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Database: UniProt
Entry: PHC1_MOUSE
LinkDB: PHC1_MOUSE
Original site: PHC1_MOUSE 
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
//
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