TOPRS_MOUSE
ID TOPRS_MOUSE Reviewed; 1033 AA.
AC Q80Z37; Q3U5B5; Q3UPZ1; Q3USN3; Q3UZ55; Q8BXP2; Q8CFF5; Q8CGC8; Q920L3;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=E3 ubiquitin-protein ligase Topors;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase Topors {ECO:0000305};
DE AltName: Full=SUMO1-protein E3 ligase Topors;
DE AltName: Full=Topoisomerase I-binding RING finger protein;
DE AltName: Full=Topoisomerase I-binding arginine/serine-rich protein;
DE AltName: Full=Tumor suppressor p53-binding protein 3;
DE Short=p53-binding protein 3;
DE Short=p53BP3;
GN Name=Topors;
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], FUNCTION, INTERACTION WITH PARK7 AND TP53, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J;
RX PubMed=15703819;
RA Shinbo Y., Taira T., Niki T., Iguchi-Ariga S.M.M., Ariga H.;
RT "DJ-1 restores p53 transcription activity inhibited by Topors/p53BP3.";
RL Int. J. Oncol. 26:641-648(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TP53, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX PubMed=15735665; DOI=10.1038/sj.onc.1208554;
RA Lin L., Ozaki T., Takada Y., Kageyama H., Nakamura Y., Hata A., Zhang J.H.,
RA Simonds W.F., Nakagawara A., Koseki H.;
RT "Topors, a p53 and topoisomerase I-binding RING finger protein, is a
RT coactivator of p53 in growth suppression induced by DNA damage.";
RL Oncogene 24:3385-3396(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland, and Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-824.
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Lung, Retina, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-861; SER-863;
RP SER-909; SER-911; SER-999; SER-1016 AND SER-1025, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Spleen, and 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).
CC -!- FUNCTION: Functions as an E3 ubiquitin-protein ligase and as a E3
CC SUMO1-protein ligase. Probable tumor suppressor involved in cell
CC growth, cell proliferation and apoptosis that regulates p53/TP53
CC stability through ubiquitin-dependent degradation. May regulate
CC chromatin modification through sumoylation of several chromatin
CC modification-associated proteins. May be involved in DNA-damage-induced
CC cell death through IKBKE sumoylation. {ECO:0000269|PubMed:15703819,
CC ECO:0000269|PubMed:15735665}.
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 -!- SUBUNIT: Interacts with TOP1. Interacts with the SUMO1 conjugating
CC enzyme UBE2I. Interacts with SUMO1. Interacts with NKX3-1;
CC polyubiquitinates NKX3-1 and induces its proteasomal degradation.
CC Interacts with SIN3A; sumoylates SIN3A. Interacts with IKBKE; induced
CC by DNA damage (By similarity). Interacts with p53/TP53. Interacts with
CC PARK7/DJ-1. {ECO:0000250|UniProtKB:Q9NS56, ECO:0000269|PubMed:15703819,
CC ECO:0000269|PubMed:15735665}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15703819,
CC ECO:0000269|PubMed:15735665}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:Q9NS56}. Note=Localizes to discrete nuclear foci
CC which partly overlap with PML nuclear bodies. Targeted to PML nuclear
CC bodies upon DNA damage. {ECO:0000250|UniProtKB:Q9NS56}.
CC -!- INDUCTION: By genotoxic agents such as cisplatin and camptothecin.
CC {ECO:0000269|PubMed:15735665}.
CC -!- PTM: Phosphorylation at Ser-99 regulates the E3 ubiquitin-protein
CC ligase activity but not the SUMO1-protein ligase activity.
CC Phosphorylation at Ser-718 increases the E3 ubiquitin-protein ligase
CC activity versus the E3 SUMO1-protein ligase activity resulting in
CC increased p53/TP53 ubiquitination and degradation.
CC {ECO:0000250|UniProtKB:Q9NS56}.
CC -!- PTM: Sumoylated. {ECO:0000250|UniProtKB:Q9NS56}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37141.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB072395; BAB69457.1; -; mRNA.
DR EMBL; AB104865; BAC65157.1; -; mRNA.
DR EMBL; BC037141; AAH37141.1; ALT_SEQ; mRNA.
DR EMBL; BC040797; AAH40797.1; -; mRNA.
DR EMBL; AK044564; BAC31981.2; -; mRNA.
DR EMBL; AK134075; BAE22003.1; -; mRNA.
DR EMBL; AK140250; BAE24298.1; -; mRNA.
DR EMBL; AK143025; BAE25253.1; -; mRNA.
DR EMBL; AK153743; BAE32164.1; -; mRNA.
DR CCDS; CCDS38710.1; -.
DR RefSeq; NP_598858.2; NM_134097.3.
DR AlphaFoldDB; Q80Z37; -.
DR SMR; Q80Z37; -.
DR BioGRID; 222976; 8.
DR IntAct; Q80Z37; 1.
DR MINT; Q80Z37; -.
DR STRING; 10090.ENSMUSP00000046843; -.
DR iPTMnet; Q80Z37; -.
DR PhosphoSitePlus; Q80Z37; -.
DR EPD; Q80Z37; -.
DR jPOST; Q80Z37; -.
DR MaxQB; Q80Z37; -.
DR PaxDb; Q80Z37; -.
DR PeptideAtlas; Q80Z37; -.
DR PRIDE; Q80Z37; -.
DR ProteomicsDB; 259290; -.
DR Antibodypedia; 25068; 216 antibodies from 25 providers.
DR DNASU; 106021; -.
DR Ensembl; ENSMUST00000042575; ENSMUSP00000046843; ENSMUSG00000036822.
DR GeneID; 106021; -.
DR KEGG; mmu:106021; -.
DR UCSC; uc008shi.1; mouse.
DR CTD; 10210; -.
DR MGI; MGI:2146189; Topors.
DR VEuPathDB; HostDB:ENSMUSG00000036822; -.
DR eggNOG; KOG4430; Eukaryota.
DR GeneTree; ENSGT00530000064170; -.
DR HOGENOM; CLU_012046_0_0_1; -.
DR InParanoid; Q80Z37; -.
DR OMA; ERHYYCY; -.
DR OrthoDB; 528095at2759; -.
DR PhylomeDB; Q80Z37; -.
DR TreeFam; TF339497; -.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4755510; SUMOylation of immune response proteins.
DR BioGRID-ORCS; 106021; 8 hits in 71 CRISPR screens.
DR ChiTaRS; Topors; mouse.
DR PRO; PR:Q80Z37; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q80Z37; protein.
DR Bgee; ENSMUSG00000036822; Expressed in primitive streak and 246 other tissues.
DR Genevisible; Q80Z37; MM.
DR GO; GO:0005814; C:centriole; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:BHF-UCL.
DR GO; GO:0000930; C:gamma-tubulin complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:BHF-UCL.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0003823; F:antigen binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0044547; F:DNA topoisomerase binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019789; F:SUMO transferase activity; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISS:UniProtKB.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:MGI.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:MGI.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW DNA damage; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..1033
FT /note="E3 ubiquitin-protein ligase Topors"
FT /id="PRO_0000232627"
FT ZN_FING 104..143
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..376
FT /note="Required for DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 414..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..654
FT /note="Interaction with SUMO1"
FT /evidence="ECO:0000250"
FT REGION 438..574
FT /note="Sumoylation and localization to discrete nuclear
FT foci"
FT /evidence="ECO:0000250"
FT REGION 457..879
FT /note="Interaction with TOP1"
FT /evidence="ECO:0000250"
FT REGION 457..731
FT /note="Interaction with p53/TP53"
FT /evidence="ECO:0000250"
FT REGION 496..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..914
FT /note="Interaction with UBE2I"
FT /evidence="ECO:0000250"
FT REGION 970..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..629
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..849
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..896
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS56"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS56"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS56"
FT MOD_RES 718
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q9NS56"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS56"
FT MOD_RES 861
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 909
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1016
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1025
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 74
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NS56"
FT CROSSLNK 77
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NS56"
FT CROSSLNK 84
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NS56"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NS56"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NS56"
FT CROSSLNK 251
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NS56"
FT CROSSLNK 561
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 701
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NS56"
FT CROSSLNK 818
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NS56"
FT CROSSLNK 834
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NS56"
FT CONFLICT 40
FT /note="S -> F (in Ref. 1; BAB69457)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="L -> P (in Ref. 3; AAH40797)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="S -> A (in Ref. 1; BAB69457)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="S -> A (in Ref. 3; AAH40797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1033 AA; 117082 MW; 3A99C00491D7EFD2 CRC64;
MGSQPPPPGS PLSREEGEAP PLVPAEEGRR RSRRVRLRGS CRHRPSLLSR RELASNGPAV
PATASSEIMA SAAKEFKMDN FSPKAGTSKL QQTVPADASP DSKCPICLDR FDNVSYLDRC
LHKFCFRCVQ EWSKNKAECP LCKQPFDSIF HSVRAEDDFK EYVLRPSYNG SFTNPEVRRF
RYRTTMTRER SASLYSPSST VSRRTTTPPD SGVLFEGLGI STRPRDVDIP QFMRQMALRG
PTTTDERSLR KIQEQDIINF RRTLYRAGVR VRSIEDGGRY RDISAEFFRR NPACLHRLVP
WLKRELTVLF GAHGSLVNIV QHIIMSNVTR YDLESQAFVS DLRPFLLNRT EHFIHEFISF
ARSPFNMAAF DQHANYDCPP SSEEGSRSDS SVITISPDEA ETQELDMNAS TVRQAPWDDE
TPGPSYSSSE QVHVGVSSLL NSSDSSDEEL VSGGTTSQIQ GVQTNDDVNN DSDSSSDNCV
IVGFVKPLAE RTPELVELSS DSEELGPYEK VETVKTQEQE QSYSSGDSDV SRASSPRSVL
GKDEQMSKSH CDSDTRISSK KEEKRSTSLP APRDSSSTRG DRVCSPYNHR HRKGGRSRSS
DSRSQSRSGH DPRNHRKHGK KRLRNKRSRS RESSSRPRAR KDKKRSRTRD SSWSRRSQTL
SLSSGSTSRS RSRSSDHGKR RSRSRNRDRY YLRNNYGSKY KWEYTYYSRN KDRDGYESSY
RRRTLSRAHY SRQSSSPEFR IQSFSERTNA RKKNHSERKY YYYERRRSRS VSSNRSRTTS
AGPDRVRNEK PGGKRKYKTR HLEGTSEEAQ PAREFTSKGK DSHYQKSKLD GSYKNESDSF
SDSRSSDRET KHKRRRRRTR SLSVEIVYEG KATDTSKHHK KKKKKHKKKH KKHHGDNTSR
SPVVITIDSD SDGESEVKAG IECSNGSLPQ PIQDGAFETK DVVTIEDELG VLDKDCDVTA
LADDLSTSQT VENCDSPAVP VEQTLDVREE STFASDLESQ SSNVSIQAEP SRPVPSPRTS
LSSVSPGRDC DVS
