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Protein

Protein lin-7 homolog C

Gene

LIN7C

Organism
Homo sapiens (Human)
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.

GO - Molecular functioni

  1. cytoskeletal protein binding Source: UniProtKB
  2. L27 domain binding Source: UniProtKB
  3. protein domain specific binding Source: BHF-UCL

GO - Biological processi

  1. asymmetric protein localization Source: GO_Central
  2. exocytosis Source: GO_Central
  3. maintenance of epithelial cell apical/basal polarity Source: GO_Central
  4. morphogenesis of an epithelial sheet Source: UniProtKB
  5. neurotransmitter secretion Source: GO_Central
  6. protein localization to basolateral plasma membrane Source: GO_Central
  7. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Exocytosis, Protein transport, Transport

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:17789. LIN7C.

Subcellular locationi

Cell membrane 1 Publication; Peripheral membrane protein 1 Publication. Basolateral cell membrane 1 Publication; Peripheral membrane protein 1 Publication. Cell junction By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity; 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.By similarity

GO - Cellular componenti

  1. basolateral plasma membrane Source: GO_Central
  2. cell-cell junction Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. MPP7-DLG1-LIN7 complex Source: UniProtKB
  6. neuron projection Source: UniProtKB-SubCell
  7. plasma membrane Source: UniProtKB
  8. postsynaptic density Source: UniProtKB-SubCell
  9. postsynaptic membrane Source: UniProtKB-KW
  10. synapse Source: GO_Central
  11. tight junction Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134891786.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 197196Protein lin-7 homolog CPRO_0000189629Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NUP9.
PaxDbiQ9NUP9.
PeptideAtlasiQ9NUP9.
PRIDEiQ9NUP9.

PTM databases

PhosphoSiteiQ9NUP9.

Expressioni

Gene expression databases

BgeeiQ9NUP9.
CleanExiHS_LIN7C.
ExpressionAtlasiQ9NUP9. baseline and differential.
GenevestigatoriQ9NUP9.

Organism-specific databases

HPAiHPA051118.

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 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).By similarity

Protein-protein interaction databases

BioGridi120608. 32 interactions.
IntActiQ9NUP9. 9 interactions.
MINTiMINT-5002028.
STRINGi9606.ENSP00000278193.

Structurei

Secondary structure

1
197
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2620Combined sources
Helixi33 – 4311Combined sources
Helixi45 – 6016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LRAX-ray2.95A3-64[»]
ProteinModelPortaliQ9NUP9.
SMRiQ9NUP9. Positions 3-64, 93-175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NUP9.

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

eggNOGiNOG320117.
GeneTreeiENSGT00550000074582.
HOGENOMiHOG000285929.
HOVERGENiHBG052329.
InParanoidiQ9NUP9.
OMAiRRQQNNF.
OrthoDBiEOG75MVXG.
PhylomeDBiQ9NUP9.
TreeFamiTF316850.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR004172. L27.
IPR014775. L27_C.
IPR017365. Lin-7_homologue.
IPR001478. PDZ.
[Graphical view]
PfamiPF02828. L27. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PIRSFiPIRSF038039. Lin-7_homologue. 1 hit.
SMARTiSM00569. L27. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. 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.

Q9NUP9-1 [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:October 1, 2000 - v1
Checksum:i7410FBFA3BD24F45
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002077 mRNA. Translation: BAA92072.1.
BC053907 mRNA. Translation: AAH53907.1.
CCDSiCCDS7864.1.
RefSeqiNP_060832.1. NM_018362.3.
UniGeneiHs.91393.

Genome annotation databases

EnsembliENST00000278193; ENSP00000278193; ENSG00000148943.
GeneIDi55327.
KEGGihsa:55327.
UCSCiuc001mrl.3. human.

Polymorphism databases

DMDMi59798474.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002077 mRNA. Translation: BAA92072.1.
BC053907 mRNA. Translation: AAH53907.1.
CCDSiCCDS7864.1.
RefSeqiNP_060832.1. NM_018362.3.
UniGeneiHs.91393.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LRAX-ray2.95A3-64[»]
ProteinModelPortaliQ9NUP9.
SMRiQ9NUP9. Positions 3-64, 93-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120608. 32 interactions.
IntActiQ9NUP9. 9 interactions.
MINTiMINT-5002028.
STRINGi9606.ENSP00000278193.

PTM databases

PhosphoSiteiQ9NUP9.

Polymorphism databases

DMDMi59798474.

Proteomic databases

MaxQBiQ9NUP9.
PaxDbiQ9NUP9.
PeptideAtlasiQ9NUP9.
PRIDEiQ9NUP9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000278193; ENSP00000278193; ENSG00000148943.
GeneIDi55327.
KEGGihsa:55327.
UCSCiuc001mrl.3. human.

Organism-specific databases

CTDi55327.
GeneCardsiGC11M027472.
HGNCiHGNC:17789. LIN7C.
HPAiHPA051118.
MIMi612332. gene.
neXtProtiNX_Q9NUP9.
PharmGKBiPA134891786.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG320117.
GeneTreeiENSGT00550000074582.
HOGENOMiHOG000285929.
HOVERGENiHBG052329.
InParanoidiQ9NUP9.
OMAiRRQQNNF.
OrthoDBiEOG75MVXG.
PhylomeDBiQ9NUP9.
TreeFamiTF316850.

Miscellaneous databases

ChiTaRSiLIN7C. human.
EvolutionaryTraceiQ9NUP9.
GeneWikiiLIN7C.
GenomeRNAii55327.
NextBioi59604.
PROiQ9NUP9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NUP9.
CleanExiHS_LIN7C.
ExpressionAtlasiQ9NUP9. baseline and differential.
GenevestigatoriQ9NUP9.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR004172. L27.
IPR014775. L27_C.
IPR017365. Lin-7_homologue.
IPR001478. PDZ.
[Graphical view]
PfamiPF02828. L27. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PIRSFiPIRSF038039. Lin-7_homologue. 1 hit.
SMARTiSM00569. L27. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS51022. L27. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  8. "Structural basis for tandem L27 domain-mediated polymerization."
    Yang X., Xie X., Chen L., Zhou H., Wang Z., Zhao W., Tian R., Zhang R., Tian C., Long J., Shen Y.
    FASEB J. 24:4806-4815(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 3-64 IN COMPLEX WITH MPP7 AND DLG1, SUBUNIT.

Entry informationi

Entry nameiLIN7C_HUMAN
AccessioniPrimary (citable) accession number: Q9NUP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: October 1, 2000
Last modified: March 4, 2015
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.