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O14910 (LIN7A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein lin-7 homolog A

Short name=Lin-7A
Short name=hLin-7
Alternative name(s):
Mammalian lin-seven protein 1
Short name=MALS-1
Tax interaction protein 33
Short name=TIP-33
Vertebrate lin-7 homolog 1
Short name=Veli-1
Gene names
Name:LIN7A
Synonyms:MALS1, VELI1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length233 AA.
Sequence statusComplete.
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. Ref.8

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, GRIN2B and MARCH11 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). Ref.1 Ref.6 Ref.7 Ref.8 Ref.9

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.8

Tissue specificity

Expressed in brain, testis, kidney, placenta and liver. Ref.7

Domain

The kinase interacting site is required for proper delivery of ERBB2 to the basolateral membrane. Ref.8

The PDZ domain regulates endocytosis and recycling of the receptor at the membrane. Ref.8

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. Ref.8

Sequence similarities

Belongs to the lin-7 family.

Contains 1 L27 domain.

Contains 1 PDZ (DHR) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CASKO149363EBI-2513988,EBI-1215506

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 233233Protein lin-7 homolog A
PRO_0000189623

Regions

Domain25 – 8056L27
Domain108 – 19083PDZ
Motif14 – 2815Kinase interacting site
Compositional bias210 – 2134Poly-Gln
Compositional bias217 – 22913Poly-Gln

Experimental info

Sequence conflict1571S → P in CAG28608. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O14910 [UniParc].

Last modified May 1, 1999. Version 2.
Checksum: D8D05EF16A93BE7B

FASTA23325,997
        10         20         30         40         50         60 
MLKPSVTSAP TADMATLTVV QPLTLDRDVA RAIELLEKLQ ESGEVPVHKL QSLKKVLQSE 

        70         80         90        100        110        120 
FCTAIREVYQ YMHETITVNG CPEFRARATA KATVAAFAAS EGHSHPRVVE LPKTDEGLGF 

       130        140        150        160        170        180 
NVMGGKEQNS PIYISRIIPG GVAERHGGLK RGDQLLSVNG VSVEGEHHEK AVELLKAAKD 

       190        200        210        220        230 
SVKLVVRYTP KVLEEMEARF EKLRTARRRQ QQQLLIQQQQ QQQQQQTQQN HMS 

« Hide

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH APBA1; CASK; DLG2 AND DLG3.
Tissue: Testis.
[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]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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: Corpus callosum.
[5]"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: Mammary gland.
[6]"The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins."
Rousset R., Fabre S., Desbois C., Bantignies F., Jalinot P.
Oncogene 16:643-654(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-233, INTERACTION WITH VIRAL ONCOPROTEIN TAX.
[7]"VAM-1: a new member of the MAGUK family binds to human Veli-1 through a conserved domain."
Tseng T.-C., Marfatia S.M., Bryant P.J., Pack S., Zhuang Z., O'Brien J.E., Lin L., Hanada T., Chishti A.H.
Biochim. Biophys. Acta 1518:249-259(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MPP6, TISSUE SPECIFICITY.
[8]"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; ERBB2; ERBB3 AND ERBB4, FUNCTION, DOMAIN.
[9]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF087693 mRNA. Translation: AAC78481.1.
AF173081 mRNA. Translation: AAD48500.1.
CR407680 mRNA. Translation: CAG28608.1.
AK315321 mRNA. Translation: BAG37724.1.
BC099921 mRNA. Translation: AAH99921.1.
BC118609 mRNA. Translation: AAI18610.1.
BC122561 mRNA. Translation: AAI22562.1.
AF028826 mRNA. Translation: AAB84251.1.
CCDSCCDS9021.1.
RefSeqNP_004655.1. NM_004664.2.
UniGeneHs.144333.

3D structure databases

ProteinModelPortalO14910.
SMRO14910. Positions 21-79, 108-190.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114352. 13 interactions.
IntActO14910. 18 interactions.
MINTMINT-1539466.
STRING9606.ENSP00000261203.

PTM databases

PhosphoSiteO14910.

Proteomic databases

MaxQBO14910.
PaxDbO14910.
PRIDEO14910.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000552864; ENSP00000447488; ENSG00000111052.
GeneID8825.
KEGGhsa:8825.
UCSCuc001szj.1. human.

Organism-specific databases

CTD8825.
GeneCardsGC12M081166.
HGNCHGNC:17787. LIN7A.
MIM603380. gene.
neXtProtNX_O14910.
PharmGKBPA134881936.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320117.
HOGENOMHOG000285929.
HOVERGENHBG052329.
InParanoidO14910.
OMAPGHKLQS.
OrthoDBEOG75MVXG.
PhylomeDBO14910.
TreeFamTF316850.

Gene expression databases

ArrayExpressO14910.
BgeeO14910.
CleanExHS_LIN7A.
GenevestigatorO14910.

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

GeneWikiLIN7A.
GenomeRNAi8825.
NextBio33110.
PROO14910.
SOURCESearch...

Entry information

Entry nameLIN7A_HUMAN
AccessionPrimary (citable) accession number: O14910
Secondary accession number(s): A4FTY3 expand/collapse secondary AC list , Q147W1, Q6LES3, Q7LDS4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 114 of the entry and version 2 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

MIM cross-references

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

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM