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Q7TSN7

- IGSF5_MOUSE

UniProt

Q7TSN7 - IGSF5_MOUSE

Protein

Immunoglobulin superfamily member 5

Gene

Igsf5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    Provides, together with MAGI1, an adhesion machinery at tight junctions, which may regulate the permeability of kidney glomerulus and small intestinal epithelial cells. Mediates calcium-independent homophilic cell adhesion. In testis, it may function as a cell adhesion molecule rather than a tight-junction protein. It may participate in the adhesion between spermatogonia-spermatogonia, spermatogonia-Sertoli cells, and Sertoli cells-Sertoli cells.2 Publications

    GO - Molecular functioni

    1. PDZ domain binding Source: MGI

    GO - Biological processi

    1. single organismal cell-cell adhesion Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Immunoglobulin superfamily member 5
    Short name:
    IgSF5
    Alternative name(s):
    Junctional adhesion molecule 4
    Short name:
    JAM-4
    Gene namesi
    Name:Igsf5
    Synonyms:Jam4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:1919308. Igsf5.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein. Cell junctiontight junction
    Note: In kidney glomeruli, it is localized at slit diaphragm.

    GO - Cellular componenti

    1. cell surface Source: MGI
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB-SubCell
    4. tight junction Source: MGI

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Tight junction

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 370346Immunoglobulin superfamily member 5PRO_0000316296Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi33 – 331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi45 – 451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi46 ↔ 109PROSITE-ProRule annotation
    Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi149 ↔ 201PROSITE-ProRule annotation
    Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ7TSN7.
    PRIDEiQ7TSN7.

    PTM databases

    PhosphoSiteiQ7TSN7.

    Expressioni

    Tissue specificityi

    Localized to kidney glomeruli and small intestinal epithelial cells. Also found in spermatogonia, gonocytes, hematopoietic stem cells and Sertoli cells.2 Publications

    Gene expression databases

    ArrayExpressiQ7TSN7.
    BgeeiQ7TSN7.
    CleanExiMM_IGSF5.
    GenevestigatoriQ7TSN7.

    Interactioni

    Subunit structurei

    Interacts with MAGI1 at tight junctions, forms a tripartite complex with NPHS1 By similarity. Interacts with LNX1 isoform 2 via its PDZ 2 domain, it may also interact with other isoforms containing this domain.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi215124. 3 interactions.

    Structurei

    Secondary structure

    1
    370
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi368 – 3703

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3VQGX-ray1.35B363-370[»]
    ProteinModelPortaliQ7TSN7.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 239215ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini261 – 370110CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei240 – 26021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 125101Ig-like V-type 1Add
    BLAST
    Domaini128 – 21588Ig-like V-type 2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi262 – 2654Poly-Cys

    Sequence similaritiesi

    Belongs to the immunoglobulin superfamily.Curated

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG47258.
    GeneTreeiENSGT00390000018711.
    HOGENOMiHOG000113018.
    HOVERGENiHBG059033.
    KOiK06786.

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    [Graphical view]
    PfamiPF07679. I-set. 1 hit.
    [Graphical view]
    SMARTiSM00409. IG. 2 hits.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q7TSN7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGSWRDVLA VLVILAQLTA SGSSYQIIEG PQNVTVLKDS EAHFNCTVTH    50
    GWKLLMWTLN QMVVLSLTTQ GPIITNNRFT YASYNSTDSF ISELIIHDVQ 100
    PSDSGSVQCS LQNSHGFGSA FLSVQVMGTL NIPSNNLIVT EGEPCNVTCY 150
    AVGWTSLPDI SWELEVPVSH SSYNSFLESG NFMRVLSVLD LTPLGNGTLT 200
    CVAELKDLQA SKSLTVNLTV VQPPPDSIGE EGPALPTWAI ILLAVAFSLL 250
    LILIIVLIII FCCCCASRRE KEESTYQNEI RKSANMRTNK ADPETKLKGG 300
    KENYGYSSDE AKAAQTASLP PKSAEVSLPE KRSSSLPYQE LNKHQPGPAT 350
    HPRVSFDIAS PQKVRNVTLV 370
    Length:370
    Mass (Da):40,292
    Last modified:October 1, 2003 - v1
    Checksum:i001B40AC535C96EF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti126 – 225100Missing in BAB25436. (PubMed:16141072)CuratedAdd
    BLAST
    Sequence conflicti126 – 225100Missing in AAH04806. (PubMed:16141072)CuratedAdd
    BLAST
    Sequence conflicti299 – 2991G → S in BAB25436. (PubMed:16141072)Curated
    Sequence conflicti299 – 2991G → S in AAH04806. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF537215 mRNA. Translation: AAP49218.1.
    AK008060 mRNA. Translation: BAB25436.1.
    BC004806 mRNA. Translation: AAH04806.1.
    CCDSiCCDS49924.1.
    RefSeqiNP_082354.1. NM_028078.3.
    UniGeneiMm.119714.

    Genome annotation databases

    EnsembliENSMUST00000081093; ENSMUSP00000079874; ENSMUSG00000000159.
    GeneIDi72058.
    KEGGimmu:72058.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF537215 mRNA. Translation: AAP49218.1 .
    AK008060 mRNA. Translation: BAB25436.1 .
    BC004806 mRNA. Translation: AAH04806.1 .
    CCDSi CCDS49924.1.
    RefSeqi NP_082354.1. NM_028078.3.
    UniGenei Mm.119714.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3VQG X-ray 1.35 B 363-370 [» ]
    ProteinModelPortali Q7TSN7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 215124. 3 interactions.

    PTM databases

    PhosphoSitei Q7TSN7.

    Proteomic databases

    PaxDbi Q7TSN7.
    PRIDEi Q7TSN7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000081093 ; ENSMUSP00000079874 ; ENSMUSG00000000159 .
    GeneIDi 72058.
    KEGGi mmu:72058.

    Organism-specific databases

    CTDi 150084.
    MGIi MGI:1919308. Igsf5.

    Phylogenomic databases

    eggNOGi NOG47258.
    GeneTreei ENSGT00390000018711.
    HOGENOMi HOG000113018.
    HOVERGENi HBG059033.
    KOi K06786.

    Miscellaneous databases

    ChiTaRSi IGSF5. mouse.
    NextBioi 335340.
    PROi Q7TSN7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7TSN7.
    Bgeei Q7TSN7.
    CleanExi MM_IGSF5.
    Genevestigatori Q7TSN7.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    [Graphical view ]
    Pfami PF07679. I-set. 1 hit.
    [Graphical view ]
    SMARTi SM00409. IG. 2 hits.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "JAM4, a junctional cell adhesion molecule interacting with a tight junction protein, MAGI-1."
      Hirabayashi S., Tajima M., Yao I., Nishimura W., Mori H., Hata Y.
      Mol. Cell. Biol. 23:4267-4282(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MAGI1, TISSUE SPECIFICITY, GLYCOSYLATION.
      Strain: Swiss Webster.
    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].
      Strain: C57BL/6J.
      Tissue: 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].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    4. "A CTX family cell adhesion molecule, JAM4, is expressed in stem cell and progenitor cell populations of both male germ cell and hematopoietic cell lineages."
      Nagamatsu G., Ohmura M., Mizukami T., Hamaguchi I., Hirabayashi S., Yoshida S., Hata Y., Suda T., Ohbo K.
      Mol. Cell. Biol. 26:8498-8506(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    5. "Ligand-of-Numb protein X is an endocytic scaffold for junctional adhesion molecule 4."
      Kansaku A., Hirabayashi S., Mori H., Fujiwara N., Kawata A., Ikeda M., Rokukawa C., Kurihara H., Hata Y.
      Oncogene 25:5071-5084(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LNX1 ISOFORM 2.

    Entry informationi

    Entry nameiIGSF5_MOUSE
    AccessioniPrimary (citable) accession number: Q7TSN7
    Secondary accession number(s): Q9D8G2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 93 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

    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