LIN7A_MOUSE
ID LIN7A_MOUSE Reviewed; 233 AA.
AC Q8JZS0;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein lin-7 homolog A;
DE Short=Lin-7A;
DE Short=mLin-7;
DE AltName: Full=Mammalian lin-seven protein 1;
DE Short=MALS-1;
DE AltName: Full=Vertebrate lin-7 homolog 1;
DE Short=Veli-1;
GN Name=Lin7a; Synonyms=Mals1, Veli1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-111.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Aizawa K., Akimura T., Arakawa T., Carninci P., Fukuda S., Hirozane T.,
RA Imotani K., Ishii Y., Itoh M., Kawai J., Konno H., Miyazaki A., Murata M.,
RA Nakamura M., Nomura K., Numazaki R., Ohno M., Sakai K., Sakazume N.,
RA Sasaki D., Sato K., Shibata K., Shiraki T., Tagami M., Waki K.,
RA Watahiki A., Muramatsu M., Hayashizaki Y.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-233.
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH CDH1 AND CTNNB1.
RX PubMed=10921879; DOI=10.1093/emboj/19.15.3978;
RA Perego C., Vanoni C., Massari S., Longhi R., Pietrini G.;
RT "Mammalian LIN-7 PDZ proteins associate with beta-catenin at the cell-cell
RT junctions of epithelia and neurons.";
RL EMBO J. 19:3978-3989(2000).
RN [4]
RP FUNCTION, AND IDENTIFICATION IN COMPLEX WITH APBA1 AND CASK.
RX PubMed=10846156; DOI=10.1126/science.288.5472.1796;
RA Setou M., Nakagawa T., Seog D.-H., Hirokawa N.;
RT "Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-
RT containing vesicle transport.";
RL Science 288:1796-1802(2000).
RN [5]
RP FUNCTION IN SYNAPTIC VESICLE LOCALIZATION.
RX PubMed=14622577; DOI=10.1016/s0896-6273(03)00718-9;
RA Bamji S.X., Shimazu K., Kimes N., Huelsken J., Birchmeier W., Lu B.,
RA Reichardt L.F.;
RT "Role of beta-catenin in synaptic vesicle localization and presynaptic
RT assembly.";
RL Neuron 40:719-731(2003).
RN [6]
RP INTERACTION WITH HTR4.
RX PubMed=15466885; DOI=10.1242/jcs.01379;
RA Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA Marin P., Dumuis A., Bockaert J.;
RT "New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a
RT receptor splice variant: roles in receptor targeting.";
RL J. Cell Sci. 117:5367-5379(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15494546; DOI=10.1152/ajprenal.00235.2004;
RA Olsen O., Wade J.B., Morin N., Bredt D.S., Welling P.A.;
RT "Differential localization of the Mammalian Lin 7 (MALS/Veli) PDZ proteins
RT in the kidney.";
RL Am. J. Physiol. 288:F345-F352(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in establishing and maintaining the asymmetric
CC distribution of channels and receptors at the plasma membrane of
CC polarized cells. Forms membrane-associated multiprotein complexes that
CC may regulate delivery and recycling of proteins to the correct membrane
CC domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or
CC LIN7C), CASK and APBA1 associates with the motor protein KIF17 to
CC transport vesicles containing N-methyl-D-aspartate (NMDA) receptor
CC subunit NR2B along microtubules (PubMed:10846156). This complex may
CC have the potential to couple synaptic vesicle exocytosis to cell
CC adhesion in brain. Ensures the proper localization of GRIN2B (subunit
CC 2B of the NMDA receptor) to neuronal postsynaptic density and may
CC function in localizing synaptic vesicles at synapses where it is
CC recruited by beta-catenin and cadherin. Required to localize Kir2
CC channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and
CC ERBB4 to the basolateral membrane of epithelial cells.
CC {ECO:0000269|PubMed:10846156, ECO:0000269|PubMed:14622577}.
CC -!- SUBUNIT: Forms a complex with CASK and CASKIN1 (By similarity).
CC Component of the brain-specific heterotrimeric complex (LIN-10-LIN-2-
CC LIN-7 complex) composed of at least APBA1, CASK, and LIN7, which
CC associates with the motor protein KIF17 to transport vesicles along
CC microtubules (PubMed:10846156). Can also interact with other modular
CC proteins containing protein-protein interaction domains like PALS1,
CC PALS2, MPP7, DLG1, DLG2 and DLG3 through its L27 domain. Interacts with
CC DLG4, GRIN2B and MARCHF11 as well as CDH1 and CTNNB1, the channels
CC KCNJ12/Kir2.2, KCNJ4/Kir2.3 and probably KCNJ2/Kir2.1 and SLC6A12/BGT-1
CC via its PDZ domain. The association of LIN7A with cadherin and beta-
CC catenin is calcium-dependent, occurs at synaptic junctions and requires
CC the actin cytoskeleton. Interacts with EGFR, ERBB2, ERBB3 and ERBB4
CC with both PDZ and KID domains. Associates with KIF17 via APBA1.
CC Interacts with HTR4. Forms a tripartite complex composed of DLG1, MPP7
CC and LIN7 (LIN7A or LIN7C) (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10846156}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15494546};
CC Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Basolateral
CC cell membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane
CC protein {ECO:0000269|PubMed:15494546}. Cell junction
CC {ECO:0000269|PubMed:15494546}. Postsynaptic density membrane
CC {ECO:0000269|PubMed:15494546}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15494546}. Cell junction, tight junction
CC {ECO:0000269|PubMed:15494546}. Note=Mainly basolateral in renal
CC epithelial cells.
CC -!- TISSUE SPECIFICITY: Expressed in the kidney, along the length of the
CC nephron. {ECO:0000269|PubMed:15494546}.
CC -!- DOMAIN: The kinase interacting site is required for proper delivery of
CC ERBB2 to the basolateral membrane. {ECO:0000250}.
CC -!- DOMAIN: The PDZ domain regulates endocytosis and recycling of the
CC receptor at the membrane. {ECO:0000250}.
CC -!- DOMAIN: The L27 domain mediates interaction with CASK and is involved
CC in the formation of multimeric complexes and the association of LIN7 to
CC membranes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lin-7 family. {ECO:0000305}.
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DR EMBL; BY123635; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC029721; AAH29721.1; -; mRNA.
DR CCDS; CCDS24160.1; -.
DR RefSeq; NP_001034443.1; NM_001039354.1.
DR AlphaFoldDB; Q8JZS0; -.
DR SMR; Q8JZS0; -.
DR BioGRID; 223780; 5.
DR CORUM; Q8JZS0; -.
DR IntAct; Q8JZS0; 3.
DR MINT; Q8JZS0; -.
DR STRING; 10090.ENSMUSP00000020057; -.
DR iPTMnet; Q8JZS0; -.
DR PhosphoSitePlus; Q8JZS0; -.
DR jPOST; Q8JZS0; -.
DR MaxQB; Q8JZS0; -.
DR PaxDb; Q8JZS0; -.
DR PeptideAtlas; Q8JZS0; -.
DR PRIDE; Q8JZS0; -.
DR ProteomicsDB; 290029; -.
DR Antibodypedia; 29812; 188 antibodies from 26 providers.
DR DNASU; 108030; -.
DR Ensembl; ENSMUST00000020057; ENSMUSP00000020057; ENSMUSG00000019906.
DR GeneID; 108030; -.
DR KEGG; mmu:108030; -.
DR UCSC; uc007gyy.1; mouse.
DR CTD; 8825; -.
DR MGI; MGI:2135609; Lin7a.
DR VEuPathDB; HostDB:ENSMUSG00000019906; -.
DR eggNOG; KOG3550; Eukaryota.
DR GeneTree; ENSGT00940000153222; -.
DR HOGENOM; CLU_097962_0_0_1; -.
DR InParanoid; Q8JZS0; -.
DR OMA; AIRERKH; -.
DR OrthoDB; 1335138at2759; -.
DR PhylomeDB; Q8JZS0; -.
DR TreeFam; TF316850; -.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR BioGRID-ORCS; 108030; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Lin7a; mouse.
DR PRO; PR:Q8JZS0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8JZS0; protein.
DR Bgee; ENSMUSG00000019906; Expressed in cerebellum lobe and 138 other tissues.
DR ExpressionAtlas; Q8JZS0; baseline and differential.
DR Genevisible; Q8JZS0; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0097025; C:MPP7-DLG1-LIN7 complex; IBA:GO_Central.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
DR GO; GO:0097016; F:L27 domain binding; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR GO; GO:1903361; P:protein localization to basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:MGI.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR017365; LIN7.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF02828; L27; 1.
DR Pfam; PF00595; PDZ; 1.
DR PIRSF; PIRSF038039; Lin-7_homologue; 1.
DR SMART; SM00569; L27; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF101288; SSF101288; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Exocytosis; Membrane;
KW Postsynaptic cell membrane; Protein transport; Reference proteome; Synapse;
KW Tight junction; Transport.
FT CHAIN 1..233
FT /note="Protein lin-7 homolog A"
FT /id="PRO_0000189624"
FT DOMAIN 25..80
FT /note="L27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 108..190
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 214..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 14..28
FT /note="Kinase interacting site"
SQ SEQUENCE 233 AA; 25993 MW; D8D05EF16A93B8BB CRC64;
MLKPSVTSAP TADMATLTVV QPLTLDRDVA RAIELLEKLQ ESGEVPVHKL QSLKKVLQSE
FCTAIREVYQ YMHETITVNG CPEFRARATA KATVAAFAAS EGHSHPRVVE LPKTDEGLGF
NVMGGKEQNS PIYISRIIPG GVAERHGGLK RGDQLLSVNG VSVEGEHHEK AVELLKAAKD
SVKLVVRYTP KVLEEMEARF EKLRTARRRQ QQQLLIQQQQ QQQQQQPQQN HMS
