ID LIN7C_MOUSE Reviewed; 197 AA.
AC O88952;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 27-MAR-2024, entry version 183.
DE RecName: Full=Protein lin-7 homolog C;
DE Short=Lin-7C;
DE Short=mLin7C;
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 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.
RC TISSUE=Heart;
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=C57BL/6J; TISSUE=Cecum, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP PROTEIN SEQUENCE OF 169-184, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH SLC6A12.
RX PubMed=10710551; DOI=10.1152/ajprenal.2000.278.3.f464;
RA Straight S.W., Karnak D., Borg J.-P., Kamberov E., Dare H., Margolis B.,
RA Wade J.B.;
RT "mLin-7 is localized to the basolateral surface of renal epithelia via its
RT NH(2) terminus.";
RL Am. J. Physiol. 278:F464-F475(2000).
RN [7]
RP INTERACTION WITH PALS1.
RX PubMed=10753959; DOI=10.1074/jbc.275.15.11425;
RA Kamberov E., Makarova O., Roh M., Liu A., Karnak D., Straight S.,
RA Margolis B.;
RT "Molecular cloning and characterization of Pals, proteins associated with
RT mLin-7.";
RL J. Biol. Chem. 275:11425-11431(2000).
RN [8]
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 [9]
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 [10]
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 [11]
RP INTERACTION WITH MAPK12.
RX PubMed=15878399; DOI=10.1016/j.bbamcr.2004.11.008;
RA Court N.W., Ingley E., Klinken S.P., Bogoyevitch M.A.;
RT "Outer membrane protein 25-a mitochondrial anchor and inhibitor of stress-
RT activated protein kinase-3.";
RL Biochim. Biophys. Acta 1744:68-75(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Testis;
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}.
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 and GRIN2B as well as CDH1 and CTNNB1, the channels KCNJ12/Kir2.2,
CC KCNJ4/Kir2.3 and probably KCNJ2/Kir2.1 and SLC6A12/BGT-1 via its PDZ
CC domain. 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. 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. {ECO:0000250,
CC ECO:0000269|PubMed:10710551, ECO:0000269|PubMed:10753959,
CC ECO:0000269|PubMed:10846156, ECO:0000269|PubMed:15466885,
CC ECO:0000269|PubMed:15878399, ECO:0000269|PubMed:9753324}.
CC -!- INTERACTION:
CC O88952; Q08460: Kcnma1; NbExp=4; IntAct=EBI-821316, EBI-1633915;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Basolateral cell membrane; Peripheral membrane protein. Cell junction.
CC Postsynaptic density membrane; Peripheral membrane protein. Cell
CC junction, tight junction. Note=Mainly basolateral in renal epithelial
CC cells.
CC -!- TISSUE SPECIFICITY: Expressed in the kidney; particularly in the outer
CC medullary collecting duct. {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:0000269|PubMed:10710551}.
CC -!- SIMILARITY: Belongs to the lin-7 family. {ECO:0000305}.
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DR EMBL; AF087695; AAC78483.1; -; mRNA.
DR EMBL; AF173083; AAD48502.1; -; mRNA.
DR EMBL; AK015399; BAB29830.1; -; mRNA.
DR EMBL; AK078923; BAC37462.1; -; mRNA.
DR EMBL; BC046966; AAH46966.1; -; mRNA.
DR CCDS; CCDS16509.1; -.
DR RefSeq; NP_035829.1; NM_011699.3.
DR AlphaFoldDB; O88952; -.
DR SMR; O88952; -.
DR BioGRID; 204516; 51.
DR ComplexPortal; CPX-7742; LIN-10-LIN-2-LIN-7 complex, LIN7C variant.
DR IntAct; O88952; 25.
DR STRING; 10090.ENSMUSP00000028583; -.
DR iPTMnet; O88952; -.
DR PhosphoSitePlus; O88952; -.
DR SwissPalm; O88952; -.
DR EPD; O88952; -.
DR jPOST; O88952; -.
DR MaxQB; O88952; -.
DR PaxDb; 10090-ENSMUSP00000028583; -.
DR PeptideAtlas; O88952; -.
DR ProteomicsDB; 252477; -.
DR Pumba; O88952; -.
DR Antibodypedia; 25423; 154 antibodies from 27 providers.
DR DNASU; 22343; -.
DR Ensembl; ENSMUST00000028583.8; ENSMUSP00000028583.8; ENSMUSG00000027162.8.
DR GeneID; 22343; -.
DR KEGG; mmu:22343; -.
DR UCSC; uc008lmo.1; mouse.
DR AGR; MGI:1330839; -.
DR CTD; 55327; -.
DR MGI; MGI:1330839; Lin7c.
DR VEuPathDB; HostDB:ENSMUSG00000027162; -.
DR eggNOG; KOG3550; Eukaryota.
DR GeneTree; ENSGT00940000153222; -.
DR HOGENOM; CLU_097962_0_0_1; -.
DR InParanoid; O88952; -.
DR OMA; ARRRTNY; -.
DR OrthoDB; 4175920at2759; -.
DR PhylomeDB; O88952; -.
DR TreeFam; TF316850; -.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR BioGRID-ORCS; 22343; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Lin7c; mouse.
DR PRO; PR:O88952; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O88952; Protein.
DR Bgee; ENSMUSG00000027162; Expressed in olfactory epithelium and 255 other cell types or tissues.
DR Genevisible; O88952; 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:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0097025; C:MPP7-DLG1-LIN7 complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO: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; IDA:MGI.
DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0097016; F:L27 domain binding; ISO:MGI.
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:0002011; P:morphogenesis of an epithelial sheet; ISO:MGI.
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 CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.10.287.650; L27 domain; 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 PANTHER; PTHR14063; PROTEIN LIN-7 HOMOLOG; 1.
DR PANTHER; PTHR14063:SF5; PROTEIN LIN-7 HOMOLOG C; 1.
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; L27 domain; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 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_0000189630"
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
//
