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 24-JAN-2024, entry version 172.
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 -!- SUBUNIT: Interacts with ZMYND8. {ECO:0000250|UniProtKB:Q8N1G0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N1G0}. Nucleus
CC {ECO:0000250|UniProtKB:Q8N1G0}. Note=Predominantly nuclear. Localizes
CC to sites of DNA damage. {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; 5.
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; 10090-ENSMUSP00000019482; -.
DR PeptideAtlas; Q9D2D7; -.
DR ProteomicsDB; 299596; -. [Q9D2D7-1]
DR ProteomicsDB; 299597; -. [Q9D2D7-2]
DR ProteomicsDB; 299598; -. [Q9D2D7-3]
DR Pumba; Q9D2D7; -.
DR Antibodypedia; 20323; 111 antibodies from 21 providers.
DR DNASU; 78266; -.
DR Ensembl; ENSMUST00000019482.8; ENSMUSP00000019482.2; ENSMUSG00000019338.14. [Q9D2D7-1]
DR Ensembl; ENSMUST00000137799.2; ENSMUSP00000123335.2; ENSMUSG00000019338.14. [Q9D2D7-2]
DR GeneID; 78266; -.
DR KEGG; mmu:78266; -.
DR UCSC; uc008qhp.1; mouse. [Q9D2D7-1]
DR AGR; MGI:1925516; -.
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; NGAPWSL; -.
DR OrthoDB; 5400362at2759; -.
DR PhylomeDB; Q9D2D7; -.
DR TreeFam; TF329009; -.
DR BioGRID-ORCS; 78266; 7 hits in 76 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 230 other cell types or 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 Gene3D; 3.30.160.60; Classic Zinc Finger; 5.
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; ZINC FINGER PROTEIN 532-RELATED; 1.
DR PANTHER; PTHR47222:SF2; ZINC FINGER PROTEIN 687; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR Pfam; PF16622; zf-C2H2_11; 1.
DR SMART; SM00355; ZnF_C2H2; 14.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 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
//
