ID ZN638_MOUSE Reviewed; 1960 AA.
AC Q61464; Q6DFV9; Q8C941;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 10-MAY-2017, entry version 133.
DE RecName: Full=Zinc finger protein 638 {ECO:0000312|MGI:MGI:1203484};
DE AltName: Full=Nuclear protein 220 {ECO:0000303|PubMed:8670298};
DE AltName: Full=Zinc finger matrin-like protein {ECO:0000250|UniProtKB:Q14966};
GN Name=Znf638 {ECO:0000250|UniProtKB:Q14966};
GN Synonyms=Np220 {ECO:0000312|MGI:MGI:1203484},
GN Zfml {ECO:0000312|MGI:MGI:1203484},
GN Zfp638 {ECO:0000312|MGI:MGI:1203484};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 6).
RC TISSUE=Heart;
RX PubMed=8670298; DOI=10.1006/bbrc.1996.0910;
RA Matsushima Y., Ohshima M., Sonoda M., Kitagawa Y.;
RT "A family of novel DNA-binding nuclear proteins having polypyrimidine
RT tract-binding motif and arginine/serine-rich motif.";
RL Biochem. Biophys. Res. Commun. 223:427-433(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA 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 STRAIN=C57BL/6J; TISSUE=Head;
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 PROTEIN SEQUENCE OF 761-768; 873-891; 1395-1404; 1506-1513 AND
RP 1874-1881, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128 AND SER-1635, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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
RT expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, INTERACTION WITH CEBPA; CEBPD AND CEBPG, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=21602272; DOI=10.1074/jbc.M110.212506;
RA Meruvu S., Hugendubler L., Mueller E.;
RT "Regulation of adipocyte differentiation by the zinc finger protein
RT ZNF638.";
RL J. Biol. Chem. 286:26516-26523(2011).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=25024404; DOI=10.1194/jlr.M047555;
RA Du C., Ma X., Meruvu S., Hugendubler L., Mueller E.;
RT "The adipogenic transcriptional cofactor ZNF638 interacts with
RT splicing regulators and influences alternative splicing.";
RL J. Lipid Res. 55:1886-1896(2014).
CC -!- FUNCTION: Early regulator of adipogenesis that works as a
CC transcription cofactor of CEBPs, controlling the expression of
CC PPARG and probably of other proadipogenic genes, such as SREBF1
CC (PubMed:21602272). Binds to cytidine clusters in double-stranded
CC DNA (By similarity). May also regulate alternative splicing of
CC target genes during adipogenesis (PubMed:25024404).
CC {ECO:0000250|UniProtKB:Q14966, ECO:0000269|PubMed:21602272,
CC ECO:0000269|PubMed:25024404}.
CC -!- SUBUNIT: Interacts with FHL2 (By similarity). Interacts with
CC CEBPA, CEBPD and CEBPG. {ECO:0000250|UniProtKB:Q14966,
CC ECO:0000269|PubMed:21602272}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000255|PROSITE-
CC ProRule:PRU00130, ECO:0000269|PubMed:21602272,
CC ECO:0000269|PubMed:25024404}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q61464-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61464-2; Sequence=VSP_014809, VSP_014812, VSP_014813,
CC VSP_014814;
CC Note=No experimental confirmation available.;
CC Name=3;
CC IsoId=Q61464-3; Sequence=VSP_014807, VSP_014808;
CC Note=Due to intron retention. No experimental confirmation
CC available.;
CC Name=4; Synonyms=Beta;
CC IsoId=Q61464-4; Sequence=VSP_014814;
CC Name=5; Synonyms=Gamma;
CC IsoId=Q61464-5; Sequence=VSP_014811;
CC Name=6; Synonyms=Delta;
CC IsoId=Q61464-7; Sequence=VSP_014810;
CC -!- DEVELOPMENTAL STAGE: In an vitro adipocyte differentiation system,
CC induced at the protein and RNA levels shortly after exposure to
CC the induction mixture. Levels peak before PPARG induction and
CC rapidly decrease during later stages of differentiation.
CC {ECO:0000269|PubMed:21602272}.
CC -!- DOMAIN: The matrin-type zinc finger domain is required for
CC localization to nuclear speckles. {ECO:0000269|PubMed:25024404}.
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DR EMBL; D83033; BAA11749.1; -; mRNA.
DR EMBL; AK043029; BAC31439.1; -; mRNA.
DR EMBL; BC076615; AAH76615.1; -; mRNA.
DR CCDS; CCDS20288.1; -. [Q61464-4]
DR CCDS; CCDS51823.1; -. [Q61464-2]
DR PIR; JC4842; JC4842.
DR RefSeq; NP_001159843.1; NM_001166371.1. [Q61464-2]
DR RefSeq; NP_032743.2; NM_008717.3.
DR UniGene; Mm.132392; -.
DR ProteinModelPortal; Q61464; -.
DR SMR; Q61464; -.
DR BioGrid; 201815; 2.
DR IntAct; Q61464; 1.
DR MINT; MINT-4109575; -.
DR STRING; 10090.ENSMUSP00000032088; -.
DR iPTMnet; Q61464; -.
DR PhosphoSitePlus; Q61464; -.
DR EPD; Q61464; -.
DR PaxDb; Q61464; -.
DR PeptideAtlas; Q61464; -.
DR PRIDE; Q61464; -.
DR Ensembl; ENSMUST00000113835; ENSMUSP00000109466; ENSMUSG00000030016. [Q61464-2]
DR GeneID; 18139; -.
DR KEGG; mmu:18139; -.
DR UCSC; uc009coo.2; mouse. [Q61464-3]
DR UCSC; uc009coq.2; mouse. [Q61464-2]
DR CTD; 18139; -.
DR MGI; MGI:1203484; Zfp638.
DR eggNOG; ENOG410IN3N; Eukaryota.
DR eggNOG; ENOG4111GCE; LUCA.
DR GeneTree; ENSGT00850000132416; -.
DR HOGENOM; HOG000082488; -.
DR HOVERGEN; HBG094186; -.
DR InParanoid; Q61464; -.
DR PhylomeDB; Q61464; -.
DR Reactome; R-MMU-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-MMU-442533; Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
DR PRO; PR:Q61464; -.
DR Proteomes; UP000000589; Chromosome 6.
DR Bgee; ENSMUSG00000030016; -.
DR CleanEx; MM_ZFML; -.
DR ExpressionAtlas; Q61464; baseline and differential.
DR Genevisible; Q61464; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR033096; ZNF638.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15592:SF11; PTHR15592:SF11; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF54928; SSF54928; 3.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Complete proteome;
KW Direct protein sequencing; DNA-binding; Metal-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1 1960 Zinc finger protein 638.
FT /FTId=PRO_0000082012.
FT DOMAIN 676 751 RRM 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00176}.
FT DOMAIN 902 976 RRM 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00176}.
FT ZN_FING 1876 1906 Matrin-type. {ECO:0000255|PROSITE-
FT ProRule:PRU00130}.
FT REGION 470 573 Involved in localization to nuclear
FT speckles. {ECO:0000269|PubMed:25024404}.
FT COMPBIAS 470 575 Arg-rich.
FT COMPBIAS 1577 1582 Poly-Lys.
FT MOD_RES 47 47 Asymmetric dimethylarginine.
FT {ECO:0000250|UniProtKB:Q14966}.
FT MOD_RES 49 49 Asymmetric dimethylarginine.
FT {ECO:0000250|UniProtKB:Q14966}.
FT MOD_RES 54 54 Asymmetric dimethylarginine.
FT {ECO:0000250|UniProtKB:Q14966}.
FT MOD_RES 128 128 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 288 288 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q14966}.
FT MOD_RES 298 298 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q14966}.
FT MOD_RES 367 367 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q14966}.
FT MOD_RES 381 381 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q14966}.
FT MOD_RES 418 418 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q14966}.
FT MOD_RES 554 554 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q14966}.
FT MOD_RES 606 606 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q14966}.
FT MOD_RES 615 615 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q14966}.
FT MOD_RES 637 637 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q14966}.
FT MOD_RES 1099 1099 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q14966}.
FT MOD_RES 1400 1400 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q14966}.
FT MOD_RES 1635 1635 Phosphoserine.
FT {ECO:0000244|PubMed:21183079}.
FT MOD_RES 1661 1661 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q14966}.
FT MOD_RES 1864 1864 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q14966}.
FT VAR_SEQ 438 454 DWIQHQNTSTHIESCRQ -> VSVFKRLLYNDAQCPGF
FT (in isoform 3).
FT {ECO:0000303|PubMed:16141072}.
FT /FTId=VSP_014807.
FT VAR_SEQ 456 1960 Missing (in isoform 3).
FT {ECO:0000303|PubMed:16141072}.
FT /FTId=VSP_014808.
FT VAR_SEQ 810 832 Missing (in isoform 2).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_014809.
FT VAR_SEQ 1147 1866 Missing (in isoform 6).
FT {ECO:0000303|PubMed:8670298}.
FT /FTId=VSP_014810.
FT VAR_SEQ 1147 1832 Missing (in isoform 5).
FT {ECO:0000303|PubMed:8670298}.
FT /FTId=VSP_014811.
FT VAR_SEQ 1147 1200 KEEPKQALCESDFAIQTLELEAQGAEVSIEIPLVASTPANI
FT ELFSENIDESALN -> PGSETVTQKDLKTMPERHLAAKTP
FT MKRVRIGKSSPSQKVAEPTKGEEAFQMSEG (in
FT isoform 2).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_014812.
FT VAR_SEQ 1201 1832 Missing (in isoform 2).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_014813.
FT VAR_SEQ 1833 1866 Missing (in isoform 2 and isoform 4).
FT {ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8670298}.
FT /FTId=VSP_014814.
FT CONFLICT 32 32 V -> L (in Ref. 3; AAH76615).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 677 747 ismart:RRM [T]
FT MYHIT 1910 1940 iprf:ZF_MATRIN [T]
FT MYHIT 1910 1934 ismart:ZnF_C2H2 [T]
FT MYHIT 1907 1941 ismart:ZnF_U1 [T]
FT MYHIT 421 455 ismart:ZnF_U1 [T]
FT MYHIT 424 448 ismart:ZnF_C2H2 [T]
FT MYHIT 903 972 ismart:RRM [T]
FT MYHIT 676 746 iprf:RRM [T]
FT MYHIT 1912 1934 ipat:ZINC_FINGER_C2H2_1 [T]
SQ SEQUENCE 1960 AA; 218134 MW; 27DF6740BFE410ED CRC64;
MSRPRFNPRG TFPLQRPRAP NPPGMRPPGP FVRPGSMGLP RFYPAGRARG IPHRFPGHGS
YQNMGPQRMN VQVTQHRTDP RLTKEKLDFP EAQQKKGKPH GSRWDDESHI TPPVEVKQSS
VTQVTEQSPK VQSRYTKESA SSILASFGLS NEDLEELSRY PDEQLTPENM PLILRDIRMR
KMSRRLPNLP SHSRNKETLS NETVSSNVID YGHASKYGYT EDPLEVRIYD PEIPTDEVKN
EFQPQQSISA TVSTPNVICN SVFPGGDMFR QMDFPGESSS QSFFPVESGT KMSGLHISGQ
SVLEPVKSIS QSISQTVSQT TSQSLNPPSM NQVPFTFELD AVLRQQERIS QKSVISSADA
HGGPTESKKD YQSEADLPIR SPFGIVKASW LPKFTQAGAQ KMKRLPTPSM MNDYYAASPR
IFPHLCSLCN VECSHLKDWI QHQNTSTHIE SCRQLRQQYP DWNPEILPSR RNESNRKENE
TPRRRSHSPS PRHSRRSSSG HRIRRSRSPV RYIYRPRSRS PRICHRFISK YRSRSRSRSR
SRSPYRSRNL LRRSPKSYRS ASPERTSRKS VRSDRKKALE DGGQRSVHGT EVTKQKHTET
VDKGLSPAQK PKLASGTKPS AKSLSSVKSD SHLGAYSAHK SENLEDDTLP EGKQESGKSA
LAQRKPQKDQ SLSSNSILLV SELPEDGFTE EDIRKAFLPF GKISDVLLVP CRNEAYLEME
LRKAVTSIMK YIETMPLVIK GKSVKVCVPG KKKPQNKEMK KKPSDIKKSS ASALKKETDA
SKTMETVSSS SSAKSGQIKS STVKVNKCAG KSAGSVKSVV TVAAKGKASI KTAKSGKKSL
EAKKSGNIKN KDSNKPVTVP ANSEIKASSE DKATGKSAEE SPSGTLEATE KEPVNKESEE
MSVVFISNLP NKGYSTEEIY NLAKPFGALK DILVLSSHKK AYIEINKKSA DSMVKFYTCF
PISMDGNQLS ISMAPEHVDL KDEEALFTTL IQENDPEANI DKIYNRFVHL DNLPEDGLQC
VLCVGHQFGK VDRYMFMSNK NKVILQLESP ESALSMYNFL KQNPQNIGEH VLTCTLSPKT
DSEVQRKNDL ELGKGSTFSP DLKNSPVDES EVQTAADSSS VKPSEVEEET TSNIGTETSV
HQEELGKEEP KQALCESDFA IQTLELEAQG AEVSIEIPLV ASTPANIELF SENIDESALN
QQMYTSDFEK EEAEVTNPET ELAVSDSVFI EERNIKGIIE DSPSETEDIF SGIVQPMVDA
IAEVDKHETV SEVLPSACNV TQAPGSYIED EKVVSKKDIA EKVILDEKEE DEFNVKETRM
DLQVKTEKAE KNEAIIFKEK LEKIIAAIRE KPIESSVIKA DPTKGLDQTS KPDETGKSSV
LTVSNVYSSK SSIKATVVSS PKAKSTPSKT ESHSTFPKPV LREQIKADKK VSAKEFGLLK
NTRSGLAESN SKSKPTQIGV NRGCSGRISA LQCKDSKVDY KDITKQSQET ETKPPIMKRD
DSNNKALALQ NTKNSKSTTD RSSKSKEEPL FTFNLDEFVT VDEVIEEVNP SQAKQNPLKG
KRKEALKISP SPELNLKKKK GKTSVPHSVE GELSFVTLDE IGEEEDATVQ ALVTVDEVID
EEELNMEEMV KNSNSLLTLD ELIDQDDCIP HSGPKDVTVL SMAEEQDLQQ ERLVTVDEIG
EVEESADITF ATLNAKRDKR DSIGFISSQM PEDPSTLVTV DEIQDDSSDF HLMTLDEVTE
EDENSLADFN NLKEELNFVT VDEVGDEEDG DNDSKVELAR GKIEHHTDKK GNRKRRAVDP
KKSKLDSFSQ VGPGSETVTQ KDLKTMPERH LAAKTPMKRV RLGKSSPSQK VAEPTKGEEA
FQMSEGVDDA ELKDSEPDEK RRKTQDSSVG KSMTSDVPGD LDFLVPKAGF FCPICSLFYS
GEKAMANHCK STRHKQNTEK FMAKQRKEKE QNETEERSSR
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