UHRF2_MOUSE
ID UHRF2_MOUSE Reviewed; 803 AA.
AC Q7TMI3; Q8BG56; Q8BJP6; Q8BY30; Q8K1I5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=E3 ubiquitin-protein ligase UHRF2;
DE EC=2.3.2.27;
DE AltName: Full=NIRF;
DE AltName: Full=Np95-like ring finger protein;
DE AltName: Full=Nuclear protein 97;
DE AltName: Full=Nuclear zinc finger protein Np97;
DE AltName: Full=RING-type E3 ubiquitin transferase UHRF2;
DE AltName: Full=Ubiquitin-like PHD and RING finger domain-containing protein 2;
DE AltName: Full=Ubiquitin-like-containing PHD and RING finger domains protein 2;
GN Name=Uhrf2; Synonyms=Nirf;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Leukemic T-cell;
RA Davenport J.W., Fernandes E.R., Neale G.A.M., Goorha R.M.;
RT "LMO2-induced T cell leukemias overexpress a novel gene, Uhr1, containing
RT RING and PHD zinc fingers and an ubiquitin-like domain.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RA Mori T., Li Y., Kochi H.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-195.
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, Spinal ganglion, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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 [6]
RP FUNCTION, DNA-BINDING, INTERACTION WITH H3, SUBCELLULAR LOCATION,
RP INDUCTION, AND MUTAGENESIS OF TYR-214 AND TYR-217.
RX PubMed=21598301; DOI=10.1002/jcb.23185;
RA Pichler G., Wolf P., Schmidt C.S., Meilinger D., Schneider K., Frauer C.,
RA Fellinger K., Rottach A., Leonhardt H.;
RT "Cooperative DNA and histone binding by Uhrf2 links the two major
RT repressive epigenetic pathways.";
RL J. Cell. Biochem. 112:2585-2593(2011).
RN [7]
RP FUNCTION, AND HYDROXYMETHYLCYTOSINE-BINDING.
RX PubMed=23434322; DOI=10.1016/j.cell.2013.02.004;
RA Spruijt C.G., Gnerlich F., Smits A.H., Pfaffeneder T., Jansen P.W.,
RA Bauer C., Munzel M., Wagner M., Muller M., Khan F., Eberl H.C.,
RA Mensinga A., Brinkman A.B., Lephikov K., Muller U., Walter J., Boelens R.,
RA van Ingen H., Leonhardt H., Carell T., Vermeulen M.;
RT "Dynamic readers for 5-(hydroxy)methylcytosine and its oxidized
RT derivatives.";
RL Cell 152:1146-1159(2013).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28402695; DOI=10.1080/15592294.2017.1314423;
RA Liu Y., Zhang B., Meng X., Korn M.J., Parent J.M., Lu L.Y., Yu X.;
RT "UHRF2 regulates local 5-methylcytosine and suppresses spontaneous
RT seizures.";
RL Epigenetics 12:551-560(2017).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=28115522; DOI=10.1074/jbc.m116.754580;
RA Chen R., Zhang Q., Duan X., York P., Chen G.D., Yin P., Zhu H., Xu M.,
RA Chen P., Wu Q., Li D., Samarut J., Xu G., Zhang P., Cao X., Li J., Wong J.;
RT "The 5-Hydroxymethylcytosine (5hmC) Reader UHRF2 Is Required for Normal
RT Levels of 5hmC in Mouse Adult Brain and Spatial Learning and Memory.";
RL J. Biol. Chem. 292:4533-4543(2017).
CC -!- FUNCTION: E3 ubiquitin ligase that plays important roles in DNA
CC methylation, histone modifications, cell cycle and DNA repair. Acts as
CC a specific reader for 5-hydroxymethylcytosine (5hmC) and thereby
CC recruits various substrates to these sites to ubiquitinate them
CC (PubMed:23434322, PubMed:28402695). This activity also allows the
CC maintenance of 5mC levels at specific genomic loci and regulates
CC neuron-related gene expression (PubMed:28115522). Participates in cell
CC cycle regulation by ubiquitinating cyclins CCND1 and CCNE1 and thus
CC inducing G1 arrest. Ubiquitinates also PCNP leading to its degradation
CC by the proteasome. Plays an active role in DNA damage repair by
CC ubiquitinating p21/CDKN1A leading to its proteosomal degradation.
CC Promotes also DNA repair by acting as an interstrand cross-links (ICLs)
CC sensor. Mechanistically, cooperates with UHRF1 to ensure recruitment of
CC FANCD2 to ICLs, leading to FANCD2 monoubiquitination and subsequent
CC activation. Contributes to UV-induced DNA damage response by physically
CC interacting with ATR in response to irradiation, thereby promoting ATR
CC activation (By similarity). {ECO:0000250|UniProtKB:Q96PU4,
CC ECO:0000269|PubMed:23434322, ECO:0000269|PubMed:28115522,
CC ECO:0000269|PubMed:28402695}.
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;
CC -!- ACTIVITY REGULATION: E3 ligase activity is robustly activated by 5-
CC hydroxy-methylcytosine. {ECO:0000250|UniProtKB:Q96PU4}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Binds methylated CpG containing
CC oligonucleotides. Interacts with H3; the interaction has a preference
CC for the 'Lys-9' trimethylated form of H3 (H3K9me3) (By similarity).
CC Interacts with PCNP. Interacts with HDAC1. Interacts directly with
CC CCNE1; the interaction ubiquitinates CCNE1 and appears independent of
CC CCNE1 phosphorylation. Interacts with CCND1; the interaction
CC ubiquitinates CCND1 and appears independent of CCND1 phosphorylation.
CC Interacts with p53/TP53 and RB1. Interacts with UBE2I. Interacts with
CC ZNF618. Interacts with UHRF1. Interacts with FANCD2. Interacts with
CC ATR. Interacts with PCNA (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q96PU4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358,
CC ECO:0000269|PubMed:21598301}. Chromosome
CC {ECO:0000250|UniProtKB:Q96PU4}. Note=Enriched at genomic loci that are
CC enriched for 5-hydroxy-methylcytosine (5hmC).
CC {ECO:0000250|UniProtKB:Q96PU4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7TMI3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TMI3-2; Sequence=VSP_013877, VSP_013878;
CC Name=3;
CC IsoId=Q7TMI3-3; Sequence=VSP_013876;
CC -!- TISSUE SPECIFICITY: Mostly detected in several tissues, including the
CC thymus, spleen, lung, adrenal gland, and ovary. In addition, found in
CC several tissues in the brain (cerebellum, hippocampus, and cerebral
CC cortex). {ECO:0000269|PubMed:28115522}.
CC -!- INDUCTION: Up-regulated during cell differentiation.
CC {ECO:0000269|PubMed:21598301}.
CC -!- PTM: May be autoubiquitinated; which may lead to proteasomal
CC degradation. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation may be mediated by CDK2 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Autosumoylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Deletion mice are viable, fertile, and grossly
CC normal (PubMed:28402695, PubMed:28115522). However, adult mice develop
CC frequent spontaneous seizures and display abnormal electrical
CC activities in brain (PubMed:28402695). In addition, they display
CC reduced 5-hydroxymethylcytosine (5hmC) in genomic DNA in the brain
CC together with impaired spatial memory acquisition and retention
CC (PubMed:28115522). {ECO:0000269|PubMed:28115522,
CC ECO:0000269|PubMed:28402695}.
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DR EMBL; AB116653; BAC81739.1; -; mRNA.
DR EMBL; AF274047; AAM33798.1; -; mRNA.
DR EMBL; AK031036; BAC27224.1; -; mRNA.
DR EMBL; AK041564; BAC30987.1; -; mRNA.
DR EMBL; AK042321; BAC31223.1; -; mRNA.
DR EMBL; AK051743; BAC34750.1; -; mRNA.
DR EMBL; AK080925; BAC38081.1; -; mRNA.
DR EMBL; BC060241; AAH60241.1; -; mRNA.
DR CCDS; CCDS37955.1; -. [Q7TMI3-1]
DR RefSeq; NP_659122.2; NM_144873.2. [Q7TMI3-1]
DR AlphaFoldDB; Q7TMI3; -.
DR BMRB; Q7TMI3; -.
DR SMR; Q7TMI3; -.
DR STRING; 10090.ENSMUSP00000025739; -.
DR iPTMnet; Q7TMI3; -.
DR PhosphoSitePlus; Q7TMI3; -.
DR EPD; Q7TMI3; -.
DR MaxQB; Q7TMI3; -.
DR PaxDb; Q7TMI3; -.
DR PeptideAtlas; Q7TMI3; -.
DR PRIDE; Q7TMI3; -.
DR ProteomicsDB; 298475; -. [Q7TMI3-1]
DR ProteomicsDB; 298476; -. [Q7TMI3-2]
DR ProteomicsDB; 298477; -. [Q7TMI3-3]
DR Antibodypedia; 9697; 310 antibodies from 30 providers.
DR DNASU; 109113; -.
DR Ensembl; ENSMUST00000025739; ENSMUSP00000025739; ENSMUSG00000024817. [Q7TMI3-1]
DR GeneID; 109113; -.
DR KEGG; mmu:109113; -.
DR UCSC; uc008hef.1; mouse. [Q7TMI3-3]
DR UCSC; uc008heh.1; mouse. [Q7TMI3-2]
DR UCSC; uc008hei.1; mouse. [Q7TMI3-1]
DR CTD; 115426; -.
DR MGI; MGI:1923718; Uhrf2.
DR VEuPathDB; HostDB:ENSMUSG00000024817; -.
DR eggNOG; ENOG502QRDQ; Eukaryota.
DR GeneTree; ENSGT00390000008296; -.
DR HOGENOM; CLU_022357_0_0_1; -.
DR InParanoid; Q7TMI3; -.
DR OMA; CHMCSCH; -.
DR OrthoDB; 705927at2759; -.
DR PhylomeDB; Q7TMI3; -.
DR TreeFam; TF106434; -.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 109113; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Uhrf2; mouse.
DR PRO; PR:Q7TMI3; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q7TMI3; protein.
DR Bgee; ENSMUSG00000024817; Expressed in superior cervical ganglion and 244 other tissues.
DR Genevisible; Q7TMI3; MM.
DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005721; C:pericentric heterochromatin; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0019789; F:SUMO transferase activity; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:HGNC-UCL.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; ISS:HGNC-UCL.
DR GO; GO:0010216; P:maintenance of DNA methylation; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:HGNC-UCL.
DR GO; GO:0016567; P:protein ubiquitination; ISS:HGNC-UCL.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR Gene3D; 2.30.280.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036987; SRA-YDG_sf.
DR InterPro; IPR003105; SRA_YDG.
DR InterPro; IPR021991; TTD_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR045134; UHRF1/2-like.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14140; PTHR14140; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF02182; SAD_SRA; 1.
DR Pfam; PF12148; TTD; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SMART; SM00466; SRA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS51015; YDG; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Chromosome; Disulfide bond; DNA-binding;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..803
FT /note="E3 ubiquitin-protein ligase UHRF2"
FT /id="PRO_0000056148"
FT DOMAIN 1..78
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 449..613
FT /note="YDG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00358"
FT ZN_FING 340..396
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 734..773
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 79..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..312
FT /note="Required for interaction with histone H3"
FT REGION 154..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..289
FT /note="Interaction with PCNP"
FT /evidence="ECO:0000250"
FT REGION 415..645
FT /note="Methyl-CpG binding and interaction with HDAC1"
FT /evidence="ECO:0000250"
FT REGION 643..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT DISULFID 705
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VAR_SEQ 217..803
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013876"
FT VAR_SEQ 501..516
FT /note="DRGDEFTYTGSGGKNL -> VSNDVTLFFRTNLDHF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013877"
FT VAR_SEQ 517..803
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013878"
FT MUTAGEN 214
FT /note="Y->A: Abolishes in vitro binding to H3K9me3.
FT Prevents enrichment at pericentric heterochromatin."
FT /evidence="ECO:0000269|PubMed:21598301"
FT MUTAGEN 217
FT /note="Y->A: Abolishes in vitro binding to 'Lys-10'
FT methylated H3, H3K9me3. Prevents enrichment at pericentric
FT heterochromatin."
FT /evidence="ECO:0000269|PubMed:21598301"
FT CONFLICT 274
FT /note="T -> S (in Ref. 1; AAM33798)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="T -> S (in Ref. 1; AAM33798)"
FT /evidence="ECO:0000305"
FT CONFLICT 793
FT /note="D -> E (in Ref. 1; AAM33798)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 803 AA; 90106 MW; D799B0205E0E036E CRC64;
MWIQVRTIDG SQTRTIEDVS RKATIEELRE RVWALFDVRP ECQRLFYRGK QLENGYTLFD
YDVGLNDIIQ LLVRPDSSLP STSKQNDAQV KPSSHNPPKV KKTARGGSSS QPSTSARTCL
IDPGFGLYKV NELVDARDVG LGAWFEAHIH SVTRASDGHS RGKTPLKNGS SYKRTNGNVN
HNSKENTNKL DNVPSTSNSD SVAADEDVIY HIEYDEYPES GILEMNVKDL RPRARTILKW
NELNVGDVVM VNYNVENPGK RGFWYDAEIT TLKTISRTKK EVRVKVFLGG SEGTLNDCRV
MSVDEIFKIE KPGAHPISFA DGKFLRKNDP ECDLCGGDPD KTCHMCSCHK CGEKRDPNMQ
LLCDECNMAY HIYCLSPPLD KVPEEEYWYC PSCKTDSSEV VKAGERLKLS KKKAKMPSAS
TESRRDWGRG MACVGRTKEC TIVPSNHYGP IPGIPVGSTW RFRVQVSEAG VHRPHVGGIH
GRSNDGAYSL VLAGGFEDEV DRGDEFTYTG SGGKNLAGNK RIGAPSADQT LTNMNRALAL
NCDAPLDDKI GAESRNWRAG KPVRVIRSFK GRKISKYAPE EGNRYDGIYK VVKYWPEISS
SHGFLVWRYL LRRDDVEPAP WTSEGIERSR RLCLRLQYPA GYPSEKEGKK TKGQSKKQGS
EATKRPASDD ECPGDSKVLK ASDSTDAVEA FQLTPQQQRL IREDCQNQKL WDEVLASLVE
GPNFLKKLEQ SFMCVCCQEL VYQPVTTECF HNVCKDCLQR SFKAQVFSCP ACRHDLGQNY
VMVLNETLQT LLDLFFPGYS KGR
