LIN7B_MOUSE
ID LIN7B_MOUSE Reviewed; 207 AA.
AC O88951;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Protein lin-7 homolog B;
DE Short=Lin-7B;
DE AltName: Full=Mammalian lin-seven protein 2;
DE Short=MALS-2;
DE AltName: Full=Vertebrate lin-7 homolog 2;
DE Short=Veli-2;
GN Name=Lin7b; Synonyms=Mals2, Veli2;
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], AND INTERACTION WITH DLG2 AND DLG3.
RX PubMed=9753324; DOI=10.1016/s0092-8674(00)81736-5;
RA Butz S., Okamoto M., Suedhof T.C.;
RT "A tripartite protein complex with the potential to couple synaptic vesicle
RT exocytosis to cell adhesion in brain.";
RL Cell 94:773-782(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10341223; DOI=10.1523/jneurosci.19-11-04189.1999;
RA Jo K., Derin R., Li M., Bredt D.S.;
RT "Characterization of MALS/Velis-1, -2, and -3: a family of mammalian LIN-7
RT homologs enriched at brain synapses in association with the postsynaptic
RT density-95/NMDA receptor postsynaptic complex.";
RL J. Neurosci. 19:4189-4199(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [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 TISSUE SPECIFICITY.
RX PubMed=11742811; DOI=10.1152/ajpcell.00249.2001;
RA Olsen O., Liu H., Wade J.B., Merot J., Welling P.A.;
RT "Basolateral membrane expression of the Kir 2.3 channel is coordinated by
RT PDZ interaction with Lin-7/CASK complex.";
RL Am. J. Physiol. 282:C183-C195(2002).
RN [6]
RP INTERACTION WITH ASIC3, AND FUNCTION.
RX PubMed=15317815; DOI=10.1074/jbc.m405874200;
RA Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J.;
RT "PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have
RT opposite effects on H+- gated current.";
RL J. Biol. Chem. 279:46962-46968(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;
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).
RN [9]
RP STRUCTURE BY NMR OF 8-64, AND INTERACTION WITH CASK.
RX PubMed=15863617; DOI=10.1073/pnas.0409346102;
RA Feng W., Long J.-F., Zhang M.;
RT "A unified assembly mode revealed by the structures of tetrameric L27
RT domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:6861-6866(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 3-66 IN COMPLEX WITH HUMAN PALS1
RP AND RAT PATJ, AND IDENTIFICATION IN A COMPLEX WITH DLG1 AND CASK.
RX PubMed=22337881; DOI=10.1074/jbc.m111.321216;
RA Zhang J., Yang X., Wang Z., Zhou H., Xie X., Shen Y., Long J.;
RT "Structure of an L27 domain heterotrimer from cell polarity complex
RT Patj/Pals1/Mals2 reveals mutually independent L27 domain assembly mode.";
RL J. Biol. Chem. 287:11132-11140(2012).
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. May increase the
CC amplitude of ASIC3 acid-evoked currents by stabilizing the channel at
CC the cell surface. {ECO:0000269|PubMed:10846156,
CC ECO:0000269|PubMed:15317815}.
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). Forms a heterotrimeric complex composed
CC of MMP5, LIN7B and PATJ; the N-terminal L27 domain of PALS1 interacts
CC with the L27 domain of PATJ and the C-terminal L27 domain of PALS1
CC interacts with the L27 domain of LIN7B (PubMed:22337881). Forms a
CC heterotrimeric complex with DLG1 and CASK via their L27 domains
CC (PubMed:22337881, PubMed:15863617). Interacts with DLG4 and GRIN2B as
CC well as CDH1 and CTNNB1, the channels KCNJ12/Kir2.2, KCNJ4/Kir2.3 and
CC probably KCNJ2/Kir2.1 and SLC6A12/BGT-1 via its PDZ domain (By
CC similarity). The association of LIN7A with cadherin and beta-catenin is
CC calcium-dependent, occurs at synaptic junctions and requires the actin
CC cytoskeleton. Interacts with EGFR, ERBB2, ERBB3 and ERBB4 with both PDZ
CC and KID domains (By similarity). Associates with KIF17 via APBA1 (By
CC similarity). Interacts with ASIC3 (PubMed:15317815). Interacts with
CC TOPK. Interacts with RTKN (By similarity). Interacts with APBA1
CC (PubMed:15863617). Interacts with MPP7 (By similarity). Interacts with
CC DLG2 (PubMed:9753324). Interacts with DLG3 (PubMed:9753324).
CC {ECO:0000250|UniProtKB:Q9HAP6, ECO:0000250|UniProtKB:Q9Z252,
CC ECO:0000269|PubMed:10846156, ECO:0000269|PubMed:15317815,
CC ECO:0000269|PubMed:15863617, ECO:0000269|PubMed:22337881,
CC ECO:0000269|PubMed:9753324}.
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; predominantly in the vasa
CC recta. {ECO:0000269|PubMed:11742811, 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF087694; AAC78482.1; -; mRNA.
DR EMBL; AF173082; AAD48501.1; -; mRNA.
DR EMBL; BC031780; AAH31780.1; -; mRNA.
DR CCDS; CCDS21239.1; -.
DR RefSeq; NP_035828.1; NM_011698.1.
DR PDB; 1Y74; NMR; -; A/C=8-64.
DR PDB; 3UIT; X-ray; 2.05 A; A/B/C/D=3-66.
DR PDBsum; 1Y74; -.
DR PDBsum; 3UIT; -.
DR AlphaFoldDB; O88951; -.
DR SMR; O88951; -.
DR BioGRID; 204515; 6.
DR CORUM; O88951; -.
DR IntAct; O88951; 2.
DR STRING; 10090.ENSMUSP00000003971; -.
DR iPTMnet; O88951; -.
DR PhosphoSitePlus; O88951; -.
DR jPOST; O88951; -.
DR MaxQB; O88951; -.
DR PaxDb; O88951; -.
DR PeptideAtlas; O88951; -.
DR PRIDE; O88951; -.
DR ProteomicsDB; 265072; -.
DR Antibodypedia; 31908; 265 antibodies from 27 providers.
DR DNASU; 22342; -.
DR Ensembl; ENSMUST00000003971; ENSMUSP00000003971; ENSMUSG00000003872.
DR GeneID; 22342; -.
DR KEGG; mmu:22342; -.
DR UCSC; uc009guv.1; mouse.
DR CTD; 64130; -.
DR MGI; MGI:1330858; Lin7b.
DR VEuPathDB; HostDB:ENSMUSG00000003872; -.
DR eggNOG; KOG3550; Eukaryota.
DR GeneTree; ENSGT00940000153222; -.
DR HOGENOM; CLU_097962_0_0_1; -.
DR InParanoid; O88951; -.
DR OMA; YYHPGKE; -.
DR OrthoDB; 1335138at2759; -.
DR PhylomeDB; O88951; -.
DR TreeFam; TF316850; -.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR BioGRID-ORCS; 22342; 4 hits in 71 CRISPR screens.
DR EvolutionaryTrace; O88951; -.
DR PRO; PR:O88951; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O88951; protein.
DR Bgee; ENSMUSG00000003872; Expressed in facial nucleus and 143 other tissues.
DR ExpressionAtlas; O88951; baseline and differential.
DR Genevisible; O88951; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0097025; C:MPP7-DLG1-LIN7 complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
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; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
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 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 3D-structure; Cell junction; Cell membrane; Exocytosis; Membrane;
KW Postsynaptic cell membrane; Protein transport; Reference proteome; Synapse;
KW Tight junction; Transport.
FT CHAIN 1..207
FT /note="Protein lin-7 homolog B"
FT /id="PRO_0000189627"
FT DOMAIN 10..65
FT /note="L27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 93..175
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 187..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..13
FT /note="Kinase interacting site"
FT /evidence="ECO:0000250"
FT HELIX 7..27
FT /evidence="ECO:0007829|PDB:3UIT"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:3UIT"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:3UIT"
SQ SEQUENCE 207 AA; 22914 MW; BC6B6754B8C89F03 CRC64;
MAALVEPLGL ERDVSRAVEL LERLQRSGEL PPQKLQALQR VLQSRFCSAI REVYEQLYDT
LDITGSAEVR AHATAKATVA AFTASEGHAH PRVVELPKTD EGLGFNIMGG KEQNSPIYIS
RVIPGGVADR HGGLKRGDQL LSVNGVSVEG EHHEKAVELL KAAQGSVKLV VRYTPRVLEE
MEARFEKMRS ARRRQQHHSY TSLESRG
