Reviewed, UniProtKB/Swiss-Prot O88952 (LIN7C_MOUSE)

Names and origin

Protein names

Recommended name:
    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 protein

Gene names

Name:	Lin7c
Synonyms:	Mals3, Veli3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	197 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C) By similarity.
Subcellular location	Cell membrane; Peripheral membrane protein. Basolateral cell membrane; Peripheral membrane protein. Cell junction. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density; Peripheral membrane protein. Cell junction › tight junction. Cell junction › synapse › synaptosome. Note= Enriched in synaptosomes and at epithelial cell-cell junctions. Mainly basolateral in renal epithelial cells. Ref.6 Ref.9
Tissue specificity	Expressed in the kidney; particularly in the outer medullary collecting duct. Ref.9
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. Ref.6
Sequence similarities	Belongs to the lin-7 family. Contains 1 L27 domain. Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
Biological process	Exocytosis Protein transport Transport
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse Synaptosome Tight junction
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	exocytosis Inferred from electronic annotation. Source: UniProtKB-KW neurotransmitter secretion Inferred from genetic interaction. Source: MGI protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	basolateral plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW synaptosome Inferred from direct assay. Source: MGI tight junction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABCA1	O95477	1	EBI-821316,EBI-784112	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 197	197	Lin-7 homolog C		PRO_0000189630
Regions
	Domain	10 – 65	56	L27
	Domain	93 – 175	83	PDZ
	Motif	1 – 13	13	Kinase interacting site By similarity

Sequences

	Sequence		Length	Mass (Da)
	O88952-1 [UniParc]. Last modified January 1, 1999. Version 2. Checksum: 7410FBFA3BD24F45	FASTA	197	21,834
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9753324] [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: 10341223] [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: 16141072] [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: 15489334] [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, MASS SPECTROMETRY. Strain: C57BL/6. 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: 10710551] [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: 10753959] [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: 15466885] [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: 15494546] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
RefSeq	NP_035829.1.
UniGene	Mm.235300 Mm.465298
3D structure databases
HSSP	HSSP built from PDB template 1GM1 based on UniProtKB Q64512.
SMR	O88952. Positions 10-64, 93-175.
ModBase	Search...
Protein-protein interaction databases
IntAct	O88952. 2 interactions.
PTM databases
PhosphoSite	O88952.
Proteomic databases
PRIDE	O88952.
Genome annotation databases
Ensembl	ENSMUSG00000027162. Mus musculus. [Contig view]
GeneID	22343.
KEGG	mmu:22343.
Organism-specific databases
MGI	MGI:1330839. Lin7c.
Phylogenomic databases
HOGENOM	O88952.
HOVERGEN	O88952.
Gene expression databases
ArrayExpress	O88952.
CleanEx	MM_LIN7C.
GermOnline	ENSMUSG00000027162. Mus musculus.
Family and domain databases
InterPro	IPR004172. L27. IPR014775. L27_C. IPR017365. Lin-7_homologue. IPR001478. PDZ. [Graphical view]
Pfam	PF02828. L27. 1 hit. PF00595. PDZ. 1 hit. [Graphical view]
PIRSF	PIRSF038039. Lin-7_homologue. 1 hit.
SMART	SM00569. L27. 1 hit. SM00228. PDZ. 1 hit. [Graphical view]
PROSITE	PS51022. L27. 1 hit. PS50106. PDZ. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	302613.
SOURCE	Search...

Entry information

Entry name

LIN7C_MOUSE

Accession

Primary (citable) accession number: O88952

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	January 1, 1999
Last modified:	December 16, 2008
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)