DTL_MOUSE
ID DTL_MOUSE Reviewed; 729 AA.
AC Q3TLR7; Q3TTE9; Q6PAN1; Q80WY1; Q80WY2; Q8BW38; Q9CZ76;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Denticleless protein homolog;
DE AltName: Full=Lethal(2) denticleless protein homolog;
DE AltName: Full=Meth A retinoic acid-regulated nuclear matrix-associated protein;
DE Short=Meth A RAMP;
DE AltName: Full=Retinoic acid-regulated nuclear matrix-associated protein;
GN Name=Dtl; Synonyms=Cdt2, L2dtl, Ramp;
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] (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ;
RX PubMed=12707369; DOI=10.4049/jimmunol.170.9.4862;
RA Uenaka A., Hirano Y., Hata H., Win S., Aji T., Tanaka M., Ono T.,
RA Skipper J.C.A., Shimizu K., Nakayama E.;
RT "Cryptic CTL epitope on a murine sarcoma Meth A generated by exon extension
RT as a novel mechanism.";
RL J. Immunol. 170:4862-4868(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Mammary gland, Ovary, and Testis;
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 [3]
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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=17107960; DOI=10.1074/jbc.m606535200;
RA Liu C.L., Yu I.S., Pan H.W., Lin S.W., Hsu H.C.;
RT "L2dtl is essential for cell survival and nuclear division in early mouse
RT embryonic development.";
RL J. Biol. Chem. 282:1109-1118(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-515, 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-511; THR-515 AND THR-701, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3
CC ubiquitin-protein ligase complex required for cell cycle control, DNA
CC damage response and translesion DNA synthesis. The DCX(DTL) complex,
CC also named CRL4(CDT2) complex, mediates the polyubiquitination and
CC subsequent degradation of CDT1, CDKN1A/p21(CIP1), FBH1, KMT5A and SDE2.
CC CDT1 degradation in response to DNA damage is necessary to ensure
CC proper cell cycle regulation of DNA replication. CDKN1A/p21(CIP1)
CC degradation during S phase or following UV irradiation is essential to
CC control replication licensing. KMT5A degradation is also important for
CC a proper regulation of mechanisms such as TGF-beta signaling, cell
CC cycle progression, DNA repair and cell migration. Most substrates
CC require their interaction with PCNA for their polyubiquitination:
CC substrates interact with PCNA via their PIP-box, and those containing
CC the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading
CC to their degradation. In undamaged proliferating cells, the DCX(DTL)
CC complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby
CC being involved in PCNA-dependent translesion DNA synthesis. The DDB1-
CC CUL4A-DTL E3 ligase complex regulates the circadian clock function by
CC mediating the ubiquitination and degradation of CRY1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9NZJ0}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the DCX(DTL) E3 ubiquitin ligase complex (also
CC called CRL4(CDT2)), at least composed of CUL4 (CUL4A or CUL4B), DDB1,
CC DTL/CDT2 and RBX1 (By similarity). Interacts with CDKN1A and DDB1 (By
CC similarity). Interacts with FBXO11; SCF(FBXWO11) controls DTL stability
CC but DCX(DTL) does not control FBXO11 stability (By similarity).
CC Interacts with CRY1 (By similarity). {ECO:0000250|UniProtKB:Q9NZJ0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NZJ0}. Nucleus
CC membrane {ECO:0000250|UniProtKB:Q9NZJ0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9NZJ0}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:Q9NZJ0}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q9NZJ0}.
CC Chromosome {ECO:0000250|UniProtKB:Q9NZJ0}. Note=Nuclear matrix-
CC associated protein. Translocates from the interphase nucleus to the
CC metaphase cytoplasm during mitosis (By similarity).
CC {ECO:0000250|UniProtKB:Q9NZJ0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3TLR7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TLR7-2; Sequence=VSP_022886;
CC Name=3;
CC IsoId=Q3TLR7-4; Sequence=VSP_022884, VSP_022885;
CC -!- PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C).
CC Autoubiquitinated through 'Lys-48'-polyubiquitin chains in a PCNA-
CC independent reaction, allowing proteasomal turnover. Polyubiquitinated
CC by SCF(FBXO11) when not phosphorylated, leading to its degradation. A
CC tight regulation of the polyubiquitination by SCF(FBXO11) is involved
CC in the control of different processes such as TGF-beta signaling, cell
CC cycle progression and exit (By similarity).
CC {ECO:0000250|UniProtKB:Q9NZJ0}.
CC -!- PTM: Phosphorylated at Thr-463 by CDK1/Cyclin B and CDK2/Cycnlin A but
CC not by CDK2/Cyclin E, MAPK1 or PLK1. Phosphorylation at Thr-463
CC inhibits the interaction with FBXO11 and decreases upon cell cycle exit
CC induced by TGF-beta or serum starvation (By similarity).
CC {ECO:0000250|UniProtKB:Q9NZJ0}.
CC -!- DISRUPTION PHENOTYPE: Early embryonic lethality due to cell cycle
CC progression failure, termination of cell division, and, eventually,
CC embryonic death during the preimplantation stage.
CC {ECO:0000269|PubMed:17107960}.
CC -!- SIMILARITY: Belongs to the WD repeat cdt2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE36376.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BC060208; Type=Frameshift; 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; AB095735; BAC76404.1; -; mRNA.
DR EMBL; AB095736; BAC76405.1; -; mRNA.
DR EMBL; AK012919; BAB28549.1; -; mRNA.
DR EMBL; AK054412; BAC35769.1; -; mRNA.
DR EMBL; AK133177; BAE21543.1; -; mRNA.
DR EMBL; AK161401; BAE36376.1; ALT_INIT; mRNA.
DR EMBL; AK166351; BAE38725.1; -; mRNA.
DR EMBL; BC060208; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS15621.1; -. [Q3TLR7-1]
DR RefSeq; NP_001292162.1; NM_001305233.1.
DR RefSeq; NP_084042.1; NM_029766.3. [Q3TLR7-1]
DR AlphaFoldDB; Q3TLR7; -.
DR SMR; Q3TLR7; -.
DR BioGRID; 218345; 33.
DR IntAct; Q3TLR7; 31.
DR STRING; 10090.ENSMUSP00000027933; -.
DR iPTMnet; Q3TLR7; -.
DR PhosphoSitePlus; Q3TLR7; -.
DR EPD; Q3TLR7; -.
DR jPOST; Q3TLR7; -.
DR MaxQB; Q3TLR7; -.
DR PaxDb; Q3TLR7; -.
DR PeptideAtlas; Q3TLR7; -.
DR PRIDE; Q3TLR7; -.
DR ProteomicsDB; 277629; -. [Q3TLR7-1]
DR ProteomicsDB; 277630; -. [Q3TLR7-2]
DR ProteomicsDB; 277631; -. [Q3TLR7-4]
DR Antibodypedia; 34605; 227 antibodies from 29 providers.
DR Ensembl; ENSMUST00000027933; ENSMUSP00000027933; ENSMUSG00000037474. [Q3TLR7-1]
DR GeneID; 76843; -.
DR KEGG; mmu:76843; -.
DR UCSC; uc007eck.2; mouse. [Q3TLR7-1]
DR UCSC; uc007ecn.2; mouse. [Q3TLR7-4]
DR CTD; 51514; -.
DR MGI; MGI:1924093; Dtl.
DR VEuPathDB; HostDB:ENSMUSG00000037474; -.
DR eggNOG; KOG0321; Eukaryota.
DR GeneTree; ENSGT00530000064210; -.
DR HOGENOM; CLU_023407_0_0_1; -.
DR InParanoid; Q3TLR7; -.
DR OMA; VSMRKIC; -.
DR OrthoDB; 1288134at2759; -.
DR PhylomeDB; Q3TLR7; -.
DR TreeFam; TF324483; -.
DR Reactome; R-MMU-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-MMU-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 76843; 27 hits in 96 CRISPR screens.
DR ChiTaRS; Dtl; mouse.
DR PRO; PR:Q3TLR7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3TLR7; protein.
DR Bgee; ENSMUSG00000037474; Expressed in metanephric mesenchyme and 174 other tissues.
DR ExpressionAtlas; Q3TLR7; baseline and differential.
DR Genevisible; Q3TLR7; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Biological rhythms; Chromosome;
KW Cytoplasm; Cytoskeleton; DNA damage; DNA replication; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..729
FT /note="Denticleless protein homolog"
FT /id="PRO_0000274868"
FT REPEAT 47..89
FT /note="WD 1"
FT REPEAT 96..135
FT /note="WD 2"
FT REPEAT 138..178
FT /note="WD 3"
FT REPEAT 214..253
FT /note="WD 4"
FT REPEAT 269..308
FT /note="WD 5"
FT REPEAT 313..354
FT /note="WD 6"
FT REPEAT 358..398
FT /note="WD 7"
FT REGION 189..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 168..171
FT /note="DDB1-binding motif"
FT /evidence="ECO:0000250"
FT MOTIF 197..203
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 243..246
FT /note="DDB1-binding motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 420..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZJ0"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZJ0"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZJ0"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZJ0"
FT MOD_RES 463
FT /note="Phosphothreonine; by CDK1 and CDK2"
FT /evidence="ECO:0000250|UniProtKB:Q9NZJ0"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZJ0"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZJ0"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZJ0"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 515
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZJ0"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZJ0"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZJ0"
FT MOD_RES 683
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZJ0"
FT MOD_RES 701
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 214..216
FT /note="DSQ -> VR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022884"
FT VAR_SEQ 217..729
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022885"
FT VAR_SEQ 699..729
FT /note="TITPSSMRKICTYFRRKTQDDFCSPEHSTEL -> SLNVGGHMSYLKGTRCS
FT SQDCLGIQANNFALLLH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12707369"
FT /id="VSP_022886"
FT CONFLICT 110
FT /note="E -> G (in Ref. 2; BAE36376)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="P -> S (in Ref. 2; BAE38725)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="P -> L (in Ref. 2; BAB28549)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="M -> T (in Ref. 1; BAC76405/BAC76404)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="C -> Y (in Ref. 1; BAC76405/BAC76404)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="T -> A (in Ref. 2; BAE38725)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 729 AA; 79131 MW; C828FAFBA9929360 CRC64;
MLFNSVLRQP QLGVLRNGWS SHYPLQSLLS GYQCNCNDEH TSYGETGVPV PPFGCTFCTA
PSMEHILAVA NEEGFVRLYN TESQTSKKTC FKEWMAHWNA VFDLAWVPGE LKLVTAAGDQ
TAKFWDVRAG ELMGTCKGHQ CSLKSVAFPK FQKAVFSTGG RDGNIMIWDT RCNKKDGFYR
QVNQISGAHN TADKQTPSKP KKKQNSKGLA PAVDSQQSVT VVLFQDENTL VSAGAVDGII
KVWDLRKNYT AYRQEPIASK SFLYPGTSTR KLGYSSLVLD STGSTLFANC TDDNIYMFNM
TGLKTSPVAV FNGHQNSTFY VKSSLSPDDQ FLISGSSDEA AYIWKVSMPW HPPTVLLGHS
QEVTSVCWCP SDFTKIATCS DDNTLKIWRL NRGLEEKPGD KHSIVGWTSQ KKKEVKACPV
TVPSSQSTPA KAPRAKSSPS ISSPSSAACT PSCAGDLPLP SSTPTFSVKT TPATTRSSVS
RRGSISSVSP KPLSSFKMSL RNWVTRTPSS SPPVTPPASE TKISSPRKAL IPVSQKSSQA
DACSESRNRV KRRLDSSCLE SVKQKCVKSC NCVTELDGQA ESLRLDLCCL SGTQEVLSQD
SEGPTKSSKT EGAGTSISEP PSPVSPYASE GCGPLPLPLR PCGEGSEMVG KENSSPENKN
WLLAIAAKRK AENSSPRSPS SQTPSSRRQS GKTSPGPVTI TPSSMRKICT YFRRKTQDDF
CSPEHSTEL
