ID PHC1_MOUSE Reviewed; 1010 AA. AC Q64028; P70359; Q64307; Q7TT35; Q8BZ80; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 14-DEC-2022, sequence version 3. DT 24-JAN-2024, entry version 177. DE RecName: Full=Polyhomeotic-like protein 1 {ECO:0000305}; DE Short=mPH1; DE AltName: Full=Early development regulatory protein 1; DE AltName: Full=RAE-28; GN Name=Phc1 {ECO:0000312|MGI:MGI:103248}; Synonyms=Edr, Edr1, Rae28; 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 [MRNA] (ISOFORM 1), AND INDUCTION. RC STRAIN=BALB/cJ; RX PubMed=8070621; DOI=10.1046/j.1432-0436.1994.5710039.x; RA Nomura M., Takihara Y., Shimada K.; RT "Isolation and characterization of retinoic acid-inducible cDNA clones in RT F9 cells: one of the early inducible clones encodes a novel protein sharing RT several highly homologous regions with a Drosophila polyhomeotic protein."; RL Differentiation 57:39-50(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND INTERACTION WITH RP BMI1. RC TISSUE=Embryo; RX PubMed=9009205; DOI=10.1101/gad.11.2.226; RA Alkema M.J., Bronk M., Verhoeven E., Otte A., van't Veer L.J., Berns A., RA van Lohuizen M.; RT "Identification of Bmi1-interacting proteins as constituents of a RT multimeric mammalian polycomb complex."; RL Genes Dev. 11:226-240(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=NMRI; TISSUE=Mammary gland; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-844 (ISOFORM 1). 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., 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 [6] RP FUNCTION. RX PubMed=9367423; DOI=10.1242/dev.124.19.3673; RA Takihara Y., Tomotsune D., Shirai M., Katoh-Fukui Y., Nishii K., RA Motaleb M.A., Nomura M., Tsuchiya R., Fujita Y., Shibata Y., RA Higashinakagawa T., Shimada K.; RT "Targeted disruption of the mouse homologue of the Drosophila polyhomeotic RT gene leads to altered anteroposterior patterning and neural crest RT defects."; RL Development 124:3673-3682(1997). RN [7] RP DEVELOPMENTAL STAGE, AND INTERACTION WITH SCMH1. RX PubMed=10653359; DOI=10.1046/j.1432-0436.1999.6540229.x; RA Tomotsune D., Takihara Y., Berger J., Duhl D., Joo S., Kyba M., Shirai M., RA Ohta H., Matsuda Y., Honda B.M., Simon J., Shimada K., Brock H.W., RA Randazzo F.; RT "A novel member of murine polycomb-group proteins, Sex comb on midleg RT homolog protein, is highly conserved, and interacts with RAE28/mph1 in RT vitro."; RL Differentiation 65:229-239(1999). RN [8] RP INTERACTION WITH PHC2. RX PubMed=16024804; DOI=10.1128/mcb.25.15.6694-6706.2005; RA Isono K., Fujimura Y., Shinga J., Yamaki M., O-Wang J., Takihara Y., RA Murahashi Y., Takada Y., Mizutani-Koseki Y., Koseki H.; RT "Mammalian polyhomeotic homologues Phc2 and Phc1 act in synergy to mediate RT polycomb repression of Hox genes."; RL Mol. Cell. Biol. 25:6694-6706(2005). RN [9] RP INTERACTION WITH RNF2 AND CBX7, AND TISSUE SPECIFICITY. RX PubMed=22226355; DOI=10.1016/j.stem.2011.12.006; RA Morey L., Pascual G., Cozzuto L., Roma G., Wutz A., Benitah S.A., RA Di Croce L.; RT "Nonoverlapping functions of the Polycomb group Cbx family of proteins in RT embryonic stem cells."; RL Cell Stem Cell 10:47-62(2012). CC -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like CC complex, a complex class required to maintain the transcriptionally CC repressive state of many genes, including Hox genes, throughout CC development. PcG PRC1 complex acts via chromatin remodeling and CC modification of histones; it mediates monoubiquitination of histone H2A CC 'Lys-119', rendering chromatin heritably changed in its expressibility. CC Required for proper control of cellular levels of GMNN expression (By CC similarity). {ECO:0000250, ECO:0000269|PubMed:9367423}. CC -!- SUBUNIT: Homodimer. Component of a PRC1-like complex (By similarity). CC Interacts with the SAM domain of SCMH1 via its SAM domain in vitro CC (PubMed:10653359). Interacts with RNF2 and CBX7 (PubMed:22226355). CC Interacts with PHC2 (PubMed:16024804). Interacts with BMI1 CC (PubMed:9009205). {ECO:0000250|UniProtKB:P78364, CC ECO:0000269|PubMed:10653359, ECO:0000269|PubMed:16024804, CC ECO:0000269|PubMed:22226355, ECO:0000269|PubMed:9009205}. CC -!- INTERACTION: CC Q64028; P49138: Mapkapk2; NbExp=2; IntAct=EBI-927346, EBI-298776; CC Q64028; P23798: Pcgf2; NbExp=4; IntAct=EBI-927346, EBI-926857; CC Q64028; Q9QWH1: Phc2; NbExp=2; IntAct=EBI-927346, EBI-642357; CC Q64028; Q9CQJ4: Rnf2; NbExp=7; IntAct=EBI-927346, EBI-927321; CC Q64028; Q8K214: Scmh1; NbExp=2; IntAct=EBI-927346, EBI-445955; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q64028-1; Sequence=Displayed; CC Name=2; CC IsoId=Q64028-2; Sequence=VSP_004040; CC Name=3; CC IsoId=Q64028-3; Sequence=VSP_004041; CC -!- TISSUE SPECIFICITY: Highly expressed in testis with lower levels in CC most other tissues. Expressed in embryonic stem cells CC (PubMed:22226355). {ECO:0000269|PubMed:22226355}. CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously in 8.5 dpc embryos. At 10.5 CC dpc, strongly expressed in pharyngeal arches and weakly expressed in CC heart. By 14.5 dpc, expression is detected throughout the central CC nervous system. {ECO:0000269|PubMed:10653359}. CC -!- INDUCTION: By retinoic acid. {ECO:0000269|PubMed:8070621}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; S73882; AAB31766.1; -; mRNA. DR EMBL; U63386; AAC28974.1; -; mRNA. DR EMBL; AC153579; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC046535; AAH46535.1; -; mRNA. DR EMBL; BC052394; AAH52394.1; -; mRNA. DR EMBL; AK036370; BAC29400.1; -; mRNA. DR CCDS; CCDS20494.1; -. [Q64028-1] DR CCDS; CCDS39620.1; -. [Q64028-3] DR RefSeq; NP_001258508.1; NM_001271579.1. [Q64028-1] DR RefSeq; NP_031931.2; NM_007905.3. [Q64028-1] DR AlphaFoldDB; Q64028; -. DR SMR; Q64028; -. DR BioGRID; 199382; 14. DR CORUM; Q64028; -. DR DIP; DIP-456N; -. DR IntAct; Q64028; 11. DR MINT; Q64028; -. DR STRING; 10090.ENSMUSP00000125580; -. DR GlyGen; Q64028; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q64028; -. DR PhosphoSitePlus; Q64028; -. DR MaxQB; Q64028; -. DR PaxDb; 10090-ENSMUSP00000125580; -. DR ProteomicsDB; 287923; -. [Q64028-1] DR ProteomicsDB; 287924; -. [Q64028-2] DR ProteomicsDB; 287925; -. [Q64028-3] DR ProteomicsDB; 330592; -. DR Pumba; Q64028; -. DR Antibodypedia; 1884; 226 antibodies from 28 providers. DR DNASU; 13619; -. DR Ensembl; ENSMUST00000079560.10; ENSMUSP00000078514.4; ENSMUSG00000040669.15. [Q64028-1] DR Ensembl; ENSMUST00000081849.10; ENSMUSP00000080532.4; ENSMUSG00000040669.15. [Q64028-3] DR Ensembl; ENSMUST00000112600.9; ENSMUSP00000108219.3; ENSMUSG00000040669.15. [Q64028-3] DR Ensembl; ENSMUST00000160696.8; ENSMUSP00000125580.2; ENSMUSG00000040669.15. [Q64028-1] DR Ensembl; ENSMUST00000161054.8; ENSMUSP00000123911.2; ENSMUSG00000040669.15. [Q64028-3] DR Ensembl; ENSMUST00000161739.8; ENSMUSP00000125568.2; ENSMUSG00000040669.15. [Q64028-1] DR GeneID; 13619; -. DR KEGG; mmu:13619; -. DR AGR; MGI:103248; -. DR CTD; 1911; -. DR MGI; MGI:103248; Phc1. DR VEuPathDB; HostDB:ENSMUSG00000040669; -. DR eggNOG; ENOG502QUTP; Eukaryota. DR GeneTree; ENSGT00940000156612; -. DR HOGENOM; CLU_012048_1_0_1; -. DR InParanoid; Q64028; -. DR OMA; HTNEINL; -. DR OrthoDB; 5399754at2759; -. DR PhylomeDB; Q64028; -. DR TreeFam; TF331299; -. DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins. DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors. DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins. DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins. DR Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known. DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription. DR Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6. DR BioGRID-ORCS; 13619; 1 hit in 79 CRISPR screens. DR ChiTaRS; Phc1; mouse. DR PRO; PR:Q64028; -. DR Proteomes; UP000000589; Chromosome 6. DR RNAct; Q64028; Protein. DR Bgee; ENSMUSG00000040669; Expressed in seminiferous tubule of testis and 273 other cell types or tissues. DR GO; GO:0016604; C:nuclear body; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0031519; C:PcG protein complex; ISO:MGI. DR GO; GO:0035102; C:PRC1 complex; ISS:UniProtKB. DR GO; GO:0001739; C:sex chromatin; IDA:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0042393; F:histone binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI. DR GO; GO:0071300; P:cellular response to retinoic acid; IDA:MGI. DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central. DR CDD; cd09577; SAM_Ph1_2_3; 1. DR Gene3D; 3.30.60.160; -; 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1. DR InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM/pointed_sf. DR InterPro; IPR012313; Znf_FCS. DR InterPro; IPR038603; Znf_FCS_sf. DR PANTHER; PTHR12247; POLYCOMB GROUP PROTEIN; 1. DR PANTHER; PTHR12247:SF20; POLYHOMEOTIC-LIKE PROTEIN 1; 1. DR Pfam; PF16616; PHC2_SAM_assoc; 1. DR Pfam; PF00536; SAM_1; 1. DR Pfam; PF21319; zf-FCS_1; 1. DR SMART; SM00454; SAM; 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 1. DR PROSITE; PS50105; SAM_DOMAIN; 1. DR PROSITE; PS51024; ZF_FCS; 1. PE 1: Evidence at protein level; KW Alternative splicing; Developmental protein; DNA-binding; Isopeptide bond; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..1010 FT /note="Polyhomeotic-like protein 1" FT /id="PRO_0000058376" FT DOMAIN 946..1010 FT /note="SAM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184" FT ZN_FING 797..831 FT /note="FCS-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 212..243 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 259..312 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 444..506 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 565..588 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 646..678 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 772..794 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 854..928 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 259..273 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 464..485 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 486..506 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 570..584 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 854..892 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 806 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367" FT BINDING 809 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367" FT BINDING 825 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367" FT BINDING 829 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367" FT MOD_RES 651 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P78364" FT MOD_RES 904 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P78364" FT MOD_RES 928 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P78364" FT CROSSLNK 769 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P78364" FT VAR_SEQ 153..204 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9009205" FT /id="VSP_004041" FT VAR_SEQ 153..159 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9009205" FT /id="VSP_004040" FT CONFLICT 127 FT /note="T -> A (in Ref. 2; AAC28974)" FT /evidence="ECO:0000305" FT CONFLICT 131 FT /note="S -> W (in Ref. 2; AAC28974)" FT /evidence="ECO:0000305" FT CONFLICT 401 FT /note="I -> Y (in Ref. 1; AAB31766)" FT /evidence="ECO:0000305" FT CONFLICT 446 FT /note="Q -> QQQ (in Ref. 1; AAB31766, 4; AAH46535 and 2; FT AAC28974)" FT /evidence="ECO:0000305" FT CONFLICT 768 FT /note="K -> E (in Ref. 1; AAB31766, 4; AAH46535 and 2; FT AAC28974)" FT /evidence="ECO:0000305" SQ SEQUENCE 1010 AA; 106060 MW; 086BB97C290243C8 CRC64; METESEQNSS STNGSSSSGA SSRPQIAQMS LYERQAVQAL QALQRQPNAA QYFHQFMLQQ QLSNAQLHSL AAVQQATIAA SRQASSPNSS TAQQQTATTQ ASMNLATTSA AQLISRSQSV SSPSATTLTQ SVLLGNTTSP PLNQSQAQMY LRPQLGNLLQ VNRTLGRNVP LASQLILMPN GAVAAVQQEV PPAQSPGVHA DADQVQNLAV RNQQASAQGP QMPGSTQKAI PPGASPVSGL SQTSSQALAV AQASSGASGQ SLNLSQAGGG SGNSLPGSMG PGGGGQAPGG LGQLPSSGLT GGSCPRKGTG VVQPLPAAQT VTVSQGSQTE AESAAAKKAE ADGSGQQSVG MNLTRTATPA PSQTLISSAT YTQIQPHSLI QQQQQIHLQQ KQVVIQQQIA IHHQQQFQHR QSQLLHTATH LQLAQQQQQQ QQQQQQQQQQ QQQQQQGTTL TAPQPPQVPP TQQVPPSQSQ QQAQTLVVQP MLQSSPLTLP PEPTSKPPIP IQSKPPVAPI KPPQLGAAKM SATQQPPPHI PVQVVGTRQP GSAQAQALGL AQLAAAVPTP RGITGAVQPG QAHLASSPPS SQAAPGALQE CPPALAAGMT LAPVQGTAHV VKGGPTASSP VVAQVPAAFY MQSVHLPGKA QTLAVKRKAE SEEERDDLSA LASVLPTKAS PAAESPKVIE EKNSLGEKAE PVASLNANPP NSDLVALAPT PSAPPPTLAL VSRQMGDSKP PQAIVKPQIL THIIEGFVIQ EGAEPFPVGC SQFLKETKKP LQAGLPTGLN ESQPSGPLGG DSPSVELEKK ANLLKCEYCG KYAPAEQFRG SKRFCSMTCA KRYNVSCSHQ FRLKRKKMKE FQEASYARVR RRGPRRSSSD IARAKIQGKR HRGQEDSSRG SDNSSYDEAL SPTSPGPLSV RAGHGERDLG NTITTPSTPE LQGINPVFLS SNPSQWSVEE VYEFIASLQG CQEIAEEFRS QEIDGQALLL LKEEHLMSAM NIKLGPALKI CAKINVLKET //