TRAF4_HUMAN
ID TRAF4_HUMAN Reviewed; 470 AA.
AC Q9BUZ4; O75615; Q14848; Q2KJU4; Q2PJN8;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=TNF receptor-associated factor 4;
DE EC=2.3.2.27 {ECO:0000269|PubMed:31076633, ECO:0000269|PubMed:32357935, ECO:0000269|PubMed:33991522};
DE AltName: Full=Cysteine-rich domain associated with RING and Traf domains protein 1;
DE AltName: Full=Metastatic lymph node gene 62 protein;
DE Short=MLN 62;
DE AltName: Full=RING finger protein 83;
GN Name=TRAF4; Synonyms=CART1, MLN62, RNF83;
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 1), AND VARIANT GLY-178.
RC TISSUE=Mammary tumor;
RX PubMed=7490069; DOI=10.1006/geno.1995.1163;
RA Tomasetto C.L., Regnier C.H., Moog-Lutz C., Mattei M.-G., Chenard M.-P.,
RA Lidereau R., Basset P., Rio M.-C.;
RT "Identification of four novel human genes amplified and overexpressed in
RT breast carcinoma and localized to the q11-q21.3 region of chromosome 17.";
RL Genomics 28:367-376(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Lung;
RA Miller H.G., Pullen S.P., White H.E., Phipps R.P., Kehry M.R., Crute J.J.;
RT "TRAF4 expression in proliferating cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cervix carcinoma;
RA Cai C.L., Li R., Wang R.S., Miao S.Y., Wang L.F.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-173.
RG NIEHS SNPs program;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retinoblastoma;
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 [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=7592751; DOI=10.1074/jbc.270.43.25715;
RA Regnier C.H., Tomasetto C., Moog-Lutz C., Chenard M.-P., Wendling C.,
RA Basset P., Rio M.-C.;
RT "Presence of a new conserved domain in CART1, a novel member of the tumor
RT necrosis factor receptor-associated protein family, which is expressed in
RT breast carcinoma.";
RL J. Biol. Chem. 270:25715-25721(1995).
RN [8]
RP INTERACTION WITH LTBR AND TNFRSDF16, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=9626059;
RA Krajewska M., Krajewski S., Zapata J.M., VanArsdale T., Gascoyne R.D.,
RA Berern K., McFadden D., Shabaik A., Hugh J., Reynolds A., Clevenger C.V.,
RA Reed J.C.;
RT "TRAF-4 expression in epithelial progenitor cells. Analysis in normal
RT adult, fetal, and tumor tissues.";
RL Am. J. Pathol. 152:1549-1561(1998).
RN [9]
RP INTERACTION WITH TNFRSF16.
RX PubMed=10514511; DOI=10.1074/jbc.274.42.30202;
RA Ye X., Mehlen P., Rabizadeh S., VanArsdale T., Zhang H., Shin H.,
RA Wang J.J.L., Leo E., Zapata J.M., Hauser C.A., Reed J.C., Bredesen D.E.;
RT "TRAF family proteins interact with the common neurotrophin receptor and
RT modulate apoptosis induction.";
RL J. Biol. Chem. 274:30202-30208(1999).
RN [10]
RP FUNCTION, INTERACTION WITH NCF1, AND SUBCELLULAR LOCATION.
RX PubMed=12023963; DOI=10.1074/jbc.m202665200;
RA Xu Y.C., Wu R.F., Gu Y., Yang Y.S., Yang M.C., Nwariaku F.E., Terada L.S.;
RT "Involvement of TRAF4 in oxidative activation of c-Jun N-terminal kinase.";
RL J. Biol. Chem. 277:28051-28057(2002).
RN [11]
RP FUNCTION, AND INTERACTION WITH RPS6KB1.
RX PubMed=12801526; DOI=10.1016/s0145-2126(02)00325-9;
RA Fleckenstein D.S., Dirks W.G., Drexler H.G., Quentmeier H.;
RT "Tumor necrosis factor receptor-associated factor (TRAF) 4 is a new binding
RT partner for the p70S6 serine/threonine kinase.";
RL Leuk. Res. 27:687-694(2003).
RN [12]
RP FUNCTION, INTERACTION WITH NCF1; TICAM1; IRAK1 AND TRAF6, AND INDUCTION.
RX PubMed=16052631; DOI=10.1002/eji.200526151;
RA Takeshita F., Ishii K.J., Kobiyama K., Kojima Y., Coban C., Sasaki S.,
RA Ishii N., Klinman D.M., Okuda K., Akira S., Suzuki K.;
RT "TRAF4 acts as a silencer in TLR-mediated signaling through the association
RT with TRAF6 and TRIF.";
RL Eur. J. Immunol. 35:2477-2485(2005).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAP3K4.
RX PubMed=16157600; DOI=10.1074/jbc.c500260200;
RA Abell A.N., Johnson G.L.;
RT "MEKK4 is an effector of the embryonic TRAF4 for JNK activation.";
RL J. Biol. Chem. 280:35793-35796(2005).
RN [14]
RP INTERACTION WITH TGFB1I1.
RX PubMed=16330715; DOI=10.1083/jcb.200507004;
RA Wu R.F., Xu Y.C., Ma Z., Nwariaku F.E., Sarosi G.A. Jr., Terada L.S.;
RT "Subcellular targeting of oxidants during endothelial cell migration.";
RL J. Cell Biol. 171:893-904(2005).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=18087216; DOI=10.4161/cbt.6.12.5002;
RA Gu X., Coates P.J., MacCallum S.F., Boldrup L., Sjostrom B., Nylander K.;
RT "TRAF4 is potently induced by TAp63 isoforms and localised according to
RT differentiation in SCCHN.";
RL Cancer Biol. Ther. 6:1986-1990(2007).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18953416; DOI=10.1371/journal.pone.0003518;
RA Kedinger V., Alpy F., Baguet A., Polette M., Stoll I., Chenard M.P.,
RA Tomasetto C., Rio M.C.;
RT "Tumor necrosis factor receptor-associated factor 4 is a dynamic tight
RT junction-related shuttle protein involved in epithelium homeostasis.";
RL PLoS ONE 3:E3518-E3518(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP FUNCTION, INTERACTION WITH SMURF1, AND UBIQUITINATION.
RX PubMed=19937093; DOI=10.1007/s11010-009-0315-y;
RA Li S., Lu K., Wang J., An L., Yang G., Chen H., Cui Y., Yin X., Xie P.,
RA Xing G., He F., Zhang L.;
RT "Ubiquitin ligase Smurf1 targets TRAF family proteins for ubiquitination
RT and degradation.";
RL Mol. Cell. Biochem. 338:11-17(2010).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426, AND IDENTIFICATION BY
RP 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 [20]
RP FUNCTION, AND INTERACTION WITH GP1BB AND GP6.
RX PubMed=20946164; DOI=10.1111/j.1538-7836.2010.04091.x;
RA Arthur J.F., Shen Y., Gardiner E.E., Coleman L., Murphy D., Kenny D.,
RA Andrews R.K., Berndt M.C.;
RT "TNF receptor-associated factor 4 (TRAF4) is a novel binding partner of
RT glycoprotein Ib and glycoprotein VI in human platelets.";
RL J. Thromb. Haemost. 9:163-172(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP FUNCTION, AND INTERACTION WITH EGFR.
RX PubMed=30352854; DOI=10.1073/pnas.1809599115;
RA Cai G., Zhu L., Chen X., Sun K., Liu C., Sen G.C., Stark G.R., Qin J.,
RA Li X.;
RT "TRAF4 binds to the juxtamembrane region of EGFR directly and promotes
RT kinase activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:11531-11536(2018).
RN [23]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31076633; DOI=10.1038/s41418-019-0328-3;
RA Li J., Wang P., Xie Z., Wang S., Cen S., Li M., Liu W., Tang S., Ye G.,
RA Zheng G., Su H., Ma M., Wu X., Wu Y., Shen H.;
RT "TRAF4 positively regulates the osteogenic differentiation of mesenchymal
RT stem cells by acting as an E3 ubiquitin ligase to degrade Smurf2.";
RL Cell Death Differ. 26:2652-2666(2019).
RN [24]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-18.
RX PubMed=32357935; DOI=10.1186/s13045-020-00869-3;
RA Yu X., Li W., Liu H., Deng Q., Wang X., Hu H., Xu-Monette Z.Y., Xiong W.,
RA Lu Z., Young K.H., Wang W., Li Y.;
RT "Ubiquitination of the DNA-damage checkpoint kinase CHK1 by TRAF4 is
RT required for CHK1 activation.";
RL J. Hematol. Oncol. 13:40-40(2020).
RN [25]
RP FUNCTION, INTERACTION WITH PKM, AND SUBCELLULAR LOCATION.
RX PubMed=32268273; DOI=10.1016/j.ebiom.2020.102722;
RA Cen S., Li J., Cai Z., Pan Y., Sun Z., Li Z., Ye G., Zheng G., Li M.,
RA Liu W., Yu W., Wang S., Xie Z., Wang P., Shen H.;
RT "TRAF4 acts as a fate checkpoint to regulate the adipogenic differentiation
RT of MSCs by activating PKM2.";
RL EBioMedicine 54:102722-102722(2020).
RN [26]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33991522; DOI=10.1016/j.jbc.2021.100739;
RA Yu W., Singh R., Wang Z., O'Malley B.W., Yi P.;
RT "The E3 ligase TRAF4 Promotes IGF Signaling by Mediating Atypical
RT Ubiquitination of IRS-1.";
RL J. Biol. Chem. 296:100739-100739(2021).
RN [27]
RP STRUCTURE BY NMR OF 101-248.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of TRAF-type zinc finger domains from human TNF
RT receptor-associated factor 4.";
RL Submitted (APR-2008) to the PDB data bank.
RN [28] {ECO:0007744|PDB:5YC1}
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 290-470, AND INTERACTION WITH
RP GP1BB AND GP6.
RX PubMed=29073066; DOI=10.1073/pnas.1708688114;
RA Kim C.M., Son Y.J., Kim S., Kim S.Y., Park H.H.;
RT "Molecular basis for unique specificity of human TRAF4 for platelets
RT GPIbbeta and GPVI.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:11422-11427(2017).
CC -!- FUNCTION: Adapter protein with E3 ligase activity that is involved in
CC many diverse biological processes including cell proliferation,
CC migration, differentiation, DNA repair, platelet activation or
CC apoptosis (PubMed:30352854, PubMed:31076633, PubMed:32268273,
CC PubMed:33991522). Promotes EGFR-mediated signaling by facilitating the
CC dimerization of EGFR and downstream AKT activation thereby promoting
CC cell proliferation (PubMed:30352854). Ubiquitinates SMURF2 through
CC 'Lys-48'-linked ubiquitin chain leading to SMURF2 degradation through
CC the proteasome and subsequently osteogenic differentiation
CC (PubMed:31076633). Promotes 'Lys-63'-mediated ubiquitination of CHK1
CC which in turn activates cell cycle arrest and activation of DNA repair
CC (PubMed:32357935). In addition, promotes an atypical 'Lys-29'-linked
CC ubiquitination at the C-terminal end of IRS1 which is crucial for
CC insulin-like growth factor (IGF) signal transduction (PubMed:33991522).
CC Regulates activation of NF-kappa-B in response to signaling through
CC Toll-like receptors. Required for normal skeleton development, and for
CC normal development of the respiratory tract (By similarity). Required
CC for activation of RPS6KB1 in response to TNF signaling. Modulates TRAF6
CC functions. Inhibits adipogenic differentiation by activating pyruvate
CC kinase PKM activity and subsequently the beta-catenin signaling pathway
CC (PubMed:32268273). {ECO:0000250, ECO:0000269|PubMed:12023963,
CC ECO:0000269|PubMed:12801526, ECO:0000269|PubMed:16052631,
CC ECO:0000269|PubMed:16157600, ECO:0000269|PubMed:18953416,
CC ECO:0000269|PubMed:19937093, ECO:0000269|PubMed:30352854,
CC ECO:0000269|PubMed:31076633, ECO:0000269|PubMed:32268273,
CC ECO:0000269|PubMed:32357935, ECO:0000269|PubMed:33991522}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:31076633,
CC ECO:0000269|PubMed:32357935, ECO:0000269|PubMed:33991522};
CC -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent pathway.
CC {ECO:0000269|PubMed:31076633, ECO:0000269|PubMed:32357935,
CC ECO:0000269|PubMed:33991522}.
CC -!- SUBUNIT: Homotrimer (Probable). Interacts with LTBR/TNFRSF3,
CC NGFR/TNFRSF16, RPS6KB1 and TGFB1I1. Interacts with SMURF1. Interacts
CC (via TRAF domain) with MAP3K4 (via kinase domain). Interacts with NCF1,
CC TICAM1, IRAK1 and TRAF6, and is probably part of a complex containing
CC TRAF4, NCF1, TICAM1, IRAK1 and TRAF6. Interacts (via MATH domain) with
CC GP6 and GP1BB (PubMed:20946164, PubMed:29073066). Interacts with EGFR
CC (via C-terminal region); this interaction promotes the formation of
CC EGFR asymmetric dimers (PubMed:30352854). Interacts with PKM; this
CC interaction promotes PKM kinase activity (PubMed:32268273).
CC {ECO:0000269|PubMed:10514511, ECO:0000269|PubMed:12023963,
CC ECO:0000269|PubMed:12801526, ECO:0000269|PubMed:16052631,
CC ECO:0000269|PubMed:16157600, ECO:0000269|PubMed:16330715,
CC ECO:0000269|PubMed:19937093, ECO:0000269|PubMed:20946164,
CC ECO:0000269|PubMed:29073066, ECO:0000269|PubMed:32268273,
CC ECO:0000269|PubMed:9626059, ECO:0000305}.
CC -!- INTERACTION:
CC Q9BUZ4; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-3650647, EBI-742038;
CC Q9BUZ4; Q9NXW9: ALKBH4; NbExp=4; IntAct=EBI-3650647, EBI-8637516;
CC Q9BUZ4; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-3650647, EBI-1642333;
CC Q9BUZ4; Q8TBE0: BAHD1; NbExp=6; IntAct=EBI-3650647, EBI-742750;
CC Q9BUZ4; A0A0S2Z5G4: BANP; NbExp=3; IntAct=EBI-3650647, EBI-16429704;
CC Q9BUZ4; B4DE54: BANP; NbExp=3; IntAct=EBI-3650647, EBI-16429313;
CC Q9BUZ4; Q8N9N5: BANP; NbExp=3; IntAct=EBI-3650647, EBI-744695;
CC Q9BUZ4; Q8N9N5-2: BANP; NbExp=6; IntAct=EBI-3650647, EBI-11524452;
CC Q9BUZ4; Q8N9N5-7: BANP; NbExp=3; IntAct=EBI-3650647, EBI-16429296;
CC Q9BUZ4; A8KA13: BCL6B; NbExp=3; IntAct=EBI-3650647, EBI-10174813;
CC Q9BUZ4; Q9BUH8: BEGAIN; NbExp=3; IntAct=EBI-3650647, EBI-742722;
CC Q9BUZ4; Q13895: BYSL; NbExp=9; IntAct=EBI-3650647, EBI-358049;
CC Q9BUZ4; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-3650647, EBI-11976299;
CC Q9BUZ4; Q8N187: CARF; NbExp=3; IntAct=EBI-3650647, EBI-745541;
CC Q9BUZ4; Q6P2H3-3: CEP85; NbExp=3; IntAct=EBI-3650647, EBI-12368239;
CC Q9BUZ4; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-3650647, EBI-11988027;
CC Q9BUZ4; P50570: DNM2; NbExp=3; IntAct=EBI-3650647, EBI-346547;
CC Q9BUZ4; P50570-2: DNM2; NbExp=3; IntAct=EBI-3650647, EBI-10968534;
CC Q9BUZ4; A0A0U1RQF7: DPEP2NB; NbExp=3; IntAct=EBI-3650647, EBI-18398199;
CC Q9BUZ4; Q8N9I9: DTX3; NbExp=4; IntAct=EBI-3650647, EBI-2340258;
CC Q9BUZ4; Q96BU6: EXOC7; NbExp=3; IntAct=EBI-3650647, EBI-10282504;
CC Q9BUZ4; O00167-2: EYA2; NbExp=3; IntAct=EBI-3650647, EBI-12807776;
CC Q9BUZ4; Q86X51: EZHIP; NbExp=3; IntAct=EBI-3650647, EBI-12827735;
CC Q9BUZ4; Q7L5A3: FAM214B; NbExp=5; IntAct=EBI-3650647, EBI-745689;
CC Q9BUZ4; Q96D16: FBXL18; NbExp=3; IntAct=EBI-3650647, EBI-744419;
CC Q9BUZ4; O43559: FRS3; NbExp=3; IntAct=EBI-3650647, EBI-725515;
CC Q9BUZ4; Q08379: GOLGA2; NbExp=5; IntAct=EBI-3650647, EBI-618309;
CC Q9BUZ4; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-3650647, EBI-11163335;
CC Q9BUZ4; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-3650647, EBI-5916454;
CC Q9BUZ4; Q9BQQ3: GORASP1; NbExp=3; IntAct=EBI-3650647, EBI-2561458;
CC Q9BUZ4; Q9H8Y8: GORASP2; NbExp=4; IntAct=EBI-3650647, EBI-739467;
CC Q9BUZ4; Q9UBP5: HEY2; NbExp=3; IntAct=EBI-3650647, EBI-750630;
CC Q9BUZ4; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-3650647, EBI-16429135;
CC Q9BUZ4; O14964: HGS; NbExp=6; IntAct=EBI-3650647, EBI-740220;
CC Q9BUZ4; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-3650647, EBI-740641;
CC Q9BUZ4; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-3650647, EBI-10172004;
CC Q9BUZ4; P49639: HOXA1; NbExp=3; IntAct=EBI-3650647, EBI-740785;
CC Q9BUZ4; P09067: HOXB5; NbExp=3; IntAct=EBI-3650647, EBI-3893317;
CC Q9BUZ4; Q9NPH2: ISYNA1; NbExp=6; IntAct=EBI-3650647, EBI-720563;
CC Q9BUZ4; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-3650647, EBI-2556193;
CC Q9BUZ4; Q7Z3B3: KANSL1; NbExp=3; IntAct=EBI-3650647, EBI-740244;
CC Q9BUZ4; O60341: KDM1A; NbExp=4; IntAct=EBI-3650647, EBI-710124;
CC Q9BUZ4; Q15323: KRT31; NbExp=6; IntAct=EBI-3650647, EBI-948001;
CC Q9BUZ4; O76013-2: KRT36; NbExp=3; IntAct=EBI-3650647, EBI-11958506;
CC Q9BUZ4; Q6A162: KRT40; NbExp=6; IntAct=EBI-3650647, EBI-10171697;
CC Q9BUZ4; Q96PV6: LENG8; NbExp=3; IntAct=EBI-3650647, EBI-739546;
CC Q9BUZ4; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-3650647, EBI-739832;
CC Q9BUZ4; Q13084: MRPL28; NbExp=4; IntAct=EBI-3650647, EBI-723426;
CC Q9BUZ4; P14598: NCF1; NbExp=5; IntAct=EBI-3650647, EBI-395044;
CC Q9BUZ4; O75052: NOS1AP; NbExp=3; IntAct=EBI-3650647, EBI-780467;
CC Q9BUZ4; E9PJI5: NPIPA7; NbExp=3; IntAct=EBI-3650647, EBI-10177044;
CC Q9BUZ4; Q9BRJ7: NUDT16L1; NbExp=3; IntAct=EBI-3650647, EBI-2949792;
CC Q9BUZ4; Q92824-2: PCSK5; NbExp=3; IntAct=EBI-3650647, EBI-11956269;
CC Q9BUZ4; A2BDE7: PHLDA1; NbExp=3; IntAct=EBI-3650647, EBI-14084211;
CC Q9BUZ4; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-3650647, EBI-79165;
CC Q9BUZ4; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-3650647, EBI-2876622;
CC Q9BUZ4; Q6IQ23-2: PLEKHA7; NbExp=3; IntAct=EBI-3650647, EBI-12069346;
CC Q9BUZ4; P52435: POLR2J; NbExp=3; IntAct=EBI-3650647, EBI-394753;
CC Q9BUZ4; Q9H1A7: POLR2J3; NbExp=3; IntAct=EBI-3650647, EBI-12818681;
CC Q9BUZ4; P17980: PSMC3; NbExp=4; IntAct=EBI-3650647, EBI-359720;
CC Q9BUZ4; P47897: QARS1; NbExp=6; IntAct=EBI-3650647, EBI-347462;
CC Q9BUZ4; P47897-2: QARS1; NbExp=3; IntAct=EBI-3650647, EBI-10209725;
CC Q9BUZ4; Q9Y4B4: RAD54L2; NbExp=3; IntAct=EBI-3650647, EBI-948156;
CC Q9BUZ4; Q8IX06: REXO1L1P; NbExp=3; IntAct=EBI-3650647, EBI-10262361;
CC Q9BUZ4; P78317: RNF4; NbExp=5; IntAct=EBI-3650647, EBI-2340927;
CC Q9BUZ4; Q15427: SF3B4; NbExp=3; IntAct=EBI-3650647, EBI-348469;
CC Q9BUZ4; Q15599: SLC9A3R2; NbExp=3; IntAct=EBI-3650647, EBI-1149760;
CC Q9BUZ4; Q9HCE7-2: SMURF1; NbExp=4; IntAct=EBI-3650647, EBI-9845742;
CC Q9BUZ4; P14678-2: SNRPB; NbExp=3; IntAct=EBI-3650647, EBI-372475;
CC Q9BUZ4; Q96EA4: SPDL1; NbExp=3; IntAct=EBI-3650647, EBI-715381;
CC Q9BUZ4; P63165: SUMO1; NbExp=3; IntAct=EBI-3650647, EBI-80140;
CC Q9BUZ4; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-3650647, EBI-529518;
CC Q9BUZ4; Q9P0N9: TBC1D7; NbExp=9; IntAct=EBI-3650647, EBI-3258000;
CC Q9BUZ4; Q01664: TFAP4; NbExp=3; IntAct=EBI-3650647, EBI-2514218;
CC Q9BUZ4; O43294: TGFB1I1; NbExp=8; IntAct=EBI-3650647, EBI-1051449;
CC Q9BUZ4; O14656-2: TOR1A; NbExp=3; IntAct=EBI-3650647, EBI-25847109;
CC Q9BUZ4; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-3650647, EBI-10175039;
CC Q9BUZ4; O14773: TPP1; NbExp=3; IntAct=EBI-3650647, EBI-2800203;
CC Q9BUZ4; Q9BUZ4: TRAF4; NbExp=6; IntAct=EBI-3650647, EBI-3650647;
CC Q9BUZ4; P14373: TRIM27; NbExp=3; IntAct=EBI-3650647, EBI-719493;
CC Q9BUZ4; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-3650647, EBI-10241197;
CC Q9BUZ4; P29597: TYK2; NbExp=3; IntAct=EBI-3650647, EBI-1383454;
CC Q9BUZ4; P22314: UBA1; NbExp=3; IntAct=EBI-3650647, EBI-709688;
CC Q9BUZ4; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-3650647, EBI-10180829;
CC Q9BUZ4; P11441: UBL4A; NbExp=6; IntAct=EBI-3650647, EBI-356983;
CC Q9BUZ4; Q8N7F7: UBL4B; NbExp=7; IntAct=EBI-3650647, EBI-10267507;
CC Q9BUZ4; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-3650647, EBI-947187;
CC Q9BUZ4; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-3650647, EBI-2799833;
CC Q9BUZ4; Q9Y2W2: WBP11; NbExp=3; IntAct=EBI-3650647, EBI-714455;
CC Q9BUZ4; Q9H0M0: WWP1; NbExp=3; IntAct=EBI-3650647, EBI-742157;
CC Q9BUZ4; O00308: WWP2; NbExp=7; IntAct=EBI-3650647, EBI-743923;
CC Q9BUZ4; Q05516: ZBTB16; NbExp=3; IntAct=EBI-3650647, EBI-711925;
CC Q9BUZ4; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-3650647, EBI-3918996;
CC Q9BUZ4; Q9C0D7: ZC3H12C; NbExp=3; IntAct=EBI-3650647, EBI-2857430;
CC Q9BUZ4; Q9UJ78-2: ZMYM5; NbExp=3; IntAct=EBI-3650647, EBI-17634549;
CC Q9BUZ4; Q13360-2: ZNF177; NbExp=3; IntAct=EBI-3650647, EBI-12272076;
CC Q9BUZ4; Q9NSD4: ZNF275; NbExp=3; IntAct=EBI-3650647, EBI-17263125;
CC Q9BUZ4; P17036: ZNF3; NbExp=8; IntAct=EBI-3650647, EBI-1640965;
CC Q9BUZ4; Q86U76: ZNF3; NbExp=3; IntAct=EBI-3650647, EBI-10258769;
CC Q9BUZ4; Q9P0T4: ZNF581; NbExp=6; IntAct=EBI-3650647, EBI-745520;
CC Q9BUZ4; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-3650647, EBI-4395669;
CC Q9BUZ4; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-3650647, EBI-16429014;
CC Q9BUZ4; Q8NCA9: ZNF784; NbExp=3; IntAct=EBI-3650647, EBI-7138303;
CC Q9BUZ4; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-3650647, EBI-5667516;
CC Q9BUZ4; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-3650647, EBI-527853;
CC Q9BUZ4; P07174: Ngfr; Xeno; NbExp=3; IntAct=EBI-3650647, EBI-1038810;
CC Q9BUZ4; Q9E7P0; Xeno; NbExp=2; IntAct=EBI-3650647, EBI-11361108;
CC Q9BUZ4-1; Q9BUZ4-1: TRAF4; NbExp=4; IntAct=EBI-16084295, EBI-16084295;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32268273}. Nucleus
CC {ECO:0000269|PubMed:32268273}. Cytoplasm, perinuclear region. Cell
CC junction, tight junction. Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BUZ4-1; Sequence=Displayed;
CC Name=2; Synonyms=TRAF4 variant 5;
CC IsoId=Q9BUZ4-2; Sequence=VSP_007403;
CC -!- TISSUE SPECIFICITY: Expressed in epithelial cells of thymus, dendritic
CC cells of lymph node, and in the basal cell layer of epithelia such as
CC epidermis, nasopharynx, respiratory tract, salivary gland, and
CC esophagus. {ECO:0000269|PubMed:7592751, ECO:0000269|PubMed:9626059}.
CC -!- INDUCTION: Up-regulated by bacterial lipopolysaccharides (LPS) and by
CC single-stranded CpG oligodeoxynucleotide.
CC {ECO:0000269|PubMed:16052631}.
CC -!- DOMAIN: The coiled coil domain mediates homo- and hetero-
CC oligomerization. {ECO:0000250}.
CC -!- DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains.
CC {ECO:0000250}.
CC -!- PTM: Polyubiquitinated, leading to its proteasomal degradation.
CC {ECO:0000269|PubMed:19937093}.
CC -!- SIMILARITY: Belongs to the TNF receptor-associated factor family. B
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TRAF4ID204.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/traf4/";
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DR EMBL; X80200; CAA56491.1; -; mRNA.
DR EMBL; AF082185; AAC32376.1; -; mRNA.
DR EMBL; AY937224; AAY16990.1; -; mRNA.
DR EMBL; DQ323999; ABC40750.1; -; Genomic_DNA.
DR EMBL; AC010761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001769; AAH01769.1; -; mRNA.
DR CCDS; CCDS11243.1; -. [Q9BUZ4-1]
DR PIR; I38026; I38026.
DR RefSeq; NP_004286.2; NM_004295.3. [Q9BUZ4-1]
DR PDB; 2EOD; NMR; -; A=190-248.
DR PDB; 2YUC; NMR; -; A=102-164.
DR PDB; 3ZJB; X-ray; 1.84 A; A/B/C=283-470.
DR PDB; 4K8U; X-ray; 2.30 A; A/B/C=281-470.
DR PDB; 4M4E; X-ray; 2.60 A; A/B/C=292-466.
DR PDB; 5YC1; X-ray; 2.51 A; A/B/C/D/E/F=290-470.
DR PDBsum; 2EOD; -.
DR PDBsum; 2YUC; -.
DR PDBsum; 3ZJB; -.
DR PDBsum; 4K8U; -.
DR PDBsum; 4M4E; -.
DR PDBsum; 5YC1; -.
DR AlphaFoldDB; Q9BUZ4; -.
DR PCDDB; Q9BUZ4; -.
DR SMR; Q9BUZ4; -.
DR BioGRID; 114979; 184.
DR DIP; DIP-40910N; -.
DR IntAct; Q9BUZ4; 126.
DR MINT; Q9BUZ4; -.
DR STRING; 9606.ENSP00000262395; -.
DR iPTMnet; Q9BUZ4; -.
DR PhosphoSitePlus; Q9BUZ4; -.
DR BioMuta; TRAF4; -.
DR DMDM; 30580636; -.
DR EPD; Q9BUZ4; -.
DR jPOST; Q9BUZ4; -.
DR MassIVE; Q9BUZ4; -.
DR MaxQB; Q9BUZ4; -.
DR PaxDb; Q9BUZ4; -.
DR PeptideAtlas; Q9BUZ4; -.
DR PRIDE; Q9BUZ4; -.
DR ProteomicsDB; 79148; -. [Q9BUZ4-1]
DR ProteomicsDB; 79149; -. [Q9BUZ4-2]
DR Antibodypedia; 3961; 324 antibodies from 39 providers.
DR DNASU; 9618; -.
DR Ensembl; ENST00000262395.10; ENSP00000262395.5; ENSG00000076604.16. [Q9BUZ4-1]
DR GeneID; 9618; -.
DR KEGG; hsa:9618; -.
DR MANE-Select; ENST00000262395.10; ENSP00000262395.5; NM_004295.4; NP_004286.2.
DR UCSC; uc002hcq.2; human. [Q9BUZ4-1]
DR CTD; 9618; -.
DR DisGeNET; 9618; -.
DR GeneCards; TRAF4; -.
DR HGNC; HGNC:12034; TRAF4.
DR HPA; ENSG00000076604; Low tissue specificity.
DR MIM; 602464; gene.
DR neXtProt; NX_Q9BUZ4; -.
DR OpenTargets; ENSG00000076604; -.
DR PharmGKB; PA36711; -.
DR VEuPathDB; HostDB:ENSG00000076604; -.
DR eggNOG; KOG0297; Eukaryota.
DR GeneTree; ENSGT00940000158628; -.
DR HOGENOM; CLU_021061_6_0_1; -.
DR InParanoid; Q9BUZ4; -.
DR OMA; MKQLQSH; -.
DR PhylomeDB; Q9BUZ4; -.
DR TreeFam; TF321154; -.
DR PathwayCommons; Q9BUZ4; -.
DR SignaLink; Q9BUZ4; -.
DR SIGNOR; Q9BUZ4; -.
DR UniPathway; UPA00144; -.
DR BioGRID-ORCS; 9618; 16 hits in 1122 CRISPR screens.
DR ChiTaRS; TRAF4; human.
DR EvolutionaryTrace; Q9BUZ4; -.
DR GeneWiki; TRAF4; -.
DR GenomeRNAi; 9618; -.
DR Pharos; Q9BUZ4; Tbio.
DR PRO; PR:Q9BUZ4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BUZ4; protein.
DR Bgee; ENSG00000076604; Expressed in olfactory segment of nasal mucosa and 186 other tissues.
DR ExpressionAtlas; Q9BUZ4; baseline and differential.
DR Genevisible; Q9BUZ4; HS.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0031996; F:thioesterase binding; IPI:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0050699; F:WW domain binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:Ensembl.
DR GO; GO:0030323; P:respiratory tube development; IEA:Ensembl.
DR CDD; cd03781; MATH_TRAF4; 1.
DR Gene3D; 2.60.210.10; -; 1.
DR Gene3D; 3.30.40.10; -; 4.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR043211; TNF_rcpt-assoc_TRAF.
DR InterPro; IPR012227; TNF_rcpt-assoc_TRAF_met.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR027138; TRAF4.
DR InterPro; IPR037307; TRAF4_MATH.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR InterPro; IPR001293; Znf_TRAF.
DR PANTHER; PTHR10131; PTHR10131; 2.
DR PANTHER; PTHR10131:SF120; PTHR10131:SF120; 2.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF02176; zf-TRAF; 2.
DR PIRSF; PIRSF015614; TRAF; 1.
DR SMART; SM00061; MATH; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50145; ZF_TRAF; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cell junction;
KW Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Immunity; Innate immunity; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Tight junction; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..470
FT /note="TNF receptor-associated factor 4"
FT /id="PRO_0000056403"
FT DOMAIN 307..462
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT ZN_FING 18..58
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 102..154
FT /note="TRAF-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT ZN_FING 155..208
FT /note="TRAF-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT ZN_FING 209..266
FT /note="TRAF-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT COILED 277..309
FT /evidence="ECO:0000255"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 157..428
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.3"
FT /id="VSP_007403"
FT VARIANT 173
FT /note="A -> T (in dbSNP:rs35932778)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025805"
FT VARIANT 178
FT /note="R -> G (in dbSNP:rs1044066)"
FT /evidence="ECO:0000269|PubMed:7490069"
FT /id="VAR_052150"
FT MUTAGEN 18
FT /note="C->A: Complete loss of E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:32357935"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:2YUC"
FT TURN 127..132
FT /evidence="ECO:0007829|PDB:2YUC"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2YUC"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:2YUC"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:2YUC"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2EOD"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:2EOD"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:2EOD"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:2EOD"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:2EOD"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:2EOD"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:2EOD"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:2EOD"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2EOD"
FT HELIX 286..301
FT /evidence="ECO:0007829|PDB:3ZJB"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:3ZJB"
FT HELIX 317..326
FT /evidence="ECO:0007829|PDB:3ZJB"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:3ZJB"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:3ZJB"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:3ZJB"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:3ZJB"
FT STRAND 362..370
FT /evidence="ECO:0007829|PDB:3ZJB"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:3ZJB"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:3ZJB"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:3ZJB"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:3ZJB"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:3ZJB"
FT HELIX 427..431
FT /evidence="ECO:0007829|PDB:4M4E"
FT STRAND 434..441
FT /evidence="ECO:0007829|PDB:3ZJB"
FT HELIX 442..445
FT /evidence="ECO:0007829|PDB:3ZJB"
FT TURN 446..450
FT /evidence="ECO:0007829|PDB:3ZJB"
FT STRAND 455..462
FT /evidence="ECO:0007829|PDB:3ZJB"
SQ SEQUENCE 470 AA; 53543 MW; A3F57E0E1081AB88 CRC64;
MPGFDYKFLE KPKRRLLCPL CGKPMREPVQ VSTCGHRFCD TCLQEFLSEG VFKCPEDQLP
LDYAKIYPDP ELEVQVLGLP IRCIHSEEGC RWSGPLRHLQ GHLNTCSFNV IPCPNRCPMK
LSRRDLPAHL QHDCPKRRLK CEFCGCDFSG EAYESHEGMC PQESVYCENK CGARMMRRLL
AQHATSECPK RTQPCTYCTK EFVFDTIQSH QYQCPRLPVA CPNQCGVGTV AREDLPGHLK
DSCNTALVLC PFKDSGCKHR CPKLAMARHV EESVKPHLAM MCALVSRQRQ ELQELRRELE
ELSVGSDGVL IWKIGSYGRR LQEAKAKPNL ECFSPAFYTH KYGYKLQVSA FLNGNGSGEG
THLSLYIRVL PGAFDNLLEW PFARRVTFSL LDQSDPGLAK PQHVTETFHP DPNWKNFQKP
GTWRGSLDES SLGFGYPKFI SHQDIRKRNY VRDDAVFIRA AVELPRKILS
