LIN7B_RAT
ID LIN7B_RAT Reviewed; 207 AA.
AC Q9Z252;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 158.
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, Veli1a, Veli2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10362251; DOI=10.1038/sj.onc.1202652;
RA Irie M., Hata Y., Deguchi M., Ide N., Hirao K., Yao I., Nishioka H.,
RA Takai Y.;
RT "Isolation and characterization of mammalian homologues of Caenorhabditis
RT elegans lin-7: localization at cell-cell junctions.";
RL Oncogene 18:2811-2817(1999).
RN [2]
RP TISSUE SPECIFICITY, AND INTERACTION WITH CASK AND APBA1.
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 [3]
RP TISSUE SPECIFICITY, AND INTERACTION WITH DLG4 AND GRIN2B.
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 [4]
RP INDUCTION.
RX PubMed=12393911; DOI=10.1074/jbc.m207826200;
RA Sanna B., Kramer D., Genazzani A.A.;
RT "The expression of the PDZ protein MALS-1/velis is regulated by calcium and
RT calcineurin in cerebellar granule cells.";
RL J. Biol. Chem. 277:49585-49590(2002).
RN [5]
RP INTERACTION WITH CASK; APBA1 AND CASKIN1.
RX PubMed=12040031; DOI=10.1523/jneurosci.22-11-04264.2002;
RA Tabuchi K., Biederer T., Butz S., Suedhof T.C.;
RT "CASK participates in alternative tripartite complexes in which Mint 1
RT competes for binding with Caskin 1, a novel CASK-binding protein.";
RL J. Neurosci. 22:4264-4273(2002).
RN [6]
RP INTERACTION WITH KCNJ12; KIF17; CASK AND APBA1, AND FUNCTION.
RX PubMed=14960569; DOI=10.1074/jbc.m400284200;
RA Leonoudakis D., Conti L.R., Radeke C.M., McGuire L.M., Vandenberg C.A.;
RT "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and
RT Mint1 is associated with inward rectifier Kir2 potassium channels.";
RL J. Biol. Chem. 279:19051-19063(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).
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 (By similarity). This complex may have
CC the potential to couple synaptic vesicle exocytosis to cell adhesion in
CC brain. Ensures the proper localization of GRIN2B (subunit 2B of the
CC NMDA receptor) to neuronal postsynaptic density and may function in
CC localizing synaptic vesicles at synapses where it is recruited by beta-
CC catenin and cadherin. Required to localize Kir2 channels, GABA
CC transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the
CC basolateral membrane of epithelial cells. May increase the amplitude of
CC ASIC3 acid-evoked currents by stabilizing the channel at the cell
CC surface (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O88951,
CC ECO:0000269|PubMed:14960569}.
CC -!- SUBUNIT: Forms two exclusive ternary complexes with CASK and CASKIN1
CC (PubMed:12040031). The brain-specific heterotrimeric complex (LIN-10-
CC LIN-2-LIN-7 complex) composed of at least APBA1, CASK, and LIN7,
CC associates with the motor protein KIF17 to transport vesicles along
CC microtubules (By similarity). 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 (By similarity). Forms a
CC heterotrimeric complex with DLG1 and CASK via their L27 domains
CC (PubMed:9753324, PubMed:14960569). 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
CC (PubMed:10341223, PubMed:14960569). The association of LIN7A with
CC cadherin and beta-catenin is calcium-dependent, occurs at synaptic
CC junctions and requires the actin cytoskeleton. Interacts with EGFR,
CC ERBB2, ERBB3 and ERBB4 with both PDZ and KID domains (By similarity).
CC Associates with KIF17 via APBA1 (PubMed:14960569). Interacts with ASIC3
CC (By similarity). Interacts with TOPK. Interacts with RTKN (By
CC similarity). Interacts with APBA1 (PubMed:9753324, PubMed:14960569).
CC Interacts with MPP7 (By similarity). Interacts with DLG2 (By
CC similarity). Interacts with DLG3 (By similarity).
CC {ECO:0000250|UniProtKB:O88951, ECO:0000250|UniProtKB:Q9HAP6,
CC ECO:0000269|PubMed:10341223, ECO:0000269|PubMed:12040031,
CC ECO:0000269|PubMed:14960569, ECO:0000269|PubMed:9753324}.
CC -!- INTERACTION:
CC Q9Z252; Q6GMN2: Baiap2; NbExp=3; IntAct=EBI-7001699, EBI-6997402;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15494546};
CC Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Basolateral
CC cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Cell junction {ECO:0000269|PubMed:15494546}. Postsynaptic density
CC membrane {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 (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed only in brain.
CC {ECO:0000269|PubMed:10341223, ECO:0000269|PubMed:15494546,
CC ECO:0000269|PubMed:9753324}.
CC -!- INDUCTION: Up-regulated by cell depolarization and calcium entry
CC through L-type calcium channels. {ECO:0000269|PubMed:12393911}.
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; AF090133; AAC78072.1; -; mRNA.
DR RefSeq; NP_068526.1; NM_021758.1.
DR AlphaFoldDB; Q9Z252; -.
DR SMR; Q9Z252; -.
DR BioGRID; 248805; 2.
DR CORUM; Q9Z252; -.
DR IntAct; Q9Z252; 2.
DR MINT; Q9Z252; -.
DR STRING; 10116.ENSRNOP00000028164; -.
DR iPTMnet; Q9Z252; -.
DR PhosphoSitePlus; Q9Z252; -.
DR PaxDb; Q9Z252; -.
DR PRIDE; Q9Z252; -.
DR Ensembl; ENSRNOT00000028164; ENSRNOP00000028164; ENSRNOG00000020746.
DR GeneID; 60377; -.
DR KEGG; rno:60377; -.
DR CTD; 64130; -.
DR RGD; 620730; Lin7b.
DR eggNOG; KOG3550; Eukaryota.
DR GeneTree; ENSGT00940000153222; -.
DR HOGENOM; CLU_097962_0_0_1; -.
DR InParanoid; Q9Z252; -.
DR OMA; YYHPGKE; -.
DR OrthoDB; 1335138at2759; -.
DR PhylomeDB; Q9Z252; -.
DR TreeFam; TF316850; -.
DR Reactome; R-RNO-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR PRO; PR:Q9Z252; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020746; Expressed in frontal cortex and 12 other tissues.
DR Genevisible; Q9Z252; RN.
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; IDA:RGD.
DR GO; GO:0097025; C:MPP7-DLG1-LIN7 complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0097016; F:L27 domain binding; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; IDA:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0007043; P:cell-cell junction assembly; NAS:RGD.
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; ISO:RGD.
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 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_0000189628"
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"
SQ SEQUENCE 207 AA; 22900 MW; BC6B6754B8C89B13 CRC64;
MAALVEPLGL ERDVSRAVEL LERLQRSGEL PPQKLQALQR VLQSRFCSAI REVYEQLYDT
LDITGSAEVR AHATAKATVA AFTASEGHAH PRVVELPKTD EGLGFNIMGG KEQNSPIYIS
RVIPGGVADR HGGLKRGDQL LSVNGVSVEG EHHEKAVELL KAAQGSVKLV VRYTPRVLEE
MEARFEKMRS ARRRQQHHSY SSLESRG
