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Protein

Junctional adhesion molecule A

Gene

F11r

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3. The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly. Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier. Involved in platelet activation. In case of orthoreovirus infection, serves as receptor for the virus (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • actomyosin structure organization Source: MGI
  • cell adhesion Source: MGI
  • epithelial cell differentiation Source: MGI
  • establishment of endothelial intestinal barrier Source: MGI
  • establishment of protein localization to plasma membrane Source: MGI
  • intestinal absorption Source: UniProtKB
  • negative regulation of GTPase activity Source: MGI
  • positive regulation of blood pressure Source: Ensembl
  • positive regulation of GTPase activity Source: MGI
  • regulation of actin cytoskeleton reorganization Source: MGI
  • regulation of cytokine production Source: CACAO
  • regulation of membrane permeability Source: UniProtKB
  • response to radiation Source: Ensembl
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiR-MMU-202733. Cell surface interactions at the vascular wall.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-MMU-420029. Tight junction interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Junctional adhesion molecule A
Short name:
JAM-A
Alternative name(s):
Junctional adhesion molecule 1
Short name:
JAM-1
CD_antigen: CD321
Gene namesi
Name:F11r
Synonyms:Jam1, Jcam, Jcam1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1321398. F11r.

Subcellular locationi

  • Cell junctiontight junction 1 Publication
  • Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

  • Note: Localized at tight junctions of both epithelial and endothelial cells.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 238212ExtracellularSequence analysisAdd
BLAST
Transmembranei239 – 25921HelicalSequence analysisAdd
BLAST
Topological domaini260 – 29940CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 300274Junctional adhesion molecule APRO_0000015067Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421N-linked (GlcNAc...)1 Publication
Disulfide bondi49 ↔ 108Combined sources1 Publication
Disulfide bondi152 ↔ 212Combined sources1 Publication
Glycosylationi185 – 1851N-linked (GlcNAc...)2 Publications
Modified residuei282 – 2821PhosphoserineBy similarity
Modified residuei285 – 2851PhosphoserineCombined sources
Modified residuei288 – 2881PhosphoserineCombined sources

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO88792.
PeptideAtlasiO88792.
PRIDEiO88792.

PTM databases

iPTMnetiO88792.
PhosphoSiteiO88792.

Expressioni

Gene expression databases

CleanExiMM_F11R.
GenevisibleiO88792. MM.

Interactioni

Subunit structurei

Interacts with the ninth PDZ domain of MPDZ. Interacts with the first PDZ domain of PARD3. The association between PARD3 and PARD6B probably disrupts this interaction. Interacts with the orthoreovirus sigma-1 capsid protein (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200861. 2 interactions.
DIPiDIP-41166N.
IntActiO88792. 2 interactions.
MINTiMINT-247376.
STRINGi10090.ENSMUSP00000041907.

Structurei

Secondary structure

1
300
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 313Combined sources
Beta strandi35 – 406Combined sources
Beta strandi45 – 484Combined sources
Beta strandi50 – 534Combined sources
Beta strandi55 – 6511Combined sources
Beta strandi68 – 747Combined sources
Helixi80 – 823Combined sources
Turni83 – 853Combined sources
Beta strandi86 – 894Combined sources
Beta strandi92 – 965Combined sources
Helixi100 – 1023Combined sources
Beta strandi104 – 1129Combined sources
Beta strandi115 – 12915Combined sources
Beta strandi135 – 1373Combined sources
Beta strandi140 – 1434Combined sources
Beta strandi148 – 1536Combined sources
Beta strandi162 – 1676Combined sources
Beta strandi170 – 1734Combined sources
Beta strandi184 – 1863Combined sources
Beta strandi188 – 1903Combined sources
Turni192 – 1943Combined sources
Beta strandi197 – 2015Combined sources
Helixi204 – 2063Combined sources
Beta strandi208 – 2158Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi227 – 2348Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F97X-ray2.50A27-238[»]
ProteinModelPortaliO88792.
SMRiO88792. Positions 27-238.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88792.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 12295Ig-like V-type 1Add
BLAST
Domaini134 – 23097Ig-like V-type 2Add
BLAST

Sequence similaritiesi

Belongs to the immunoglobulin superfamily.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IWUE. Eukaryota.
ENOG410YHHV. LUCA.
GeneTreeiENSGT00730000110678.
HOGENOMiHOG000247041.
HOVERGENiHBG000518.
InParanoidiO88792.
KOiK06089.
OMAiSCSYSGF.
OrthoDBiEOG7MH0Z1.
TreeFamiTF331459.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
SM00406. IGv. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O88792-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTEGKAGRK LLFLFTSMIL GSLVQGKGSV YTAQSDVQVP ENESIKLTCT
60 70 80 90 100
YSGFSSPRVE WKFVQGSTTA LVCYNSQITA PYADRVTFSS SGITFSSVTR
110 120 130 140 150
KDNGEYTCMV SEEGGQNYGE VSIHLTVLVP PSKPTISVPS SVTIGNRAVL
160 170 180 190 200
TCSEHDGSPP SEYSWFKDGI SMLTADAKKT RAFMNSSFTI DPKSGDLIFD
210 220 230 240 250
PVTAFDSGEY YCQAQNGYGT AMRSEAAHMD AVELNVGGIV AAVLVTLILL
260 270 280 290 300
GLLIFGVWFA YSRGYFERTK KGTAPGKKVI YSQPSTRSEG EFKQTSSFLV
Length:300
Mass (Da):32,424
Last modified:October 3, 2012 - v2
Checksum:i3CE561E8FF3B97EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti268 – 2681R → T in AAC32982 (PubMed:9660867).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89915 mRNA. Translation: AAC32982.1.
AK033574 mRNA. Translation: BAC28369.1.
CT010347 mRNA. Translation: CAJ18555.1.
AC087229 Genomic DNA. No translation available.
BC021876 mRNA. Translation: AAH21876.1.
CCDSiCCDS15496.1.
RefSeqiNP_766235.1. NM_172647.2.
UniGeneiMm.294882.

Genome annotation databases

EnsembliENSMUST00000043839; ENSMUSP00000041907; ENSMUSG00000038235.
GeneIDi16456.
KEGGimmu:16456.
UCSCiuc007doo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89915 mRNA. Translation: AAC32982.1.
AK033574 mRNA. Translation: BAC28369.1.
CT010347 mRNA. Translation: CAJ18555.1.
AC087229 Genomic DNA. No translation available.
BC021876 mRNA. Translation: AAH21876.1.
CCDSiCCDS15496.1.
RefSeqiNP_766235.1. NM_172647.2.
UniGeneiMm.294882.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F97X-ray2.50A27-238[»]
ProteinModelPortaliO88792.
SMRiO88792. Positions 27-238.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200861. 2 interactions.
DIPiDIP-41166N.
IntActiO88792. 2 interactions.
MINTiMINT-247376.
STRINGi10090.ENSMUSP00000041907.

PTM databases

iPTMnetiO88792.
PhosphoSiteiO88792.

Proteomic databases

PaxDbiO88792.
PeptideAtlasiO88792.
PRIDEiO88792.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043839; ENSMUSP00000041907; ENSMUSG00000038235.
GeneIDi16456.
KEGGimmu:16456.
UCSCiuc007doo.1. mouse.

Organism-specific databases

CTDi50848.
MGIiMGI:1321398. F11r.

Phylogenomic databases

eggNOGiENOG410IWUE. Eukaryota.
ENOG410YHHV. LUCA.
GeneTreeiENSGT00730000110678.
HOGENOMiHOG000247041.
HOVERGENiHBG000518.
InParanoidiO88792.
KOiK06089.
OMAiSCSYSGF.
OrthoDBiEOG7MH0Z1.
TreeFamiTF331459.

Enzyme and pathway databases

ReactomeiR-MMU-202733. Cell surface interactions at the vascular wall.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-MMU-420029. Tight junction interactions.

Miscellaneous databases

ChiTaRSiF11r. mouse.
EvolutionaryTraceiO88792.
PROiO88792.
SOURCEiSearch...

Gene expression databases

CleanExiMM_F11R.
GenevisibleiO88792. MM.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
SM00406. IGv. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Junctional adhesion molecule, a novel member of the immunoglobulin superfamily that distributes at intercellular junctions and modulates monocyte transmigration."
    Martin-Padura I., Lostaglio S., Schneemann M., Williams L., Romano M., Fruscella P., Panzeri C., Stoppacciaro A., Ruco L., Villa A., Simmons D., Dejana E.
    J. Cell Biol. 142:117-127(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Cecum.
  3. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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.
  6. "Cloning of JAM-2 and JAM-3: an emerging junctional adhesion molecular family?"
    Aurrand-Lions M.A., Duncan L., Du Pasquier L., Imhof B.A.
    Curr. Top. Microbiol. Immunol. 251:91-98(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM)."
    Ebnet K., Suzuki A., Horikoshi Y., Hirose T., Meyer zu Brickwedde M.-K., Ohno S., Vestweber D.
    EMBO J. 20:3738-3748(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PARD3.
  8. "Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response."
    Muller W.A.
    Trends Immunol. 24:327-334(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, NOMENCLATURE.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185.
    Tissue: Myoblast.
  11. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-42 AND ASN-185.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas and Testis.
  13. "X-ray structure of junctional adhesion molecule: structural basis for homophilic adhesion via a novel dimerization motif."
    Kostrewa D., Brockhaus M., D'Arcy A., Dale G.E., Nelboeck P., Schmid G., Mueller F., Bazzoni G., Dejana E., Bartfai T., Winkler F.K., Hennig M.
    EMBO J. 20:4391-4398(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 27-238, DISULFIDE BONDS.

Entry informationi

Entry nameiJAM1_MOUSE
AccessioniPrimary (citable) accession number: O88792
Secondary accession number(s): Q8VC39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 3, 2012
Last modified: July 6, 2016
This is version 140 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.