Q9NUP9 (LIN7C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	LIN7C
Synonyms:	MALS3, VELI3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	197 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 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 junction › synapse › postsynaptic cell membrane › postsynaptic density; Peripheral membrane protein By similarity. Cell junction › tight junction By similarity. Cell junction › synapse › synaptosome 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 process	Exocytosis Protein transport Transport
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse Synaptosome Tight junction
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	exocytosis Inferred from electronic annotation. Source: UniProtKB-KW neurotransmitter secretion Inferred from electronic annotation. Source: Compara protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	basolateral plasma membrane 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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 197

196

Protein lin-7 homolog C

PRO_0000189629

Regions

Domain

10 – 65

56

L27

Domain

93 – 175

83

PDZ

Motif

2 – 13

12

Kinase interacting site By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.3

Secondary structure

1

.

.

.

.

.

.

.

197

Helix Strand Turn

Details...

Helix

7 – 26

20

Helix

33 – 43

11

Helix

45 – 60

16

Sequences

	Sequence		Length	Mass (Da)
	Q9NUP9 [UniParc]. Last modified October 1, 2000. Version 1. 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]	"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, 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].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK002077 mRNA. Translation: BAA92072.1.
BC053907 mRNA. Translation: AAH53907.1.

IPI

IPI00019997.

RefSeq

NP_060832.1. NM_018362.3.

UniGene

Hs.91393.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3LRA	X-ray	2.95	A	3-64	[»]

ProteinModelPortal

Q9NUP9.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NUP9. 5 interactions.

STRING

9606.ENSP00000278193.

PTM databases

PhosphoSite

Q9NUP9.

Polymorphism databases

DMDM

59798474.

Proteomic databases

PaxDb

Q9NUP9.

PeptideAtlas

Q9NUP9.

PRIDE

Q9NUP9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000278193; ENSP00000278193; ENSG00000148943.

GeneID

55327.

KEGG

hsa:55327.

UCSC

uc001mrl.3. human.

Organism-specific databases

CTD

55327.

GeneCards

GC11M027472.

HGNC

HGNC:17789. LIN7C.

HPA

HPA051118.

MIM

612332. gene.

neXtProt

NX_Q9NUP9.

PharmGKB

PA134891786.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG320117.

HOGENOM

HOG000285929.

HOVERGEN

HBG052329.

InParanoid

Q9NUP9.

OMA

VDINSSP.

OrthoDB

EOG4J1198.

PhylomeDB

Q9NUP9.

Gene expression databases

ArrayExpress

Q9NUP9.

Bgee

Q9NUP9.

CleanEx

HS_LIN7C.

Genevestigator

Q9NUP9.

GermOnline

ENSG00000148943. Homo sapiens.

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]

SUPFAM

SSF50156. PDZ. 1 hit.

PROSITE

PS51022. L27. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9NUP9.

GenomeRNAi

55327.

NextBio

59604.

SOURCE

Search...

Entry information

Entry name

LIN7C_HUMAN

Accession

Primary (citable) accession number: Q9NUP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.