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ZN687_MOUSE
ID   ZN687_MOUSE             Reviewed;        1237 AA.
AC   Q9D2D7; Q6PAP3; Q6ZPQ9;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=Zinc finger protein 687;
GN   Name=Znf687; Synonyms=Kiaa1441, Zfp687;
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 1).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
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 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 219-1237 (ISOFORM 3).
RC   TISSUE=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-254; SER-433;
RP   SER-1184 AND SER-1191, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, Pancreas, 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   [6]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1061 AND ARG-1102, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N1G0}. Nucleus
CC       {ECO:0000250|UniProtKB:Q8N1G0}. Note=Predominantly nuclear.
CC       {ECO:0000250|UniProtKB:Q8N1G0}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9D2D7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D2D7-2; Sequence=VSP_018170, VSP_018173;
CC       Name=3;
CC         IsoId=Q9D2D7-3; Sequence=VSP_018171, VSP_018172;
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AK019851; BAB31881.1; -; mRNA.
DR   EMBL; BC056943; AAH56943.1; -; mRNA.
DR   EMBL; BC060179; AAH60179.1; -; mRNA.
DR   EMBL; AK129360; BAC98170.1; -; mRNA.
DR   CCDS; CCDS17600.1; -. [Q9D2D7-1]
DR   RefSeq; NP_084350.1; NM_030074.2. [Q9D2D7-1]
DR   RefSeq; XP_006502370.1; XM_006502307.3. [Q9D2D7-1]
DR   RefSeq; XP_006502371.1; XM_006502308.1.
DR   AlphaFoldDB; Q9D2D7; -.
DR   BioGRID; 219291; 4.
DR   IntAct; Q9D2D7; 1.
DR   MINT; Q9D2D7; -.
DR   STRING; 10090.ENSMUSP00000019482; -.
DR   iPTMnet; Q9D2D7; -.
DR   PhosphoSitePlus; Q9D2D7; -.
DR   EPD; Q9D2D7; -.
DR   jPOST; Q9D2D7; -.
DR   MaxQB; Q9D2D7; -.
DR   PaxDb; Q9D2D7; -.
DR   PeptideAtlas; Q9D2D7; -.
DR   PRIDE; Q9D2D7; -.
DR   ProteomicsDB; 299596; -. [Q9D2D7-1]
DR   ProteomicsDB; 299597; -. [Q9D2D7-2]
DR   ProteomicsDB; 299598; -. [Q9D2D7-3]
DR   Antibodypedia; 20323; 94 antibodies from 21 providers.
DR   DNASU; 78266; -.
DR   Ensembl; ENSMUST00000019482; ENSMUSP00000019482; ENSMUSG00000019338. [Q9D2D7-1]
DR   Ensembl; ENSMUST00000137799; ENSMUSP00000123335; ENSMUSG00000019338. [Q9D2D7-2]
DR   GeneID; 78266; -.
DR   KEGG; mmu:78266; -.
DR   UCSC; uc008qhp.1; mouse. [Q9D2D7-1]
DR   CTD; 78266; -.
DR   MGI; MGI:1925516; Zfp687.
DR   VEuPathDB; HostDB:ENSMUSG00000019338; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000156524; -.
DR   HOGENOM; CLU_006283_1_0_1; -.
DR   InParanoid; Q9D2D7; -.
DR   OMA; TSWPGSD; -.
DR   OrthoDB; 180681at2759; -.
DR   PhylomeDB; Q9D2D7; -.
DR   TreeFam; TF329009; -.
DR   BioGRID-ORCS; 78266; 7 hits in 70 CRISPR screens.
DR   ChiTaRS; Zfp687; mouse.
DR   PRO; PR:Q9D2D7; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9D2D7; protein.
DR   Bgee; ENSMUSG00000019338; Expressed in dorsal pancreas and 227 other tissues.
DR   ExpressionAtlas; Q9D2D7; baseline and differential.
DR   Genevisible; Q9D2D7; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR045914; Zn532-like.
DR   InterPro; IPR041697; Znf-C2H2_11.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR47222; PTHR47222; 1.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   Pfam; PF16622; zf-C2H2_11; 1.
DR   SMART; SM00355; ZnF_C2H2; 14.
DR   SUPFAM; SSF57667; SSF57667; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; DNA-binding; Isopeptide bond;
KW   Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1237
FT                   /note="Zinc finger protein 687"
FT                   /id="PRO_0000234006"
FT   ZN_FING         533..552
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         705..727
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         764..787
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         792..815
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         827..849
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         858..881
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         964..987
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         994..1017
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1135..1158
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1200..1222
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1052..1117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1166..1195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..200
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        917..932
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        935..950
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         104
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         142
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   MOD_RES         228
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   MOD_RES         243
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   MOD_RES         252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   MOD_RES         254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         266
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   MOD_RES         271
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   MOD_RES         374
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   MOD_RES         377
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   MOD_RES         433
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         495
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   MOD_RES         901
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   MOD_RES         1058
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   MOD_RES         1061
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         1083
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   MOD_RES         1084
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   MOD_RES         1086
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   MOD_RES         1102
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         1107
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   MOD_RES         1184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   CROSSLNK        286
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   CROSSLNK        336
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   CROSSLNK        372
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   CROSSLNK        384
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   CROSSLNK        397
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   CROSSLNK        422
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   CROSSLNK        435
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   CROSSLNK        439
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   CROSSLNK        451
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   CROSSLNK        464
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   CROSSLNK        955
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   CROSSLNK        1044
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G0"
FT   VAR_SEQ         766..786
FT                   /note="CPSCAVVFGGVNSIKSHIQAS -> TLTSLDVWGKRQLGKGLEVPF (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_018170"
FT   VAR_SEQ         767..775
FT                   /note="PSCAVVFGG -> LMLNSSLEL (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14621295"
FT                   /id="VSP_018171"
FT   VAR_SEQ         776..1237
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14621295"
FT                   /id="VSP_018172"
FT   VAR_SEQ         787..1237
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_018173"
SQ   SEQUENCE   1237 AA;  130350 MW;  61016AFB31FE90D0 CRC64;
     MGDMKTPDFD DLLAAFDIPD IDANEAIHSG PEENEGPGGQ GKPEPSVGGD SKDREEAAAA
     ENDPESPAEA SDHGLPQPPD TSTVSVIVKN TVCPEQSESL TGDSGEEETK AGGITKEGPV
     GSCLMQNGFG GPEPSLSENP HSSAHASGNA WKDKAVEGKT CLDLFAHFGS EPGDHPDPLP
     PEPSQPRGGD MAPPPFSTPF ELAPENGSTL LPPASLLPQG ALKQESCSPH HSQGLTQRGP
     GSSPETAGIP ASVSPPQVAG VSFKQSPGHQ SPPASPVKAP SCKPLKEEDE GTVDKSPPRS
     PQSPSSGAEA ADEDSNDSPT SSSSSRPLKV RIKTIKTSCG NITRTVTRVP SEPDPPAPLA
     EGAFLAETSF LKLSPVTPTP EGPKVVSVQL GDGTRLKGTV LPVATIQNAS TAMLMAASVA
     RKAVVLPGGN ATSPKTMTKS VLGLVPQTLP KAEVRTGFSL GGQKVNGASV VMVQPSKSAT
     GPGTAGGSVI SRTQSSLVEA FNKILNSKNL LPAYRPNLSP PAEAGLALPP TGYRCLECGD
     AFSLEKSLAR HYDRRSMRIE VTCNHCARRL VFFNKCSLLL HAREHKDKGL VMQCSHLVMR
     PVALDQMVGQ PDITPLLPVA VPPVPGPLAL PVLGKGEGAV TSSTITTVAT EAPVLPLPTE
     PPAPPTASVY TCFRCLECKE QCRDKAGMAA HFQQLGPPAL GSTSNVCPSC PMMLPNRCSF
     SAHQRTHKNR APHVCPECGG NFLQANFQTH LREACLHFSR RVGYRCPSCA VVFGGVNSIK
     SHIQASHCEV FHKCPICPMA FKSAPSAHAH LYSQHPSFLT QQAKLIYKCA MCDTVFTHKP
     LLSSHFDQHL LPQRVSVFKC PSCPLLFAQK RTMLEHLKNT HQSGRVGEEA VGKGAGGALL
     TPKTEPEELA VSQAEAAPAT EESSSSSEEE LPSSPEPPRP TKRARRGELG NKGIKGGGGG
     PGGWTCGLCH SWCPERDEYV THMKKEHGKS VKKFPCRLCE RSFCSAPSLR RHVRVNHEGI
     KRVYPCRYCT EGKRTFSSRL ILEKHVQVRH GLPLGTQSSG RGGSLARGSG GRAQGPGRKR
     RQSSDSCSEE PDSTTPPAKS LRGGPGSGGH GPLRYRSSGS AEQSLVGLRV DGGTQQCLDC
     GLCFASPGSL SRHRFISHKK RRAGGKASVL GLGDGEEAAP PLRSDPEGGD SPLPAPGDPL
     TCKVCGKSCD SPLNLKTHFR THGMAFIRAR QGGSGDN
 
 
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