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}.
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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
//