NELFE_MOUSE
ID NELFE_MOUSE Reviewed; 375 AA.
AC P19426; P97485; P97486; Q9CZN3;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Negative elongation factor E;
DE Short=NELF-E;
DE AltName: Full=RNA-binding protein RD;
GN Name=Nelfe; Synonyms=D17h6s45, Rd, Rdbp;
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 [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=3353717; DOI=10.1126/science.3353717;
RA Levi-Strauss M., Carroll M.C., Steinmetz M., Meo T.;
RT "A previously undetected MHC gene with an unusual periodic structure.";
RL Science 240:201-204(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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).
RC TISSUE=Mammary gland;
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 GENOMIC DNA] OF 26-375.
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 196-247, POLYMORPHISM, AND VARIANTS
RP 228-ARG-ASP-229 DEL AND 229-ASP--ARG-236 DEL.
RC STRAIN=129/Sv, and LP.RIII/Sn;
RX PubMed=9321489; DOI=10.1007/s003359900579;
RA Taylor P.R., Slingsby J.H., Walport M.J., Botto M.;
RT "Murine D17H6S45 (Rd) gene: polymorphism and overlap with complement factor
RT B.";
RL Mamm. Genome 8:796-797(1997).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, 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 [8]
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 [9]
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115; SER-131 AND SER-357, 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 [11]
RP INTERACTION WITH NELFB.
RX PubMed=26010750; DOI=10.1371/journal.pone.0127422;
RA Pan H., Zhao X., Zhang X., Abouelsoud M., Sun J., April C., Amleh A.,
RA Fan J.B., Hu Y., Li R.;
RT "Translational initiation at a non-AUG start codon for human and mouse
RT negative elongation factor-B.";
RL PLoS ONE 10:E0127422-E0127422(2015).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=31399344; DOI=10.1016/j.molcel.2019.06.034;
RA Etchegaray J.P., Zhong L., Li C., Henriques T., Ablondi E., Nakadai T.,
RA Van Rechem C., Ferrer C., Ross K.N., Choi J.E., Samarakkody A., Ji F.,
RA Chang A., Sadreyev R.I., Ramaswamy S., Nechaev S., Whetstine J.R.,
RA Roeder R.G., Adelman K., Goren A., Mostoslavsky R.;
RT "The histone deacetylase SIRT6 restrains transcription elongation via
RT promoter-proximal pausing.";
RL Mol. Cell 75:683-699(2019).
CC -!- FUNCTION: Essential component of the NELF complex, a complex that
CC negatively regulates the elongation of transcription by RNA polymerase
CC II (PubMed:31399344). The NELF complex, which acts via an association
CC with the DSIF complex and causes transcriptional pausing, is
CC counteracted by the P-TEFb kinase complex (PubMed:31399344). Provides
CC the strongest RNA binding activity of the NELF complex and may
CC initially recruit the NELF complex to RNA (By similarity).
CC {ECO:0000250|UniProtKB:P18615, ECO:0000269|PubMed:31399344}.
CC -!- SUBUNIT: The NELF complex is composed of NELFA, NELFB, NELFCD and NELFE
CC (By similarity). Interacts with NELFB (PubMed:26010750).
CC {ECO:0000250|UniProtKB:P18615, ECO:0000269|PubMed:26010750}.
CC -!- INTERACTION:
CC P19426; P11499: Hsp90ab1; NbExp=2; IntAct=EBI-6142845, EBI-492813;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31399344}. Chromosome
CC {ECO:0000269|PubMed:31399344}. Note=Localizes to chromatin
CC (PubMed:31399344). Phosphorylation by the P-TEFb complex promotes its
CC release from chromatin (PubMed:31399344).
CC {ECO:0000269|PubMed:31399344}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P19426-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P19426-2; Sequence=VSP_008960;
CC -!- DOMAIN: The RRM domain interacts with RNA, and is essential for NELF
CC complex function. It is however not required for the NELF complex
CC formation (By similarity). {ECO:0000250|UniProtKB:P18615}.
CC -!- PTM: Phosphorylated by the P-TEFb complex at sites next to its RNA
CC recognition motif, promoting its release from chromatin.
CC {ECO:0000269|PubMed:31399344}.
CC -!- PTM: Sumoylated. {ECO:0000250|UniProtKB:P18615}.
CC -!- POLYMORPHISM: The length of the RD repeats is variable.
CC {ECO:0000269|PubMed:9321489}.
CC -!- SIMILARITY: Belongs to the RRM NELF-E family. {ECO:0000305}.
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DR EMBL; M21332; AAA39680.1; -; Genomic_DNA.
DR EMBL; AK012389; BAB28206.1; -; mRNA.
DR EMBL; BC034867; AAH34867.1; -; mRNA.
DR EMBL; AF109906; AAC84161.1; -; Genomic_DNA.
DR EMBL; U83841; AAB41535.1; -; Genomic_DNA.
DR EMBL; U83842; AAB41536.1; -; Genomic_DNA.
DR CCDS; CCDS28662.1; -. [P19426-2]
DR PIR; A40112; A40112.
DR RefSeq; NP_001039328.1; NM_001045863.1. [P19426-2]
DR RefSeq; NP_001039329.1; NM_001045864.1. [P19426-2]
DR RefSeq; NP_613046.2; NM_138580.2. [P19426-2]
DR AlphaFoldDB; P19426; -.
DR BMRB; P19426; -.
DR SMR; P19426; -.
DR BioGRID; 205393; 8.
DR IntAct; P19426; 1.
DR STRING; 10090.ENSMUSP00000134272; -.
DR iPTMnet; P19426; -.
DR PhosphoSitePlus; P19426; -.
DR EPD; P19426; -.
DR jPOST; P19426; -.
DR MaxQB; P19426; -.
DR PaxDb; P19426; -.
DR PeptideAtlas; P19426; -.
DR PRIDE; P19426; -.
DR ProteomicsDB; 287370; -. [P19426-1]
DR ProteomicsDB; 287371; -. [P19426-2]
DR Antibodypedia; 1924; 160 antibodies from 27 providers.
DR DNASU; 27632; -.
DR Ensembl; ENSMUST00000097343; ENSMUSP00000094956; ENSMUSG00000024369. [P19426-2]
DR Ensembl; ENSMUST00000165953; ENSMUSP00000131195; ENSMUSG00000024369. [P19426-2]
DR Ensembl; ENSMUST00000173357; ENSMUSP00000134272; ENSMUSG00000024369. [P19426-2]
DR GeneID; 27632; -.
DR KEGG; mmu:27632; -.
DR CTD; 7936; -.
DR MGI; MGI:102744; Nelfe.
DR VEuPathDB; HostDB:ENSMUSG00000024369; -.
DR eggNOG; ENOG502QQQ4; Eukaryota.
DR GeneTree; ENSGT00630000089917; -.
DR HOGENOM; CLU_055643_0_0_1; -.
DR InParanoid; P19426; -.
DR OMA; SQKSAHK; -.
DR PhylomeDB; P19426; -.
DR TreeFam; TF324087; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-113418; Formation of the Early 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-75955; RNA Polymerase II Transcription Elongation.
DR BioGRID-ORCS; 27632; 16 hits in 75 CRISPR screens.
DR ChiTaRS; Nelfe; mouse.
DR PRO; PR:P19426; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P19426; protein.
DR Bgee; ENSMUSG00000024369; Expressed in seminiferous tubule of testis and 257 other tissues.
DR ExpressionAtlas; P19426; baseline and differential.
DR Genevisible; P19426; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032021; C:NELF complex; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IMP:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR CDD; cd12305; RRM_NELFE; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR033102; NELFE.
DR InterPro; IPR034637; NELFE_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR17250; PTHR17250; 2.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Coiled coil; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..375
FT /note="Negative elongation factor E"
FT /id="PRO_0000081803"
FT REPEAT 184..185
FT /note="1"
FT REPEAT 186..187
FT /note="2"
FT REPEAT 188..189
FT /note="3"
FT REPEAT 190..191
FT /note="4"
FT REPEAT 192..193
FT /note="5; approximate"
FT REPEAT 194..195
FT /note="6"
FT REPEAT 196..197
FT /note="7"
FT REPEAT 198..199
FT /note="8"
FT REPEAT 200..201
FT /note="9"
FT REPEAT 202..203
FT /note="10; approximate"
FT REPEAT 204..205
FT /note="11"
FT REPEAT 206..207
FT /note="12"
FT REPEAT 208..209
FT /note="13"
FT REPEAT 210..211
FT /note="14"
FT REPEAT 212..213
FT /note="15"
FT REPEAT 214..215
FT /note="16"
FT REPEAT 216..217
FT /note="17"
FT REPEAT 218..219
FT /note="18; approximate"
FT REPEAT 220..221
FT /note="19; approximate"
FT REPEAT 222..223
FT /note="20"
FT REPEAT 224..225
FT /note="21"
FT REPEAT 226..227
FT /note="22"
FT REPEAT 228..229
FT /note="23"
FT REPEAT 230..231
FT /note="24; approximate"
FT REPEAT 232..233
FT /note="25"
FT REPEAT 234..235
FT /note="26"
FT REPEAT 236..237
FT /note="27"
FT REPEAT 238..239
FT /note="28"
FT REPEAT 240..241
FT /note="29"
FT REPEAT 242..243
FT /note="30"
FT REPEAT 244..245
FT /note="31"
FT REPEAT 246..247
FT /note="32"
FT DOMAIN 266..336
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 30..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..247
FT /note="32 X 2 AA approximate tandem repeats of R-[DSE]"
FT COILED 7..36
FT /evidence="ECO:0000255"
FT COMPBIAS 35..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 276
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 278
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P18615"
FT VAR_SEQ 224..231
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_008960"
FT VARIANT 228..229
FT /note="Missing (in strain: LP.RIII/Sn)"
FT /evidence="ECO:0000269|PubMed:9321489"
FT VARIANT 229..236
FT /note="Missing (in strain: 129/Sv)"
FT /evidence="ECO:0000269|PubMed:9321489"
FT CONFLICT 18
FT /note="K -> E (in Ref. 1; AAA39680)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 42554 MW; E7B5D51A366B7949 CRC64;
MLVIPPGLSE EEEALQKKFN KLKKKKKALL ALKKQSSSGP ASQGGVKRSL SEQPVVDTAT
ATEQAKQLVK SGAISAIKAE TKNSGFKRSR TLEGKLKDPE KGPVPTFQPF QRSMSADEDL
QEPSRRPQRK SLYESFVSSS DRLRELGQDG EEAEAPGAGD GPPRGFDWSY EEHGSARSSA
SPPRSRSRDR SHDRSRDRDR DKERDRDRDR DRDRDRDKDK DRDRDRDRDK ERDRDRDRDR
DRERDREGPF RRSDSFPERR APRKGNTLYV YGEDMTPTLL RGAFSPFGNI IDLSMDPPRN
CAFVTYEKME SADQAVAELN GTQVESVQLK VNIARKQPML DAATGKSVWG SLAVQNSPKG
CHRDKRTQIV YSDDL
