Entry sw:ZN830_HUMAN

ID   ZN830_HUMAN             Reviewed;         372 AA.
AC   Q96NB3; Q96F60; Q96GZ5; Q9BU38;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   30-NOV-2016, entry version 125.
DE   RecName: Full=Zinc finger protein 830 {ECO:0000312|HGNC:HGNC:28291};
DE   AltName: Full=Coiled-coil domain-containing protein 16 {ECO:0000305};
GN   Name=ZNF830 {ECO:0000312|HGNC:HGNC:28291};
GN   Synonyms=CCDC16 {ECO:0000312|HGNC:HGNC:28291};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-99.
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-372, AND VARIANTS GLN-99
RP   AND THR-154.
RC   TISSUE=Colon, and Skin;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351 AND SER-362, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [6]
RP   IDENTIFICATION AS PART OF THE XAB2 COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=17981804; DOI=10.1074/jbc.M706647200;
RA   Kuraoka I., Ito S., Wada T., Hayashida M., Lee L., Saijo M.,
RA   Nakatsu Y., Matsumoto M., Matsunaga T., Handa H., Qin J., Nakatani Y.,
RA   Tanaka K.;
RT   "Isolation of XAB2 complex involved in pre-mRNA splicing,
RT   transcription, and transcription-coupled repair.";
RL   J. Biol. Chem. 283:940-950(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND SER-351, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [14]
RP   VARIANT [LARGE SCALE ANALYSIS] GLN-99, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: Acts as an important regulator of the cell cycle that
CC       participates in the maintenance of genome integrity. During cell
CC       cycle progression in embryonic fibroblast, prevents replication
CC       fork collapse, double-strand break formation and cell cycle
CC       checkpoint activation. Controls mitotic cell cycle progression and
CC       cell survival in rapidly proliferating intestinal epithelium and
CC       embryonic stem cells. During the embryo preimplantation, controls
CC       different aspects of M phase. During early oocyte growth, plays a
CC       role in oocyte survival by preventing chromosomal breaks
CC       formation, activation of TP63 and reduction of transcription.
CC       {ECO:0000250|UniProtKB:Q8R1N0}.
CC   -!- SUBUNIT: Component of the XAB2 complex, a multimeric protein
CC       complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE;
CC       this complex binds preferentially to RNA. Interacts with XAB2.
CC       {ECO:0000269|PubMed:17981804}.
CC   -!- INTERACTION:
CC       O60306:AQR; NbExp=2; IntAct=EBI-3920997, EBI-2512328;
CC       Q13123:IK; NbExp=2; IntAct=EBI-3920997, EBI-713456;
CC       Q15365:PCBP1; NbExp=2; IntAct=EBI-3920997, EBI-946095;
CC       Q13356:PPIL2; NbExp=2; IntAct=EBI-3920997, EBI-7705988;
CC       Q6P2Q9:PRPF8; NbExp=2; IntAct=EBI-3920997, EBI-538479;
CC       Q13435:SF3B2; NbExp=2; IntAct=EBI-3920997, EBI-749111;
CC       Q13573:SNW1; NbExp=2; IntAct=EBI-3920997, EBI-632715;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8R1N0}.
CC       Chromosome {ECO:0000250|UniProtKB:Q8R1N0}. Nucleus speckle
CC       {ECO:0000250|UniProtKB:Q8R1N0}. Note=Excluded from nucleolus.
CC       {ECO:0000250|UniProtKB:Q8R1N0}.
CC   -!- PTM: Phosphorylated in response to DNA damage by the cell cycle
CC       checkpoint kinases ATR/ATM. {ECO:0000250|UniProtKB:Q8R1N0}.
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger. {ECO:0000305}.
DR   EMBL; AK055707; BAB70992.1; -; mRNA.
DR   EMBL; AC022903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002913; AAH02913.2; -; mRNA.
DR   EMBL; BC009044; AAH09044.1; -; mRNA.
DR   EMBL; BC011584; AAH11584.2; -; mRNA.
DR   CCDS; CCDS32618.1; -.
DR   RefSeq; NP_443089.3; NM_052857.3.
DR   UniGene; Hs.413678; -.
DR   ProteinModelPortal; Q96NB3; -.
DR   SMR; Q96NB3; -.
DR   BioGrid; 124850; 23.
DR   DIP; DIP-61544N; -.
DR   IntAct; Q96NB3; 14.
DR   STRING; 9606.ENSP00000354518; -.
DR   iPTMnet; Q96NB3; -.
DR   PhosphoSitePlus; Q96NB3; -.
DR   BioMuta; ZNF830; -.
DR   DMDM; 313104066; -.
DR   EPD; Q96NB3; -.
DR   MaxQB; Q96NB3; -.
DR   PaxDb; Q96NB3; -.
DR   PeptideAtlas; Q96NB3; -.
DR   PRIDE; Q96NB3; -.
DR   DNASU; 91603; -.
DR   Ensembl; ENST00000361952; ENSP00000354518; ENSG00000198783.
DR   GeneID; 91603; -.
DR   KEGG; hsa:91603; -.
DR   UCSC; uc002hih.5; human.
DR   CTD; 91603; -.
DR   GeneCards; ZNF830; -.
DR   HGNC; HGNC:28291; ZNF830.
DR   HPA; HPA024754; -.
DR   HPA; HPA027211; -.
DR   neXtProt; NX_Q96NB3; -.
DR   OpenTargets; ENSG00000198783; -.
DR   PharmGKB; PA162410767; -.
DR   eggNOG; KOG3032; Eukaryota.
DR   eggNOG; ENOG4111GTR; LUCA.
DR   GeneTree; ENSGT00390000012151; -.
DR   HOGENOM; HOG000246999; -.
DR   HOVERGEN; HBG105347; -.
DR   InParanoid; Q96NB3; -.
DR   KO; K13104; -.
DR   OMA; VLGKQHR; -.
DR   OrthoDB; EOG091G0MBX; -.
DR   PhylomeDB; Q96NB3; -.
DR   TreeFam; TF315895; -.
DR   BioCyc; ZFISH:G66-33507-MONOMER; -.
DR   Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR   Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR   Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   GenomeRNAi; 91603; -.
DR   PRO; PR:Q96NB3; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000198783; -.
DR   CleanEx; HS_ZNF830; -.
DR   ExpressionAtlas; Q96NB3; baseline and differential.
DR   Genevisible; Q96NB3; HS.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0001832; P:blastocyst growth; IEA:Ensembl.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051276; P:chromosome organization; IEA:Ensembl.
DR   GO; GO:0060729; P:intestinal epithelial structure maintenance; IEA:Ensembl.
DR   GO; GO:0044773; P:mitotic DNA damage checkpoint; IEA:Ensembl.
DR   GO; GO:0033314; P:mitotic DNA replication checkpoint; ISS:UniProtKB.
DR   GO; GO:0007067; P:mitotic nuclear division; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0033260; P:nuclear DNA replication; IEA:Ensembl.
DR   GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR   GO; GO:0001546; P:preantral ovarian follicle growth; ISS:UniProtKB.
DR   GO; GO:0048478; P:replication fork protection; ISS:UniProtKB.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
DR   InterPro; IPR003604; Znf_U1.
DR   SMART; SM00451; ZnF_U1; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; Cell division; Chromosome; Coiled coil;
KW   Complete proteome; Developmental protein; Metal-binding; Mitosis;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Zinc;
KW   Zinc-finger.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:19413330}.
FT   CHAIN         2    372       Zinc finger protein 830.
FT                                /FTId=PRO_0000076193.
FT   ZN_FING      53     75       C2H2-type.
FT   COILED      312    349       {ECO:0000255}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|PubMed:19413330}.
FT   MOD_RES     225    225       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     351    351       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:17525332,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     362    362       Phosphoserine.
FT                                {ECO:0000244|PubMed:17525332}.
FT   VARIANT      16     16       I -> V (in dbSNP:rs8073825).
FT                                /FTId=VAR_030940.
FT   VARIANT      93     93       S -> P (in dbSNP:rs8078059).
FT                                /FTId=VAR_030941.
FT   VARIANT      99     99       H -> Q (in dbSNP:rs931196).
FT                                {ECO:0000244|PubMed:21269460,
FT                                ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_024059.
FT   VARIANT     135    135       F -> L (in dbSNP:rs8078217).
FT                                /FTId=VAR_030942.
FT   VARIANT     154    154       S -> T (in dbSNP:rs3744355).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_024060.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        48     82       ismart:ZnF_U1 [T]
SQ   SEQUENCE   372 AA;  41999 MW;  A06403B117672C8C CRC64;
     MASSASARTP AGKRVINQEE LRRLMKEKQR LSTSRKRIES PFAKYNRLGQ LSCALCNTPV
     KSELLWQTHV LGKQHREKVA ELKGAKEASQ GSSASSAPHS VKRKAPDADD QDVKRAKATL
     VPQVQPSTSA WTTNFDKIGK EFIRATPSKP SGLSLLPDYE DEEEEEEEEE GDGERKRGDA
     SKPLSDAQGK EHSVSSSREV TSSVLPNDFF STNPPKAPII PHSGSIEKAE IHEKVVERRE
     NTAEALPEGF FDDPEVDARV RKVDAPKDQM DKEWDEFQKA MRQVNTISEA IVAEEDEEGR
     LDRQIGEIDE QIECYRRVEK LRNRQDEIKN KLKEILTIKE LQKKEEENAD SDDEGELQDL
     LSQDWRVKGA LL
//