XPC_MOUSE
ID XPC_MOUSE Reviewed; 930 AA.
AC P51612; P54732; Q3TKI2; Q920M1; Q9DBW7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=DNA repair protein complementing XP-C cells homolog;
DE AltName: Full=Xeroderma pigmentosum group C-complementing protein homolog;
DE AltName: Full=p125;
GN Name=Xpc;
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] OF 3-930.
RX PubMed=8604333; DOI=10.1093/nar/24.6.1026;
RA Li L., Peterson C., Legerski R.;
RT "Sequence of the mouse XPC cDNA and genomic structure of the human XPC
RT gene.";
RL Nucleic Acids Res. 24:1026-1028(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yokoi M., Hanaoka F.;
RT "Molecular cloning of mouse XPC.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung, and Skin;
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 [MRNA] OF 59-617.
RC STRAIN=129/Sv;
RX PubMed=7675084; DOI=10.1038/377162a0;
RA Sands A.T., Abuin A., Sanchez A., Conti C.J., Bradley A.;
RT "High susceptibility to ultraviolet-induced carcinogenesis in mice lacking
RT XPC.";
RL Nature 377:162-165(1995).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-875 AND SER-876, AND
RP IDENTIFICATION BY 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-875 AND SER-876, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-875 AND SER-876, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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: Involved in global genome nucleotide excision repair (GG-NER)
CC by acting as damage sensing and DNA-binding factor component of the XPC
CC complex. Has only a low DNA repair activity by itself which is
CC stimulated by RAD23B and RAD23A. Has a preference to bind DNA
CC containing a short single-stranded segment but not to damaged
CC oligonucleotides. This feature is proposed to be related to a dynamic
CC sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-
CC bonded bases by forming a transient nucleoprotein intermediate complex
CC which matures into a stable recognition complex through an intrinsic
CC single-stranded DNA-binding activity. The XPC complex is proposed to
CC represent the first factor bound at the sites of DNA damage and
CC together with other core recognition factors, XPA, RPA and the TFIIH
CC complex, is part of the pre-incision (or initial recognition) complex.
CC The XPC complex recognizes a wide spectrum of damaged DNA characterized
CC by distortions of the DNA helix such as single-stranded loops,
CC mismatched bubbles or single-stranded overhangs. The orientation of XPC
CC complex binding appears to be crucial for inducing a productive NER.
CC XPC complex is proposed to recognize and to interact with unpaired
CC bases on the undamaged DNA strand which is followed by recruitment of
CC the TFIIH complex and subsequent scanning for lesions in the opposite
CC strand in a 5'-to-3' direction by the NER machinery. Cyclobutane
CC pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage
CC esacpe detection by the XPC complex due to a low degree of structural
CC perurbation. Instead they are detected by the UV-DDB complex which in
CC turn recruits and cooperates with the XPC complex in the respective DNA
CC repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER;
CC it preferentially binds to cisplatin and UV-damaged double-stranded DNA
CC and also binds to a variety of chemically and structurally diverse DNA
CC adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion
CC with a preference for the 5' side. XPC:RAD23B induces a bend in DNA
CC upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases
CC TDG and SMUG1. {ECO:0000250|UniProtKB:Q01831}.
CC -!- FUNCTION: In absence of DNA repair, the XPC complex also acts as a
CC transcription coactivator: XPC interacts with the DNA-binding
CC transcription factor E2F1 at a subset of promoters to recruit KAT2A and
CC histone acetyltransferase complexes (HAT). KAT2A recruitment
CC specifically promotes acetylation of histone variant H2A.Z.1/H2A.Z, but
CC not H2A.Z.2/H2A.V, thereby promoting expression of target genes.
CC {ECO:0000250|UniProtKB:Q01831}.
CC -!- SUBUNIT: Component of the XPC complex composed of XPC, RAD23B and
CC CETN2. Interacts with RAD23A; the interaction is suggesting the
CC existence of a functional equivalent variant XPC complex. Interacts
CC with TDG; the interaction is demonstrated using the XPC:RAD23B dimer.
CC Interacts with SMUG1; the interaction is demonstrated using the
CC XPC:RAD23B dimer. Interacts with DDB2. Interacts with CCNH, GTF2H1 and
CC ERCC3. Interacts with E2F1 and KAT2A; leading to KAT2A recruitment to
CC promoters and subsequent acetylation of histones.
CC {ECO:0000250|UniProtKB:Q01831}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01831}.
CC Chromosome {ECO:0000250|UniProtKB:Q01831}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q01831}. Note=Omnipresent in the nucleus and
CC consistently associates with and dissociates from DNA in the absence of
CC DNA damage. Continuously shuttles between the cytoplasm and the
CC nucleus, which is impeded by the presence of NER lesions.
CC {ECO:0000250|UniProtKB:Q01831}.
CC -!- PTM: Ubiquitinated upon UV irradiation; the ubiquitination requires the
CC UV-DDB complex, appears to be reversible and does not serve as a signal
CC for degradation. Ubiquitinated by RNF11 via 'Lys-63'-linked
CC ubiquitination. Ubiquitination by RNF111 is polysumoylation-dependent
CC and promotes nucleotide excision repair.
CC {ECO:0000250|UniProtKB:Q01831}.
CC -!- PTM: Sumoylated; sumoylation promotes ubiquitination by RNF111.
CC {ECO:0000250|UniProtKB:Q01831}.
CC -!- SIMILARITY: Belongs to the XPC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52500.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U27398; AAC52500.1; ALT_FRAME; mRNA.
DR EMBL; AB071144; BAB64540.1; -; mRNA.
DR EMBL; AK004713; BAB23497.1; -; mRNA.
DR EMBL; AK028595; BAC26023.1; -; mRNA.
DR EMBL; AK166981; BAE39163.1; -; mRNA.
DR EMBL; U40005; AAA82720.1; -; mRNA.
DR CCDS; CCDS39569.1; -.
DR PIR; S70630; S70630.
DR RefSeq; NP_033557.2; NM_009531.2.
DR AlphaFoldDB; P51612; -.
DR BioGRID; 204605; 3.
DR IntAct; P51612; 2.
DR STRING; 10090.ENSMUSP00000032182; -.
DR iPTMnet; P51612; -.
DR PhosphoSitePlus; P51612; -.
DR EPD; P51612; -.
DR jPOST; P51612; -.
DR MaxQB; P51612; -.
DR PaxDb; P51612; -.
DR PeptideAtlas; P51612; -.
DR PRIDE; P51612; -.
DR ProteomicsDB; 297654; -.
DR Antibodypedia; 4092; 332 antibodies from 31 providers.
DR Ensembl; ENSMUST00000032182; ENSMUSP00000032182; ENSMUSG00000030094.
DR GeneID; 22591; -.
DR KEGG; mmu:22591; -.
DR UCSC; uc009cyd.2; mouse.
DR CTD; 7508; -.
DR MGI; MGI:103557; Xpc.
DR VEuPathDB; HostDB:ENSMUSG00000030094; -.
DR eggNOG; KOG2179; Eukaryota.
DR GeneTree; ENSGT00390000005194; -.
DR HOGENOM; CLU_009925_1_1_1; -.
DR InParanoid; P51612; -.
DR OMA; PLTCYKY; -.
DR OrthoDB; 750482at2759; -.
DR PhylomeDB; P51612; -.
DR TreeFam; TF101242; -.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR BioGRID-ORCS; 22591; 1 hit in 112 CRISPR screens.
DR ChiTaRS; Xpc; mouse.
DR PRO; PR:P51612; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P51612; protein.
DR Bgee; ENSMUSG00000030094; Expressed in granulocyte and 237 other tissues.
DR ExpressionAtlas; P51612; baseline and differential.
DR Genevisible; P51612; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000109; C:nucleotide-excision repair complex; ISS:UniProtKB.
DR GO; GO:0000111; C:nucleotide-excision repair factor 2 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0090734; C:site of DNA damage; IDA:MGI.
DR GO; GO:0071942; C:XPC complex; ISS:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; IDA:MGI.
DR GO; GO:0140612; F:DNA damage sensor activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0006281; P:DNA repair; IMP:MGI.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IGI:MGI.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0000720; P:pyrimidine dimer repair by nucleotide-excision repair; IMP:MGI.
DR GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
DR GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; ISO:MGI.
DR GO; GO:0010996; P:response to auditory stimulus; IEA:Ensembl.
DR GO; GO:0010224; P:response to UV-B; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0070914; P:UV-damage excision repair; IDA:MGI.
DR Gene3D; 3.30.70.2460; -; 1.
DR Gene3D; 3.90.260.10; -; 2.
DR InterPro; IPR018327; BHD_2.
DR InterPro; IPR004583; DNA_repair_Rad4.
DR InterPro; IPR018026; DNA_repair_Rad4_subgr.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR018325; Rad4/PNGase_transGLS-fold.
DR InterPro; IPR018326; Rad4_beta-hairpin_dom1.
DR InterPro; IPR018328; Rad4_beta-hairpin_dom3.
DR InterPro; IPR042488; Rad4_BHD3_sf.
DR InterPro; IPR036985; Transglutaminase-like_sf.
DR PANTHER; PTHR12135; PTHR12135; 1.
DR Pfam; PF10403; BHD_1; 1.
DR Pfam; PF10404; BHD_2; 1.
DR Pfam; PF10405; BHD_3; 1.
DR Pfam; PF03835; Rad4; 1.
DR SMART; SM01030; BHD_1; 1.
DR SMART; SM01031; BHD_2; 1.
DR SMART; SM01032; BHD_3; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR TIGRFAMs; TIGR00605; rad4; 1.
PE 1: Evidence at protein level;
KW Chromosome; Cytoplasm; DNA damage; DNA repair; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..930
FT /note="DNA repair protein complementing XP-C cells homolog"
FT /id="PRO_0000218294"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..727
FT /note="Interaction with RAD23B"
FT /evidence="ECO:0000250"
FT REGION 600..759
FT /note="Minimal sensor domain involved in damage
FT recognition"
FT /evidence="ECO:0000250"
FT REGION 600..734
FT /note="DNA-binding; preference for heteroduplex DNA"
FT /evidence="ECO:0000250"
FT REGION 760..824
FT /note="DNA-binding; preference for single stranded DNA;
FT required for formation of stable nucleoprotein complex"
FT /evidence="ECO:0000250"
FT REGION 809..930
FT /note="Interaction with ERCC2 and GTF2H1"
FT /evidence="ECO:0000250"
FT REGION 840..859
FT /note="Interaction with CETN2"
FT /evidence="ECO:0000250"
FT REGION 867..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 388..393
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01831"
FT MOD_RES 165
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01831"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01831"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01831"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01831"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01831"
FT CROSSLNK 40
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01831"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01831"
FT CROSSLNK 88
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01831"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01831"
FT CONFLICT 13
FT /note="K -> N (in Ref. 2; BAB64540)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="L -> S (in Ref. 1; AAC52500)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="F -> L (in Ref. 1; AAC52500)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="S -> L (in Ref. 1; AAC52500)"
FT /evidence="ECO:0000305"
FT CONFLICT 148..149
FT /note="AT -> CP (in Ref. 2; BAB64540)"
FT /evidence="ECO:0000305"
FT CONFLICT 165..166
FT /note="TP -> RG (in Ref. 1; AAC52500)"
FT /evidence="ECO:0000305"
FT CONFLICT 196..201
FT /note="EVQENM -> GVHEDT (in Ref. 4; AAA82720)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="S -> N (in Ref. 4; AAA82720)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="S -> N (in Ref. 4; AAA82720)"
FT /evidence="ECO:0000305"
FT CONFLICT 221..223
FT /note="RQP -> SQL (in Ref. 4; AAA82720)"
FT /evidence="ECO:0000305"
FT CONFLICT 373..375
FT /note="GKA -> AKP (in Ref. 4; AAA82720)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="G -> GS (in Ref. 1; AAC52500)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="S -> R (in Ref. 1; AAC52500)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="E -> K (in Ref. 2; BAB64540)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="R -> C (in Ref. 4; AAA82720)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="S -> C (in Ref. 1; AAC52500)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="E -> K (in Ref. 1; AAC52500)"
FT /evidence="ECO:0000305"
FT CONFLICT 621..622
FT /note="KH -> ND (in Ref. 1; AAC52500)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="W -> R (in Ref. 1; AAC52500)"
FT /evidence="ECO:0000305"
FT CONFLICT 712..715
FT /note="LSEP -> HLGA (in Ref. 1; AAC52500)"
FT /evidence="ECO:0000305"
FT CONFLICT 751
FT /note="N -> K (in Ref. 1; AAC52500)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="R -> H (in Ref. 1; AAC52500)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="C -> S (in Ref. 1; AAC52500)"
FT /evidence="ECO:0000305"
FT CONFLICT 921
FT /note="A -> P (in Ref. 1; AAC52500)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 930 AA; 104522 MW; 0C469AB21B4E4EE9 CRC64;
MAPKRTADGR RRKRGQKTED NKVARHEESV ADDFEDEKQK PRRKSSFPKV SQGKRKRGCS
DPGDPTNGAA KKKVAKATAK SKNLKVLKEE ALSDGDDFRD SPADCKKAKK HPKSKVVDQG
TDEDDSEDDW EEVEELTEPV LDMGENSATS PSDMPVKAVE IEIETPQQAK ERERSEKIKM
EFETYLRRMM KRFNKEVQEN MHKVHLLCLL ASGFYRNSIC RQPDLLAIGL SIIPIRFTKV
PLQDRDAYYL SNLVKWFIGT FTVNADLSAS EQDDLQTTLE RRIAIYSARD NEELVHIFLL
ILRALQLLTR LVLSLQPIPL KSAVTKGRKS SKETSVEGPG GSSELSSNSP ESHNKPTTSR
RIKEEETLSE GRGKATARGK RGTGTAGSRQ RRKPSCSEGE EAEQKVQGRP HARKRRVAAK
VSYKEESESD GAGSGSDFEP SSGEGQHSSD EDCEPGPRKQ KRASAPQRTK AGSKSASKTQ
RGSQCEPSSF PEASSSSSGC KRGKKVSSGA EEMADRKPAG VDQWLEVYCE PQAKWVCVDC
VHGVVGQPVA CYKYATKPMT YVVGIDSDGW VRDVTQRYDP AWMTATRKCR VDAEWWAETL
RPYRSLLTER EKKEDQEFQA KHLDQPLPTS ISTYKNHPLY ALKRHLLKFQ AIYPETAAVL
GYCRGEAVYS RDCVHTLHSR DTWLKQARVV RLGEVPYKMV KGFSNRARKA RLSEPQLHDH
NDLGLYGHWQ TEEYQPPIAV DGKVPRNEFG NVYLFLPSMM PVGCVQMTLP NLNRVARKLG
IDCVQAITGF DFHGGYCHPV TDGYIVCEEF RDVLLAAWEN EQAIIEKKEK EKKEKRALGN
WKLLVRGLLI RERLKLRYGA KSEAAAPHAA GGGLSSDEEE GTSSQAEAAR VLAASWPQNR
EDPEQKSEYT KMTRKRRAAE ASHLFPFEKL
