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O14910

- LIN7A_HUMAN

UniProt

O14910 - LIN7A_HUMAN

Protein

Protein lin-7 homolog A

Gene

LIN7A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (01 May 1999)
      Previous versions | rss
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    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.1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. exocytosis Source: ProtInc
    2. inner ear development Source: Ensembl
    3. neurotransmitter secretion Source: Ensembl
    4. protein complex assembly Source: ProtInc
    5. protein transport Source: UniProtKB-KW
    6. synaptic vesicle transport Source: Ensembl

    Keywords - Biological processi

    Exocytosis, Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:LIN7A
    Synonyms:MALS1, VELI1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:17787. LIN7A.

    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: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. neuron projection Source: UniProtKB-SubCell
    4. postsynaptic density Source: UniProtKB-SubCell
    5. postsynaptic membrane Source: UniProtKB-KW
    6. tight junction Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134881936.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 233233Protein lin-7 homolog APRO_0000189623Add
    BLAST

    Proteomic databases

    MaxQBiO14910.
    PaxDbiO14910.
    PRIDEiO14910.

    PTM databases

    PhosphoSiteiO14910.

    Expressioni

    Tissue specificityi

    Expressed in brain, testis, kidney, placenta and liver.1 Publication

    Gene expression databases

    ArrayExpressiO14910.
    BgeeiO14910.
    CleanExiHS_LIN7A.
    GenevestigatoriO14910.

    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, 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).By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CASKO149363EBI-2513988,EBI-1215506

    Protein-protein interaction databases

    BioGridi114352. 13 interactions.
    IntActiO14910. 18 interactions.
    MINTiMINT-1539466.
    STRINGi9606.ENSP00000261203.

    Structurei

    3D structure databases

    ProteinModelPortaliO14910.
    SMRiO14910. Positions 21-79, 108-190.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 8056L27PROSITE-ProRule annotationAdd
    BLAST
    Domaini108 – 19083PDZPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi14 – 2815Kinase interacting siteAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi210 – 2134Poly-Gln
    Compositional biasi217 – 22913Poly-GlnAdd
    BLAST

    Domaini

    The kinase interacting site is required for proper delivery of ERBB2 to the basolateral membrane.1 Publication
    The PDZ domain regulates endocytosis and recycling of the receptor at the membrane.1 Publication
    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.
    HOGENOMiHOG000285929.
    HOVERGENiHBG052329.
    InParanoidiO14910.
    OMAiPGHKLQS.
    OrthoDBiEOG75MVXG.
    PhylomeDBiO14910.
    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.

    O14910-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLKPSVTSAP TADMATLTVV QPLTLDRDVA RAIELLEKLQ ESGEVPVHKL    50
    QSLKKVLQSE FCTAIREVYQ YMHETITVNG CPEFRARATA KATVAAFAAS 100
    EGHSHPRVVE LPKTDEGLGF NVMGGKEQNS PIYISRIIPG GVAERHGGLK 150
    RGDQLLSVNG VSVEGEHHEK AVELLKAAKD SVKLVVRYTP KVLEEMEARF 200
    EKLRTARRRQ QQQLLIQQQQ QQQQQQTQQN HMS 233
    Length:233
    Mass (Da):25,997
    Last modified:May 1, 1999 - v2
    Checksum:iD8D05EF16A93BE7B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti157 – 1571S → P in CAG28608. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS9021.1.
    RefSeqiNP_004655.1. NM_004664.2.
    UniGeneiHs.144333.

    Genome annotation databases

    EnsembliENST00000552864; ENSP00000447488; ENSG00000111052.
    GeneIDi8825.
    KEGGihsa:8825.
    UCSCiuc001szj.1. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS9021.1.
    RefSeqi NP_004655.1. NM_004664.2.
    UniGenei Hs.144333.

    3D structure databases

    ProteinModelPortali O14910.
    SMRi O14910. Positions 21-79, 108-190.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114352. 13 interactions.
    IntActi O14910. 18 interactions.
    MINTi MINT-1539466.
    STRINGi 9606.ENSP00000261203.

    PTM databases

    PhosphoSitei O14910.

    Proteomic databases

    MaxQBi O14910.
    PaxDbi O14910.
    PRIDEi O14910.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000552864 ; ENSP00000447488 ; ENSG00000111052 .
    GeneIDi 8825.
    KEGGi hsa:8825.
    UCSCi uc001szj.1. human.

    Organism-specific databases

    CTDi 8825.
    GeneCardsi GC12M081166.
    HGNCi HGNC:17787. LIN7A.
    MIMi 603380. gene.
    neXtProti NX_O14910.
    PharmGKBi PA134881936.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG320117.
    HOGENOMi HOG000285929.
    HOVERGENi HBG052329.
    InParanoidi O14910.
    OMAi PGHKLQS.
    OrthoDBi EOG75MVXG.
    PhylomeDBi O14910.
    TreeFami TF316850.

    Miscellaneous databases

    GeneWikii LIN7A.
    GenomeRNAii 8825.
    NextBioi 33110.
    PROi O14910.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14910.
    Bgeei O14910.
    CleanExi HS_LIN7A.
    Genevestigatori O14910.

    Family and domain databases

    Gene3Di 2.30.42.10. 1 hit.
    InterProi IPR004172. L27.
    IPR014775. L27_C.
    IPR017365. Lin-7_homologue.
    IPR001478. PDZ.
    [Graphical view ]
    Pfami PF02828. L27. 1 hit.
    PF00595. PDZ. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038039. Lin-7_homologue. 1 hit.
    SMARTi SM00569. L27. 1 hit.
    SM00228. PDZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    PROSITEi PS51022. L27. 1 hit.
    PS50106. PDZ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiLIN7A_HUMAN
    AccessioniPrimary (citable) accession number: O14910
    Secondary accession number(s): A4FTY3
    , Q147W1, Q6LES3, Q7LDS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3