ID   POGZ_MOUSE              Reviewed;        1409 AA.
AC   Q8BZH4; Q4VA94; Q80TZ8; Q8C0K1; Q8K294;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 2.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Pogo transposable element with ZNF domain;
GN   Name=Pogz; Synonyms=Kiaa0461;
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].
RC   STRAIN=C57BL/6J; TISSUE=Thymus, and Urinary bladder;
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].
RC   STRAIN=C3H/He; TISSUE=Mammary tumor, and Mesenchymal stem cell;
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 557-1409.
RC   TISSUE=Brain;
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=Brain, Kidney, Lung, and Spleen;
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).
CC   -!- FUNCTION: Plays a role in mitotic cell cycle progression and is
CC       involved in kinetochore assembly and mitotic sister chromatid cohesion.
CC       Probably through its association with CBX5 plays a role in mitotic
CC       chromosome segregation by regulating aurora kinase B/AURKB activation
CC       and AURKB and CBX5 dissociation from chromosome arms (By similarity).
CC       Promotes the repair of DNA double-strand breaks through the homologous
CC       recombination pathway (By similarity). {ECO:0000250|UniProtKB:Q7Z3K3}.
CC   -!- SUBUNIT: Interacts with CBX1, CBX3, MAD2L2 and CHAMP1. Interacts with
CC       CBX5; POGZ competes with PXVXL motif-containing proteins such as INCENP
CC       and TRIM28 for interaction with CBX5 (By similarity). Interacts (via
CC       IBM motif) with PSIP1 (via IBD domain); phosphorylation increases its
CC       affinity for PSIP1 (By similarity). Interacts with HDGFL2 (By
CC       similarity). {ECO:0000250|UniProtKB:Q7Z3K3}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00583}.
CC       Chromosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Recruited to
CC       trimethylated 'Lys-9' of histone H3 (H3K9me3). {ECO:0000250}.
CC   -!- PTM: Phosphorylation increases its interaction with PSIP1.
CC       {ECO:0000250|UniProtKB:Q7Z3K3}.
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DR   EMBL; AK030880; BAC27169.1; -; mRNA.
DR   EMBL; AK035255; BAC29003.1; -; mRNA.
DR   EMBL; BC032176; AAH32176.1; -; mRNA.
DR   EMBL; BC096492; AAH96492.1; -; mRNA.
DR   EMBL; AK122288; BAC65570.1; -; mRNA.
DR   CCDS; CCDS17596.1; -.
DR   RefSeq; NP_766271.2; NM_172683.3.
DR   RefSeq; XP_011238392.1; XM_011240090.2.
DR   AlphaFoldDB; Q8BZH4; -.
DR   BMRB; Q8BZH4; -.
DR   BioGRID; 230865; 10.
DR   IntAct; Q8BZH4; 1.
DR   STRING; 10090.ENSMUSP00000102891; -.
DR   GlyGen; Q8BZH4; 12 sites, 1 O-linked glycan (12 sites).
DR   iPTMnet; Q8BZH4; -.
DR   PhosphoSitePlus; Q8BZH4; -.
DR   EPD; Q8BZH4; -.
DR   jPOST; Q8BZH4; -.
DR   MaxQB; Q8BZH4; -.
DR   PaxDb; 10090-ENSMUSP00000102891; -.
DR   ProteomicsDB; 289360; -.
DR   Pumba; Q8BZH4; -.
DR   Antibodypedia; 1872; 175 antibodies from 28 providers.
DR   DNASU; 229584; -.
DR   Ensembl; ENSMUST00000107270.9; ENSMUSP00000102891.3; ENSMUSG00000038902.16.
DR   GeneID; 229584; -.
DR   KEGG; mmu:229584; -.
DR   UCSC; uc008qhc.2; mouse.
DR   AGR; MGI:2442117; -.
DR   CTD; 23126; -.
DR   MGI; MGI:2442117; Pogz.
DR   VEuPathDB; HostDB:ENSMUSG00000038902; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; KOG3105; Eukaryota.
DR   GeneTree; ENSGT00940000160649; -.
DR   InParanoid; Q8BZH4; -.
DR   OMA; KSMKNTC; -.
DR   OrthoDB; 2883180at2759; -.
DR   PhylomeDB; Q8BZH4; -.
DR   TreeFam; TF331707; -.
DR   BioGRID-ORCS; 229584; 4 hits in 76 CRISPR screens.
DR   ChiTaRS; Pogz; mouse.
DR   PRO; PR:Q8BZH4; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q8BZH4; Protein.
DR   Bgee; ENSMUSG00000038902; Expressed in embryonic post-anal tail and 232 other cell types or tissues.
DR   ExpressionAtlas; Q8BZH4; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0051382; P:kinetochore assembly; ISS:UniProtKB.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 2.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   InterPro; IPR004875; DDE_SF_endonuclease_dom.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR006600; HTH_CenpB_DNA-bd_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24403:SF59; POGO TRANSPOSABLE ELEMENT WITH ZNF DOMAIN; 1.
DR   PANTHER; PTHR24403; ZINC FINGER PROTEIN; 1.
DR   Pfam; PF03184; DDE_1; 1.
DR   Pfam; PF03221; HTH_Tnp_Tc5; 1.
DR   SMART; SM00674; CENPB; 1.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS51253; HTH_CENPB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
DR   Genevisible; Q8BZH4; MM.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Chromosome; Coiled coil; Cytoplasm; DNA damage;
KW   DNA recombination; DNA repair; DNA-binding; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1409
FT                   /note="Pogo transposable element with ZNF domain"
FT                   /id="PRO_0000047225"
FT   DOMAIN          1011..1081
FT                   /note="HTH CENPB-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00583"
FT   DOMAIN          1113..1319
FT                   /note="DDE-1"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         372..394
FT                   /note="C2H2-type 1; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         491..513
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         527..550
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         557..580
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         587..610
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         616..638
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         644..667
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         767..790
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         811..836
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          238..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          806..846
FT                   /note="Required for interaction with CBX5"
FT                   /evidence="ECO:0000250"
FT   REGION          904..966
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1356..1399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1336..1364
FT                   /evidence="ECO:0000255"
FT   MOTIF           1379..1403
FT                   /note="Integrase domain-binding motif (IBM)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   COMPBIAS        238..286
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        910..924
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        925..948
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1364..1388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         333
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   MOD_RES         360
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   MOD_RES         422
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   MOD_RES         436
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   MOD_RES         442
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   MOD_RES         460
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   MOD_RES         1334
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   MOD_RES         1360
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   MOD_RES         1366
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   MOD_RES         1372
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   MOD_RES         1373
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   MOD_RES         1377
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   MOD_RES         1391
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   MOD_RES         1393
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   MOD_RES         1395
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   CROSSLNK        319
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   CROSSLNK        356
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   CROSSLNK        419
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   CROSSLNK        446
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   CROSSLNK        486
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   CROSSLNK        626
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   CROSSLNK        674
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   CROSSLNK        797
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   CROSSLNK        879
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3K3"
FT   CONFLICT        513..515
FT                   /note="HVE -> TRP (in Ref. 2; AAH32176)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1342
FT                   /note="Q -> E (in Ref. 1; BAC29003)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1409 AA;  154910 MW;  ED08A5E2C1E719A5 CRC64;
     MADTDLFMEC EEEELEPWQK ISDVIEDSVV EDYNSVDKTT SVSVSQQPVS APVPIAAHAS
     VAGHLSTSTT VSNSGAQNSD STKKTLVTLI ANNNAGNTLV QQGGQPLILT QNPAPGLGTM
     VTQPVLRPVQ VMQNANHVTS SPVASQPIFI TTQGFPVRNV RPVQNAMNQV GIVLNVQQGQ
     TVRPITLVPA PGTQFVKPTV GVPQVFSQMT PVRPGSTMPV RPTTNTFTTV IPATLTIRST
     VPQSQSQQTK STPSTSTTPT ATQPTSLGQL AGQPPGQSNQ TSNPKLAPSF PSPPAVSIAS
     FVTVKRPGVT GENSNEVAKL VNTLNTVPSL GQSPGPVVVS NNSSAQRTSG PESSVKVTSS
     IPVFDLQDGG RKICPRCNAQ FRVTEALRGH MCYCCPEMVE YQKKGKSLDA EPSVPSAAKP
     SSPEKTAPVT STPSSTPIPA LSPPTKVPEP NENAGDAVQT KLIMLVDDFY YGRDGGKAAQ
     LTSFPKVATS FRCPHCTKRL KNNIRFMNHM KHHVELDQQN GEVDGHTICQ HCYRQFSTPF
     QLQCHLENVH SPYESTTKCK ICEWAFESEP LFLQHMKDTH KPGEMPYVCQ VCQYRSSLYS
     EVDVHFRMIH EDTRHLLCPY CLKVFKNGNA FQQHYMRHQK RNVYHCNKCR LQFLFAKDKI
     EHKLQHHKTF RKPKQLEGLK PGTKVTIRAS RGQPRTVPVS SNDAPSGTLQ EAAALTSTDP
     LPVFLYPPVQ RNIQKRAVRK MSVMGRQTCL ECSFEIPDFP NHFPTYVHCS LCRYSTCCSR
     AYANHMINNH VPRKSPKYLA LFKNSVSGIK LACTSCTFAT SVGDAMAKHL VFNPSHRSSN
     ILPRGLSWMS HLRPGQASER VFDWSMKNTY LPPPLVPNKA ATVKPVGVTP AEPQELAGPV
     LQALPSPAST ATPPATPTHP QPSALPPSAT EGTECLNVSE QEEGSPVTQD PEPASGGGGG
     SGVGKKEQLS VKKLRVVLFA LCCNTEQAAE HFRNPQRRIR RWLRRFQASQ GENLEGKYLS
     FEAEEKLAEW VLIQREQQLP VNEETLFQKA TKIGRSLEGG FKISYEWAVR FMLRHHLTPH
     ARRAVAHTLP KHVAENAGLF IEFVQRQIHN QDLPLSMIVA IDEISLFLDT EVLSSDDRKE
     NALQTVGTGE PWCDVVLAIL ADGTVLPTLV FFRGQANRFA NVPDSILLEA KDSGYSDDEI
     MELWSTRVWK KHTACQHSKS MLVMDCHRTH LSEEVLALLS ASSTLPAVVP AGCSSKIQPL
     DVCIKRTVKN FLHKKWKEQA REMADAACDS DVLLQLVLVW LGEVLGVIGD SPELVQRSFL
     VASVLPGPDG NVNSPTRNAD MQEELIASLE EQLKLNGEQS EEHSASAPRP RSSPEETVEP
     ESLHQLFEGE SETESFYGFE EADLDLMEI
//