SSRP1_MOUSE
ID SSRP1_MOUSE Reviewed; 708 AA.
AC Q08943; Q3U9Z2; Q3UJ75; Q4V9U4; Q8CGA6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=FACT complex subunit SSRP1;
DE AltName: Full=Facilitates chromatin transcription complex subunit SSRP1;
DE AltName: Full=Recombination signal sequence recognition protein 1;
DE AltName: Full=Structure-specific recognition protein 1;
DE AltName: Full=T160;
GN Name=Ssrp1;
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=B-cell;
RX PubMed=1678855; DOI=10.1128/mcb.11.9.4528-4536.1991;
RA Shirakata M., Hueppi K., Usada S., Okazaki K., Yoshida K., Sakano H.;
RT "HMG1-related DNA-binding protein isolated with V-(D)-J recombination
RT signal probes.";
RL Mol. Cell. Biol. 11:4528-4536(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Heart, Liver, Stomach, and Visual cortex;
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 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 589-708 (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N-3; 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 DISRUPTION PHENOTYPE.
RX PubMed=12861016; DOI=10.1128/mcb.23.15.5301-5307.2003;
RA Cao S., Bendall H., Hicks G.G., Nashabi A., Sakano H., Shinkai Y.,
RA Gariglio M., Oltz E.M., Ruley H.E.;
RT "The high-mobility-group box protein SSRP1/T160 is essential for cell
RT viability in day 3.5 mouse embryos.";
RL Mol. Cell. Biol. 23:5301-5307(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, 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-444, AND IDENTIFICATION BY
RP 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-444, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-441; SER-444 AND TYR-452, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
RN [9]
RP FUNCTION, AND INTERACTION WITH MYOG.
RX PubMed=23364797; DOI=10.1074/jbc.m112.426718;
RA Lolis A.A., Londhe P., Beggs B.C., Byrum S.D., Tackett A.J., Davie J.K.;
RT "Myogenin recruits the histone chaperone facilitates chromatin
RT transcription (FACT) to promote nucleosome disassembly at muscle-specific
RT genes.";
RL J. Biol. Chem. 288:7676-7687(2013).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-542, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Component of the FACT complex, a general chromatin factor
CC that acts to reorganize nucleosomes. The FACT complex is involved in
CC multiple processes that require DNA as a template such as mRNA
CC elongation, DNA replication and DNA repair. During transcription
CC elongation the FACT complex acts as a histone chaperone that both
CC destabilizes and restores nucleosomal structure. It facilitates the
CC passage of RNA polymerase II and transcription by promoting the
CC dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC subsequently promotes the reestablishment of the nucleosome following
CC the passage of RNA polymerase II. The FACT complex is probably also
CC involved in phosphorylation of 'Ser-392' of p53/TP53 via its
CC association with CK2 (casein kinase II). Binds specifically to double-
CC stranded DNA. Also acts as a transcriptional coactivator for p63/TP63.
CC {ECO:0000269|PubMed:23364797}.
CC -!- SUBUNIT: Interacts with MYOG (via C-terminal region) (PubMed:23364797).
CC Component of the FACT complex, a stable heterodimer of SSRP1 and
CC SUPT16H. Also a component of a CK2-SPT16-SSRP1 complex which forms
CC following UV irradiation, composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2
CC and CSNK2B. Binds to histone H3-H4 tetramers, but not to intact
CC nucleosomes. Identified in a centromere complex containing histones
CC H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP,
CC SUPT16H, SSRP1 and RSF1. Interacts with isoform gamma of TP63.
CC Interacts with FYTTD1/UIF (By similarity). Interacts with SRF (By
CC similarity). Interacts with NEK9 (By similarity).
CC {ECO:0000250|UniProtKB:Q04931, ECO:0000250|UniProtKB:Q08945,
CC ECO:0000269|PubMed:23364797}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q05344}.
CC Chromosome {ECO:0000250|UniProtKB:Q05344}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q05344}. Note=Colocalizes with RNA polymerase II
CC on chromatin. Recruited to actively transcribed loci.
CC {ECO:0000250|UniProtKB:Q05344}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q08943-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08943-2; Sequence=VSP_019626;
CC -!- PTM: Phosphorylated by CK2 following UV but not gamma irradiation.
CC Phosphorylation inhibits its DNA-binding activity (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Polyubiquitinated following caspase cleavage
CC resulting in degradation of the N-terminal ubiquitinated part of the
CC cleaved protein (By similarity). {ECO:0000250}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryos die soon after implantation while
CC preimplantation blastocysts are defective for cell outgrowth.
CC {ECO:0000269|PubMed:12861016}.
CC -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH42502.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; S50213; AAB19500.2; -; mRNA.
DR EMBL; AK146446; BAE27178.1; -; mRNA.
DR EMBL; AK146585; BAE27280.1; -; mRNA.
DR EMBL; AK146607; BAE27299.1; -; mRNA.
DR EMBL; AK151584; BAE30524.1; -; mRNA.
DR EMBL; AK158552; BAE34555.1; -; mRNA.
DR EMBL; BC042502; AAH42502.1; ALT_FRAME; mRNA.
DR EMBL; BC096682; AAH96682.1; -; mRNA.
DR CCDS; CCDS38165.1; -. [Q08943-1]
DR PIR; A41265; A41265.
DR RefSeq; NP_001129553.1; NM_001136081.2. [Q08943-1]
DR RefSeq; NP_892035.2; NM_182990.4. [Q08943-1]
DR RefSeq; XP_006499133.1; XM_006499070.1. [Q08943-1]
DR AlphaFoldDB; Q08943; -.
DR SMR; Q08943; -.
DR BioGRID; 203512; 4.
DR ComplexPortal; CPX-433; FACT complex.
DR IntAct; Q08943; 6.
DR MINT; Q08943; -.
DR STRING; 10090.ENSMUSP00000076971; -.
DR iPTMnet; Q08943; -.
DR PhosphoSitePlus; Q08943; -.
DR SwissPalm; Q08943; -.
DR EPD; Q08943; -.
DR jPOST; Q08943; -.
DR MaxQB; Q08943; -.
DR PaxDb; Q08943; -.
DR PeptideAtlas; Q08943; -.
DR PRIDE; Q08943; -.
DR ProteomicsDB; 257478; -. [Q08943-1]
DR ProteomicsDB; 257479; -. [Q08943-2]
DR Antibodypedia; 1060; 360 antibodies from 34 providers.
DR DNASU; 20833; -.
DR Ensembl; ENSMUST00000077798; ENSMUSP00000076971; ENSMUSG00000027067. [Q08943-1]
DR Ensembl; ENSMUST00000168266; ENSMUSP00000127058; ENSMUSG00000027067. [Q08943-1]
DR GeneID; 20833; -.
DR KEGG; mmu:20833; -.
DR UCSC; uc008kju.2; mouse. [Q08943-1]
DR CTD; 6749; -.
DR MGI; MGI:107912; Ssrp1.
DR VEuPathDB; HostDB:ENSMUSG00000027067; -.
DR eggNOG; KOG0526; Eukaryota.
DR GeneTree; ENSGT00940000157117; -.
DR InParanoid; Q08943; -.
DR OMA; SKQPGKC; -.
DR OrthoDB; 915055at2759; -.
DR PhylomeDB; Q08943; -.
DR TreeFam; TF315228; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR BioGRID-ORCS; 20833; 25 hits in 112 CRISPR screens.
DR ChiTaRS; Ssrp1; mouse.
DR PRO; PR:Q08943; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q08943; protein.
DR Bgee; ENSMUSG00000027067; Expressed in otic placode and 265 other tissues.
DR ExpressionAtlas; Q08943; baseline and differential.
DR Genevisible; Q08943; MM.
DR GO; GO:0035101; C:FACT complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR GO; GO:0006337; P:nucleosome disassembly; ISO:MGI.
DR GO; GO:1902275; P:regulation of chromatin organization; ISO:MGI.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 2.30.29.220; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR013719; DUF1747.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR035417; POB3_N.
DR InterPro; IPR000969; SSrcognition.
DR InterPro; IPR024954; SSRP1_dom.
DR InterPro; IPR038167; SSRP1_sf.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF17292; POB3_N; 1.
DR Pfam; PF08512; Rtt106; 1.
DR Pfam; PF03531; SSrecog; 1.
DR PRINTS; PR00887; SSRCOGNITION.
DR SMART; SM00398; HMG; 1.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosome; DNA damage; DNA repair;
KW DNA replication; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT CHAIN 2..708
FT /note="FACT complex subunit SSRP1"
FT /id="PRO_0000048607"
FT DNA_BIND 547..615
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 458..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..495
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..638
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 450..451
FT /note="Cleavage; by caspase-3 and/or caspase-7"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 413
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 441
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 452
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 510
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 542
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 657
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 688
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT CROSSLNK 90
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT CROSSLNK 296
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT CROSSLNK 364
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT VAR_SEQ 621
FT /note="S -> SSKRDK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019626"
FT CONFLICT 27..28
FT /note="RQ -> PS (in Ref. 1; AAB19500)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="R -> P (in Ref. 1; AAB19500)"
FT /evidence="ECO:0000305"
FT CONFLICT 138..144
FT /note="QCTTGKN -> SVPQARI (in Ref. 1; AAB19500)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="A -> P (in Ref. 1; AAB19500)"
FT /evidence="ECO:0000305"
FT CONFLICT 589..590
FT /note="SK -> HE (in Ref. 3; AAH96682)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="R -> S (in Ref. 3; AAH96682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 708 AA; 80860 MW; 8259C1A6E9899843 CRC64;
MAETLEFNDI FQEVKGSMND GRLRLSRQGI IFKNSKTGKV DNIQAGELTE GIWRRVALGH
GLKLLTKNGH VYKYDGFRES EFEKLSDFFK THYRLELMEK DLCVKGWNWG TVKFGGQLLS
FDIGDQPVFE IPLSNVSQCT TGKNEVTLEF HQNDDAEVSL MEVRFYVPPT QEDGVDPVEA
FAQNVLSKAD VIQATGDAIC IFRELQCLTP RGRYDIRIYP TFLHLHGKTF DYKIPYTTVL
RLFLLPHKDQ RQMFFVISLD PPIKQGQTRY HFLILLFSKD EDISLTLNMN EEEVEKRFEG
RLTKNMSGSL YEMVSRVMKA LVNRKITVPG NFQGHSGAQC ITCSYKASSG LLYPLERGFI
YVHKPPVHIR FDEISFVNFA RGTTTTRSFD FEIETKQGTQ YTFSSIEREE YGKLFDFVNA
KKLNIKNRGL KEGINPGYDD YADSDEDQHD AYLERMKEEG KIREENANDS SDDSGEETDE
SFNPGEEEED VAEEFDSNAS ASSSSNEGDS DREEKKREQL KRAKMAKDRK SRRKSSEAKK
GKDPNAPKRP MSAYMLWLNA SREKIKSDHP GISITDLSKK AGEIWKGMSK EKKEEWDRKA
EDARREYEKA MKEYEGGRGD SSKRDKSKKK KKVKAKMEKK STPSRGSSSK SSSRQLSDSF
KSKEFVSSDE SSSGENKSKK KRRRSEDSEE ELASTPPSSE DSASGSDE
