Full text data of LIN7C
LIN7C
(MALS3, VELI3)
[Confidence: low (only semi-automatic identification from reviews)]
Protein lin-7 homolog C; Lin-7C (Mammalian lin-seven protein 3; MALS-3; Vertebrate lin-7 homolog 3; Veli-3)
Protein lin-7 homolog C; Lin-7C (Mammalian lin-seven protein 3; MALS-3; Vertebrate lin-7 homolog 3; Veli-3)
UniProt
Q9NUP9
ID LIN7C_HUMAN Reviewed; 197 AA.
AC Q9NUP9;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 114.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-12; 17-23 AND 77-92, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Osteosarcoma;
RA Bienvenut W.V., Lao L., Ryan K.M.;
RL Submitted (JUN-2009) to UniProtKB.
RN [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH EGFR.
RX PubMed=12967566; DOI=10.1016/j.devcel.2003.08.001;
RA Shelly M., Mosesson Y., Citri A., Lavi S., Zwang Y., Melamed-Book N.,
RA Aroeti B., Yarden Y.;
RT "Polar expression of ErbB-2/HER2 in epithelia. Bimodal regulation by
RT Lin-7.";
RL Dev. Cell 5:475-486(2003).
RN [5]
RP INTERACTION WITH DLG1 AND MPP7.
RX PubMed=17237226; DOI=10.1074/jbc.M610002200;
RA Bohl J., Brimer N., Lyons C., Vande Pol S.B.;
RT "The stardust family protein MPP7 forms a tripartite complex with LIN7
RT and DLG1 that regulates the stability and localization of DLG1 to cell
RT junctions.";
RL J. Biol. Chem. 282:9392-9400(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Plays a role in establishing and maintaining the
CC asymmetric distribution of channels and receptors at the plasma
CC membrane of polarized cells. Forms membrane-associated
CC multiprotein complexes that may regulate delivery and recycling of
CC proteins to the correct membrane domains. The tripartite complex
CC composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have
CC the potential to couple synaptic vesicle exocytosis to cell
CC adhesion in brain. Ensures the proper localization of GRIN2B
CC (subunit 2B of the NMDA receptor) to neuronal postsynaptic density
CC and may function in localizing synaptic vesicles at synapses where
CC it is recruited by beta-catenin and cadherin. Required to localize
CC Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2,
CC ERBB3 and ERBB4 to the basolateral membrane of epithelial cells.
CC -!- SUBUNIT: Forms two exclusive ternary complexes with CASK and APBA1
CC or CASKIN1 (By similarity). Can also interact with other modular
CC proteins containing protein-protein interaction domains like MPP5,
CC MPP6, MPP7, DLG1, DLG2 and DLG3 through its L27 domain. Interacts
CC with DLG4 and GRIN2B as well as CDH1 and CTNNB1, the channels
CC KCNJ12/Kir2.2, KCNJ4/Kir2.3 and probably KCNJ2/Kir2.1 and
CC SLC6A12/BGT-1 via its PDZ domain. 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
CC EGFR, ERBB2, ERBB3 and ERBB4 with both PDZ and KID domains.
CC Associates with KIF17 via APBA1. Interacts with HTR4 (By
CC similarity). Forms a tripartite complex composed of DLG1, MPP7 and
CC LIN7 (LIN7A or LIN7C). Interacts with MAPK12 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Basolateral cell membrane; Peripheral membrane protein. Cell
CC junction (By similarity). Cell junction, synapse, postsynaptic
CC cell membrane, postsynaptic density; Peripheral membrane protein
CC (By similarity). Cell junction, tight junction (By similarity).
CC Cell junction, synapse, synaptosome (By similarity). Note=Enriched
CC in synaptosomes and at epithelial cell-cell junctions (By
CC similarity). Mainly basolateral in renal epithelial cells.
CC -!- DOMAIN: The kinase interacting site is required for proper
CC delivery of ERBB2 to the basolateral membrane (By similarity).
CC -!- DOMAIN: The PDZ domain regulates endocytosis and recycling of the
CC receptor at the membrane (By similarity).
CC -!- DOMAIN: The L27 domain mediates interaction with CASK and is
CC involved in the formation of multimeric complexes and the
CC association of LIN7 to membranes (By similarity).
CC -!- SIMILARITY: Belongs to the lin-7 family.
CC -!- SIMILARITY: Contains 1 L27 domain.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK002077; BAA92072.1; -; mRNA.
DR EMBL; BC053907; AAH53907.1; -; mRNA.
DR RefSeq; NP_060832.1; NM_018362.3.
DR UniGene; Hs.91393; -.
DR PDB; 3LRA; X-ray; 2.95 A; A=3-64.
DR PDBsum; 3LRA; -.
DR ProteinModelPortal; Q9NUP9; -.
DR SMR; Q9NUP9; 3-64, 93-175.
DR IntAct; Q9NUP9; 8.
DR MINT; MINT-5002028; -.
DR STRING; 9606.ENSP00000278193; -.
DR PhosphoSite; Q9NUP9; -.
DR DMDM; 59798474; -.
DR PaxDb; Q9NUP9; -.
DR PeptideAtlas; Q9NUP9; -.
DR PRIDE; Q9NUP9; -.
DR Ensembl; ENST00000278193; ENSP00000278193; ENSG00000148943.
DR GeneID; 55327; -.
DR KEGG; hsa:55327; -.
DR UCSC; uc001mrl.3; human.
DR CTD; 55327; -.
DR GeneCards; GC11M027472; -.
DR HGNC; HGNC:17789; LIN7C.
DR HPA; HPA051118; -.
DR MIM; 612332; gene.
DR neXtProt; NX_Q9NUP9; -.
DR PharmGKB; PA134891786; -.
DR eggNOG; NOG320117; -.
DR HOGENOM; HOG000285929; -.
DR HOVERGEN; HBG052329; -.
DR InParanoid; Q9NUP9; -.
DR OMA; VDINSSP; -.
DR OrthoDB; EOG75MVXG; -.
DR PhylomeDB; Q9NUP9; -.
DR EvolutionaryTrace; Q9NUP9; -.
DR GeneWiki; LIN7C; -.
DR GenomeRNAi; 55327; -.
DR NextBio; 59604; -.
DR PRO; PR:Q9NUP9; -.
DR ArrayExpress; Q9NUP9; -.
DR Bgee; Q9NUP9; -.
DR CleanEx; HS_LIN7C; -.
DR Genevestigator; Q9NUP9; -.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007269; P:neurotransmitter secretion; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR004172; L27.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR017365; Lin-7_homologue.
DR InterPro; IPR001478; PDZ.
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; SSF50156; SSF50156; 1.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell junction; Cell membrane;
KW Complete proteome; Direct protein sequencing; Exocytosis; Membrane;
KW Postsynaptic cell membrane; Protein transport; Reference proteome;
KW Synapse; Synaptosome; Tight junction; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 197 Protein lin-7 homolog C.
FT /FTId=PRO_0000189629.
FT DOMAIN 10 65 L27.
FT DOMAIN 93 175 PDZ.
FT MOTIF 2 13 Kinase interacting site (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT HELIX 7 26
FT HELIX 33 43
FT HELIX 45 60
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
//
ID LIN7C_HUMAN Reviewed; 197 AA.
AC Q9NUP9;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 114.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-12; 17-23 AND 77-92, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Osteosarcoma;
RA Bienvenut W.V., Lao L., Ryan K.M.;
RL Submitted (JUN-2009) to UniProtKB.
RN [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH EGFR.
RX PubMed=12967566; DOI=10.1016/j.devcel.2003.08.001;
RA Shelly M., Mosesson Y., Citri A., Lavi S., Zwang Y., Melamed-Book N.,
RA Aroeti B., Yarden Y.;
RT "Polar expression of ErbB-2/HER2 in epithelia. Bimodal regulation by
RT Lin-7.";
RL Dev. Cell 5:475-486(2003).
RN [5]
RP INTERACTION WITH DLG1 AND MPP7.
RX PubMed=17237226; DOI=10.1074/jbc.M610002200;
RA Bohl J., Brimer N., Lyons C., Vande Pol S.B.;
RT "The stardust family protein MPP7 forms a tripartite complex with LIN7
RT and DLG1 that regulates the stability and localization of DLG1 to cell
RT junctions.";
RL J. Biol. Chem. 282:9392-9400(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Plays a role in establishing and maintaining the
CC asymmetric distribution of channels and receptors at the plasma
CC membrane of polarized cells. Forms membrane-associated
CC multiprotein complexes that may regulate delivery and recycling of
CC proteins to the correct membrane domains. The tripartite complex
CC composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have
CC the potential to couple synaptic vesicle exocytosis to cell
CC adhesion in brain. Ensures the proper localization of GRIN2B
CC (subunit 2B of the NMDA receptor) to neuronal postsynaptic density
CC and may function in localizing synaptic vesicles at synapses where
CC it is recruited by beta-catenin and cadherin. Required to localize
CC Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2,
CC ERBB3 and ERBB4 to the basolateral membrane of epithelial cells.
CC -!- SUBUNIT: Forms two exclusive ternary complexes with CASK and APBA1
CC or CASKIN1 (By similarity). Can also interact with other modular
CC proteins containing protein-protein interaction domains like MPP5,
CC MPP6, MPP7, DLG1, DLG2 and DLG3 through its L27 domain. Interacts
CC with DLG4 and GRIN2B as well as CDH1 and CTNNB1, the channels
CC KCNJ12/Kir2.2, KCNJ4/Kir2.3 and probably KCNJ2/Kir2.1 and
CC SLC6A12/BGT-1 via its PDZ domain. 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
CC EGFR, ERBB2, ERBB3 and ERBB4 with both PDZ and KID domains.
CC Associates with KIF17 via APBA1. Interacts with HTR4 (By
CC similarity). Forms a tripartite complex composed of DLG1, MPP7 and
CC LIN7 (LIN7A or LIN7C). Interacts with MAPK12 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Basolateral cell membrane; Peripheral membrane protein. Cell
CC junction (By similarity). Cell junction, synapse, postsynaptic
CC cell membrane, postsynaptic density; Peripheral membrane protein
CC (By similarity). Cell junction, tight junction (By similarity).
CC Cell junction, synapse, synaptosome (By similarity). Note=Enriched
CC in synaptosomes and at epithelial cell-cell junctions (By
CC similarity). Mainly basolateral in renal epithelial cells.
CC -!- DOMAIN: The kinase interacting site is required for proper
CC delivery of ERBB2 to the basolateral membrane (By similarity).
CC -!- DOMAIN: The PDZ domain regulates endocytosis and recycling of the
CC receptor at the membrane (By similarity).
CC -!- DOMAIN: The L27 domain mediates interaction with CASK and is
CC involved in the formation of multimeric complexes and the
CC association of LIN7 to membranes (By similarity).
CC -!- SIMILARITY: Belongs to the lin-7 family.
CC -!- SIMILARITY: Contains 1 L27 domain.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK002077; BAA92072.1; -; mRNA.
DR EMBL; BC053907; AAH53907.1; -; mRNA.
DR RefSeq; NP_060832.1; NM_018362.3.
DR UniGene; Hs.91393; -.
DR PDB; 3LRA; X-ray; 2.95 A; A=3-64.
DR PDBsum; 3LRA; -.
DR ProteinModelPortal; Q9NUP9; -.
DR SMR; Q9NUP9; 3-64, 93-175.
DR IntAct; Q9NUP9; 8.
DR MINT; MINT-5002028; -.
DR STRING; 9606.ENSP00000278193; -.
DR PhosphoSite; Q9NUP9; -.
DR DMDM; 59798474; -.
DR PaxDb; Q9NUP9; -.
DR PeptideAtlas; Q9NUP9; -.
DR PRIDE; Q9NUP9; -.
DR Ensembl; ENST00000278193; ENSP00000278193; ENSG00000148943.
DR GeneID; 55327; -.
DR KEGG; hsa:55327; -.
DR UCSC; uc001mrl.3; human.
DR CTD; 55327; -.
DR GeneCards; GC11M027472; -.
DR HGNC; HGNC:17789; LIN7C.
DR HPA; HPA051118; -.
DR MIM; 612332; gene.
DR neXtProt; NX_Q9NUP9; -.
DR PharmGKB; PA134891786; -.
DR eggNOG; NOG320117; -.
DR HOGENOM; HOG000285929; -.
DR HOVERGEN; HBG052329; -.
DR InParanoid; Q9NUP9; -.
DR OMA; VDINSSP; -.
DR OrthoDB; EOG75MVXG; -.
DR PhylomeDB; Q9NUP9; -.
DR EvolutionaryTrace; Q9NUP9; -.
DR GeneWiki; LIN7C; -.
DR GenomeRNAi; 55327; -.
DR NextBio; 59604; -.
DR PRO; PR:Q9NUP9; -.
DR ArrayExpress; Q9NUP9; -.
DR Bgee; Q9NUP9; -.
DR CleanEx; HS_LIN7C; -.
DR Genevestigator; Q9NUP9; -.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007269; P:neurotransmitter secretion; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR004172; L27.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR017365; Lin-7_homologue.
DR InterPro; IPR001478; PDZ.
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; SSF50156; SSF50156; 1.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell junction; Cell membrane;
KW Complete proteome; Direct protein sequencing; Exocytosis; Membrane;
KW Postsynaptic cell membrane; Protein transport; Reference proteome;
KW Synapse; Synaptosome; Tight junction; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 197 Protein lin-7 homolog C.
FT /FTId=PRO_0000189629.
FT DOMAIN 10 65 L27.
FT DOMAIN 93 175 PDZ.
FT MOTIF 2 13 Kinase interacting site (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT HELIX 7 26
FT HELIX 33 43
FT HELIX 45 60
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
//
MIM
612332
*RECORD*
*FIELD* NO
612332
*FIELD* TI
*612332 LIN7, C. ELEGANS, HOMOLOG OF, C; LIN7C
;;VERTEBRATE LIN7 HOMOLOG 3; VELI3;;
read moreMAMMALIAN LIN7 HOMOLOG 3; MALS3
*FIELD* TX
CLONING
By searching EST databases for homologs of C. elegans Lin7, Butz et al.
(1998) identified murine Lin7c, which they called Veli3. The deduced
197-amino acid Veli3 protein has a C-terminal PDZ domain.
By Northern blot analysis, Jo et al. (1999) found that rat Lin7c, which
they called Mals3, showed highest expression in kidney, followed by
brain and liver. Weak expression was detected in thymus and heart, and
no expression was detected in spleen. Mals3 had an apparent molecular
mass of 25 kD by Western blot analysis.
By immunohistochemistry and in situ hybridization using antibodies and
cRNAs specific for mouse Mals1 (LIN7A; 603380), Mals2 (LIN7B; 612331),
and Mals3, Misawa et al. (2001) showed that each Mals protein localized
to distinct brain regions. The Mals proteins were predominantly
expressed in both neuronal cell bodies and neuropil, and they were not
detected in most nonneuronal cells in brain.
GENE FUNCTION
Butz et al. (1998) identified a complex of 3 proteins in rat brain that
had the potential to couple synaptic vesicle exocytosis to neuronal cell
adhesion. The 3 proteins were Cask (300172), a protein related to
membrane-associated guanylate kinases (MAGUKs); Mint1 (APBA1; 602414), a
putative vesicular trafficking protein; and the Velis. Cask, Mint1, and
the Velis formed a tight, salt-resistant complex. Butz et al. (1998)
determined that the N-terminal domains of Cask, Mint1, and the Velis
were involved in complex formation, leaving their C-terminal PDZ domains
free to recruit adhesion molecules, receptors, and channels to the
complex. Butz et al. (1998) proposed that the tripartite complex acts as
a nucleation site for the assembly of proteins involved in synaptic
vesicle exocytosis and synaptic junctions.
Jo et al. (1999) found that rat Mals proteins immunoprecipitated with
Psd95 (DLG4; 602887) and NMDA receptor-2B (GRIN2B; 138252) from
solubilized rat cerebral cortex membranes.
Misawa et al. (2001) found that Mals1 -/- Mals2 -/- double-knockout mice
appeared normal and showed normal excitatory synaptic activity in the
CA1 region of the hippocampus. Mals3 expression was upregulated in most
brain regions of the double-knockout mice, suggesting that Mals3 may
compensate for loss of Mals1 and Mals2 expression.
Aartsen et al. (2006) found that Mpp4 -/- mouse retinas showed
downregulation of Psd95 and mislocalization of both Psd95 and Veli3 at
the photoreceptor presynaptic membrane. They proposed that MPP4 may
function as a recruitment factor to organize signal transducers at the
photoreceptor synapse.
Onda et al. (2007) found that the expression of LIN7C was downregulated
in oral squamous cell carcinomas (OSCC; see 275355) compared with normal
oral keratinocytes. Overexpression of LIN7C in OSCC cells resulted in a
noninvasive phenotype with elevated beta-catenin (CTNNB1; 116806)
expression. In immunodeficient mice, tumor cells expressing LIN7C showed
reduced metastases. Onda et al. (2007) concluded that LIN7C in a tumor
suppressor that functions in the beta-catenin signaling pathway.
MAPPING
By genomic sequence analysis, Taylor et al. (2006) mapped the LIN7C gene
to chromosome 11p14.1.
*FIELD* RF
1. Aartsen, W. M.; Kantardzhieva, A.; Klooster, J.; van Rossum, A.
G. S. H.; van de Pavert, S. A.; Versteeg, I.; Cardozo, B. N.; Tonagel,
F.; Beck, S. C.; Tanimoto, N.; Seeliger, M. W.; Wijnholds, J.: Mpp4
recruits Psd95 and Veli3 towards the photoreceptor synapse. Hum.
Molec. Genet. 15: 1291-1302, 2006.
2. Butz, S.; Okamoto, M.; Sudhof, T. C.: A tripartite protein complex
with the potential to couple synaptic vesicle exocytosis to cell adhesion
in brain. Cell 94: 773-782, 1998.
3. Jo, K.; Derin, R.; Li, M.; Bredt, D. S.: Characterization of MALS/Velis-1,
-2, and -3: a family of mammalian LIN-7 homologs enriched at brain
synapses in association with the postsynaptic density-95/NMDA receptor
postsynaptic complex. J. Neurosci. 19: 4189-4199, 1999.
4. Misawa, H.; Kawasaki, Y.; Mellor, J.; Sweeney, N.; Jo, K.; Nicoll,
R. A.; Bredt, D. S.: Contrasting localizations of MALS/LIN-7 PDZ
proteins in brain and molecular compensation in knockout mice. J.
Biol. Chem. 276: 9264-9272, 2001.
5. Onda, T.; Uzawa, K.; Nakashima, D.; Saito, K.; Iwadate, Y.; Seki,
N.; Shibahara, T.; Tanzawa, H.: Lin-7C/VELI3/MALS-3: an essential
component in metastasis of human squamous cell carcinoma. Cancer
Res. 67: 9643-9648, 2007.
6. Taylor, T. D.; Noguchi, H.; Totoki, Y.; Toyoda, A.; Kuroki, Y.;
Dewar, K.; Lloyd, C.; Itoh, T.; Takeda, T.; Kim, D.-W.; She, X.; Barlow,
K. F.; and 22 others: Human chromosome 11 DNA sequence and analysis
including novel gene identification. Nature 440: 497-500, 2006.
*FIELD* CN
Patricia A. Hartz - updated: 10/28/2010
*FIELD* CD
Patricia A. Hartz: 9/29/2008
*FIELD* ED
mgross: 11/10/2010
terry: 10/28/2010
mgross: 9/30/2008
mgross: 9/29/2008
*RECORD*
*FIELD* NO
612332
*FIELD* TI
*612332 LIN7, C. ELEGANS, HOMOLOG OF, C; LIN7C
;;VERTEBRATE LIN7 HOMOLOG 3; VELI3;;
read moreMAMMALIAN LIN7 HOMOLOG 3; MALS3
*FIELD* TX
CLONING
By searching EST databases for homologs of C. elegans Lin7, Butz et al.
(1998) identified murine Lin7c, which they called Veli3. The deduced
197-amino acid Veli3 protein has a C-terminal PDZ domain.
By Northern blot analysis, Jo et al. (1999) found that rat Lin7c, which
they called Mals3, showed highest expression in kidney, followed by
brain and liver. Weak expression was detected in thymus and heart, and
no expression was detected in spleen. Mals3 had an apparent molecular
mass of 25 kD by Western blot analysis.
By immunohistochemistry and in situ hybridization using antibodies and
cRNAs specific for mouse Mals1 (LIN7A; 603380), Mals2 (LIN7B; 612331),
and Mals3, Misawa et al. (2001) showed that each Mals protein localized
to distinct brain regions. The Mals proteins were predominantly
expressed in both neuronal cell bodies and neuropil, and they were not
detected in most nonneuronal cells in brain.
GENE FUNCTION
Butz et al. (1998) identified a complex of 3 proteins in rat brain that
had the potential to couple synaptic vesicle exocytosis to neuronal cell
adhesion. The 3 proteins were Cask (300172), a protein related to
membrane-associated guanylate kinases (MAGUKs); Mint1 (APBA1; 602414), a
putative vesicular trafficking protein; and the Velis. Cask, Mint1, and
the Velis formed a tight, salt-resistant complex. Butz et al. (1998)
determined that the N-terminal domains of Cask, Mint1, and the Velis
were involved in complex formation, leaving their C-terminal PDZ domains
free to recruit adhesion molecules, receptors, and channels to the
complex. Butz et al. (1998) proposed that the tripartite complex acts as
a nucleation site for the assembly of proteins involved in synaptic
vesicle exocytosis and synaptic junctions.
Jo et al. (1999) found that rat Mals proteins immunoprecipitated with
Psd95 (DLG4; 602887) and NMDA receptor-2B (GRIN2B; 138252) from
solubilized rat cerebral cortex membranes.
Misawa et al. (2001) found that Mals1 -/- Mals2 -/- double-knockout mice
appeared normal and showed normal excitatory synaptic activity in the
CA1 region of the hippocampus. Mals3 expression was upregulated in most
brain regions of the double-knockout mice, suggesting that Mals3 may
compensate for loss of Mals1 and Mals2 expression.
Aartsen et al. (2006) found that Mpp4 -/- mouse retinas showed
downregulation of Psd95 and mislocalization of both Psd95 and Veli3 at
the photoreceptor presynaptic membrane. They proposed that MPP4 may
function as a recruitment factor to organize signal transducers at the
photoreceptor synapse.
Onda et al. (2007) found that the expression of LIN7C was downregulated
in oral squamous cell carcinomas (OSCC; see 275355) compared with normal
oral keratinocytes. Overexpression of LIN7C in OSCC cells resulted in a
noninvasive phenotype with elevated beta-catenin (CTNNB1; 116806)
expression. In immunodeficient mice, tumor cells expressing LIN7C showed
reduced metastases. Onda et al. (2007) concluded that LIN7C in a tumor
suppressor that functions in the beta-catenin signaling pathway.
MAPPING
By genomic sequence analysis, Taylor et al. (2006) mapped the LIN7C gene
to chromosome 11p14.1.
*FIELD* RF
1. Aartsen, W. M.; Kantardzhieva, A.; Klooster, J.; van Rossum, A.
G. S. H.; van de Pavert, S. A.; Versteeg, I.; Cardozo, B. N.; Tonagel,
F.; Beck, S. C.; Tanimoto, N.; Seeliger, M. W.; Wijnholds, J.: Mpp4
recruits Psd95 and Veli3 towards the photoreceptor synapse. Hum.
Molec. Genet. 15: 1291-1302, 2006.
2. Butz, S.; Okamoto, M.; Sudhof, T. C.: A tripartite protein complex
with the potential to couple synaptic vesicle exocytosis to cell adhesion
in brain. Cell 94: 773-782, 1998.
3. Jo, K.; Derin, R.; Li, M.; Bredt, D. S.: Characterization of MALS/Velis-1,
-2, and -3: a family of mammalian LIN-7 homologs enriched at brain
synapses in association with the postsynaptic density-95/NMDA receptor
postsynaptic complex. J. Neurosci. 19: 4189-4199, 1999.
4. Misawa, H.; Kawasaki, Y.; Mellor, J.; Sweeney, N.; Jo, K.; Nicoll,
R. A.; Bredt, D. S.: Contrasting localizations of MALS/LIN-7 PDZ
proteins in brain and molecular compensation in knockout mice. J.
Biol. Chem. 276: 9264-9272, 2001.
5. Onda, T.; Uzawa, K.; Nakashima, D.; Saito, K.; Iwadate, Y.; Seki,
N.; Shibahara, T.; Tanzawa, H.: Lin-7C/VELI3/MALS-3: an essential
component in metastasis of human squamous cell carcinoma. Cancer
Res. 67: 9643-9648, 2007.
6. Taylor, T. D.; Noguchi, H.; Totoki, Y.; Toyoda, A.; Kuroki, Y.;
Dewar, K.; Lloyd, C.; Itoh, T.; Takeda, T.; Kim, D.-W.; She, X.; Barlow,
K. F.; and 22 others: Human chromosome 11 DNA sequence and analysis
including novel gene identification. Nature 440: 497-500, 2006.
*FIELD* CN
Patricia A. Hartz - updated: 10/28/2010
*FIELD* CD
Patricia A. Hartz: 9/29/2008
*FIELD* ED
mgross: 11/10/2010
terry: 10/28/2010
mgross: 9/30/2008
mgross: 9/29/2008