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Q7TSN7 (IGSF5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Immunoglobulin superfamily member 5

Short name=IgSF5
Alternative name(s):
Junctional adhesion molecule 4
Short name=JAM-4
Gene names
Name:Igsf5
Synonyms:Jam4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.4

Subunit structure

Interacts with MAGI1 at tight junctions, forms a tripartite complex with NPHS1 By similarity. Interacts with LNX1 isoform 2via its PDZ 2 domain, it may also interact with other isoforms containing this domain. Ref.1 Ref.5

Subcellular location

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

Tissue specificity

Localized to kidney glomeruli and small intestinal epithelial cells. Also found in spermatogonia, gonocytes, hematopoietic stem cells and Sertoli cells. Ref.1 Ref.4

Post-translational modification

N-glycosylated. Ref.1

Disruption phenotype

No visible phenotype. Ref.4

Sequence similarities

Belongs to the immunoglobulin superfamily.

Contains 2 Ig-like V-type (immunoglobulin-like) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 370346Immunoglobulin superfamily member 5
PRO_0000316296

Regions

Topological domain25 – 239215Extracellular Potential
Transmembrane240 – 26021Helical; Potential
Topological domain261 – 370110Cytoplasmic Potential
Domain25 – 125101Ig-like V-type 1
Domain128 – 21588Ig-like V-type 2
Compositional bias262 – 2654Poly-Cys

Amino acid modifications

Glycosylation331N-linked (GlcNAc...) Potential
Glycosylation451N-linked (GlcNAc...) Potential
Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation2171N-linked (GlcNAc...) Potential
Disulfide bond46 ↔ 109 By similarity
Disulfide bond149 ↔ 201 By similarity

Experimental info

Sequence conflict126 – 225100Missing in BAB25436. Ref.2
Sequence conflict126 – 225100Missing in AAH04806. Ref.2
Sequence conflict2991G → S in BAB25436. Ref.2
Sequence conflict2991G → S in AAH04806. Ref.2

Secondary structure

.. 370
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7TSN7 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 001B40AC535C96EF

FASTA37040,292
        10         20         30         40         50         60 
MEGSWRDVLA VLVILAQLTA SGSSYQIIEG PQNVTVLKDS EAHFNCTVTH GWKLLMWTLN 

        70         80         90        100        110        120 
QMVVLSLTTQ GPIITNNRFT YASYNSTDSF ISELIIHDVQ PSDSGSVQCS LQNSHGFGSA 

       130        140        150        160        170        180 
FLSVQVMGTL NIPSNNLIVT EGEPCNVTCY AVGWTSLPDI SWELEVPVSH SSYNSFLESG 

       190        200        210        220        230        240 
NFMRVLSVLD LTPLGNGTLT CVAELKDLQA SKSLTVNLTV VQPPPDSIGE EGPALPTWAI 

       250        260        270        280        290        300 
ILLAVAFSLL LILIIVLIII FCCCCASRRE KEESTYQNEI RKSANMRTNK ADPETKLKGG 

       310        320        330        340        350        360 
KENYGYSSDE AKAAQTASLP PKSAEVSLPE KRSSSLPYQE LNKHQPGPAT HPRVSFDIAS 

       370 
PQKVRNVTLV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF537215 mRNA. Translation: AAP49218.1.
AK008060 mRNA. Translation: BAB25436.1.
BC004806 mRNA. Translation: AAH04806.1.
CCDSCCDS49924.1.
RefSeqNP_082354.1. NM_028078.3.
UniGeneMm.119714.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3VQGX-ray1.35B363-370[»]
ProteinModelPortalQ7TSN7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid215124. 3 interactions.

PTM databases

PhosphoSiteQ7TSN7.

Proteomic databases

PaxDbQ7TSN7.
PRIDEQ7TSN7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000081093; ENSMUSP00000079874; ENSMUSG00000000159.
GeneID72058.
KEGGmmu:72058.

Organism-specific databases

CTD150084.
MGIMGI:1919308. Igsf5.

Phylogenomic databases

eggNOGNOG47258.
GeneTreeENSGT00390000018711.
HOGENOMHOG000113018.
HOVERGENHBG059033.
KOK06786.

Gene expression databases

ArrayExpressQ7TSN7.
BgeeQ7TSN7.
CleanExMM_IGSF5.
GenevestigatorQ7TSN7.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
[Graphical view]
PfamPF07679. I-set. 1 hit.
[Graphical view]
SMARTSM00409. IG. 2 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIGSF5. mouse.
NextBio335340.
PROQ7TSN7.
SOURCESearch...

Entry information

Entry nameIGSF5_MOUSE
AccessionPrimary (citable) accession number: Q7TSN7
Secondary accession number(s): Q9D8G2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 1, 2003
Last modified: July 9, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot