RNF31_MOUSE
ID RNF31_MOUSE Reviewed; 1066 AA.
AC Q924T7;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=E3 ubiquitin-protein ligase RNF31;
DE EC=2.3.2.31 {ECO:0000250|UniProtKB:Q96EP0};
DE AltName: Full=HOIL-1-interacting protein {ECO:0000250|UniProtKB:Q96EP0};
DE Short=HOIP {ECO:0000250|UniProtKB:Q96EP0};
DE AltName: Full=Putative Ariadne-like ubiquitin ligase {ECO:0000303|PubMed:14678832};
DE Short=PAUL {ECO:0000303|PubMed:14678832};
DE AltName: Full=RING finger protein 31 {ECO:0000312|MGI:MGI:1934704};
DE AltName: Full=RING-type E3 ubiquitin transferase RNF31 {ECO:0000305};
GN Name=Rnf31 {ECO:0000312|MGI:MGI:1934704};
GN Synonyms=Paul {ECO:0000303|PubMed:14678832};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RC STRAIN=129/SvJ;
RX PubMed=11345588; DOI=10.1007/s002510100308;
RA Yawata M., Murata S., Tanaka K., Ishigatsubo Y., Kasahara M.;
RT "Nucleotide sequence analysis of the ~35-kb segment containing interferon-
RT gamma-inducible mouse proteasome activator genes.";
RL Immunogenetics 53:119-129(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP INTERACTION WITH MUSK, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14678832; DOI=10.1016/s1567-133x(03)00146-7;
RA Bromann P.A., Weiner J.A., Apel E.D., Lewis R.M., Sanes J.R.;
RT "A putative ariadne-like E3 ubiquitin ligase (PAUL) that interacts with the
RT muscle-specific kinase (MuSK).";
RL Gene Expr. Patterns 4:77-84(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH OTULIN.
RX PubMed=23708998; DOI=10.1038/nature12296;
RA Rivkin E., Almeida S.M., Ceccarelli D.F., Juang Y.C., Maclean T.A.,
RA Srikumar T., Huang H., Dunham W.H., Fukumura R., Xie G., Gondo Y.,
RA Raught B., Gingras A.C., Sicheri F., Cordes S.P.;
RT "The linear ubiquitin-specific deubiquitinase gumby regulates
RT angiogenesis.";
RL Nature 498:318-324(2013).
RN [6]
RP FUNCTION.
RX PubMed=28701375; DOI=10.1101/gad.299776.117;
RA Wei R., Xu L.W., Liu J., Li Y., Zhang P., Shan B., Lu X., Qian L., Wu Z.,
RA Dong K., Zhu H., Pan L., Yuan J., Pan H.;
RT "SPATA2 regulates the activation of RIPK1 by modulating linear
RT ubiquitination.";
RL Genes Dev. 31:1162-1176(2017).
RN [7]
RP AUTOUBIQUITINATION, AND INTERACTION WITH OTULIN.
RX PubMed=29950720; DOI=10.1038/s41586-018-0256-2;
RA Heger K., Wickliffe K.E., Ndoja A., Zhang J., Murthy A., Dugger D.L.,
RA Maltzman A., de Sousa E Melo F., Hung J., Zeng Y., Verschueren E.,
RA Kirkpatrick D.S., Vucic D., Lee W.P., Roose-Girma M., Newman R.J.,
RA Warming S., Hsiao Y.C., Komuves L.G., Webster J.D., Newton K., Dixit V.M.;
RT "OTULIN limits cell death and inflammation by deubiquitinating LUBAC.";
RL Nature 559:120-124(2018).
CC -!- FUNCTION: E3 ubiquitin-protein ligase component of the LUBAC complex
CC which conjugates linear ('Met-1'-linked) polyubiquitin chains to
CC substrates and plays a key role in NF-kappa-B activation and regulation
CC of inflammation (PubMed:28701375). LUBAC conjugates linear
CC polyubiquitin to IKBKG and RIPK1 and is involved in activation of the
CC canonical NF-kappa-B and the JNK signaling pathways (By similarity).
CC Linear ubiquitination mediated by the LUBAC complex interferes with
CC TNF-induced cell death and thereby prevents inflammation
CC (PubMed:28701375). LUBAC is recruited to the TNF-R1 signaling complex
CC (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2
CC and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and
CC possibly other components contributing to the stability of the complex
CC (By similarity). The LUBAC complex is also involved in innate immunity
CC by conjugating linear polyubiquitin chains at the surface of bacteria
CC invading the cytosol to form the ubiquitin coat surrounding bacteria
CC (By similarity). LUBAC is not able to initiate formation of the
CC bacterial ubiquitin coat, and can only promote formation of linear
CC polyubiquitins on pre-existing ubiquitin (By similarity). Recruited to
CC the surface of bacteria by RNF213, which initiates the bacterial
CC ubiquitin coat (By similarity). The bacterial ubiquitin coat acts as an
CC 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (By
CC similarity). Together with OTULIN, the LUBAC complex regulates the
CC canonical Wnt signaling during angiogenesis (By similarity). RNF31 is
CC required for linear ubiquitination of BCL10, thereby promoting TCR-
CC induced NF-kappa-B activation (By similarity). Binds polyubiquitin of
CC different linkage types (By similarity). {ECO:0000250|UniProtKB:Q96EP0,
CC ECO:0000269|PubMed:28701375}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:Q96EP0};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q96EP0}.
CC -!- SUBUNIT: Component of the LUBAC complex (linear ubiquitin chain
CC assembly complex) which consists of SHARPIN, RBCK1 and RNF31 (By
CC similarity). LUBAC has a MW of approximately 600 kDa suggesting a
CC heteromultimeric assembly of its subunits (By similarity). Associates
CC with the TNF-R1 signaling complex (TNF-RSC) in a stimulation-dependent
CC manner (By similarity). Interacts (via the PUB domain) with OTULIN (via
CC the PIM motif); the interaction is direct (PubMed:23708998). Interacts
CC (via the PUB domain) with VCP (via the PIM motif) (By similarity).
CC Interacts (via the PUB domain) with SPATA2 (via the PIM motif);
CC interaction is direct and bridges RNF31 and CYLD (By similarity).
CC Interacts with CYLD; the interaction is indirect and is mediated via
CC SPATA2 (By similarity). Interacts with MUSK (PubMed:14678832).
CC Interacts with CARD11, promoting linear ubiquitination of BCL10 (By
CC similarity). {ECO:0000250|UniProtKB:Q96EP0,
CC ECO:0000269|PubMed:14678832, ECO:0000269|PubMed:23708998}.
CC -!- INTERACTION:
CC Q924T7; O88522: Ikbkg; NbExp=7; IntAct=EBI-647680, EBI-998011;
CC Q924T7; Q9WUB0: Rbck1; NbExp=10; IntAct=EBI-647680, EBI-6141072;
CC Q924T7; Q91WA6: Sharpin; NbExp=10; IntAct=EBI-647680, EBI-646097;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14678832}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q924T7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q924T7-2; Sequence=VSP_009649;
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). Not expressed
CC in heart. {ECO:0000269|PubMed:14678832}.
CC -!- DOMAIN: The PUB domain mediates interaction with the PIM motifs of VCP
CC and RNF31, with a strong preference for RNF31.
CC {ECO:0000250|UniProtKB:Q96EP0}.
CC -!- DOMAIN: The RanBP2-type zinc fingers mediate the specific interaction
CC with ubiquitin. {ECO:0000250|UniProtKB:Q96EP0}.
CC -!- DOMAIN: The UBA domain mediates association with RBCK1/HOIL1 via
CC interaction with its UBL domain. {ECO:0000250|UniProtKB:Q96EP0}.
CC -!- DOMAIN: RING 1 and IBR zinc-fingers catalyze the first step transfer of
CC ubiquitin from the E2 onto RING 2, to transiently form a HECT-like
CC covalent thioester intermediate. {ECO:0000250|UniProtKB:Q96EP0}.
CC -!- DOMAIN: The linear ubiquitin chain determining domain (LDD) mediates
CC the final transfer of ubiquitin from RING 2 onto the N-terminus of a
CC target ubiquitin. {ECO:0000250|UniProtKB:Q96EP0}.
CC -!- PTM: Autoubiquitinated (PubMed:29950720). Interaction with OTULIN is
CC required to suppress formation of 'Met-1'-linked polyubiquitin chains
CC and prevent subsequent inactivation of the LUBAC complex
CC (PubMed:29950720). {ECO:0000269|PubMed:29950720}.
CC -!- PTM: Cleaved by caspase during apoptosis.
CC {ECO:0000250|UniProtKB:Q96EP0}.
CC -!- SIMILARITY: Belongs to the RBR family. {ECO:0000305}.
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DR EMBL; AB053120; BAB47406.1; -; Genomic_DNA.
DR EMBL; BC057595; AAH57595.1; -; mRNA.
DR CCDS; CCDS27118.1; -. [Q924T7-1]
DR RefSeq; NP_919327.2; NM_194346.2. [Q924T7-1]
DR PDB; 5Y3T; X-ray; 2.40 A; B=474-630.
DR PDBsum; 5Y3T; -.
DR AlphaFoldDB; Q924T7; -.
DR SMR; Q924T7; -.
DR BioGRID; 234548; 19.
DR DIP; DIP-49579N; -.
DR IntAct; Q924T7; 6.
DR MINT; Q924T7; -.
DR STRING; 10090.ENSMUSP00000019443; -.
DR iPTMnet; Q924T7; -.
DR PhosphoSitePlus; Q924T7; -.
DR EPD; Q924T7; -.
DR MaxQB; Q924T7; -.
DR PaxDb; Q924T7; -.
DR PRIDE; Q924T7; -.
DR ProteomicsDB; 300557; -. [Q924T7-1]
DR ProteomicsDB; 300558; -. [Q924T7-2]
DR DNASU; 268749; -.
DR Ensembl; ENSMUST00000019443; ENSMUSP00000019443; ENSMUSG00000047098. [Q924T7-1]
DR GeneID; 268749; -.
DR KEGG; mmu:268749; -.
DR UCSC; uc007tzi.1; mouse. [Q924T7-1]
DR CTD; 55072; -.
DR MGI; MGI:1934704; Rnf31.
DR VEuPathDB; HostDB:ENSMUSG00000047098; -.
DR eggNOG; KOG1812; Eukaryota.
DR GeneTree; ENSGT00530000064112; -.
DR HOGENOM; CLU_014581_0_0_1; -.
DR InParanoid; Q924T7; -.
DR OMA; RNNDPEY; -.
DR OrthoDB; 1188714at2759; -.
DR PhylomeDB; Q924T7; -.
DR TreeFam; TF350529; -.
DR Reactome; R-MMU-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-MMU-5357956; TNFR1-induced NFkappaB signaling pathway.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 268749; 31 hits in 79 CRISPR screens.
DR ChiTaRS; Rnf31; mouse.
DR PRO; PR:Q924T7; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q924T7; protein.
DR Bgee; ENSMUSG00000047098; Expressed in granulocyte and 229 other tissues.
DR ExpressionAtlas; Q924T7; baseline and differential.
DR Genevisible; Q924T7; MM.
DR GO; GO:0035631; C:CD40 receptor complex; IDA:BHF-UCL.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0071797; C:LUBAC complex; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:1990450; F:linear polyubiquitin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0023035; P:CD40 signaling pathway; IMP:BHF-UCL.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0060546; P:negative regulation of necroptotic process; IGI:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:BHF-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:1904417; P:positive regulation of xenophagy; ISS:UniProtKB.
DR GO; GO:0097039; P:protein linear polyubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IMP:BHF-UCL.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR036339; PUB-like_dom_sf.
DR InterPro; IPR018997; PUB_domain.
DR InterPro; IPR026254; RNF31-like.
DR InterPro; IPR032065; RNF31-UBA.
DR InterPro; IPR041031; RNF31_C.
DR InterPro; IPR040641; RNF31_PUB.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR16004; PTHR16004; 3.
DR Pfam; PF18091; E3_UbLigase_RBR; 1.
DR Pfam; PF16678; HOIP-UBA; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF09409; PUB; 1.
DR Pfam; PF18486; PUB_1; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00547; ZnF_RBZ; 3.
DR SUPFAM; SSF143503; SSF143503; 1.
DR SUPFAM; SSF90209; SSF90209; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 3.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1066
FT /note="E3 ubiquitin-protein ligase RNF31"
FT /id="PRO_0000056070"
FT DOMAIN 70..141
FT /note="PUB"
FT /evidence="ECO:0000255"
FT DOMAIN 558..609
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT ZN_FING 293..325
FT /note="RanBP2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 344..373
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 403..432
FT /note="RanBP2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 693..743
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 773..835
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 865..895
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 1..479
FT /note="Polyubiquitin-binding"
FT /evidence="ECO:0000250"
FT REGION 251..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..610
FT /note="Interaction with RBCK1"
FT /evidence="ECO:0000250"
FT REGION 689..923
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 904..1066
FT /note="LDD domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 256..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 879
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 693
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 696
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 716
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 719
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 793
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 796
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 811
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 814
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 819
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 822
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 830
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 835
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 865
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 868
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 887
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 892
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 910
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 919
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT SITE 384..385
FT /note="Cleavage; by caspase"
FT /evidence="ECO:0000250|UniProtKB:Q96EP0"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EP0"
FT VAR_SEQ 826..834
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_009649"
FT HELIX 474..494
FT /evidence="ECO:0007829|PDB:5Y3T"
FT HELIX 499..509
FT /evidence="ECO:0007829|PDB:5Y3T"
FT HELIX 514..536
FT /evidence="ECO:0007829|PDB:5Y3T"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:5Y3T"
FT HELIX 545..554
FT /evidence="ECO:0007829|PDB:5Y3T"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:5Y3T"
FT HELIX 559..579
FT /evidence="ECO:0007829|PDB:5Y3T"
FT HELIX 584..586
FT /evidence="ECO:0007829|PDB:5Y3T"
FT HELIX 588..594
FT /evidence="ECO:0007829|PDB:5Y3T"
FT TURN 595..597
FT /evidence="ECO:0007829|PDB:5Y3T"
FT HELIX 599..617
FT /evidence="ECO:0007829|PDB:5Y3T"
SQ SEQUENCE 1066 AA; 119314 MW; C630572B8BDFC0AD CRC64;
MPGDEERGFL AAREELASAL RWDSAQVFPL EQLMPLLATS LPPAARYLQL DAGRLVRCNA
HGEPRNYLNT LSTALNILEK YGRNLLSPQR PRYWRSVKFN NPVFRSTVDA VQGGRDVLRL
YGYTEERPDG LSFPEGQEEP DEYQVAVVTL EVLLLRTELS LLLQNTHPRQ NALDQLLRES
VEDGMLQLSE FHPLLREIVP GPRPSAQGST PGPCFLCGSA PGTLHCPACN QVSCPACDIL
FHGHPSRAHH LRQALPGSHQ TASLSSSLPA SSQPRPPSSS LALGDSSLSS PDPANACLPW
HCLTCATLNE PWAVFCAVCS QPKGCKVPGI EGSHGTGGLE PEPARDQWAC QSCTFENEAA
AVLCAICERP RLAQPPSLVV DSHDAGVCQQ SLKQEDPLLT AAQPQVWYCD HCTFCNSGPV
WVCAMCNRTR DPIPTQPALQ SYPSSLEKGR PKPGSSQHLG SSLPASCGDP EKQRQDKMRK
EGLQLVSMIQ EGETAGASPE EVFSALQYSG TEVPLQWLRS ELSYVLEMVA ELAGQQDPEL
GAFSCQEARK AWLDRHGNLD EAVEECVRAR RRKVHELQSL GFGPKEGSLQ ALFQHGGDVA
RALTELQRQR LEPFHQRLWD RDPEPTPCWD GLDRQSLVRR LLAVYTLPSW GRAELALALL
QETPRNYELL DVVEAVRHSQ DRAFLRRLLA QECAVCGWAL PRNRMQALIS CECTICPECF
RQHFTIALKE KHITDMVCPA CGRPDLTDDA QLLSYFSTLD IQLRESLDPD AYALFHKKLT
EAVLMRDPKF LWCAQCSFGF IYEREQLEAT CPQCHQTFCV RCKRQWEEQH RGRSCEDFQN
WKRTNDPEYQ AQGLAMYLQE NGIDCPKCKF SYALARGGCM HFHCTQCRHQ FCSGCYNAFY
AKNKCPDPNC KVKKSLHGHH PRDCLFYLRD WTAARLQKLL QDNNVMFNTE PPAGTRAVPG
GGCRVMEQKE VHSGFRDEAC GKETPPGYAG LCQAHYKEYL VSLINAHSLD PATLYEVEEL
ETATIRYLHL APQPADGEDL PAYQARLLQK LREEVPLGQS IARRRK
