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Q9NUP9 (LIN7C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:LIN7C
Synonyms:MALS3, VELI3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length197 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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 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 By similarity. Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C). Interacts with MAPK12 By similarity. Ref.4 Ref.5

Subcellular location

Cell membrane; Peripheral membrane protein. Basolateral cell membrane; Peripheral membrane protein. Cell junction By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density; Peripheral membrane protein By similarity. Cell junctiontight junction By similarity. Cell junctionsynapsesynaptosome By similarity. Note: Enriched in synaptosomes and at epithelial cell-cell junctions By similarity. Mainly basolateral in renal epithelial cells. Ref.4

Domain

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 similarities

Belongs to the lin-7 family.

Contains 1 L27 domain.

Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
   Biological processExocytosis
Protein transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
Synaptosome
Tight junction
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processexocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

morphogenesis of an epithelial sheet

Inferred from mutant phenotype PubMed 23201090. Source: UniProt

neurotransmitter secretion

Inferred from electronic annotation. Source: Ensembl

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMPP7-DLG1-LIN7 complex

Inferred from direct assay PubMed 20702775. Source: UniProt

basolateral plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay PubMed 23201090. Source: UniProt

neuron projection

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic density

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

tight junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL27 domain binding

Inferred from direct assay PubMed 20702775. Source: UniProt

cytoskeletal protein binding

Inferred from physical interaction PubMed 17987659. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction Ref.5. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 197196Protein lin-7 homolog C
PRO_0000189629

Regions

Domain10 – 6556L27
Domain93 – 17583PDZ
Motif2 – 1312Kinase interacting site By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.3 Ref.7

Secondary structure

....... 197
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NUP9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 7410FBFA3BD24F45

FASTA19721,834
        10         20         30         40         50         60 
MAALGEPVRL ERDICRAIEL LEKLQRSGEV PPQKLQALQR VLQSEFCNAV REVYEHVYET 

        70         80         90        100        110        120 
VDISSSPEVR ANATAKATVA AFAASEGHSH PRVVELPKTE EGLGFNIMGG KEQNSPIYIS 

       130        140        150        160        170        180 
RIIPGGIADR HGGLKRGDQL LSVNGVSVEG EHHEKAVELL KAAQGKVKLV VRYTPKVLEE 

       190 
MESRFEKMRS AKRRQQT 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[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].
Tissue: Uterus.
[3]Bienvenut W.V., Lao L., Ryan K.M.
Submitted (JUN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12; 17-23 AND 77-92, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Osteosarcoma.
[4]"Polar expression of ErbB-2/HER2 in epithelia. Bimodal regulation by Lin-7."
Shelly M., Mosesson Y., Citri A., Lavi S., Zwang Y., Melamed-Book N., Aroeti B., Yarden Y.
Dev. Cell 5:475-486(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EGFR.
[5]"The stardust family protein MPP7 forms a tripartite complex with LIN7 and DLG1 that regulates the stability and localization of DLG1 to cell junctions."
Bohl J., Brimer N., Lyons C., Vande Pol S.B.
J. Biol. Chem. 282:9392-9400(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DLG1 AND MPP7.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK002077 mRNA. Translation: BAA92072.1.
BC053907 mRNA. Translation: AAH53907.1.
RefSeqNP_060832.1. NM_018362.3.
UniGeneHs.91393.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LRAX-ray2.95A3-64[»]
ProteinModelPortalQ9NUP9.
SMRQ9NUP9. Positions 3-64, 93-175.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120608. 17 interactions.
IntActQ9NUP9. 9 interactions.
MINTMINT-5002028.
STRING9606.ENSP00000278193.

PTM databases

PhosphoSiteQ9NUP9.

Polymorphism databases

DMDM59798474.

Proteomic databases

PaxDbQ9NUP9.
PeptideAtlasQ9NUP9.
PRIDEQ9NUP9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000278193; ENSP00000278193; ENSG00000148943.
GeneID55327.
KEGGhsa:55327.
UCSCuc001mrl.3. human.

Organism-specific databases

CTD55327.
GeneCardsGC11M027472.
HGNCHGNC:17789. LIN7C.
HPAHPA051118.
MIM612332. gene.
neXtProtNX_Q9NUP9.
PharmGKBPA134891786.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320117.
HOGENOMHOG000285929.
HOVERGENHBG052329.
InParanoidQ9NUP9.
OMAVDINSSP.
OrthoDBEOG75MVXG.
PhylomeDBQ9NUP9.
TreeFamTF316850.

Gene expression databases

ArrayExpressQ9NUP9.
BgeeQ9NUP9.
CleanExHS_LIN7C.
GenevestigatorQ9NUP9.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
InterProIPR004172. L27.
IPR014775. L27_C.
IPR017365. Lin-7_homologue.
IPR001478. PDZ.
[Graphical view]
PfamPF02828. L27. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PIRSFPIRSF038039. Lin-7_homologue. 1 hit.
SMARTSM00569. L27. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
PROSITEPS51022. L27. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NUP9.
GeneWikiLIN7C.
GenomeRNAi55327.
NextBio59604.
PROQ9NUP9.
SOURCESearch...

Entry information

Entry nameLIN7C_HUMAN
AccessionPrimary (citable) accession number: Q9NUP9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM