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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)DescriptionActionsGraphical viewLength
Topological domaini21 – 281ExtracellularSequence analysisAdd BLAST261
Transmembranei282 – 302HelicalSequence analysisAdd BLAST21
Topological domaini303 – 379CytoplasmicSequence analysisAdd BLAST77

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)DescriptionActionsGraphical viewLength
Mutagenesisi59D → A, K or N: Loss of interaction with CXADR. 1 Publication1
Mutagenesisi72Y → A: Loss of interaction with CXADR. 1 Publication1
Mutagenesisi75F → A or W: Loss of interaction with CXADR. 1 Publication1
Mutagenesisi77Y → A or F: Loss of interaction with CXADR. 1 Publication1
Mutagenesisi122R → A: Loss of interaction with CXADR. 1 Publication1
Mutagenesisi334Y → F: No effect on interaction with PI3 kinase. 1 Publication1
Mutagenesisi355Y → F: Loss of interaction with PI3 kinase. 1 Publication1
Mutagenesisi360 – 366PVWPSSP → AVWASSA: Loss of interaction with PI3 kinase. 1 Publication7

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000001507521 – 379Junctional adhesion molecule-likeAdd BLAST359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi45 ↔ 119PROSITE-ProRule annotation1 Publication
Glycosylationi79N-linked (GlcNAc...)1 Publication1
Glycosylationi89N-linked (GlcNAc...)1 Publication1
Glycosylationi125N-linked (GlcNAc...)1 Publication1
Disulfide bondi158 ↔ 236PROSITE-ProRule annotation1 Publication
Modified residuei355PhosphotyrosineCurated1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ80UL9.
PaxDbiQ80UL9.
PRIDEiQ80UL9.

PTM databases

iPTMnetiQ80UL9.
PhosphoSitePlusiQ80UL9.

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

1379
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 36Combined sources5
Beta strandi41 – 43Combined sources3
Beta strandi55 – 66Combined sources12
Beta strandi71 – 77Combined sources7
Beta strandi80 – 83Combined sources4
Helixi85 – 87Combined sources3
Turni88 – 90Combined sources3
Beta strandi91 – 93Combined sources3
Turni97 – 100Combined sources4
Beta strandi104 – 106Combined sources3
Helixi111 – 113Combined sources3
Beta strandi115 – 123Combined sources9
Beta strandi129 – 139Combined sources11
Beta strandi144 – 149Combined sources6
Beta strandi154 – 156Combined sources3
Beta strandi161 – 166Combined sources6
Beta strandi170 – 176Combined sources7
Beta strandi184 – 190Combined sources7
Beta strandi193 – 195Combined sources3
Beta strandi197 – 199Combined sources3
Turni203 – 207Combined sources5
Beta strandi208 – 210Combined sources3
Helixi214 – 216Combined sources3
Beta strandi221 – 223Combined sources3
Helixi228 – 230Combined sources3
Beta strandi232 – 240Combined sources9
Beta strandi243 – 254Combined sources12

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ80UL9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 135Ig-like V-type 1Add BLAST112
Domaini140 – 250Ig-like V-type 2Add BLAST111

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)DescriptionActionsGraphical viewLength
Sequence conflicti231Q → R in AAH50133 (PubMed:15489334).Curated1

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_006510383.3.
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_006510383.3.
UniGeneiMm.190461.

3D structure databases

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

Protein-protein interaction databases

DIPiDIP-59107N.
STRINGi10090.ENSMUSP00000052033.

PTM databases

iPTMnetiQ80UL9.
PhosphoSitePlusiQ80UL9.

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: November 2, 2016
This is version 116 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.