LIN7C_RAT
ID LIN7C_RAT Reviewed; 197 AA.
AC Q792I0;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein lin-7 homolog C;
DE Short=Lin-7C;
DE AltName: Full=Mammalian lin-seven protein 3;
DE Short=MALS-3;
DE AltName: Full=Vertebrate lin-7 homolog 3;
DE Short=Veli-3;
GN Name=Lin7c; Synonyms=Mals3, Veli3;
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 PROTEIN SEQUENCE OF 52-70; 77-121 AND 136-155, AND INTERACTION WITH KCNJ12.
RX PubMed=15024025; DOI=10.1074/jbc.m400285200;
RA Leonoudakis D., Conti L.R., Anderson S., Radeke C.M., McGuire L.M.,
RA Adams M.E., Froehner S.C., Yates J.R. III, Vandenberg C.A.;
RT "Protein trafficking and anchoring complexes revealed by proteomic analysis
RT of inward rectifier potassium channel (Kir2.x)-associated proteins.";
RL J. Biol. Chem. 279:22331-22346(2004).
RN [3]
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 [4]
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 [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; CASK; APBA1 AND DLG1, 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.
CC {ECO:0000250|UniProtKB:O88952, ECO:0000269|PubMed:14960569}.
CC -!- SUBUNIT: Forms a complex with CASK and APBA1 or CASKIN1. Component of
CC the brain-specific heterotrimeric complex (LIN-10-LIN-2-LIN-7 complex)
CC composed of at least APBA1, CASK, and LIN7, which associates with the
CC motor protein KIF17 to transport vesicles along microtubules (By
CC similarity). Can also interact with other modular proteins containing
CC protein-protein interaction domains like PALS1, PALS2, MPP7, DLG1, DLG2
CC and DLG3 through its L27 domain. Interacts with DLG4 and GRIN2B as well
CC 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. The
CC association of LIN7A with cadherin and beta-catenin is calcium-
CC 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. Associates with KIF17 via APBA1. Interacts with HTR4.
CC Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or
CC LIN7C) (By similarity). Interacts with MAPK12 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:O88952}.
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 {ECO:0000250}.
CC Postsynaptic density membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}.
CC Note=Mainly basolateral in renal epithelial cells. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney (outer medullary
CC collecting duct) and liver with weak expression in thymus and heart.
CC {ECO:0000269|PubMed:10341223, ECO:0000269|PubMed:15494546,
CC ECO:0000269|PubMed:9753324}.
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; AF090136; AAC78075.1; -; mRNA.
DR RefSeq; NP_068623.1; NM_021851.1.
DR AlphaFoldDB; Q792I0; -.
DR SMR; Q792I0; -.
DR BioGRID; 248835; 1.
DR CORUM; Q792I0; -.
DR IntAct; Q792I0; 4.
DR STRING; 10116.ENSRNOP00000065941; -.
DR iPTMnet; Q792I0; -.
DR PhosphoSitePlus; Q792I0; -.
DR PaxDb; Q792I0; -.
DR PRIDE; Q792I0; -.
DR Ensembl; ENSRNOT00000103172; ENSRNOP00000093334; ENSRNOG00000062543.
DR GeneID; 60442; -.
DR KEGG; rno:60442; -.
DR UCSC; RGD:621164; rat.
DR CTD; 55327; -.
DR RGD; 621164; Lin7c.
DR eggNOG; KOG3550; Eukaryota.
DR GeneTree; ENSGT00940000153222; -.
DR HOGENOM; CLU_097962_0_0_1; -.
DR InParanoid; Q792I0; -.
DR OMA; MENRFER; -.
DR OrthoDB; 1335138at2759; -.
DR PhylomeDB; Q792I0; -.
DR TreeFam; TF316850; -.
DR Reactome; R-RNO-212676; Dopamine Neurotransmitter Release Cycle.
DR PRO; PR:Q792I0; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000045698; Expressed in jejunum and 19 other tissues.
DR Genevisible; Q792I0; 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:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0097025; C:MPP7-DLG1-LIN7 complex; ISO:RGD.
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:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR GO; GO:0097016; F:L27 domain binding; ISO:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO: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:0002011; P:morphogenesis of an epithelial sheet; ISO:RGD.
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 Acetylation; Cell junction; Cell membrane; Direct protein sequencing;
KW Exocytosis; Membrane; Postsynaptic cell membrane; Protein transport;
KW Reference proteome; Synapse; Tight junction; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NUP9"
FT CHAIN 2..197
FT /note="Protein lin-7 homolog C"
FT /id="PRO_0000189631"
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 MOTIF 2..13
FT /note="Kinase interacting site"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUP9"
SQ SEQUENCE 197 AA; 21834 MW; 7410FBFA3BD24F45 CRC64;
MAALGEPVRL ERDICRAIEL LEKLQRSGEV PPQKLQALQR VLQSEFCNAV REVYEHVYET
VDISSSPEVR ANATAKATVA AFAASEGHSH PRVVELPKTE EGLGFNIMGG KEQNSPIYIS
RIIPGGIADR HGGLKRGDQL LSVNGVSVEG EHHEKAVELL KAAQGKVKLV VRYTPKVLEE
MESRFEKMRS AKRRQQT
