal mammary, prostate, cervical, and epidermal tissues. It is greatly reduced or undetectable in transformed cells.1 Publication

    Inductioni

    By TGFB1.1 Publication

    Gene expression databases

    BgeeiP27482.
    CleanExiHS_CALML3.
    GenevestigatoriP27482.

    Organism-specific databases

    HPAiCAB010070.
    HPA044999.

    Interactioni

    Subunit structurei

    Interacts with MYO10, the interaction is calcium-dependent and essential for MYO10 function in filopodial extension.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MYO10Q9HD672EBI-747537,EBI-307061

    Protein-protein interaction databases

    BioGridi107261. 10 interactions.
    IntActiP27482. 8 interactions.
    MINTiMINT-1440064.
    STRINGi9606.ENSP00000315299.

    Structurei

    Secondary structure

    1
    149
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 2014
    Beta strandi25 – 284
    Helixi30 – 3910
    Helixi46 – 549
    Beta strandi61 – 655
    Helixi66 – 9328
    Beta strandi98 – 1014
    Helixi103 – 11210
    Helixi119 – 12911
    Beta strandi133 – 1386
    Helixi139 – 1479

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GGZX-ray1.50A2-149[»]
    ProteinModelPortaliP27482.
    SMRiP27482. Positions 5-148.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27482.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 4336EF-hand 1PROSITE-ProRule annotationsAdd
    BLAST
    Domaini44 – 7936EF-hand 2PROSITE-ProRule annotationsAdd
    BLAST
    Domaini81 – 11636EF-hand 3PROSITE-ProRule annotationsAdd
    BLAST
    Domaini117 – 14933EF-hand 4PROSITE-ProRule annotationsAdd
    BLAST

    Sequence similaritiesi

    Belongs to the calmodulin family.Curated
    Contains 4 EF-hand domains.PROSITE-ProRule annotations

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5126.
    HOGENOMiHOG000233018.
    HOVERGENiHBG012180.
    InParanoidiP27482.
    KOiK02183.
    OMAiCITTQEL.
    OrthoDBiEOG7F7WBV.
    PhylomeDBiP27482.
    TreeFamiTF300912.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view]
    PfamiPF00036. EF-hand_1. 3 hits.
    PF13405. EF-hand_6. 1 hit.
    [Graphical view]
    SMARTiSM00054. EFh. 4 hits.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 4 hits.
    PS50222. EF_HAND_2. 4 hits.
    [Graphical view]
    ProtoNetiSearch...

    Sequencei

    Sequence statusi: Complete.

    P27482-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADQLTEEQV TEFKEAFSLF DKDGDGCITT RELGTVMRSL GQNPTEAELR    50
    DMMSEIDRDG NGTVDFPEFL GMMARKMKDT DNEEEIREAF RVFDKDGNGF 100
    VSAAELRHVM TRLGEKLSDE EVDEMIRAAD TDGDGQVNYE EFVRVLVSK 149
    Length:149
    Mass (Da):16,891
    Last modified:January 23, 2007 - v2
    Checksum:i1AB883E8ED4D263D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58026 mRNA. Translation: AAA36356.1.
    X13461 Genomic DNA. Translation: CAA31809.1.
    AL732437 Genomic DNA. Translation: CAI11029.1.
    AK313934 mRNA. Translation: BAG36653.1.
    CH471072 Genomic DNA. Translation: EAW86443.1.
    BC031889 mRNA. Translation: AAH31889.1.
    CCDSiCCDS7069.1.
    PIRiA38278. MCHUNB.
    RefSeqiNP_005176.1. NM_005185.3.
    UniGeneiHs.239600.

    Genome annotation databases

    EnsembliENST00000315238; ENSP00000315299; ENSG00000178363.
    GeneIDi810.
    KEGGihsa:810.
    UCSCiuc001iie.1. human.

    Polymorphism databases

    DMDMi115502.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58026 mRNA. Translation: AAA36356.1 .
    X13461 Genomic DNA. Translation: CAA31809.1 .
    AL732437 Genomic DNA. Translation: CAI11029.1 .
    AK313934 mRNA. Translation: BAG36653.1 .
    CH471072 Genomic DNA. Translation: EAW86443.1 .
    BC031889 mRNA. Translation: AAH31889.1 .
    CCDSi CCDS7069.1.
    PIRi A38278. MCHUNB.
    RefSeqi NP_005176.1. NM_005185.3.
    UniGenei Hs.239600.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GGZ X-ray 1.50 A 2-149 [» ]
    ProteinModelPortali P27482.
    SMRi P27482. Positions 5-148.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107261. 10 interactions.
    IntActi P27482. 8 interactions.
    MINTi MINT-1440064.
    STRINGi 9606.ENSP00000315299.

    PTM databases

    PhosphoSitei P27482.

    Polymorphism databases

    DMDMi 115502.

    Proteomic databases

    MaxQBi P27482.
    PaxDbi P27482.
    PeptideAtlasi P27482.
    PRIDEi P27482.

    Protocols and materials databases

    DNASUi 810.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315238 ; ENSP00000315299 ; ENSG00000178363 .
    GeneIDi 810.
    KEGGi hsa:810.
    UCSCi uc001iie.1. human.

    Organism-specific databases

    CTDi 810.
    GeneCardsi GC10P005556.
    HGNCi HGNC:1452. CALML3.
    HPAi CAB010070.
    HPA044999.
    MIMi 114184. gene.
    neXtProti NX_P27482.
    PharmGKBi PA26044.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5126.
    HOGENOMi HOG000233018.
    HOVERGENi HBG012180.
    InParanoidi P27482.
    KOi K02183.
    OMAi CITTQEL.
    OrthoDBi EOG7F7WBV.
    PhylomeDBi P27482.
    TreeFami TF300912.

    Miscellaneous databases

    ChiTaRSi CALML3. human.
    EvolutionaryTracei P27482.
    GeneWikii CALML3.
    GenomeRNAii 810.
    NextBioi 3288.
    PROi P27482.
    SOURCEi Search...

    Gene expression databases

    Bgeei P27482.
    CleanExi HS_CALML3.
    Genevestigatori P27482.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view ]
    Pfami PF00036. EF-hand_1. 3 hits.
    PF13405. EF-hand_6. 1 hit.
    [Graphical view ]
    SMARTi SM00054. EFh. 4 hits.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 4 hits.
    PS50222. EF_HAND_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Down-regulation of a calmodulin-related gene during transformation of human mammary epithelial cells."
      Yaswen P., Smoll A., Peehl D.M., Trask D.K., Sager R., Stampfer M.R.
      Proc. Natl. Acad. Sci. U.S.A. 87:7360-7364(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY TGFB1.
    2. "Characterization of an intronless human calmodulin-like pseudogene."
      Koller M., Strehler E.E.
      FEBS Lett. 239:121-128(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Koller M.
      Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. "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: Esophagus.
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Skin.
    8. "Characterization of the human calmodulin-like protein expressed in Escherichia coli."
      Rhyner J.A., Koller M., Durussel-Gerber I., Cox J.A., Strehler E.E.
      Biochemistry 31:12826-12832(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. "The tumor-sensitive calmodulin-like protein is a specific light chain of human unconventional myosin X."
      Rogers M.S., Strehler E.E.
      J. Biol. Chem. 276:12182-12189(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MYO10.
    10. "Calmodulin-like protein enhances myosin-10 translation."
      Bennett R.D., Strehler E.E.
      Biochem. Biophys. Res. Commun. 369:654-659(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Crystal structure of human calmodulin-like protein: insights into its functional role."
      Han B.G., Han M., Sui H., Yaswen P., Walian P.J., Jap B.K.
      FEBS Lett. 521:24-30(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).

    Entry informationi

    Entry nameiCALL3_HUMAN
    AccessioniPrimary (citable) accession number: P27482
    Secondary accession number(s): B2R9V6, Q5SQI4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 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

    Miscellaneous

    Binds four calcium ions.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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