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Protein

Protein lin-7 homolog B

Gene

Lin7b

Organism
Rattus norvegicus (Rat)
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. MPP5 via its L27 domain. May increase the amplitude of ASIC3 acid-evoked currents by stabilizing the channel at the cell surface (By similarity).By similarity1 Publication

GO - Molecular functioni

  • PDZ domain binding Source: RGD

GO - Biological processi

  • cell-cell junction assembly Source: RGD
  • exocytosis Source: UniProtKB-KW
  • neurotransmitter secretion Source: Ensembl
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Exocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-212676. Dopamine Neurotransmitter Release Cycle.
R-RNO-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, Veli1a, Veli2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi620730. Lin7b.

Subcellular locationi

GO - Cellular componenti

  • basolateral plasma membrane Source: UniProtKB-SubCell
  • bicellular tight junction Source: UniProtKB-SubCell
  • cell-cell junction Source: RGD
  • neuron projection Source: UniProtKB-SubCell
  • postsynaptic density Source: UniProtKB-SubCell
  • postsynaptic membrane Source: UniProtKB-KW
  • presynapse Source: GOC
  • synapse Source: RGD
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_0000189628Add
BLAST

Proteomic databases

PaxDbiQ9Z252.
PRIDEiQ9Z252.

PTM databases

PhosphoSiteiQ9Z252.

Expressioni

Tissue specificityi

Expressed only in brain.3 Publications

Inductioni

Up-regulated by cell depolarization and calcium entry through L-type calcium channels.1 Publication

Gene expression databases

GenevisibleiQ9Z252. RN.

Interactioni

Subunit structurei

Interacts with ASIC3 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 RTKN (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Baiap2Q6GMN23EBI-7001699,EBI-6997402

GO - Molecular functioni

  • PDZ domain binding Source: RGD

Protein-protein interaction databases

BioGridi248805. 2 interactions.
IntActiQ9Z252. 2 interactions.
MINTiMINT-1588548.
STRINGi10116.ENSRNOP00000028164.

Structurei

Secondary structure

1
207
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2721Combined sources
Helixi33 – 4311Combined sources
Helixi45 – 5915Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UITX-ray2.05A/B/C/D3-66[»]
ProteinModelPortaliQ9Z252.
SMRiQ9Z252. Positions 8-64, 93-175.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ9Z252.
KOiK19931.
OMAiCLERDVC.
OrthoDBiEOG75MVXG.
PhylomeDBiQ9Z252.
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.

Q9Z252-1 [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

SSLESRG
Length:207
Mass (Da):22,900
Last modified:May 1, 1999 - v1
Checksum:iBC6B6754B8C89B13
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF090133 mRNA. Translation: AAC78072.1.
RefSeqiNP_068526.1. NM_021758.1.
UniGeneiRn.44184.

Genome annotation databases

EnsembliENSRNOT00000028164; ENSRNOP00000028164; ENSRNOG00000020746.
GeneIDi60377.
KEGGirno:60377.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF090133 mRNA. Translation: AAC78072.1.
RefSeqiNP_068526.1. NM_021758.1.
UniGeneiRn.44184.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UITX-ray2.05A/B/C/D3-66[»]
ProteinModelPortaliQ9Z252.
SMRiQ9Z252. Positions 8-64, 93-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248805. 2 interactions.
IntActiQ9Z252. 2 interactions.
MINTiMINT-1588548.
STRINGi10116.ENSRNOP00000028164.

PTM databases

PhosphoSiteiQ9Z252.

Proteomic databases

PaxDbiQ9Z252.
PRIDEiQ9Z252.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028164; ENSRNOP00000028164; ENSRNOG00000020746.
GeneIDi60377.
KEGGirno:60377.

Organism-specific databases

CTDi64130.
RGDi620730. Lin7b.

Phylogenomic databases

eggNOGiKOG3550. Eukaryota.
ENOG410XP5T. LUCA.
GeneTreeiENSGT00550000074582.
HOGENOMiHOG000285929.
HOVERGENiHBG052329.
InParanoidiQ9Z252.
KOiK19931.
OMAiCLERDVC.
OrthoDBiEOG75MVXG.
PhylomeDBiQ9Z252.
TreeFamiTF316850.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi612059.
PROiQ9Z252.

Gene expression databases

GenevisibleiQ9Z252. RN.

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

  1. "Isolation and characterization of mammalian homologues of Caenorhabditis elegans lin-7: localization at cell-cell junctions."
    Irie M., Hata Y., Deguchi M., Ide N., Hirao K., Yao I., Nishioka H., Takai Y.
    Oncogene 18:2811-2817(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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: TISSUE SPECIFICITY, INTERACTION WITH CASK AND APBA1.
  3. "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: TISSUE SPECIFICITY, INTERACTION WITH DLG4 AND GRIN2B.
  4. "The expression of the PDZ protein MALS-1/velis is regulated by calcium and calcineurin in cerebellar granule cells."
    Sanna B., Kramer D., Genazzani A.A.
    J. Biol. Chem. 277:49585-49590(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. "CASK participates in alternative tripartite complexes in which Mint 1 competes for binding with Caskin 1, a novel CASK-binding protein."
    Tabuchi K., Biederer T., Butz S., Suedhof T.C.
    J. Neurosci. 22:4264-4273(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CASK; APBA1 AND CASKIN1.
  6. "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels."
    Leonoudakis D., Conti L.R., Radeke C.M., McGuire L.M., Vandenberg C.A.
    J. Biol. Chem. 279:19051-19063(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNJ12; CASK AND APBA1, FUNCTION.
  7. "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.

Entry informationi

Entry nameiLIN7B_RAT
AccessioniPrimary (citable) accession number: Q9Z252
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 121 of the entry and version 1 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.