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Q8C2S7

- AMGO3_MOUSE

UniProt

Q8C2S7 - AMGO3_MOUSE

Protein

Amphoterin-induced protein 3

Gene

Amigo3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    May mediate heterophilic cell-cell interaction. May contribute to signal transduction through its intracellular domain By similarity.By similarity

    GO - Biological processi

    1. cell adhesion Source: MGI
    2. heterophilic cell-cell adhesion Source: UniProtKB

    Keywords - Biological processi

    Cell adhesion

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Amphoterin-induced protein 3
    Alternative name(s):
    AMIGO-3
    Alivin-3
    Gene namesi
    Name:Amigo3Imported
    Synonyms:Ali3Imported, Kiaa1851Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:2444854. Amigo3.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: MGI

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 508489Amphoterin-induced protein 3Sequence AnalysisPRO_0000014514Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi34 ↔ 40PROSITE-ProRule annotation
    Disulfide bondi38 ↔ 47PROSITE-ProRule annotation
    Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi223 ↔ 251PROSITE-ProRule annotation
    Disulfide bondi225 ↔ 273PROSITE-ProRule annotation
    Glycosylationi272 – 2721N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi300 ↔ 352PROSITE-ProRule annotation
    Glycosylationi301 – 3011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ8C2S7.

    PTM databases

    PhosphoSiteiQ8C2S7.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    BgeeiQ8C2S7.
    CleanExiMM_AMIGO3.
    GenevestigatoriQ8C2S7.

    Interactioni

    Subunit structurei

    Binds AMIGO1 or AMIGO2.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000082137.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C2S7.
    SMRiQ8C2S7. Positions 33-369.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 383364ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini405 – 508104CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei384 – 40421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 6137LRRNTAdd
    BLAST
    Repeati62 – 8322LRR 1Add
    BLAST
    Repeati86 – 10722LRR 2Add
    BLAST
    Repeati110 – 13324LRR 3Add
    BLAST
    Repeati134 – 15522LRR 4Add
    BLAST
    Repeati158 – 17821LRR 5Add
    BLAST
    Repeati184 – 20724LRR 6Add
    BLAST
    Domaini219 – 27557LRRCTAdd
    BLAST
    Domaini279 – 37092Ig-like C2-typeSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 6 LRR (leucine-rich) repeats.Sequence Analysis
    Contains 1 LRRCT domain.Curated
    Contains 1 LRRNT domain.Curated

    Keywords - Domaini

    Immunoglobulin domain, Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG146733.
    GeneTreeiENSGT00530000063545.
    HOGENOMiHOG000231327.
    HOVERGENiHBG080231.
    InParanoidiQ8C2S7.
    OMAiVCLATGP.
    OrthoDBiEOG7C8GHP.
    PhylomeDBiQ8C2S7.
    TreeFamiTF326838.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    [Graphical view]
    PfamiPF00560. LRR_1. 1 hit.
    PF13855. LRR_8. 1 hit.
    [Graphical view]
    SMARTiSM00409. IG. 1 hit.
    SM00369. LRR_TYP. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 1 hit.
    PS51450. LRR. 7 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8C2S7-1 [UniParc]FASTAAdd to Basket

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    MAWLVLSGIL LCMLGAGLGT SDLEDVLPPA PHNCPDICIC AADVLSCAGR    50
    GLQDLPVALP TTAAELDLSH NALKRLHPGW LAPLSRLRAL HLGYNKLEVL 100
    GHGAFTNASG LRTLDLSSNM LRMLHTHDLD GLEELEKLLL FNNSLMHLDL 150
    DAFQGLRMLS HLYLSCNELS SFSFNHLHGL GLTRLRTLDL SSNWLKHISI 200
    PELAALPTYL KNRLYLHNNP LPCDCSLYHL LRRWHQRGLS ALHDFEREYT 250
    CLVFKVSESR VRFFEHSRVF KNCSVAAAPG LELPEEQLHA QVGQSLRLFC 300
    NTSVPATRVA WVSPKNELLV APASQDGSIA VLADGSLAIG RVQEQHAGVF 350
    VCLASGPRLH HNQTLEYNVS VQKARPEPET FNTGFTTLLG CIVGLVLVLL 400
    YLFAPPCRGC CHCCQRACRN RCWPRASSPL QELSAQSSML STTPPDAPSR 450
    KASVHKHVVF LEPGKKGLNG RVQLAVAEDF DLCNPMGLQL KAGSESASST 500
    GSEGLVMS 508
    Length:508
    Mass (Da):55,625
    Last modified:March 1, 2003 - v1
    Checksum:i31334E42F91810C5
    GO

    Sequence cautioni

    The sequence BAC26035.1 differs from that shown. Reason: Frameshift at position 224.
    The sequence BAC98266.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY237004 mRNA. Translation: AAO48945.1.
    AB167510 mRNA. Translation: BAD12542.1.
    AK028619 mRNA. Translation: BAC26035.1. Frameshift.
    AK088051 mRNA. Translation: BAC40120.1.
    AK129456 mRNA. Translation: BAC98266.1. Different initiation.
    CCDSiCCDS23516.1.
    RefSeqiNP_796249.1. NM_177275.4.
    UniGeneiMm.449806.

    Genome annotation databases

    EnsembliENSMUST00000085060; ENSMUSP00000082137; ENSMUSG00000032593.
    GeneIDi320844.
    KEGGimmu:320844.
    UCSCiuc009rom.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY237004 mRNA. Translation: AAO48945.1 .
    AB167510 mRNA. Translation: BAD12542.1 .
    AK028619 mRNA. Translation: BAC26035.1 . Frameshift.
    AK088051 mRNA. Translation: BAC40120.1 .
    AK129456 mRNA. Translation: BAC98266.1 . Different initiation.
    CCDSi CCDS23516.1.
    RefSeqi NP_796249.1. NM_177275.4.
    UniGenei Mm.449806.

    3D structure databases

    ProteinModelPortali Q8C2S7.
    SMRi Q8C2S7. Positions 33-369.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000082137.

    PTM databases

    PhosphoSitei Q8C2S7.

    Proteomic databases

    PRIDEi Q8C2S7.

    Protocols and materials databases

    DNASUi 320844.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000085060 ; ENSMUSP00000082137 ; ENSMUSG00000032593 .
    GeneIDi 320844.
    KEGGi mmu:320844.
    UCSCi uc009rom.1. mouse.

    Organism-specific databases

    CTDi 386724.
    MGIi MGI:2444854. Amigo3.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG146733.
    GeneTreei ENSGT00530000063545.
    HOGENOMi HOG000231327.
    HOVERGENi HBG080231.
    InParanoidi Q8C2S7.
    OMAi VCLATGP.
    OrthoDBi EOG7C8GHP.
    PhylomeDBi Q8C2S7.
    TreeFami TF326838.

    Miscellaneous databases

    NextBioi 397545.
    PROi Q8C2S7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8C2S7.
    CleanExi MM_AMIGO3.
    Genevestigatori Q8C2S7.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    [Graphical view ]
    Pfami PF00560. LRR_1. 1 hit.
    PF13855. LRR_8. 1 hit.
    [Graphical view ]
    SMARTi SM00409. IG. 1 hit.
    SM00369. LRR_TYP. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 1 hit.
    PS51450. LRR. 7 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "AMIGO, a transmembrane protein implicated in axon tract development, defines a novel protein family with leucine-rich repeats."
      Kuja-Panula J., Kiiltomaeki M., Yamashiro T., Rouhiainen A., Rauvala H.
      J. Cell Biol. 160:963-973(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, TISSUE SPECIFICITY.
      Strain: C57BL/6Imported.
      Tissue: Cerebellum1 Publication.
    2. Ono T.
      Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: BrainImported.
    3. "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].
      Strain: C57BL/6J and NOD.
      Tissue: Skin and Thymus.
    4. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
      DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryonic tailImported.

    Entry informationi

    Entry nameiAMGO3_MOUSE
    AccessioniPrimary (citable) accession number: Q8C2S7
    Secondary accession number(s): Q6ZPH1, Q8CEB3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2005
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 105 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