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Protein

Protein lin-7 homolog C

Gene

Lin7c

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Exocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-212676. Dopamine Neurotransmitter Release Cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein lin-7 homolog C
Short name:
Lin-7C
Short name:
mLin7C
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1330839. 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_0000189630Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO88952.
MaxQBiO88952.
PaxDbiO88952.
PeptideAtlasiO88952.
PRIDEiO88952.

PTM databases

iPTMnetiO88952.
PhosphoSiteiO88952.

Expressioni

Tissue specificityi

Expressed in the kidney; particularly in the outer medullary collecting duct.1 Publication

Gene expression databases

BgeeiO88952.
CleanExiMM_LIN7C.
GenevisibleiO88952. MM.

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. Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C) (By similarity). Interacts with MAPK12.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Kcnma1Q084604EBI-821316,EBI-1633915

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204516. 41 interactions.
IntActiO88952. 25 interactions.
STRINGi10090.ENSMUSP00000028583.

Structurei

3D structure databases

ProteinModelPortaliO88952.
SMRiO88952. 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.1 Publication

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.
InParanoidiO88952.
KOiK19931.
OMAiRRQQNNF.
OrthoDBiEOG75MVXG.
PhylomeDBiO88952.
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.

O88952-1 [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:January 1, 1999 - v2
Checksum:i7410FBFA3BD24F45
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF087695 mRNA. Translation: AAC78483.1.
AF173083 mRNA. Translation: AAD48502.1.
AK015399 mRNA. Translation: BAB29830.1.
AK078923 mRNA. Translation: BAC37462.1.
BC046966 mRNA. Translation: AAH46966.1.
CCDSiCCDS16509.1.
RefSeqiNP_035829.1. NM_011699.3.
UniGeneiMm.235300.
Mm.478053.

Genome annotation databases

EnsembliENSMUST00000028583; ENSMUSP00000028583; ENSMUSG00000027162.
GeneIDi22343.
KEGGimmu:22343.
UCSCiuc008lmo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF087695 mRNA. Translation: AAC78483.1.
AF173083 mRNA. Translation: AAD48502.1.
AK015399 mRNA. Translation: BAB29830.1.
AK078923 mRNA. Translation: BAC37462.1.
BC046966 mRNA. Translation: AAH46966.1.
CCDSiCCDS16509.1.
RefSeqiNP_035829.1. NM_011699.3.
UniGeneiMm.235300.
Mm.478053.

3D structure databases

ProteinModelPortaliO88952.
SMRiO88952. Positions 3-64, 93-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204516. 41 interactions.
IntActiO88952. 25 interactions.
STRINGi10090.ENSMUSP00000028583.

PTM databases

iPTMnetiO88952.
PhosphoSiteiO88952.

Proteomic databases

EPDiO88952.
MaxQBiO88952.
PaxDbiO88952.
PeptideAtlasiO88952.
PRIDEiO88952.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028583; ENSMUSP00000028583; ENSMUSG00000027162.
GeneIDi22343.
KEGGimmu:22343.
UCSCiuc008lmo.1. mouse.

Organism-specific databases

CTDi55327.
MGIiMGI:1330839. Lin7c.

Phylogenomic databases

eggNOGiKOG3550. Eukaryota.
ENOG410XP5T. LUCA.
GeneTreeiENSGT00550000074582.
HOGENOMiHOG000285929.
HOVERGENiHBG052329.
InParanoidiO88952.
KOiK19931.
OMAiRRQQNNF.
OrthoDBiEOG75MVXG.
PhylomeDBiO88952.
TreeFamiTF316850.

Enzyme and pathway databases

ReactomeiR-MMU-212676. Dopamine Neurotransmitter Release Cycle.

Miscellaneous databases

ChiTaRSiLin7c. mouse.
PROiO88952.
SOURCEiSearch...

Gene expression databases

BgeeiO88952.
CleanExiMM_LIN7C.
GenevisibleiO88952. 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.
    Tissue: Heart.
  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 transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cecum and Testis.
  4. "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: Eye.
  5. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 169-184, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  6. "mLin-7 is localized to the basolateral surface of renal epithelia via its NH(2) terminus."
    Straight S.W., Karnak D., Borg J.-P., Kamberov E., Dare H., Margolis B., Wade J.B.
    Am. J. Physiol. 278:F464-F475(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH SLC6A12.
  7. "Molecular cloning and characterization of Pals, proteins associated with mLin-7."
    Kamberov E., Makarova O., Roh M., Liu A., Karnak D., Straight S., Margolis B.
    J. Biol. Chem. 275:11425-11431(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MPP5.
  8. "New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a receptor splice variant: roles in receptor targeting."
    Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W., Marin P., Dumuis A., Bockaert J.
    J. Cell Sci. 117:5367-5379(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTR4.
  9. "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.
  10. "Outer membrane protein 25-a mitochondrial anchor and inhibitor of stress-activated protein kinase-3."
    Court N.W., Ingley E., Klinken S.P., Bogoyevitch M.A.
    Biochim. Biophys. Acta 1744:68-75(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAPK12.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung and Testis.

Entry informationi

Entry nameiLIN7C_MOUSE
AccessioniPrimary (citable) accession number: O88952
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: January 1, 1999
Last modified: July 6, 2016
This is version 137 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.