E41L3_HUMAN
ID E41L3_HUMAN Reviewed; 1087 AA.
AC Q9Y2J2; B7Z4I5; F5GX05; O95713; Q9BRP5;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Band 4.1-like protein 3;
DE AltName: Full=4.1B;
DE AltName: Full=Differentially expressed in adenocarcinoma of the lung protein 1;
DE Short=DAL-1;
DE AltName: Full=Erythrocyte membrane protein band 4.1-like 3 {ECO:0000312|HGNC:HGNC:3380};
DE Contains:
DE RecName: Full=Band 4.1-like protein 3, N-terminally processed;
GN Name=EPB41L3 {ECO:0000312|HGNC:HGNC:3380};
GN Synonyms=DAL1 {ECO:0000312|HGNC:HGNC:3380},
GN KIAA0987 {ECO:0000312|HGNC:HGNC:3380};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=9892180;
RA Tran Y.K., Boegler O., Gorse K.M., Wieland I., Green M.R., Newsham I.F.;
RT "A novel member of the NF2/ERM/4.1 superfamily with growth suppressing
RT properties in lung cancer.";
RL Cancer Res. 59:35-43(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [6]
RP INTERACTION WITH CADM1.
RX PubMed=12234973;
RA Yageta M., Kuramochi M., Masuda M., Fukami T., Fukuhara H., Maruyama T.,
RA Shibuya M., Murakami Y.;
RT "Direct association of TSLC1 and DAL-1, two distinct tumor suppressor
RT proteins in lung cancer.";
RL Cancer Res. 62:5129-5133(2002).
RN [7]
RP FUNCTION, AND INTERACTION WITH PRMT3; PRMT5 AND PRMT6.
RX PubMed=15334060; DOI=10.1038/sj.onc.1208057;
RA Singh V., Miranda T.B., Jiang W., Frankel A., Roemer M.E., Robb V.A.,
RA Gutmann D.H., Herschman H.R., Clarke S., Newsham I.F.;
RT "DAL-1/4.1B tumor suppressor interacts with protein arginine N-
RT methyltransferase 3 (PRMT3) and inhibits its ability to methylate
RT substrates in vitro and in vivo.";
RL Oncogene 23:7761-7771(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH PRMT5.
RX PubMed=15737618; DOI=10.1016/j.bbrc.2005.01.153;
RA Jiang W., Roemer M.E., Newsham I.F.;
RT "The tumor suppressor DAL-1/4.1B modulates protein arginine N-
RT methyltransferase 5 activity in a substrate-specific manner.";
RL Biochem. Biophys. Res. Commun. 329:522-530(2005).
RN [9]
RP FUNCTION.
RX PubMed=16420693; DOI=10.1186/1476-4598-5-4;
RA Jiang W., Newsham I.F.;
RT "The tumor suppressor DAL-1/4.1B and protein methylation cooperate in
RT inducing apoptosis in MCF-7 breast cancer cells.";
RL Mol. Cancer 5:4-4(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-962, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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., Buerckstuemmer T.,
RA 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND THR-469, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND SER-962, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 108-390 IN COMPLEX WITH CADM1, AND
RP INTERACTION WITH CADM1.
RX PubMed=21131357; DOI=10.1074/jbc.m110.174011;
RA Busam R.D., Thorsell A.G., Flores A., Hammarstrom M., Persson C.,
RA Obrink B., Hallberg B.M.;
RT "Structural basis of tumor suppressor in lung cancer 1 (TSLC1) binding to
RT differentially expressed in adenocarcinoma of the lung (DAL-1/4.1B).";
RL J. Biol. Chem. 286:4511-4516(2011).
CC -!- FUNCTION: Tumor suppressor that inhibits cell proliferation and
CC promotes apoptosis. Modulates the activity of protein arginine N-
CC methyltransferases, including PRMT3 and PRMT5.
CC {ECO:0000269|PubMed:15334060, ECO:0000269|PubMed:15737618,
CC ECO:0000269|PubMed:16420693, ECO:0000269|PubMed:9892180}.
CC -!- SUBUNIT: Interacts (via FERM domain) with CADM1 (PubMed:12234973,
CC PubMed:21131357). Interacts (via FERM domain) with PRMT3; the
CC interaction is direct and inhibits the protein-arginine N-
CC methyltransferase activity of PRMT3 (PubMed:15334060). Interacts with
CC PRMT5 (PubMed:15334060, PubMed:15737618). Interacts with PRMT6
CC (PubMed:15334060). {ECO:0000269|PubMed:12234973,
CC ECO:0000269|PubMed:15334060, ECO:0000269|PubMed:15737618,
CC ECO:0000269|PubMed:21131357}.
CC -!- INTERACTION:
CC Q9Y2J2-2; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-11100740, EBI-12023934;
CC Q9Y2J2-3; P15884: TCF4; NbExp=3; IntAct=EBI-10326138, EBI-533224;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC junction {ECO:0000269|PubMed:9892180}. Cell membrane
CC {ECO:0000269|PubMed:9892180}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9892180}; Cytoplasmic side
CC {ECO:0000269|PubMed:9892180}. Cytoplasm {ECO:0000269|PubMed:9892180}.
CC Note=Detected in the cytoplasm of actively dividing cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9Y2J2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2J2-2; Sequence=VSP_000482, VSP_000483, VSP_000484,
CC VSP_000485;
CC Name=3;
CC IsoId=Q9Y2J2-3; Sequence=VSP_000482, VSP_000483, VSP_000484,
CC VSP_000485, VSP_000486;
CC Name=4;
CC IsoId=Q9Y2J2-4; Sequence=VSP_000482, VSP_000483, VSP_054819,
CC VSP_054820;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, with lower
CC levels in kidney, intestine, and testis. Detected in lung.
CC {ECO:0000269|PubMed:9892180}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79806.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA76831.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/40458/epb41l3-(erythrocyte-membrane-protein-band-4-1-like-3)";
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; AF069072; AAC79806.1; ALT_FRAME; mRNA.
DR EMBL; AB023204; BAA76831.1; ALT_INIT; mRNA.
DR EMBL; AK297406; BAH12571.1; -; mRNA.
DR EMBL; AP001032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006141; AAH06141.1; -; mRNA.
DR CCDS; CCDS11838.1; -. [Q9Y2J2-1]
DR CCDS; CCDS62381.1; -. [Q9Y2J2-2]
DR CCDS; CCDS62382.1; -. [Q9Y2J2-4]
DR RefSeq; NP_001268462.1; NM_001281533.1. [Q9Y2J2-4]
DR RefSeq; NP_001268463.1; NM_001281534.1. [Q9Y2J2-2]
DR RefSeq; NP_001268464.1; NM_001281535.1.
DR RefSeq; NP_036439.2; NM_012307.3. [Q9Y2J2-1]
DR RefSeq; XP_016881125.1; XM_017025636.1.
DR PDB; 2HE7; X-ray; 2.00 A; A=108-390.
DR PDB; 3BIN; X-ray; 2.30 A; A=109-390.
DR PDB; 5RYM; X-ray; 1.64 A; A=107-390.
DR PDB; 5RYN; X-ray; 1.88 A; A=107-390.
DR PDB; 5RYO; X-ray; 1.58 A; A=107-390.
DR PDB; 5RYP; X-ray; 1.63 A; A=107-390.
DR PDB; 5RYQ; X-ray; 1.64 A; A=107-390.
DR PDB; 5RYR; X-ray; 1.87 A; A=107-390.
DR PDB; 5RYS; X-ray; 1.75 A; A=107-390.
DR PDB; 5RYT; X-ray; 1.72 A; A=107-390.
DR PDB; 5RYU; X-ray; 1.63 A; A=107-390.
DR PDB; 5RYV; X-ray; 1.69 A; A=107-390.
DR PDB; 5RYW; X-ray; 1.66 A; A=107-390.
DR PDB; 5RYX; X-ray; 1.63 A; A=107-390.
DR PDB; 5RYY; X-ray; 1.69 A; A=107-390.
DR PDB; 5RYZ; X-ray; 1.61 A; A=107-390.
DR PDB; 5RZ0; X-ray; 1.74 A; A=107-390.
DR PDB; 5RZ1; X-ray; 1.62 A; A=107-390.
DR PDB; 5RZ2; X-ray; 1.77 A; A=107-390.
DR PDB; 5RZ3; X-ray; 1.74 A; A=107-390.
DR PDB; 5RZ4; X-ray; 1.61 A; A=107-390.
DR PDB; 5RZ5; X-ray; 1.63 A; A=107-390.
DR PDB; 5RZ6; X-ray; 1.64 A; A=107-390.
DR PDB; 5RZ7; X-ray; 1.76 A; A=107-390.
DR PDB; 5RZ8; X-ray; 1.66 A; A=107-390.
DR PDB; 5RZ9; X-ray; 1.79 A; A=107-390.
DR PDB; 5RZA; X-ray; 1.89 A; A=107-390.
DR PDB; 5RZB; X-ray; 1.59 A; A=107-390.
DR PDB; 5RZC; X-ray; 1.75 A; A=107-390.
DR PDB; 5RZD; X-ray; 1.81 A; A=107-390.
DR PDB; 5RZE; X-ray; 1.69 A; A=107-390.
DR PDB; 5RZF; X-ray; 1.76 A; A=107-390.
DR PDB; 5RZG; X-ray; 1.70 A; A=107-390.
DR PDB; 5RZH; X-ray; 1.88 A; A=107-390.
DR PDB; 5RZI; X-ray; 2.09 A; A=107-390.
DR PDB; 5RZJ; X-ray; 1.68 A; A=107-390.
DR PDB; 5RZK; X-ray; 1.84 A; A=107-390.
DR PDB; 5RZL; X-ray; 1.71 A; A=107-390.
DR PDB; 5RZM; X-ray; 1.71 A; A=107-390.
DR PDB; 5RZN; X-ray; 1.83 A; A=107-390.
DR PDB; 5RZO; X-ray; 1.97 A; A=107-390.
DR PDB; 5RZP; X-ray; 1.70 A; A=107-390.
DR PDB; 5RZQ; X-ray; 1.88 A; A=107-390.
DR PDB; 5RZR; X-ray; 1.78 A; A=107-390.
DR PDB; 5RZS; X-ray; 1.69 A; A=107-390.
DR PDB; 5RZT; X-ray; 1.79 A; A=107-390.
DR PDB; 5RZU; X-ray; 1.66 A; A=107-390.
DR PDB; 5RZV; X-ray; 1.75 A; A=107-390.
DR PDB; 5RZW; X-ray; 1.62 A; A=107-390.
DR PDB; 5RZX; X-ray; 1.74 A; A=107-390.
DR PDB; 5RZY; X-ray; 1.75 A; A=107-390.
DR PDB; 5RZZ; X-ray; 1.76 A; A=107-390.
DR PDB; 5S00; X-ray; 1.77 A; A=107-390.
DR PDB; 6IBE; X-ray; 1.45 A; A=107-390.
DR PDBsum; 2HE7; -.
DR PDBsum; 3BIN; -.
DR PDBsum; 5RYM; -.
DR PDBsum; 5RYN; -.
DR PDBsum; 5RYO; -.
DR PDBsum; 5RYP; -.
DR PDBsum; 5RYQ; -.
DR PDBsum; 5RYR; -.
DR PDBsum; 5RYS; -.
DR PDBsum; 5RYT; -.
DR PDBsum; 5RYU; -.
DR PDBsum; 5RYV; -.
DR PDBsum; 5RYW; -.
DR PDBsum; 5RYX; -.
DR PDBsum; 5RYY; -.
DR PDBsum; 5RYZ; -.
DR PDBsum; 5RZ0; -.
DR PDBsum; 5RZ1; -.
DR PDBsum; 5RZ2; -.
DR PDBsum; 5RZ3; -.
DR PDBsum; 5RZ4; -.
DR PDBsum; 5RZ5; -.
DR PDBsum; 5RZ6; -.
DR PDBsum; 5RZ7; -.
DR PDBsum; 5RZ8; -.
DR PDBsum; 5RZ9; -.
DR PDBsum; 5RZA; -.
DR PDBsum; 5RZB; -.
DR PDBsum; 5RZC; -.
DR PDBsum; 5RZD; -.
DR PDBsum; 5RZE; -.
DR PDBsum; 5RZF; -.
DR PDBsum; 5RZG; -.
DR PDBsum; 5RZH; -.
DR PDBsum; 5RZI; -.
DR PDBsum; 5RZJ; -.
DR PDBsum; 5RZK; -.
DR PDBsum; 5RZL; -.
DR PDBsum; 5RZM; -.
DR PDBsum; 5RZN; -.
DR PDBsum; 5RZO; -.
DR PDBsum; 5RZP; -.
DR PDBsum; 5RZQ; -.
DR PDBsum; 5RZR; -.
DR PDBsum; 5RZS; -.
DR PDBsum; 5RZT; -.
DR PDBsum; 5RZU; -.
DR PDBsum; 5RZV; -.
DR PDBsum; 5RZW; -.
DR PDBsum; 5RZX; -.
DR PDBsum; 5RZY; -.
DR PDBsum; 5RZZ; -.
DR PDBsum; 5S00; -.
DR PDBsum; 6IBE; -.
DR AlphaFoldDB; Q9Y2J2; -.
DR SMR; Q9Y2J2; -.
DR BioGRID; 116753; 201.
DR CORUM; Q9Y2J2; -.
DR DIP; DIP-17035N; -.
DR IntAct; Q9Y2J2; 119.
DR MINT; Q9Y2J2; -.
DR STRING; 9606.ENSP00000343158; -.
DR GlyConnect; 1025; 11 N-Linked glycans (1 site).
DR GlyGen; Q9Y2J2; 3 sites, 11 N-linked glycans (1 site), 1 O-linked glycan (2 sites).
DR iPTMnet; Q9Y2J2; -.
DR PhosphoSitePlus; Q9Y2J2; -.
DR SwissPalm; Q9Y2J2; -.
DR BioMuta; EPB41L3; -.
DR DMDM; 17433099; -.
DR EPD; Q9Y2J2; -.
DR jPOST; Q9Y2J2; -.
DR MassIVE; Q9Y2J2; -.
DR MaxQB; Q9Y2J2; -.
DR PaxDb; Q9Y2J2; -.
DR PeptideAtlas; Q9Y2J2; -.
DR PRIDE; Q9Y2J2; -.
DR ProteomicsDB; 24274; -.
DR ProteomicsDB; 85811; -. [Q9Y2J2-1]
DR ProteomicsDB; 85812; -. [Q9Y2J2-2]
DR ProteomicsDB; 85813; -. [Q9Y2J2-3]
DR Antibodypedia; 21920; 253 antibodies from 31 providers.
DR DNASU; 23136; -.
DR Ensembl; ENST00000341928.7; ENSP00000343158.2; ENSG00000082397.18. [Q9Y2J2-1]
DR Ensembl; ENST00000540638.6; ENSP00000442091.2; ENSG00000082397.18. [Q9Y2J2-2]
DR Ensembl; ENST00000544123.5; ENSP00000441174.1; ENSG00000082397.18. [Q9Y2J2-4]
DR GeneID; 23136; -.
DR KEGG; hsa:23136; -.
DR MANE-Select; ENST00000341928.7; ENSP00000343158.2; NM_012307.5; NP_036439.2.
DR UCSC; uc002kmt.3; human. [Q9Y2J2-1]
DR CTD; 23136; -.
DR DisGeNET; 23136; -.
DR GeneCards; EPB41L3; -.
DR HGNC; HGNC:3380; EPB41L3.
DR HPA; ENSG00000082397; Low tissue specificity.
DR MIM; 605331; gene.
DR neXtProt; NX_Q9Y2J2; -.
DR OpenTargets; ENSG00000082397; -.
DR PharmGKB; PA27813; -.
DR VEuPathDB; HostDB:ENSG00000082397; -.
DR eggNOG; KOG3527; Eukaryota.
DR GeneTree; ENSGT00940000157047; -.
DR HOGENOM; CLU_003623_3_0_1; -.
DR InParanoid; Q9Y2J2; -.
DR OMA; NDYVSEF; -.
DR OrthoDB; 193911at2759; -.
DR PhylomeDB; Q9Y2J2; -.
DR TreeFam; TF351626; -.
DR PathwayCommons; Q9Y2J2; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR SignaLink; Q9Y2J2; -.
DR SIGNOR; Q9Y2J2; -.
DR BioGRID-ORCS; 23136; 21 hits in 1071 CRISPR screens.
DR ChiTaRS; EPB41L3; human.
DR EvolutionaryTrace; Q9Y2J2; -.
DR GeneWiki; EPB41L3; -.
DR GenomeRNAi; 23136; -.
DR Pharos; Q9Y2J2; Tbio.
DR PRO; PR:Q9Y2J2; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9Y2J2; protein.
DR Bgee; ENSG00000082397; Expressed in pons and 196 other tissues.
DR ExpressionAtlas; Q9Y2J2; baseline and differential.
DR Genevisible; Q9Y2J2; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005911; C:cell-cell junction; IDA:HGNC-UCL.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0044224; C:juxtaparanode region of axon; ISS:BHF-UCL.
DR GO; GO:0033270; C:paranode region of axon; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; TAS:BHF-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:BHF-UCL.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0030865; P:cortical cytoskeleton organization; TAS:BHF-UCL.
DR GO; GO:0043217; P:myelin maintenance; ISS:BHF-UCL.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:BHF-UCL.
DR GO; GO:0030913; P:paranodal junction assembly; ISS:BHF-UCL.
DR GO; GO:0071205; P:protein localization to juxtaparanode region of axon; ISS:BHF-UCL.
DR GO; GO:0002175; P:protein localization to paranode region of axon; ISS:BHF-UCL.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:BHF-UCL.
DR GO; GO:0001558; P:regulation of cell growth; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; ISS:BHF-UCL.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR030691; Band4.1-L3.
DR InterPro; IPR008379; Band_4.1_C.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FERM-adjacent.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR007477; SAB_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23280:SF20; PTHR23280:SF20; 1.
DR Pfam; PF05902; 4_1_CTD; 1.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF04382; SAB; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; Apoptosis;
KW Cell junction; Cell membrane; Cytoplasm; Cytoskeleton; Membrane;
KW Phosphoprotein; Reference proteome; Tumor suppressor.
FT CHAIN 1..1087
FT /note="Band 4.1-like protein 3"
FT /id="PRO_0000219399"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..1087
FT /note="Band 4.1-like protein 3, N-terminally processed"
FT /id="PRO_0000423194"
FT DOMAIN 110..391
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..513
FT /note="Hydrophilic"
FT REGION 459..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..860
FT /note="Spectrin--actin-binding"
FT /evidence="ECO:0000255"
FT REGION 541..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..1083
FT /note="C-terminal (CTD)"
FT REGION 937..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Band 4.1-like protein 3, N-
FT terminally processed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV92"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV92"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 469
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 492
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV92"
FT MOD_RES 706
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV92"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV92"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV92"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1081
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV92"
FT VAR_SEQ 446
FT /note="G -> GASVNENHEIYMKDSMSAA (in isoform 2, isoform 3
FT and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9892180"
FT /id="VSP_000482"
FT VAR_SEQ 503..689
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9892180"
FT /id="VSP_000483"
FT VAR_SEQ 708..719
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9892180"
FT /id="VSP_000484"
FT VAR_SEQ 784..824
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9892180"
FT /id="VSP_000485"
FT VAR_SEQ 835..1087
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9892180"
FT /id="VSP_000486"
FT VAR_SEQ 1052
FT /note="A -> E (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054819"
FT VAR_SEQ 1053..1087
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054820"
FT VARIANT 555
FT /note="A -> T (in dbSNP:rs9966357)"
FT /id="VAR_048353"
FT VARIANT 575
FT /note="Y -> C (in dbSNP:rs8082898)"
FT /id="VAR_048354"
FT VARIANT 859
FT /note="E -> Q (in dbSNP:rs8096452)"
FT /id="VAR_048355"
FT CONFLICT 12
FT /note="K -> E (in Ref. 3; BAH12571)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="Missing (in Ref. 1; AAC79806)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="R -> Q (in Ref. 1; AAC79806)"
FT /evidence="ECO:0000305"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:6IBE"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:6IBE"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:6IBE"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:6IBE"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:6IBE"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6IBE"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6IBE"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:6IBE"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:6IBE"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:6IBE"
FT HELIX 199..214
FT /evidence="ECO:0007829|PDB:6IBE"
FT HELIX 222..237
FT /evidence="ECO:0007829|PDB:6IBE"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:6IBE"
FT TURN 249..252
FT /evidence="ECO:0007829|PDB:5RZ8"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:6IBE"
FT HELIX 261..272
FT /evidence="ECO:0007829|PDB:6IBE"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:6IBE"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:6IBE"
FT TURN 294..297
FT /evidence="ECO:0007829|PDB:6IBE"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:6IBE"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:6IBE"
FT STRAND 317..333
FT /evidence="ECO:0007829|PDB:6IBE"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:6IBE"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:6IBE"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:6IBE"
FT TURN 354..357
FT /evidence="ECO:0007829|PDB:2HE7"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:6IBE"
FT HELIX 370..389
FT /evidence="ECO:0007829|PDB:6IBE"
SQ SEQUENCE 1087 AA; 120678 MW; 0A33CA4A43F12620 CRC64;
MTTESGSDSE SKPDQEAEPQ EAAGAQGRAG APVPEPPKEE QQQALEQFAA AAAHSTPVRR
EVTDKEQEFA ARAAKQLEYQ QLEDDKLSQK SSSSKLSRSP LKIVKKPKSM QCKVILLDGS
EYTCDVEKRS RGQVLFDKVC EHLNLLEKDY FGLTYRDAEN QKNWLDPAKE IKKQVRSGAW
HFSFNVKFYP PDPAQLSEDI TRYYLCLQLR DDIVSGRLPC SFVTLALLGS YTVQSELGDY
DPDECGSDYI SEFRFAPNHT KELEDKVIEL HKSHRGMTPA EAEMHFLENA KKLSMYGVDL
HHAKDSEGVE IMLGVCASGL LIYRDRLRIN RFAWPKVLKI SYKRNNFYIK IRPGEFEQFE
STIGFKLPNH RAAKRLWKVC VEHHTFFRLL LPEAPPKKFL TLGSKFRYSG RTQAQTRRAS
ALIDRPAPYF ERSSSKRYTM SRSLDGEVGT GQYATTKGIS QTNLITTVTP EKKAEEERDE
EEDKRRKGEE VTPISAIRHE GKSPGLGTDS CPLSPPSTHC APTSPTELRR RCKENDCKLP
GYEPSRAEHL PGEPALDSDG PGRPYLGDQD VAFSYRQQTG KGTTLFSFSL QLPESFPSLL
DDDGYLSFPN LSETNLLPQS LQHYLPIRSP SLVPCFLFIF FFLLSASFSV PYALTLSFPL
ALCLCYLEPK AASLSASLDN DPSDSSEEET DSERTDTAAD GETTATESDQ EEDAELKAQE
LEKTQDDLMK HQTNISELKR TFLETSTDTA VTNEWEKRLS TSPVRLAARQ EDAPMIEPLV
PEETKQSSGE KLMDGSEIFS LLESARKPTE FIGGVTSTSQ SWVQKMETKT ESSGIETEPT
VHHLPLSTEK VVQETVLVEE RRVVHASGDA SYSAGDSGDA AAQPAFTGIK GKEGSALTEG
AKEEGGEEVA KAVLEQEETA AASRERQEEQ SAAIHISETL EQKPHFESST VKTETISFGS
VSPGGVKLEI STKEVPVVHT ETKTITYESS QVDPGTDLEP GVLMSAQTIT SETTSTTTTT
HITKTVKGGI SETRIEKRIV ITGDADIDHD QALAQAIKEA KEQHPDMSVT KVVVHKETEI
TPEDGED
