ID   NPL4_HUMAN              Reviewed;         608 AA.
AC   Q8TAT6; Q8N3J1; Q9H8V2; Q9H964; Q9NWR5; Q9P229;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Nuclear protein localization protein 4 homolog;
DE            Short=Protein NPL4;
GN   Name=NPLOC4; Synonyms=KIAA1499, NPL4;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:143-150(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
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   [4]
RP   PROTEIN SEQUENCE OF 2-8.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA   Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass spectrometric
RT   identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-608.
RC   TISSUE=Melanoma;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   INTERACTION WITH UFD1, AND TISSUE SPECIFICITY.
RX   PubMed=11574150; DOI=10.1016/s0378-1119(01)00649-7;
RA   Botta A., Tandoi C., Fini G., Calabrese G., Dallapiccola B., Novelli G.;
RT   "Cloning and characterization of the gene encoding human NPL4, a protein
RT   interacting with the ubiquitin fusion-degradation protein (UFD1L).";
RL   Gene 275:39-46(2001).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [8]
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   [9]
RP   INTERACTION WITH ZFAND2B.
RX   PubMed=24160817; DOI=10.1042/bj20130710;
RA   Glinka T., Alter J., Braunstein I., Tzach L., Wei Sheng C., Geifman S.,
RA   Edelmann M.J., Kessler B.M., Stanhill A.;
RT   "Signal-peptide-mediated translocation is regulated by a p97-AIRAPL
RT   complex.";
RL   Biochem. J. 457:253-261(2014).
RN   [10]
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   [11]
RP   FUNCTION, INTERACTION WITH UFD1 AND VCP, AND MUTAGENESIS OF 6-ILE--ARG-8;
RP   ARG-17 AND ARG-50.
RX   PubMed=26471729; DOI=10.15252/embj.201591888;
RA   Hao Q., Jiao S., Shi Z., Li C., Meng X., Zhang Z., Wang Y., Song X.,
RA   Wang W., Zhang R., Zhao Y., Wong C.C., Zhou Z.;
RT   "A non-canonical role of the p97 complex in RIG-I antiviral signaling.";
RL   EMBO J. 34:2903-2920(2015).
CC   -!- FUNCTION: The ternary complex containing UFD1, VCP and NPLOC4 binds
CC       ubiquitinated proteins and is necessary for the export of misfolded
CC       proteins from the ER to the cytoplasm, where they are degraded by the
CC       proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly
CC       at the end of mitosis and is necessary for the formation of a closed
CC       nuclear envelope (By similarity). Acts as a negative regulator of type
CC       I interferon production via the complex formed with VCP and UFD1, which
CC       binds to RIGI and recruits RNF125 to promote ubiquitination and
CC       degradation of RIGI (PubMed:26471729). {ECO:0000250|UniProtKB:Q9ES54,
CC       ECO:0000269|PubMed:26471729}.
CC   -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent pathway.
CC   -!- SUBUNIT: Heterodimer with UFD1 (PubMed:11574150, PubMed:26471729). The
CC       heterodimer binds ubiquitinated proteins (By similarity). The
CC       heterodimer binds to VCP and inhibits Golgi membrane fusion
CC       (PubMed:11574150, PubMed:26471729). Interacts with ZFAND2B; probably
CC       through VCP (PubMed:24160817). {ECO:0000250|UniProtKB:Q9ES54,
CC       ECO:0000269|PubMed:11574150, ECO:0000269|PubMed:24160817,
CC       ECO:0000269|PubMed:26471729}.
CC   -!- INTERACTION:
CC       Q8TAT6; O95786: RIGI; NbExp=6; IntAct=EBI-1994109, EBI-995350;
CC       Q8TAT6; P37173: TGFBR2; NbExp=3; IntAct=EBI-1994109, EBI-296151;
CC       Q8TAT6; Q92890: UFD1; NbExp=8; IntAct=EBI-1994109, EBI-1994090;
CC       Q8TAT6; P55072: VCP; NbExp=13; IntAct=EBI-1994109, EBI-355164;
CC       Q8TAT6; Q4G0F5: VPS26B; NbExp=3; IntAct=EBI-1994109, EBI-6151831;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9ES54}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q9ES54}. Nucleus {ECO:0000250|UniProtKB:Q9ES54}.
CC       Note=Associated with the endoplasmic reticulum and nuclear.
CC       {ECO:0000250|UniProtKB:Q9ES54}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8TAT6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8TAT6-2; Sequence=VSP_009789;
CC   -!- TISSUE SPECIFICITY: Expressed at highest levels in brain, heart,
CC       skeletal muscle, kidney and fetal liver. {ECO:0000269|PubMed:11574150}.
CC   -!- DOMAIN: Binds ubiquitinated proteins via its RanBP2-type zinc finger.
CC       {ECO:0000250|UniProtKB:Q9ES54}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the NPL4 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA91314.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA96023.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB14372.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB14499.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB040932; BAA96023.1; ALT_INIT; mRNA.
DR   EMBL; AK000664; BAA91314.1; ALT_INIT; mRNA.
DR   EMBL; AK023046; BAB14372.1; ALT_INIT; mRNA.
DR   EMBL; AK023272; BAB14499.1; ALT_INIT; mRNA.
DR   EMBL; BC025930; AAH25930.1; -; mRNA.
DR   EMBL; AL834300; CAD38971.1; -; mRNA.
DR   CCDS; CCDS45812.1; -. [Q8TAT6-1]
DR   RefSeq; NP_060391.2; NM_017921.3. [Q8TAT6-1]
DR   RefSeq; XP_011523281.1; XM_011524979.1. [Q8TAT6-2]
DR   PDB; 7WWP; X-ray; 2.99 A; A=91-560.
DR   PDB; 7WWQ; X-ray; 2.72 A; A=96-560.
DR   PDBsum; 7WWP; -.
DR   PDBsum; 7WWQ; -.
DR   AlphaFoldDB; Q8TAT6; -.
DR   SMR; Q8TAT6; -.
DR   BioGRID; 120798; 218.
DR   ComplexPortal; CPX-137; VCP-NPL4-UFD1 AAA ATPase complex.
DR   ComplexPortal; CPX-8096; VCP-NPL4-UFD1-FAF1 AAA ATPase complex.
DR   ComplexPortal; CPX-8101; VCP-NPL4-UFD1-UBXN7 AAA ATPase complex.
DR   ComplexPortal; CPX-8104; VCP-NPL4-UFD1-FAF2 AAA ATPase complex.
DR   ComplexPortal; CPX-8105; VCP-NPL4-UFD1-UBXN1 AAA ATPase complex.
DR   CORUM; Q8TAT6; -.
DR   DIP; DIP-44059N; -.
DR   IntAct; Q8TAT6; 45.
DR   MINT; Q8TAT6; -.
DR   STRING; 9606.ENSP00000331487; -.
DR   TCDB; 3.A.16.1.1; the endoplasmic reticular retrotranslocon (er-rt) family.
DR   GlyGen; Q8TAT6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8TAT6; -.
DR   PhosphoSitePlus; Q8TAT6; -.
DR   SwissPalm; Q8TAT6; -.
DR   BioMuta; NPLOC4; -.
DR   DMDM; 50428974; -.
DR   EPD; Q8TAT6; -.
DR   jPOST; Q8TAT6; -.
DR   MassIVE; Q8TAT6; -.
DR   MaxQB; Q8TAT6; -.
DR   PaxDb; 9606-ENSP00000331487; -.
DR   PeptideAtlas; Q8TAT6; -.
DR   ProteomicsDB; 73917; -. [Q8TAT6-1]
DR   ProteomicsDB; 73918; -. [Q8TAT6-2]
DR   Pumba; Q8TAT6; -.
DR   Antibodypedia; 10070; 165 antibodies from 28 providers.
DR   DNASU; 55666; -.
DR   Ensembl; ENST00000331134.11; ENSP00000331487.5; ENSG00000182446.15. [Q8TAT6-1]
DR   Ensembl; ENST00000374747.9; ENSP00000363879.5; ENSG00000182446.15. [Q8TAT6-2]
DR   GeneID; 55666; -.
DR   KEGG; hsa:55666; -.
DR   MANE-Select; ENST00000331134.11; ENSP00000331487.5; NM_017921.4; NP_060391.2.
DR   UCSC; uc002kat.5; human. [Q8TAT6-1]
DR   AGR; HGNC:18261; -.
DR   CTD; 55666; -.
DR   DisGeNET; 55666; -.
DR   GeneCards; NPLOC4; -.
DR   HGNC; HGNC:18261; NPLOC4.
DR   HPA; ENSG00000182446; Tissue enhanced (skeletal).
DR   MIM; 606590; gene.
DR   neXtProt; NX_Q8TAT6; -.
DR   OpenTargets; ENSG00000182446; -.
DR   PharmGKB; PA143485558; -.
DR   VEuPathDB; HostDB:ENSG00000182446; -.
DR   eggNOG; KOG2834; Eukaryota.
DR   GeneTree; ENSGT00390000018731; -.
DR   HOGENOM; CLU_017172_2_0_1; -.
DR   InParanoid; Q8TAT6; -.
DR   OMA; KWSRTGR; -.
DR   OrthoDB; 5400828at2759; -.
DR   PhylomeDB; Q8TAT6; -.
DR   TreeFam; TF314173; -.
DR   PathwayCommons; Q8TAT6; -.
DR   Reactome; R-HSA-110320; Translesion Synthesis by POLH.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR   SignaLink; Q8TAT6; -.
DR   SIGNOR; Q8TAT6; -.
DR   UniPathway; UPA00144; -.
DR   BioGRID-ORCS; 55666; 808 hits in 1156 CRISPR screens.
DR   ChiTaRS; NPLOC4; human.
DR   GeneWiki; NPLOC4; -.
DR   GenomeRNAi; 55666; -.
DR   Pharos; Q8TAT6; Tbio.
DR   PRO; PR:Q8TAT6; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q8TAT6; Protein.
DR   Bgee; ENSG00000182446; Expressed in gastrocnemius and 196 other cell types or tissues.
DR   ExpressionAtlas; Q8TAT6; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR   GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; ISS:HGNC-UCL.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0036501; C:UFD1-NPL4 complex; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:UniProtKB.
DR   GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR   GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR   GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0007030; P:Golgi organization; ISS:HGNC-UCL.
DR   GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; IMP:UniProtKB.
DR   GO; GO:0032480; P:negative regulation of type I interferon production; IMP:UniProtKB.
DR   GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:ComplexPortal.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   CDD; cd08061; MPN_NPL4; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR016563; Npl4.
DR   InterPro; IPR007717; NPL4_C.
DR   InterPro; IPR024682; Npl4_Ub-like_dom.
DR   InterPro; IPR007716; NPL4_Zn-bd_put.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   PANTHER; PTHR12710; NUCLEAR PROTEIN LOCALIZATION 4; 1.
DR   PANTHER; PTHR12710:SF0; NUCLEAR PROTEIN LOCALIZATION PROTEIN 4 HOMOLOG; 1.
DR   Pfam; PF05021; NPL4; 1.
DR   Pfam; PF11543; UN_NPL4; 1.
DR   Pfam; PF05020; zf-NPL4; 1.
DR   PIRSF; PIRSF010052; Polyub_prc_Npl4; 1.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50249; MPN; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
DR   Genevisible; Q8TAT6; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Chaperone; Cytoplasm;
KW   Direct protein sequencing; Endoplasmic reticulum; Metal-binding; Nucleus;
KW   Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12665801,
FT                   ECO:0007744|PubMed:19413330"
FT   CHAIN           2..608
FT                   /note="Nuclear protein localization protein 4 homolog"
FT                   /id="PRO_0000057941"
FT   DOMAIN          226..363
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   ZN_FING         580..608
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   MOD_RES         179
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P60670"
FT   VAR_SEQ         558..608
FT                   /note="TVGGQLPGLHEYGAVGGSTHTATAAMWACQHCTFMNQPGTGHCEMCSLPRT
FT                   -> EYPHPLPRHPVAGAGEQPTLHSSPLPVVPWIPHPAASWQVPSAMQRVETRPPCQAR
FT                   GRLR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10819331"
FT                   /id="VSP_009789"
FT   MUTAGEN         6..8
FT                   /note="IIR->AIA: Abolished interaction with VCP; when
FT                   associated with A-17 and A-50."
FT                   /evidence="ECO:0000269|PubMed:26471729"
FT   MUTAGEN         17
FT                   /note="R->A: Abolished interaction with VCP; when
FT                   associated with 6-A--A-8 and A-50."
FT                   /evidence="ECO:0000269|PubMed:26471729"
FT   MUTAGEN         50
FT                   /note="R->A: Abolished interaction with VCP; when
FT                   associated with 6-A--A-8 and A-17."
FT                   /evidence="ECO:0000269|PubMed:26471729"
FT   CONFLICT        246
FT                   /note="N -> S (in Ref. 2; BAB14499)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="H -> Q (in Ref. 2; BAA91314)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        573
FT                   /note="G -> E (in Ref. 2; BAA91314)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        592
FT                   /note="M -> V (in Ref. 2; BAB14499)"
FT                   /evidence="ECO:0000305"
FT   HELIX           109..114
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          127..129
FT                   /evidence="ECO:0007829|PDB:7WWP"
FT   TURN            139..141
FT                   /evidence="ECO:0007829|PDB:7WWP"
FT   HELIX           151..153
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:7WWP"
FT   STRAND          160..163
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   HELIX           164..169
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          213..215
FT                   /evidence="ECO:0007829|PDB:7WWP"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          225..230
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   HELIX           231..244
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          249..259
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          265..274
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          277..281
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          284..287
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   HELIX           293..302
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          306..313
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   TURN            320..323
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   HELIX           338..350
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          351..354
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          356..358
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          361..365
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          368..374
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          378..387
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   HELIX           389..396
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          400..403
FT                   /evidence="ECO:0007829|PDB:7WWP"
FT   STRAND          409..412
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          424..427
FT                   /evidence="ECO:0007829|PDB:7WWP"
FT   STRAND          441..444
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   HELIX           445..447
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          449..455
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   HELIX           477..479
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   HELIX           485..494
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   TURN            495..497
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   HELIX           500..504
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   HELIX           507..515
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          517..519
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   STRAND          522..524
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   HELIX           526..533
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   HELIX           537..544
FT                   /evidence="ECO:0007829|PDB:7WWQ"
FT   HELIX           547..556
FT                   /evidence="ECO:0007829|PDB:7WWQ"
SQ   SEQUENCE   608 AA;  68120 MW;  6ED6A0145F15C01D CRC64;
     MAESIIIRVQ SPDGVKRITA TKRETAATFL KKVAKEFGFQ NNGFSVYINR NKTGEITASS
     NKSLNLLKIK HGDLLFLFPS SLAGPSSEME TSVPPGFKVF GAPNVVEDEI DQYLSKQDGK
     IYRSRDPQLC RHGPLGKCVH CVPLEPFDED YLNHLEPPVK HMSFHAYIRK LTGGADKGKF
     VALENISCKI KSGCEGHLPW PNGICTKCQP SAITLNRQKY RHVDNIMFEN HTVADRFLDF
     WRKTGNQHFG YLYGRYTEHK DIPLGIRAEV AAIYEPPQIG TQNSLELLED PKAEVVDEIA
     AKLGLRKVGW IFTDLVSEDT RKGTVRYSRN KDTYFLSSEE CITAGDFQNK HPNMCRLSPD
     GHFGSKFVTA VATGGPDNQV HFEGYQVSNQ CMALVRDECL LPCKDAPELG YAKESSSEQY
     VPDVFYKDVD KFGNEITQLA RPLPVEYLII DITTTFPKDP VYTFSISQNP FPIENRDVLG
     ETQDFHSLAT YLSQNTSSVF LDTISDFHLL LFLVTNEVMP LQDSISLLLE AVRTRNEELA
     QTWKRSEQWA TIEQLCSTVG GQLPGLHEYG AVGGSTHTAT AAMWACQHCT FMNQPGTGHC
     EMCSLPRT
//