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Protein

Junctional adhesion molecule-like

Gene

Jaml

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

Functioni

Transmembrane protein of the plasma membrane of leukocytes that control their migration and activation through interaction with CXADR, a plasma membrane receptor found on adjacent epithelial and endothelial cells. The interaction between both receptors mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair. It also controls the transmigration of leukocytes within epithelial and endothelial tissues through adhesive interactions with epithelial and endothelial CXADR.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Immunity

Enzyme and pathway databases

ReactomeiR-MMU-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-MMU-202733. Cell surface interactions at the vascular wall.

Names & Taxonomyi

Protein namesi
Recommended name:
Junctional adhesion molecule-likeBy similarity
Alternative name(s):
Dendritic cell-specific protein CREA7
Short name:
mCrea7
Gene namesi
Name:JamlBy similarity
Synonyms:Amica1, Gm638
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:2685484. Amica1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 281261ExtracellularSequence analysisAdd
BLAST
Transmembranei282 – 30221HelicalSequence analysisAdd
BLAST
Topological domaini303 – 37977CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • bicellular tight junction Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 591D → A, K or N: Loss of interaction with CXADR. 1 Publication
Mutagenesisi72 – 721Y → A: Loss of interaction with CXADR. 1 Publication
Mutagenesisi75 – 751F → A or W: Loss of interaction with CXADR. 1 Publication
Mutagenesisi77 – 771Y → A or F: Loss of interaction with CXADR. 1 Publication
Mutagenesisi122 – 1221R → A: Loss of interaction with CXADR. 1 Publication
Mutagenesisi334 – 3341Y → F: No effect on interaction with PI3 kinase. 1 Publication
Mutagenesisi355 – 3551Y → F: Loss of interaction with PI3 kinase. 1 Publication
Mutagenesisi360 – 3667PVWPSSP → AVWASSA: Loss of interaction with PI3 kinase. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 379359Junctional adhesion molecule-likePRO_0000015075Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi45 ↔ 119PROSITE-ProRule annotation1 Publication
Glycosylationi79 – 791N-linked (GlcNAc...)1 Publication
Glycosylationi89 – 891N-linked (GlcNAc...)1 Publication
Glycosylationi125 – 1251N-linked (GlcNAc...)1 Publication
Disulfide bondi158 ↔ 236PROSITE-ProRule annotation1 Publication
Modified residuei355 – 3551PhosphotyrosineCurated

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ80UL9.
PaxDbiQ80UL9.
PRIDEiQ80UL9.

PTM databases

iPTMnetiQ80UL9.
PhosphoSiteiQ80UL9.

Expressioni

Tissue specificityi

Expressed by gamma-delta intraepithelial T cells (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000048534.
CleanExiMM_AMICA1.

Interactioni

Subunit structurei

Homodimer; active form in leukocyte-endothelial cell adhesion. Interacts (homodimeric form) with CXADR. Interacts (via cytoplasmic domain) with the PI3 kinase; upon CXADR-binding. Interacts with ITGA4 and ITGB1; integrin alpha-4/beta-1 may regulate leukocyte to endothelial cells adhesion by controlling JAML homodimerization.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-59107N.
STRINGi10090.ENSMUSP00000052033.

Structurei

Secondary structure

1
379
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 365Combined sources
Beta strandi41 – 433Combined sources
Beta strandi55 – 6612Combined sources
Beta strandi71 – 777Combined sources
Beta strandi80 – 834Combined sources
Helixi85 – 873Combined sources
Turni88 – 903Combined sources
Beta strandi91 – 933Combined sources
Turni97 – 1004Combined sources
Beta strandi104 – 1063Combined sources
Helixi111 – 1133Combined sources
Beta strandi115 – 1239Combined sources
Beta strandi129 – 13911Combined sources
Beta strandi144 – 1496Combined sources
Beta strandi154 – 1563Combined sources
Beta strandi161 – 1666Combined sources
Beta strandi170 – 1767Combined sources
Beta strandi184 – 1907Combined sources
Beta strandi193 – 1953Combined sources
Beta strandi197 – 1993Combined sources
Turni203 – 2075Combined sources
Beta strandi208 – 2103Combined sources
Helixi214 – 2163Combined sources
Beta strandi221 – 2233Combined sources
Helixi228 – 2303Combined sources
Beta strandi232 – 2409Combined sources
Beta strandi243 – 25412Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MJ6X-ray2.19A21-280[»]
3MJ7X-ray2.80A21-280[»]
3MJ9X-ray2.95A21-280[»]
ProteinModelPortaliQ80UL9.
SMRiQ80UL9. Positions 31-259.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ80UL9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 135112Ig-like V-type 1Add
BLAST
Domaini140 – 250111Ig-like V-type 2Add
BLAST

Domaini

The Ig-like V-type domain 1 mediates interaction with CXADR (PubMed:20813954). The Ig-like V-type domain 2 may also play a role in the interaction (PubMed:20813955).2 Publications

Sequence similaritiesi

Belongs to the immunoglobulin superfamily.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IKEA. Eukaryota.
ENOG4111DWB. LUCA.
GeneTreeiENSGT00440000034341.
HOGENOMiHOG000294145.
HOVERGENiHBG055209.
InParanoidiQ80UL9.
OMAiGHFQNRV.
OrthoDBiEOG091G0KVU.
TreeFamiTF331728.

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.
IPR029871. JAML.
IPR000920. Myelin_P0-rel.
[Graphical view]
PANTHERiPTHR13869. PTHR13869. 2 hits.
PTHR13869:SF22. PTHR13869:SF22. 2 hits.
PfamiPF07686. V-set. 2 hits.
[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.

Q80UL9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLCLLKLIVI PVILAPVGYP QGLPGLTVSS PQLRVHVGES VLMGCVVQRT
60 70 80 90 100
EEKHVDRVDW LFSKDKDDAS EYVLFYYSNL SVPTGRFQNR SHLVGDTFHN
110 120 130 140 150
DGSLLLQDVQ KADEGIYTCE IRLKNESMVM KKPVELWVLP EEPKDLRVRV
160 170 180 190 200
GDTTQMRCSI QSTEEKRVTK VNWMFSSGSH TEEETVLSYD SNMRSGKFQS
210 220 230 240 250
LGRFRNRVDL TGDISRNDGS IKLQTVKESD QGIYTCSIYV GKLESRKTIV
260 270 280 290 300
LHVVQDEFQR TISPTPPTDK GQQGILNGNQ LVIIVGIVCA TFLLLPVLIL
310 320 330 340 350
IVKKAKWNKS SVSSMASVKS LENKEKINPE KHIYSSITTW ETTERGISGE
360 370
SEGTYMTMNP VWPSSPKASS LVRSSVRSK
Length:379
Mass (Da):42,533
Last modified:July 27, 2011 - v2
Checksum:iEFC0F1A84EEC8A12
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti231 – 2311Q → R in AAH50133 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY093688 mRNA. Translation: AAM15732.1.
AC122305 Genomic DNA. No translation available.
BC050133 mRNA. Translation: AAH50133.1.
CCDSiCCDS23128.1.
RefSeqiNP_001005421.3. NM_001005421.4.
XP_006510446.1. XM_006510383.2.
UniGeneiMm.190461.

Genome annotation databases

EnsembliENSMUST00000050020; ENSMUSP00000052033; ENSMUSG00000048534.
GeneIDi270152.
KEGGimmu:270152.
UCSCiuc009pfd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY093688 mRNA. Translation: AAM15732.1.
AC122305 Genomic DNA. No translation available.
BC050133 mRNA. Translation: AAH50133.1.
CCDSiCCDS23128.1.
RefSeqiNP_001005421.3. NM_001005421.4.
XP_006510446.1. XM_006510383.2.
UniGeneiMm.190461.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MJ6X-ray2.19A21-280[»]
3MJ7X-ray2.80A21-280[»]
3MJ9X-ray2.95A21-280[»]
ProteinModelPortaliQ80UL9.
SMRiQ80UL9. Positions 31-259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59107N.
STRINGi10090.ENSMUSP00000052033.

PTM databases

iPTMnetiQ80UL9.
PhosphoSiteiQ80UL9.

Proteomic databases

EPDiQ80UL9.
PaxDbiQ80UL9.
PRIDEiQ80UL9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000050020; ENSMUSP00000052033; ENSMUSG00000048534.
GeneIDi270152.
KEGGimmu:270152.
UCSCiuc009pfd.2. mouse.

Organism-specific databases

CTDi270152.
MGIiMGI:2685484. Amica1.

Phylogenomic databases

eggNOGiENOG410IKEA. Eukaryota.
ENOG4111DWB. LUCA.
GeneTreeiENSGT00440000034341.
HOGENOMiHOG000294145.
HOVERGENiHBG055209.
InParanoidiQ80UL9.
OMAiGHFQNRV.
OrthoDBiEOG091G0KVU.
TreeFamiTF331728.

Enzyme and pathway databases

ReactomeiR-MMU-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-MMU-202733. Cell surface interactions at the vascular wall.

Miscellaneous databases

EvolutionaryTraceiQ80UL9.
PROiQ80UL9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000048534.
CleanExiMM_AMICA1.

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.
IPR029871. JAML.
IPR000920. Myelin_P0-rel.
[Graphical view]
PANTHERiPTHR13869. PTHR13869. 2 hits.
PTHR13869:SF22. PTHR13869:SF22. 2 hits.
PfamiPF07686. V-set. 2 hits.
[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...

Entry informationi

Entry nameiJAML_MOUSE
AccessioniPrimary (citable) accession number: Q80UL9
Secondary accession number(s): E9QNV7, Q5DTC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 27, 2011
Last modified: September 7, 2016
This is version 114 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.