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Protein

Protein lin-7 homolog A

Gene

Lin7a

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

Functioni

Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells.1 Publication

GO - Molecular functioni

GO - Biological processi

  • exocytosis Source: UniProtKB-KW
  • inner ear development Source: MGI
  • neurotransmitter secretion Source: MGI
  • protein transport Source: UniProtKB-KW
  • synaptic vesicle transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

Exocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-212676. Dopamine Neurotransmitter Release Cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein lin-7 homolog A
Short name:
Lin-7A
Short name:
mLin-7
Alternative name(s):
Mammalian lin-seven protein 1
Short name:
MALS-1
Vertebrate lin-7 homolog 1
Short name:
Veli-1
Gene namesi
Name:Lin7a
Synonyms:Mals1, Veli1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:2135609. Lin7a.

Subcellular locationi

GO - Cellular componenti

  • basolateral plasma membrane Source: MGI
  • bicellular tight junction Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • membrane Source: MGI
  • neuron projection Source: UniProtKB-SubCell
  • postsynaptic density Source: UniProtKB-SubCell
  • postsynaptic membrane Source: UniProtKB-KW
  • presynapse Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse, Synaptosome, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 233233Protein lin-7 homolog APRO_0000189624Add
BLAST

Proteomic databases

EPDiQ8JZS0.
MaxQBiQ8JZS0.
PaxDbiQ8JZS0.
PRIDEiQ8JZS0.

PTM databases

iPTMnetiQ8JZS0.
PhosphoSiteiQ8JZS0.

Expressioni

Tissue specificityi

Expressed in the kidney, along the length of the nephron.1 Publication

Gene expression databases

BgeeiQ8JZS0.
CleanExiMM_LIN7A.
ExpressionAtlasiQ8JZS0. baseline and differential.
GenevisibleiQ8JZS0. MM.

Interactioni

Subunit structurei

Forms two exclusive ternary complexes with CASK and APBA1 or CASKIN1 (By similarity). Can also interact with other modular proteins containing protein-protein interaction domains like MPP5, MPP6, MPP7, DLG1, DLG2 and DLG3 through its L27 domain. Interacts with DLG4, GRIN2B and MARCH11 as well as CDH1 and CTNNB1, the channels KCNJ12/Kir2.2, KCNJ4/Kir2.3 and probably KCNJ2/Kir2.1 and SLC6A12/BGT-1 via its PDZ domain. The association of LIN7A with cadherin and beta-catenin is calcium-dependent, occurs at synaptic junctions and requires the actin cytoskeleton. Interacts with EGFR, ERBB2, ERBB3 and ERBB4 with both PDZ and KID domains. Associates with KIF17 via APBA1. Interacts with HTR4. Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C) (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi223780. 1 interaction.
IntActiQ8JZS0. 6 interactions.
MINTiMINT-91208.
STRINGi10090.ENSMUSP00000020057.

Structurei

3D structure databases

ProteinModelPortaliQ8JZS0.
SMRiQ8JZS0. Positions 21-79, 108-190.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 8056L27PROSITE-ProRule annotationAdd
BLAST
Domaini108 – 19083PDZPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi14 – 2815Kinase interacting siteAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi210 – 2134Poly-Gln
Compositional biasi217 – 22913Poly-GlnAdd
BLAST

Domaini

The kinase interacting site is required for proper delivery of ERBB2 to the basolateral membrane.By similarity
The PDZ domain regulates endocytosis and recycling of the receptor at the membrane.By similarity
The L27 domain mediates interaction with CASK and is involved in the formation of multimeric complexes and the association of LIN7 to membranes.By similarity

Sequence similaritiesi

Belongs to the lin-7 family.Curated
Contains 1 L27 domain.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3550. Eukaryota.
ENOG410XP5T. LUCA.
GeneTreeiENSGT00550000074582.
HOGENOMiHOG000285929.
HOVERGENiHBG052329.
InParanoidiQ8JZS0.
KOiK19931.
OMAiVPGHKLQ.
OrthoDBiEOG75MVXG.
PhylomeDBiQ8JZS0.
TreeFamiTF316850.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR014775. L27_C.
IPR004172. L27_dom.
IPR001478. PDZ.
[Graphical view]
PfamiPF02828. L27. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00569. L27. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF101288. SSF101288. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEiPS51022. L27. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8JZS0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKPSVTSAP TADMATLTVV QPLTLDRDVA RAIELLEKLQ ESGEVPVHKL
60 70 80 90 100
QSLKKVLQSE FCTAIREVYQ YMHETITVNG CPEFRARATA KATVAAFAAS
110 120 130 140 150
EGHSHPRVVE LPKTDEGLGF NVMGGKEQNS PIYISRIIPG GVAERHGGLK
160 170 180 190 200
RGDQLLSVNG VSVEGEHHEK AVELLKAAKD SVKLVVRYTP KVLEEMEARF
210 220 230
EKLRTARRRQ QQQLLIQQQQ QQQQQQPQQN HMS
Length:233
Mass (Da):25,993
Last modified:February 15, 2005 - v2
Checksum:iD8D05EF16A93B8BB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BY123635 mRNA. No translation available.
BC029721 mRNA. Translation: AAH29721.1.
CCDSiCCDS24160.1.
RefSeqiNP_001034443.1. NM_001039354.1.
UniGeneiMm.268025.

Genome annotation databases

EnsembliENSMUST00000020057; ENSMUSP00000020057; ENSMUSG00000019906.
GeneIDi108030.
KEGGimmu:108030.
UCSCiuc007gyy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BY123635 mRNA. No translation available.
BC029721 mRNA. Translation: AAH29721.1.
CCDSiCCDS24160.1.
RefSeqiNP_001034443.1. NM_001039354.1.
UniGeneiMm.268025.

3D structure databases

ProteinModelPortaliQ8JZS0.
SMRiQ8JZS0. Positions 21-79, 108-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223780. 1 interaction.
IntActiQ8JZS0. 6 interactions.
MINTiMINT-91208.
STRINGi10090.ENSMUSP00000020057.

PTM databases

iPTMnetiQ8JZS0.
PhosphoSiteiQ8JZS0.

Proteomic databases

EPDiQ8JZS0.
MaxQBiQ8JZS0.
PaxDbiQ8JZS0.
PRIDEiQ8JZS0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020057; ENSMUSP00000020057; ENSMUSG00000019906.
GeneIDi108030.
KEGGimmu:108030.
UCSCiuc007gyy.1. mouse.

Organism-specific databases

CTDi8825.
MGIiMGI:2135609. Lin7a.

Phylogenomic databases

eggNOGiKOG3550. Eukaryota.
ENOG410XP5T. LUCA.
GeneTreeiENSGT00550000074582.
HOGENOMiHOG000285929.
HOVERGENiHBG052329.
InParanoidiQ8JZS0.
KOiK19931.
OMAiVPGHKLQ.
OrthoDBiEOG75MVXG.
PhylomeDBiQ8JZS0.
TreeFamiTF316850.

Enzyme and pathway databases

ReactomeiR-MMU-212676. Dopamine Neurotransmitter Release Cycle.

Miscellaneous databases

NextBioi359907.
PROiQ8JZS0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8JZS0.
CleanExiMM_LIN7A.
ExpressionAtlasiQ8JZS0. baseline and differential.
GenevisibleiQ8JZS0. MM.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR014775. L27_C.
IPR004172. L27_dom.
IPR001478. PDZ.
[Graphical view]
PfamiPF02828. L27. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00569. L27. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF101288. SSF101288. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEiPS51022. L27. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-111.
    Strain: C57BL/6J.
    Tissue: Brain.
  2. "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] OF 23-233.
    Tissue: Eye.
  3. "Mammalian LIN-7 PDZ proteins associate with beta-catenin at the cell-cell junctions of epithelia and neurons."
    Perego C., Vanoni C., Massari S., Longhi R., Pietrini G.
    EMBO J. 19:3978-3989(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDH1 AND CTNNB1.
  4. "Role of beta-catenin in synaptic vesicle localization and presynaptic assembly."
    Bamji S.X., Shimazu K., Kimes N., Huelsken J., Birchmeier W., Lu B., Reichardt L.F.
    Neuron 40:719-731(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SYNAPTIC VESICLE LOCALIZATION.
  5. "New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a receptor splice variant: roles in receptor targeting."
    Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W., Marin P., Dumuis A., Bockaert J.
    J. Cell Sci. 117:5367-5379(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTR4.
  6. "Differential localization of the Mammalian Lin 7 (MALS/Veli) PDZ proteins in the kidney."
    Olsen O., Wade J.B., Morin N., Bredt D.S., Welling P.A.
    Am. J. Physiol. 288:F345-F352(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Liver.

Entry informationi

Entry nameiLIN7A_MOUSE
AccessioniPrimary (citable) accession number: Q8JZS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: May 11, 2016
This is version 112 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.