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Protein

Protein lin-7 homolog C

Gene

Lin7c

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.1 Publication

GO - Molecular functioni

  • PDZ domain binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Exocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-212676. Dopamine Neurotransmitter Release Cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein lin-7 homolog C
Short name:
Lin-7C
Alternative name(s):
Mammalian lin-seven protein 3
Short name:
MALS-3
Vertebrate lin-7 homolog 3
Short name:
Veli-3
Gene namesi
Name:Lin7c
Synonyms:Mals3, Veli3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi621164. Lin7c.

Subcellular locationi

GO - Cellular componenti

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
Initiator methionineiRemovedBy similarity
Chaini2 – 197196Protein lin-7 homolog CPRO_0000189631Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ792I0.
PRIDEiQ792I0.

PTM databases

iPTMnetiQ792I0.
PhosphoSiteiQ792I0.

Expressioni

Tissue specificityi

Expressed in brain, kidney (outer medullary collecting duct) and liver with weak expression in thymus and heart.3 Publications

Gene expression databases

GenevisibleiQ792I0. RN.

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 HTR4. Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C) (By similarity). Interacts with MAPK12 (By similarity).By similarity

GO - Molecular functioni

  • PDZ domain binding Source: RGD

Protein-protein interaction databases

BioGridi248835. 1 interaction.
IntActiQ792I0. 4 interactions.
MINTiMINT-4577906.
STRINGi10116.ENSRNOP00000065941.

Structurei

3D structure databases

ProteinModelPortaliQ792I0.
SMRiQ792I0. Positions 3-64, 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
Motifi2 – 1312Kinase 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.
InParanoidiQ792I0.
KOiK19931.
OMAiRRQQNNF.
OrthoDBiEOG75MVXG.
PhylomeDBiQ792I0.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q792I0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALGEPVRL ERDICRAIEL LEKLQRSGEV PPQKLQALQR VLQSEFCNAV
60 70 80 90 100
REVYEHVYET VDISSSPEVR ANATAKATVA AFAASEGHSH PRVVELPKTE
110 120 130 140 150
EGLGFNIMGG KEQNSPIYIS RIIPGGIADR HGGLKRGDQL LSVNGVSVEG
160 170 180 190
EHHEKAVELL KAAQGKVKLV VRYTPKVLEE MESRFEKMRS AKRRQQT
Length:197
Mass (Da):21,834
Last modified:July 5, 2004 - v1
Checksum:i7410FBFA3BD24F45
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF090136 mRNA. Translation: AAC78075.1.
RefSeqiNP_068623.1. NM_021851.1.
UniGeneiRn.9461.

Genome annotation databases

EnsembliENSRNOT00000073258; ENSRNOP00000065941; ENSRNOG00000045698.
GeneIDi60442.
KEGGirno:60442.
UCSCiRGD:621164. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF090136 mRNA. Translation: AAC78075.1.
RefSeqiNP_068623.1. NM_021851.1.
UniGeneiRn.9461.

3D structure databases

ProteinModelPortaliQ792I0.
SMRiQ792I0. Positions 3-64, 93-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248835. 1 interaction.
IntActiQ792I0. 4 interactions.
MINTiMINT-4577906.
STRINGi10116.ENSRNOP00000065941.

PTM databases

iPTMnetiQ792I0.
PhosphoSiteiQ792I0.

Proteomic databases

PaxDbiQ792I0.
PRIDEiQ792I0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000073258; ENSRNOP00000065941; ENSRNOG00000045698.
GeneIDi60442.
KEGGirno:60442.
UCSCiRGD:621164. rat.

Organism-specific databases

CTDi55327.
RGDi621164. Lin7c.

Phylogenomic databases

eggNOGiKOG3550. Eukaryota.
ENOG410XP5T. LUCA.
GeneTreeiENSGT00550000074582.
HOGENOMiHOG000285929.
HOVERGENiHBG052329.
InParanoidiQ792I0.
KOiK19931.
OMAiRRQQNNF.
OrthoDBiEOG75MVXG.
PhylomeDBiQ792I0.
TreeFamiTF316850.

Enzyme and pathway databases

ReactomeiR-RNO-212676. Dopamine Neurotransmitter Release Cycle.

Miscellaneous databases

NextBioi612170.
PROiQ792I0.

Gene expression databases

GenevisibleiQ792I0. 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. "Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins."
    Leonoudakis D., Conti L.R., Anderson S., Radeke C.M., McGuire L.M., Adams M.E., Froehner S.C., Yates J.R. III, Vandenberg C.A.
    J. Biol. Chem. 279:22331-22346(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 52-70; 77-121 AND 136-155, INTERACTION WITH KCNJ12.
  3. "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.
  4. "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.
  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; APBA1 AND DLG1, 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 nameiLIN7C_RAT
AccessioniPrimary (citable) accession number: Q792I0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: July 5, 2004
Last modified: May 11, 2016
This is version 106 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.