MYCB2_DANRE
ID MYCB2_DANRE Reviewed; 4574 AA.
AC F1RD40; D3JU51; D3JU52; F1QI76; Q5IBM5; Q7ZZ57; Q8AW10;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=E3 ubiquitin-protein ligase MYCBP2 {ECO:0000305};
DE EC=2.3.2.33 {ECO:0000250|UniProtKB:O75592};
DE AltName: Full=Myc-binding protein 2 {ECO:0000305};
DE AltName: Full=Protein Esrom {ECO:0000303|PubMed:15590740};
GN Name=mycbp2 {ECO:0000312|ZFIN:ZDB-GENE-030616-132};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15590740; DOI=10.1242/dev.01578;
RA D'Souza J., Hendricks M., Le Guyader S., Subburaju S., Grunewald B.,
RA Scholich K., Jesuthasan S.;
RT "Formation of the retinotectal projection requires Esrom, an ortholog of
RT PAM (protein associated with Myc).";
RL Development 132:247-256(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 527-1089 (ISOFORM 2).
RX PubMed=20143133; DOI=10.1007/s11010-010-0385-x;
RA Wang H.;
RT "Characterization of zebrafish Esrom (Myc-binding protein 2) RCC1-like
RT domain splice variants.";
RL Mol. Cell. Biochem. 339:191-199(2010).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15617681; DOI=10.1016/j.ydbio.2004.09.029;
RA Le Guyader S., Maier J., Jesuthasan S.;
RT "Esrom, an ortholog of PAM (protein associated with c-myc), regulates
RT pteridine synthesis in the zebrafish.";
RL Dev. Biol. 277:378-386(2005).
CC -!- FUNCTION: Atypical E3 ubiquitin-protein ligase which specifically
CC mediates ubiquitination of threonine and serine residues on target
CC proteins, instead of ubiquitinating lysine residues (By similarity).
CC Shows esterification activity towards both threonine and serine, with a
CC preference for threonine, and acts via two essential catalytic cysteine
CC residues that relay ubiquitin to its substrate via thioester
CC intermediates (By similarity). Interacts with the E2 enzymes UBE2D1,
CC UBE2D3, UBE2E1 and UBE2L3 (By similarity). Plays a key role in neural
CC development, probably by mediating ubiquitination of threonine residues
CC on target proteins (By similarity). Involved in different processes
CC such as regulation of neurite outgrowth, synaptic growth,
CC synaptogenesis and axon degeneration (By similarity). Required in the
CC visual system for correct fasciculation, targeting and mapping of
CC retinal axons (PubMed:15590740). Acts as a regulator of pteridine
CC synthesis (PubMed:15617681). May play a role in the regulation of the
CC circadian clock gene expression (By similarity).
CC {ECO:0000250|UniProtKB:O75592, ECO:0000250|UniProtKB:Q7TPH6,
CC ECO:0000269|PubMed:15590740, ECO:0000269|PubMed:15617681}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-threonine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-3-O-ubiquitinyl-L-threonine.;
CC EC=2.3.2.33; Evidence={ECO:0000250|UniProtKB:O75592};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:O75592}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75592}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q7TPH6}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:Q7TPH6}. Note=Localizes to axon
CC shafts and associates with microtubule cytoskeleton.
CC {ECO:0000250|UniProtKB:Q7TPH6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Variant 2 {ECO:0000303|PubMed:20143133};
CC IsoId=F1RD40-1; Sequence=Displayed;
CC Name=2; Synonyms=Variant 3 {ECO:0000303|PubMed:20143133};
CC IsoId=F1RD40-2; Sequence=VSP_059624;
CC -!- TISSUE SPECIFICITY: Widely expressed when the visual system begins
CC developing. In the eye, expressed in all cells, including retinal
CC ganglion cells, with no obvious gradient.
CC {ECO:0000269|PubMed:15590740}.
CC -!- DOMAIN: The PHR domains are compact beta-sandwich folds composed of 11
CC antiparallel strands and decorated with conserved apical loops. They
CC are likely to play a structural role and mediate interactions with
CC substrates or partners. {ECO:0000250|UniProtKB:Q7TPH6}.
CC -!- DOMAIN: The tandem cysteine domain region confers threonine specificity
CC and contains the two essential catalytic cysteine residues that relay
CC ubiquitin. It binds four zinc ions in a C5HC7HC2 configuration.
CC {ECO:0000250|UniProtKB:O75592}.
CC -!- DISRUPTION PHENOTYPE: Fishes display defects in the projection of
CC retinal axons as well as reduced yellow pigmentation (PubMed:15590740,
CC PubMed:15617681). Mutants show failure of anterior axons to map to the
CC posterior tectum: in wild types, retinal axons from the anterior eye
CC remain unbranched and are fasciculated until reaching the posterior
CC tectum, while in mutants, anterior axons branch in the anterior tectum
CC (PubMed:15590740). The posterior tectum is very sparsely innervated
CC (PubMed:15590740). Defects are also detectable in the dorsoventral axis
CC (PubMed:15590740). Reduced yellow pigmentation is caused by a
CC deficiency of sepiapterin, a yellow pteridine (PubMed:15617681).
CC {ECO:0000269|PubMed:15590740, ECO:0000269|PubMed:15617681}.
CC -!- SIMILARITY: Belongs to the RING-Cys relay (RCR) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD58756.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAD61237.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY818192; AAW31810.1; -; mRNA.
DR EMBL; AL731656; CAD61237.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AL731859; CAD58756.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL840634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX510646; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR628366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU138551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GU299766; ADB77874.1; -; mRNA.
DR EMBL; GU299767; ADB77875.1; -; mRNA.
DR RefSeq; NP_001012247.2; NM_001012247.2. [F1RD40-1]
DR SMR; F1RD40; -.
DR STRING; 7955.ENSDARP00000111741; -.
DR Ensembl; ENSDART00000039157; ENSDARP00000028785; ENSDARG00000001220. [F1RD40-1]
DR GeneID; 368439; -.
DR KEGG; dre:368439; -.
DR CTD; 23077; -.
DR ZFIN; ZDB-GENE-030616-132; mycbp2.
DR eggNOG; KOG1428; Eukaryota.
DR GeneTree; ENSGT00940000155756; -.
DR HOGENOM; CLU_000063_0_0_1; -.
DR OMA; NKLCILD; -.
DR OrthoDB; 215263at2759; -.
DR TreeFam; TF313151; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:F1RD40; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 9.
DR Bgee; ENSDARG00000001220; Expressed in retina and 20 other tissues.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:ZFIN.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:ZFIN.
DR GO; GO:0016198; P:axon choice point recognition; IMP:ZFIN.
DR GO; GO:0048677; P:axon extension involved in regeneration; IMP:ZFIN.
DR GO; GO:0007411; P:axon guidance; IMP:ZFIN.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; ISS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0048066; P:developmental pigmentation; IMP:ZFIN.
DR GO; GO:0021986; P:habenula development; IMP:ZFIN.
DR GO; GO:0050905; P:neuromuscular process; ISS:UniProtKB.
DR GO; GO:1902667; P:regulation of axon guidance; ISS:UniProtKB.
DR GO; GO:0042068; P:regulation of pteridine metabolic process; IMP:ZFIN.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IBA:GO_Central.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:ZFIN.
DR Gene3D; 2.130.10.30; -; 2.
DR Gene3D; 2.60.120.820; -; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR012983; PHR.
DR InterPro; IPR038648; PHR_sf.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR003646; SH3-like_bac-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF08005; PHR; 2.
DR Pfam; PF00415; RCC1; 1.
DR Pfam; PF08239; SH3_3; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM01337; APC10; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF50985; SSF50985; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS00626; RCC1_2; 2.
DR PROSITE; PS50012; RCC1_3; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Biological rhythms; Cell projection; Cytoplasm;
KW Cytoskeleton; Disulfide bond; Guanine-nucleotide releasing factor;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..4574
FT /note="E3 ubiquitin-protein ligase MYCBP2"
FT /id="PRO_0000444610"
FT REPEAT 591..646
FT /note="RCC1 1"
FT /evidence="ECO:0000255"
FT REPEAT 690..746
FT /note="RCC1 2"
FT /evidence="ECO:0000255"
FT REPEAT 943..993
FT /note="RCC1 3"
FT /evidence="ECO:0000255"
FT REPEAT 995..1051
FT /note="RCC1 4"
FT /evidence="ECO:0000255"
FT REPEAT 2336..2417
FT /note="Filamin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00087"
FT DOMAIN 3617..3795
FT /note="DOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00614"
FT ZN_FING 4324..4375
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 92..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1976..1998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2313..2332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2613..2825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2845..2922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3085..3116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3345..3365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3505..3526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3815..3841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4435..4572
FT /note="Tandem cysteine domain"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT COMPBIAS 94..112
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2313..2329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2623..2639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2640..2658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2659..2673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2712..2752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2761..2791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2871..2887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3092..3116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3351..3365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3818..3841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4454
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT ACT_SITE 4506
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4471
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4474
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4483
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4486
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4495
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4498
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4499
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4513
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4516
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4534
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4548
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT BINDING 4568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT SITE 4507
FT /note="Important for catalysis"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT SITE 4512
FT /note="Important for catalysis"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT SITE 4520
FT /note="Important for catalysis"
FT /evidence="ECO:0000250|UniProtKB:O75592"
FT DISULFID 1733..1850
FT /evidence="ECO:0000250|UniProtKB:Q7TPH6"
FT VAR_SEQ 863..897
FT /note="Missing (in isoform 2)"
FT /id="VSP_059624"
FT CONFLICT 1834
FT /note="I -> M (in Ref. 1; AAW31810)"
FT /evidence="ECO:0000305"
FT CONFLICT 2427
FT /note="D -> A (in Ref. 1; AAW31810)"
FT /evidence="ECO:0000305"
FT CONFLICT 3515
FT /note="N -> T (in Ref. 1; AAW31810)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4574 AA; 501847 MW; 17005A5FCAD05F74 CRC64;
MMCAAAAAGA GGSGILSSSS HSMGLGVRVI PGAGNDFAPI GSGMGSCPVV GARSDCRSRY
QLLLSGRALA ERYRRIYTTA INDKEQGLNL GRGKKALSKK KLKRRQKVKS KVKTRTKTDT
LDGAFPVPDI KLHSNPSAFN VYCNVRHCVL DWQQKEAALA LASRNSVQSG DSDSEEEEEY
REPFVKLPKI IGIGLCGVFE LIKETRFSHP SLCLRSLQAL LDMLQGQQPE SFQTEPPDVL
ESLFHLLLET TVRSTGMNDP TGQTLTALSC ACLFSLVVAW GDTGKTLQAV SAILTNNGSH
ACQTIQVPTI LNALQRSVQA VLVGKIQIQE WFGNGIKRAA LMNKWVLKEV NIDDDEHCLL
QTDGSFLYLL CKDGLYKVGS GYSGTVRGHV YNSTSRIRNR KEKRSWLGFA QGCLLYRDMN
SHNMAAIKIN PETLEQEGTI TVPGLQADGQ NIIFTDGEYI NQIAACKDDG FVVRIYATSS
DPALQQELQL KLARKCLHAC GISLFDLEKD LHIISTGFDE EAALIGAGRE FALMKTASGK
IYYTGKYQSL GIKQGGPSSG KWVELPVTKS PKIVQFSVGH DGSHALLVAE DGSVFFTGSA
SKGEDGESTK SRRQPKPYKP KKMIKLETKM AVYTACNNGS SSIVTKDGEL YMFGKDAIYS
DSTCQVSDLK GHFVTQVAMG KAHTCVLTKS GEVWTFGVNN KGQCGRDTGA MSQAGKAFGV
ENMATAMDED LEDELDEKEE KSMMCQPGMH KWKLDQCMVC TVCGDCTGYG ASCVSSGRPD
RVPGGICGCG SGESGCSSCG CCKACARELD GQEARQRGIF DAVKEMIPLD LLLGVNIEEH
IQIRQEEKRQ RINRRHRLEE GRGPLVFPGP LFMNQREQVL ARLRPLQAVK LMREKLKDGS
SERGDKDASK ITTYPPGAVR FDCELRAVQV SCGFHHSVVL MENGDVYTFG YGQHGQLGHG
DVNSRGSPTL VQALPGPSTQ VTAGSNHTAV LLMDGQVFTF GSFSKGQLGR PILDMPYWNA
KPSPMPNIGA KYGRKATWIG ASGDQTFLRI DEALINSHVL ATSEIFANKH IIGLVPTSIS
EPPPFKCLLI NKLDGSCRTF NDSEQEDLQG FGLCLDPVYD VIWRFLPVTR EMCCYNAVIA
DARVPTASDI QALCSILSPE LALPSGSHAS TTRSHGALHI LGCLDTLAAM QELKMGVASA
EEETQAVMKV YSKEDYSVVN RFESHGGGWG YSAHSVEAIR FCADADILLG GLGLFGGRGE
YTAKIKLFEL GPDGGDHETD GDLLAETDVL AYDCAAREKY AMMFDEPVLL QLGWWYVAWA
RVSGPSSDCG SHGQATITTD DGVVFQFKSS KKSNNGTDVN AGQIPQLLYR LPSNDGNASK
GKQQTSEPVH ILKRTFARTV SVDCFESLLS ILHWSWTTLV LGVEELRGLK GFQFTATLLD
LERLRFVGTC CLRLLRVYIC DIFPISASTK AIVEESSKLA ECVGKTRSLL KKILSEGMDN
CLTKLDNDPQ GYLSQPLTLL EAVLQECHNT FTACFHSFYP TPALQWACLC DLLNCLDQDI
QEANFRTSSS RLLAAVMSAL CNTSVKLTSI LPIAYDGEVL LRSLVKQVST ENDSALAHRF
PLLVAHMEKL SHTEENLMGM TTFREVLEKM LVIVVLPVRK SLRKEVELFS PHLVSNTCGL
LASIVSELTA SALGSEVDGL NSLHSVKATP NRFTKTSQGR SWNTGNGSPD AICFTVDKPG
VVLVGFCVYG GGGIHEYELE VLADDAQTEH PGDSAHSHRW TSLELVKGTY CTDDSPSDIA
EIRLDKAVPL KENVKYAVRL RNYGSRTANG DGGITTVQCS DGVAFTFSTC SLSSNGTNQT
RGQIPQILYY RSEYDGDLQS QLLSKANEED KNCSRALSVV SVVVRAAKDL LHRAFAVDVE
DIPELLSSSS LFSMLLPLIL AYIGPVAASV PKAAVEVFGL VQELLPAVSA LNQKYAPPTF
NPNQSTDSTT GNQPEQGLSA CTTSNHYAVL ESDHPYKQAG VTQYKVSFPD CVRWMTVEFD
PQCGTAQPED VLRLLIPSRS LHFSGLSSKA LAHETINSWT ELKKFSGSSG WPTAVLVLPG
NEALFSLETA SDYVKDEKAS FYGFKCVAVG YEFNPGLDEG IIQLEKELAY LGSVCAAALM
KKDLALPIGN ELEEDLEILE EASLQVCKSH SGLLGKGLAL SHSPTILEAL EGNLPLHLQT
NEHSFLEDFI TCVQSSSGGR LARWLQPDSY ADPQKTSLIL NKDDIRCGWP TTVVVQTKDQ
YGDVVHVPNM KVEVKAVPVS QKKSIQQENM KKLQRLPGTS SNSATGTDLT FGGHPAPKLE
ATYEPMIIKE ARYIAITMMK AYENYSFEEL RFASPTPKRP SENMLIRANT DGTYSANWTP
GAVGLYTIHV TIDGIEIDAG LEVEVKDPPK GMIPPGTQMV KPKAEPQPSK VRKFVAKDSA
GLRVRSHPSL QSEQIGIVQV NGTITFIDEI HNDDGVWLRL NDETVKKYVP NMNGYTEAWC
LSFNQHLGRS LLVPVDVINS EGTWVQLDKN SVVEFCESDE GEAWSLARDR GGNQYLRHVE
EQAVLEHGAQ TPPPSPFSVQ AFNRGMASSG AQGFDYGISN NKGDRDNMAS WSVSPGSKHR
QESRSSKTDS HSNRSVDQVK SKNNESLSAS EALILKSDTG KLRSDSHSRS HSPNHNTLQA
LKADGRTSGL RAESPNPGSR SSSPKQKTFT SGRSSPSSTS SPRSSSPHDK NLPAKVSPSK
VHLDPPRERS KSDSYTLDPD TLRKKKVPLM EPLRGRSTSP KPKLPPKESK GGSSNAENRA
PSPHVVQENL HSEVVEVCRS SALLSNDEGN DENSELHNAE EGSSKVHFSI GKAPVKEELE
SRSSPKVSRK TSSRHVRPKK DKSGPLFKGE NVRPTEPAKQ AMSPSVAECA RAVFAAFLWH
EGIVHDAMAC SSFLKFNPEL TKEHAPIRNS LSCQQGFDEK ESKLKNRHSL EISSALNMFN
ISPHGPDISK MGSINKNKVL SMLKEPPLPE KCEDGKESVS YEMTSHSSMR SKSILPLTLQ
HLVAFWEDIS MATIKAATQN MIFPSPGSSA ILKKKENEKD SKKTKKEKKK KEKAEVRPRG
NLFGEMAQLA MGGPEKDTIC ELCGESHPYP VTYHMRQAHP GCGRYAGGQG YNSIGHFCGG
WAGNCGDGGI GGSTWYLVCD RCREKYLREK QTAAREKVKQ SRKKPLQVKT PRALPTMEAH
QVIRANALFL LSLSSAAEPS LLCHHPPKPF HSHLPSLKEG VSEELPNKMG CLYLQTLARQ
HTENFGVYQD DNLFQDEMRY LRSTSVPAPY ISVTPDACPN VFEEPGSNMK SMPPSLETSP
ITDSDTAKRT VFQRSYSVVA SEYDKQHSAS PARVKAVPRR RVHSGDAEVG SSLLRHPSPE
LSRLISAHGS LSKGERNFQW PVLAFVIQHH DLEGLEVAMK HALRKSACRV FAMEAFNWLL
CNVTQTTSLH DILWHFVASL TPSPFETEEE EDEENKGNKE NLEQEKDLGV CEHPLSDIII
AGEAAHPLPH TFHCLLQTIS DLMMSLPSGS SLQQMALRCW SLKFKQSDHQ FLHQSNVFHH
INNILSKSDD GDSEESFNIS VQSGYEAISQ ELCVVTCLKD LTSVVDIKTS SRPAMIGSLT
DGSTETFWES GDEDKNKTKS ITISCVKGIN ASYVSVHVDN SRDIGNKVTS MIFLCGKAVE
DLCRIKQIDL DSRHMGWVTS ELPGGDHHVI KIELKGPENT LRVRQVKVLG WKEGESIKIA
GQISASVAQQ KNCEAETLRV FRLITSQVFG KLICGDAEPT PEQEEKNLLS SPEGEDKAPS
DADLKEHMVG IIFSRSKLTN LQKQVCAHIV QAIRMEATRV REEWEHAISS KENANSQPSD
DDASSDAYCF ELLSMVLALS GSNVGRQYLA QQLTLLQDLF SLLHTASPRV QRQVTSLLRR
VLPEVTPMRL ASVIGVKALP PADISDIIHS TEKGDWTKLG ILDMFLGCIA KALTVQLKAK
GTTIVGTAGM AAGKGVTTVT LPMIFNSSYI RRGESHWWMK GSTPPQIAEI IIKLVKDMAA
GHLSDAWSRV TKNAIAETII ALTKMEEEHR SPVRCIATTR LWLALASLCV LDQDHVDRLS
SGRWMGKDGQ QKQMPMCDNH DDGETAAIIL CNACGNLCTD CDRFLHLHRR TRTHQRQVFK
EEEEAIKVDL HEGCGRTKLF WLMALADSKT MKAMVEFREH TGKPASSSSD ACRFCGTRHG
TELSAVGSVC SDQDCQEYAK LACSKTHPCG HPCGGVKNED LCLPCLHGCD KTATCLKQDA
DDMCMICFTE ALSAAPAIQL DCSHVFHLQC TRRVLENRWL GPRITFGFMS CPICKNKINH
LVLKDLLDPI KELYEDVRRK ALMRLEYEGL HKSEAITMSG ARFFNNPAGF AMNRYAYYVC
FKCKKAYFGG EARCDAEAGQ GDDYDPRELI CGACSDVSRA QMCSKHGTDF LEYKCRYCCS
VAVFFCFGTT HFCNACHDDF QRMTSVPKEE LPHCPAGPKG KQLEGSECPL HVVHPPTGEE
FALGCGVCRN AHTF
