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Protein

Protein lin-7 homolog B

Gene

Lin7b

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. May increase the amplitude of ASIC3 acid-evoked currents by stabilizing the channel at the cell surface.1 Publication

GO - Molecular functioni

GO - Biological processi

  • exocytosis Source: UniProtKB-KW
  • neurotransmitter secretion Source: MGI
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Exocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-212676. Dopamine Neurotransmitter Release Cycle.
R-MMU-5666185. RHO GTPases Activate Rhotekin and Rhophilins.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein lin-7 homolog B
Short name:
Lin-7B
Alternative name(s):
Mammalian lin-seven protein 2
Short name:
MALS-2
Vertebrate lin-7 homolog 2
Short name:
Veli-2
Gene namesi
Name:Lin7b
Synonyms:Mals2, Veli2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1330858. Lin7b.

Subcellular locationi

GO - Cellular componenti

  • basolateral plasma membrane Source: UniProtKB-SubCell
  • bicellular tight junction Source: UniProtKB-SubCell
  • neuron projection Source: UniProtKB-SubCell
  • plasma membrane Source: MGI
  • 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 – 207207Protein lin-7 homolog BPRO_0000189627Add
BLAST

Proteomic databases

EPDiO88951.
MaxQBiO88951.
PaxDbiO88951.
PRIDEiO88951.

PTM databases

iPTMnetiO88951.
PhosphoSiteiO88951.

Expressioni

Tissue specificityi

Expressed in the kidney; predominantly in the vasa recta.2 Publications

Gene expression databases

BgeeiO88951.
CleanExiMM_LIN7B.
GenevisibleiO88951. MM.

Interactioni

Subunit structurei

Forms two exclusive ternary complexes with CASK and APBA1 or CASKIN1. 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 and GRIN2B 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 ASIC3. Interacts with RTKN (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204515. 1 interaction.
IntActiO88951. 5 interactions.
MINTiMINT-4100426.
STRINGi10090.ENSMUSP00000003971.

Structurei

Secondary structure

1
207
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2718Combined sources
Helixi32 – 4312Combined sources
Helixi45 – 6319Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y74NMR-A/C8-64[»]
ProteinModelPortaliO88951.
SMRiO88951. Positions 3-65, 93-175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88951.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 6556L27PROSITE-ProRule annotationAdd
BLAST
Domaini93 – 17583PDZPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1 – 1313Kinase interacting siteBy similarityAdd
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.
InParanoidiO88951.
KOiK19931.
OMAiCLERDVC.
OrthoDBiEOG75MVXG.
PhylomeDBiO88951.
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.

O88951-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALVEPLGL ERDVSRAVEL LERLQRSGEL PPQKLQALQR VLQSRFCSAI
60 70 80 90 100
REVYEQLYDT LDITGSAEVR AHATAKATVA AFTASEGHAH PRVVELPKTD
110 120 130 140 150
EGLGFNIMGG KEQNSPIYIS RVIPGGVADR HGGLKRGDQL LSVNGVSVEG
160 170 180 190 200
EHHEKAVELL KAAQGSVKLV VRYTPRVLEE MEARFEKMRS ARRRQQHHSY

TSLESRG
Length:207
Mass (Da):22,914
Last modified:January 1, 1999 - v2
Checksum:iBC6B6754B8C89F03
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF087694 mRNA. Translation: AAC78482.1.
AF173082 mRNA. Translation: AAD48501.1.
BC031780 mRNA. Translation: AAH31780.1.
CCDSiCCDS21239.1.
RefSeqiNP_035828.1. NM_011698.1.
UniGeneiMm.20472.

Genome annotation databases

EnsembliENSMUST00000003971; ENSMUSP00000003971; ENSMUSG00000003872.
GeneIDi22342.
KEGGimmu:22342.
UCSCiuc009guv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF087694 mRNA. Translation: AAC78482.1.
AF173082 mRNA. Translation: AAD48501.1.
BC031780 mRNA. Translation: AAH31780.1.
CCDSiCCDS21239.1.
RefSeqiNP_035828.1. NM_011698.1.
UniGeneiMm.20472.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y74NMR-A/C8-64[»]
ProteinModelPortaliO88951.
SMRiO88951. Positions 3-65, 93-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204515. 1 interaction.
IntActiO88951. 5 interactions.
MINTiMINT-4100426.
STRINGi10090.ENSMUSP00000003971.

PTM databases

iPTMnetiO88951.
PhosphoSiteiO88951.

Proteomic databases

EPDiO88951.
MaxQBiO88951.
PaxDbiO88951.
PRIDEiO88951.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003971; ENSMUSP00000003971; ENSMUSG00000003872.
GeneIDi22342.
KEGGimmu:22342.
UCSCiuc009guv.1. mouse.

Organism-specific databases

CTDi64130.
MGIiMGI:1330858. Lin7b.

Phylogenomic databases

eggNOGiKOG3550. Eukaryota.
ENOG410XP5T. LUCA.
GeneTreeiENSGT00550000074582.
HOGENOMiHOG000285929.
HOVERGENiHBG052329.
InParanoidiO88951.
KOiK19931.
OMAiCLERDVC.
OrthoDBiEOG75MVXG.
PhylomeDBiO88951.
TreeFamiTF316850.

Enzyme and pathway databases

ReactomeiR-MMU-212676. Dopamine Neurotransmitter Release Cycle.
R-MMU-5666185. RHO GTPases Activate Rhotekin and Rhophilins.

Miscellaneous databases

EvolutionaryTraceiO88951.
PROiO88951.
SOURCEiSearch...

Gene expression databases

BgeeiO88951.
CleanExiMM_LIN7B.
GenevisibleiO88951. 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. "A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain."
    Butz S., Okamoto M., Suedhof T.C.
    Cell 94:773-782(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DLG2 AND DLG3.
  2. "Characterization of MALS/Velis-1, -2, and -3: a family of mammalian LIN-7 homologs enriched at brain synapses in association with the postsynaptic density-95/NMDA receptor postsynaptic complex."
    Jo K., Derin R., Li M., Bredt D.S.
    J. Neurosci. 19:4189-4199(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Salivary gland.
  4. "Basolateral membrane expression of the Kir 2.3 channel is coordinated by PDZ interaction with Lin-7/CASK complex."
    Olsen O., Liu H., Wade J.B., Merot J., Welling P.A.
    Am. J. Physiol. 282:C183-C195(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current."
    Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J.
    J. Biol. Chem. 279:46962-46968(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ASIC3, FUNCTION.
  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.
  8. "A unified assembly mode revealed by the structures of tetrameric L27 domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold proteins."
    Feng W., Long J.-F., Zhang M.
    Proc. Natl. Acad. Sci. U.S.A. 102:6861-6866(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 8-64, INTERACTION WITH CASK.

Entry informationi

Entry nameiLIN7B_MOUSE
AccessioniPrimary (citable) accession number: O88951
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: January 1, 1999
Last modified: June 8, 2016
This is version 130 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.