DI3L2_MOUSE
ID DI3L2_MOUSE Reviewed; 870 AA.
AC Q8CI75; Q8BMG9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=DIS3-like exonuclease 2 {ECO:0000255|HAMAP-Rule:MF_03045};
DE EC=3.1.13.- {ECO:0000255|HAMAP-Rule:MF_03045};
GN Name=Dis3l2;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Forelimb;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, 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).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-389.
RX PubMed=23594738; DOI=10.1038/nature12119;
RA Chang H.M., Triboulet R., Thornton J.E., Gregory R.I.;
RT "A role for the Perlman syndrome exonuclease Dis3l2 in the Lin28-let-7
RT pathway.";
RL Nature 497:244-248(2013).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 37-856 OF MUTANT ASN-389 IN
RP COMPLEX WITH MAGNESIUM AND POLY(U) RNA, FUNCTION, DOMAIN, COFACTOR, RNA
RP BINDING, AND MUTAGENESIS OF ARG-74; ASP-389; 548-ARG--LYS-553; GLN-612;
RP ASN-777; GLN-778 AND ASN-796.
RX PubMed=25119025; DOI=10.1038/nature13553;
RA Faehnle C.R., Walleshauser J., Joshua-Tor L.;
RT "Mechanism of Dis3l2 substrate recognition in the Lin28-let-7 pathway.";
RL Nature 514:252-256(2014).
CC -!- FUNCTION: 3'-5'-exoribonuclease that specifically recognizes RNAs
CC polyuridylated at their 3' end and mediates their degradation.
CC Component of an exosome-independent RNA degradation pathway that
CC mediates degradation of both mRNAs and miRNAs that have been
CC polyuridylated by a terminal uridylyltransferase, such as ZCCHC11/TUT4.
CC Mediates degradation of cytoplasmic mRNAs that have been deadenylated
CC and subsequently uridylated at their 3'. Mediates degradation of
CC uridylated pre-let-7 miRNAs, contributing to the maintenance of
CC embryonic stem (ES) cells. Essential for correct mitosis, and
CC negatively regulates cell proliferation. {ECO:0000255|HAMAP-
CC Rule:MF_03045, ECO:0000269|PubMed:23594738,
CC ECO:0000269|PubMed:25119025}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03045,
CC ECO:0000269|PubMed:25119025};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03045,
CC ECO:0000269|PubMed:25119025};
CC -!- SUBUNIT: Interacts with XRN1. {ECO:0000250|UniProtKB:Q8IYB7}.
CC -!- INTERACTION:
CC Q8CI75; Q8K3Y3: Lin28a; NbExp=2; IntAct=EBI-16045218, EBI-11109197;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03045,
CC ECO:0000269|PubMed:23594738}. Cytoplasm, P-body {ECO:0000255|HAMAP-
CC Rule:MF_03045}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CI75-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CI75-2; Sequence=VSP_030379;
CC -!- DOMAIN: Specifically recognizes and binds polyuridylated RNAs via 3
CC RNA-binding regions (named U-zone 1, U-zone 2 and U-zone 3) that form
CC an open funnel on one face of the catalytic domain, allowing RNA to
CC navigate a path to the active site. {ECO:0000269|PubMed:25119025}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. DIS3L2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03045}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27292.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK031180; BAC27292.1; ALT_FRAME; mRNA.
DR EMBL; BC036177; AAH36177.1; -; mRNA.
DR CCDS; CCDS15124.1; -. [Q8CI75-1]
DR CCDS; CCDS48304.1; -. [Q8CI75-2]
DR RefSeq; NP_001165628.1; NM_001172157.1. [Q8CI75-2]
DR RefSeq; NP_705758.1; NM_153530.2. [Q8CI75-1]
DR PDB; 4PMW; X-ray; 2.95 A; A/B=37-856.
DR PDBsum; 4PMW; -.
DR AlphaFoldDB; Q8CI75; -.
DR SMR; Q8CI75; -.
DR BioGRID; 229008; 7.
DR DIP; DIP-60224N; -.
DR IntAct; Q8CI75; 1.
DR STRING; 10090.ENSMUSP00000132673; -.
DR iPTMnet; Q8CI75; -.
DR PhosphoSitePlus; Q8CI75; -.
DR EPD; Q8CI75; -.
DR jPOST; Q8CI75; -.
DR MaxQB; Q8CI75; -.
DR PaxDb; Q8CI75; -.
DR PeptideAtlas; Q8CI75; -.
DR PRIDE; Q8CI75; -.
DR ProteomicsDB; 279688; -. [Q8CI75-1]
DR ProteomicsDB; 279689; -. [Q8CI75-2]
DR Antibodypedia; 11872; 187 antibodies from 26 providers.
DR DNASU; 208718; -.
DR Ensembl; ENSMUST00000065694; ENSMUSP00000070506; ENSMUSG00000053333. [Q8CI75-1]
DR Ensembl; ENSMUST00000168237; ENSMUSP00000132673; ENSMUSG00000053333. [Q8CI75-2]
DR GeneID; 208718; -.
DR KEGG; mmu:208718; -.
DR UCSC; uc007bvu.2; mouse. [Q8CI75-1]
DR UCSC; uc007bvw.2; mouse. [Q8CI75-2]
DR CTD; 129563; -.
DR MGI; MGI:2442555; Dis3l2.
DR VEuPathDB; HostDB:ENSMUSG00000053333; -.
DR eggNOG; KOG2102; Eukaryota.
DR GeneTree; ENSGT00530000063106; -.
DR HOGENOM; CLU_002333_5_2_1; -.
DR InParanoid; Q8CI75; -.
DR OMA; WTRMKGP; -.
DR OrthoDB; 1104619at2759; -.
DR PhylomeDB; Q8CI75; -.
DR TreeFam; TF315191; -.
DR BioGRID-ORCS; 208718; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Dis3l2; mouse.
DR PRO; PR:Q8CI75; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8CI75; protein.
DR Bgee; ENSMUSG00000053333; Expressed in spermatid and 216 other tissues.
DR ExpressionAtlas; Q8CI75; baseline and differential.
DR Genevisible; Q8CI75; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:UniProtKB.
DR GO; GO:0004540; F:ribonuclease activity; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010587; P:miRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0051306; P:mitotic sister chromatid separation; ISS:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0000291; P:nuclear-transcribed mRNA catabolic process, exonucleolytic; ISS:UniProtKB.
DR GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IEA:InterPro.
DR GO; GO:1990074; P:polyuridylation-dependent mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_03045; DIS3L2; 1.
DR InterPro; IPR041505; Dis3_CSD2.
DR InterPro; IPR028591; DIS3L2.
DR InterPro; IPR041093; Dis3l2_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR033771; Rrp44_CSD1.
DR Pfam; PF17877; Dis3l2_C_term; 1.
DR Pfam; PF17849; OB_Dis3; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF17216; Rrp44_CSD1; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 2.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Cytoplasm; Exonuclease; Hydrolase; Magnesium; Metal-binding; Mitosis;
KW Nuclease; Phosphoprotein; Reference proteome; RNA-binding;
KW Tumor suppressor.
FT CHAIN 1..870
FT /note="DIS3-like exonuclease 2"
FT /id="PRO_0000314818"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 381
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:25119025"
FT BINDING 390
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:25119025"
FT SITE 389
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:25119025"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB7"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB7"
FT MOD_RES 250
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB7"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 122
FT /note="K -> KPRITLSLPGVLGLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030379"
FT MUTAGEN 74
FT /note="R->A: Loss of enzyme activity and polyuridylated
FT RNA-binding; when associated with A-612."
FT /evidence="ECO:0000269|PubMed:25119025"
FT MUTAGEN 389
FT /note="D->N: Loss of exoribonuclease activity."
FT /evidence="ECO:0000269|PubMed:23594738"
FT MUTAGEN 548..553
FT /note="RLDQLK->AAAAAA: 40% decreased enzyme activity."
FT /evidence="ECO:0000269|PubMed:25119025"
FT MUTAGEN 612
FT /note="Q->A: Loss of enzyme activity and polyuridylated
FT RNA-binding; when associated with A-74."
FT /evidence="ECO:0000269|PubMed:25119025"
FT MUTAGEN 777
FT /note="N->A: 40% increased enzyme activity."
FT /evidence="ECO:0000269|PubMed:25119025"
FT MUTAGEN 778
FT /note="Q->A: Impaired enzyme activity and polyuridylated
FT RNA-binding."
FT /evidence="ECO:0000269|PubMed:25119025"
FT MUTAGEN 796
FT /note="N->A: Does not affect enzyme activity."
FT /evidence="ECO:0000269|PubMed:25119025"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:4PMW"
FT TURN 98..104
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 231..238
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 262..270
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 311..323
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 327..337
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 363..368
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 390..396
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 402..409
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 420..428
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 444..447
FT /evidence="ECO:0007829|PDB:4PMW"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 457..468
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 474..485
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 492..500
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 520..543
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 554..558
FT /evidence="ECO:0007829|PDB:4PMW"
FT TURN 560..562
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 565..570
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 575..598
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 604..608
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 613..624
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 635..641
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 650..662
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 671..674
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 681..684
FT /evidence="ECO:0007829|PDB:4PMW"
FT TURN 687..690
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 701..703
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 704..716
FT /evidence="ECO:0007829|PDB:4PMW"
FT HELIX 727..762
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 766..775
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 777..784
FT /evidence="ECO:0007829|PDB:4PMW"
FT TURN 785..787
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 790..794
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 800..806
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 809..811
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 813..818
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 821..825
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 829..833
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 837..844
FT /evidence="ECO:0007829|PDB:4PMW"
FT STRAND 851..854
FT /evidence="ECO:0007829|PDB:4PMW"
SQ SEQUENCE 870 AA; 97775 MW; E54474450DCD363F CRC64;
MNHPDYKLNL RSPGTPRGVS SVVGPSAVGA SPGDKKSKNK SMRGKKKSIF ETYMSKEDVS
EGLKRGTLIQ GVLRINPKKF HEAFIPSPDG DRDIFIDGVV ARNRALNGDL VVVKLLPEDQ
WKAVKPESND KEIEATYEAD IPEEGCGHHP LQQSRKGWSG PDVIIEAQFD DSDSEDRHGN
TSGLVDGVKK LSISTPDRGK EDSSTPVMKD ENTPIPQDTR GLSEKSLQKS AKVVYILEKK
HSRAATGILK LLADKNSDLF KKYALFSPSD HRVPRIYVPL KDCPQDFMTR PKDFANTLFI
CRIIDWKEDC NFALGQLAKS LGQAGEIEPE TEGILTEYGV DFSDFSSEVL ECLPQSLPWT
IPPDEVGKRR DLRKDCIFTI DPSTARDLDD ALACRRLTDG TFEVGVHIAD VSYFVPEGSS
LDKVAAERAT SVYLVQKVVP MLPRLLCEEL CSLNPMTDKL TFSVIWKLTP EGKILEEWFG
RTIIRSCTKL SYDHAQSMIE NPTEKIPEEE LPPISPEHSV EEVHQAVLNL HSIAKQLRRQ
RFVDGALRLD QLKLAFTLDH ETGLPQGCHI YEYRDSNKLV EEFMLLANMA VAHKIFRTFP
EQALLRRHPP PQTKMLSDLV EFCDQMGLPM DVSSAGALNK SLTKTFGDDK YSLARKEVLT
NMYSRPMQMA LYFCSGMLQD QEQFRHYALN VPLYTHFTSP IRRFADVIVH RLLAAALGYS
EQPDVEPDTL QKQADHCNDR RMASKRVQEL SIGLFFAVLV KESGPLESEA MVMGVLNQAF
DVLVLRFGVQ KRIYCNALAL RSYSFQKVGK KPELTLVWEP DDLEEEPTQQ VITIFSLVDV
VLQAEATALK YSAILKRPGL EKASDEEPED
