ID GFI1_HUMAN Reviewed; 422 AA. AC Q99684; Q8N564; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 15-AUG-2003, sequence version 2. DT 27-MAR-2024, entry version 200. DE RecName: Full=Zinc finger protein Gfi-1; DE AltName: Full=Growth factor independent protein 1; DE AltName: Full=Zinc finger protein 163; GN Name=GFI1; Synonyms=ZNF163; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Bone marrow; RX PubMed=9051000; DOI=10.1038/sj.onc.1200910; RA Roberts T., Cowell J.K.; RT "Cloning of the human Gfi-1 gene and its mapping to chromosome region RT 1p22."; RL Oncogene 14:1003-1005(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Testis; 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 DNA-BINDING, SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=8754800; DOI=10.1128/mcb.16.8.4024; RA Zweidler-Mckay P.A., Grimes H.L., Flubacher M.M., Tsichlis P.N.; RT "Gfi-1 encodes a nuclear zinc finger protein that binds DNA and functions RT as a transcriptional repressor."; RL Mol. Cell. Biol. 16:4024-4034(1996). RN [4] RP INTERACTION WITH PIAS3, SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=11060035; DOI=10.1093/emboj/19.21.5845; RA Roedel B., Tavassoli K., Karsunky H., Schmidt T., Bachmann M., Schaper F., RA Heinrich P., Shuai K., Elsaesser H.-P., Moeroey T.; RT "The zinc finger protein Gfi-1 can enhance STAT3 signaling by interacting RT with the STAT3 inhibitor PIAS3."; RL EMBO J. 19:5845-5855(2000). RN [5] RP IDENTIFICATION IN A COMPLEX WITH RUNX1T1; HDAC1; HDAC2 AND HDAC3, RP INTERACTION WITH RUNX1T1, AND SUBCELLULAR LOCATION. RX PubMed=12874834; DOI=10.1002/jcb.10548; RA McGhee L., Bryan J., Elliott L., Grimes H.L., Kazanjian A., Davis J.N., RA Meyers S.; RT "Gfi-1 attaches to the nuclear matrix, associates with ETO (MTG8) and RT histone deacetylase proteins, and represses transcription using a TSA- RT sensitive mechanism."; RL J. Cell. Biochem. 89:1005-1018(2003). RN [6] RP IDENTIFICATION IN A COMPLEX WITH EHMT2 AND HDAC1, INTERACTION WITH EHMT2 RP AND HDAC1, AND FUNCTION. RX PubMed=16287849; DOI=10.1128/mcb.25.23.10338-10351.2005; RA Duan Z., Zarebski A., Montoya-Durango D., Grimes H.L., Horwitz M.; RT "Gfi1 coordinates epigenetic repression of p21Cip/WAF1 by recruitment of RT histone lysine methyltransferase G9a and histone deacetylase 1."; RL Mol. Cell. Biol. 25:10338-10351(2005). RN [7] RP FUNCTION, INTERACTION WITH ARIH2, AND UBIQUITINATION. RX PubMed=17646546; DOI=10.1182/blood-2006-11-058602; RA Marteijn J.A., van der Meer L.T., van Emst L., van Reijmersdal S., RA Wissink W., de Witte T., Jansen J.H., Van der Reijden B.A.; RT "Gfi1 ubiquitination and proteasomal degradation is inhibited by the RT ubiquitin ligase Triad1."; RL Blood 110:3128-3135(2007). RN [8] RP INTERACTION WITH SPI1, DOMAIN ZINC-FINGER, FUNCTION, AND MUTAGENESIS OF RP PRO-2. RX PubMed=17197705; DOI=10.1074/jbc.m607613200; RA Dahl R., Iyer S.R., Owens K.S., Cuylear D.D., Simon M.C.; RT "The transcriptional repressor GFI-1 antagonizes PU.1 activity through RT protein-protein interaction."; RL J. Biol. Chem. 282:6473-6483(2007). RN [9] RP INTERACTION WITH AJUBA IN THE GFI1-AJUBA-HDAC COMPLEX, SUBCELLULAR RP LOCATION, AND FUNCTION. RX PubMed=18805794; DOI=10.1074/jbc.m802320200; RA Montoya-Durango D.E., Velu C.S., Kazanjian A., Rojas M.E., Jay C.M., RA Longmore G.D., Grimes H.L.; RT "Ajuba functions as a histone deacetylase-dependent co-repressor for RT autoregulation of the growth factor-independent-1 transcription factor."; RL J. Biol. Chem. 283:32056-32065(2008). RN [10] RP FUNCTION. RX PubMed=19026687; DOI=10.1016/j.jneumeth.2008.10.031; RA Ossovskaya V.S., Dolganov G., Basbaum A.I.; RT "Loss of function genetic screens reveal MTGR1 as an intracellular RT repressor of beta1 integrin-dependent neurite outgrowth."; RL J. Neurosci. Methods 177:322-333(2009). RN [11] RP FUNCTION, AND INTERACTION WITH ZBTB17. RX PubMed=19164764; DOI=10.1073/pnas.0804863106; RA Basu S., Liu Q., Qiu Y., Dong F.; RT "Gfi-1 represses CDKN2B encoding p15INK4B through interaction with Miz-1."; RL Proc. Natl. Acad. Sci. U.S.A. 106:1433-1438(2009). RN [12] RP INTERACTION WITH RELA, SUBCELLULAR LOCATION, INDUCTION, AND FUNCTION. RX PubMed=20547752; DOI=10.1128/mcb.00087-10; RA Sharif-Askari E., Vassen L., Kosan C., Khandanpour C., Gaudreau M.C., RA Heyd F., Okayama T., Jin J., Rojas M.E., Grimes H.L., Zeng H., Moroy T.; RT "Zinc finger protein Gfi1 controls the endotoxin-mediated Toll-like RT receptor inflammatory response by antagonizing NF-kappaB p65."; RL Mol. Cell. Biol. 30:3929-3942(2010). RN [13] RP INTERACTION WITH ZBTB17, FUNCTION, INDUCTION, AND CHARACTERIZATION OF RP VARIANT SER-382. RX PubMed=20190815; DOI=10.1038/onc.2010.48; RA Liu Q., Basu S., Qiu Y., Tang F., Dong F.; RT "A role of Miz-1 in Gfi-1-mediated transcriptional repression of CDKN1A."; RL Oncogene 29:2843-2852(2010). RN [14] RP VARIANT NI-CINA ARG-403, VARIANT SCN2 SER-382, CHARACTERIZATION OF VARIANTS RP NI-CINA ARG-403 AND SCN2 SER-382, AND FUNCTION. RX PubMed=12778173; DOI=10.1038/ng1170; RA Person R.E., Li F.-Q., Duan Z., Benson K.F., Wechsler J., Papadaki H.A., RA Eliopoulos G., Kaufman C., Bertolone S.J., Nakamoto B., Papayannopoulou T., RA Grimes H.L., Horwitz M.; RT "Mutations in proto-oncogene GFI1 cause human neutropenia and target RT ELA2."; RL Nat. Genet. 34:308-312(2003). CC -!- FUNCTION: Transcription repressor essential for hematopoiesis. CC Functions in a cell-context and development-specific manner. Binds to CC 5'-TAAATCAC[AT]GCA-3' in the promoter region of a large number of CC genes. Component of several complexes, including the EHMT2-GFI1-HDAC1, CC AJUBA-GFI1-HDAC1 and RCOR-GFI-KDM1A-HDAC complexes, that suppress, via CC histone deacetylase (HDAC) recruitment, a number of genes implicated in CC multilineage blood cell development. Regulates neutrophil CC differentiation, promotes proliferation of lymphoid cells, and is CC required for granulocyte development. Inhibits SPI1 transcriptional CC activity at macrophage-specific genes, repressing macrophage CC differentiation of myeloid progenitor cells and promoting granulocyte CC commitment (By similarity). Mediates, together with U2AF1L4, the CC alternative splicing of CD45 and controls T-cell receptor signaling. CC Regulates the endotoxin-mediated Toll-like receptor (TLR) inflammatory CC response by antagonizing RELA. Cooperates with CBFA2T2 to regulate CC ITGB1-dependent neurite growth. Controls cell-cycle progression by CC repressing CDKNIA/p21 transcription in response to TGFB1 via CC recruitment of GFI1 by ZBTB17 to the CDKNIA/p21 and CDKNIB promoters. CC Required for the maintenance of inner ear hair cells. CC {ECO:0000250|UniProtKB:P70338, ECO:0000269|PubMed:11060035, CC ECO:0000269|PubMed:12778173, ECO:0000269|PubMed:16287849, CC ECO:0000269|PubMed:17197705, ECO:0000269|PubMed:17646546, CC ECO:0000269|PubMed:18805794, ECO:0000269|PubMed:19026687, CC ECO:0000269|PubMed:19164764, ECO:0000269|PubMed:20190815, CC ECO:0000269|PubMed:20547752, ECO:0000269|PubMed:8754800}. CC -!- SUBUNIT: Interacts with U2AF1L4. Component of RCOR-GFI-KDM1A-HDAC CC complexes. Interacts directly with RCOR1, KDM1A and HDAC2 (By CC similarity). Also interacts with HDAC1. Interacts (via the zinc-finger CC domain) with ARIH2; the interaction prevents GFI1 ubiquitination and CC proteasomal degradation. Interacts with PIAS3; the interaction relieves CC the inhibitory effect of PIAS3 on STAT3-mediated transcriptional CC activity. Forms a complex with EHMT2 and HDAC1 to promote 'Lys-9' CC dimethylation of H3 (H3K9Me2) and repress expression of target genes. CC Interacts directly with EHMT2. Component of the GFI1-AJUBA-HDAC1 CC repressor complex. Interacts directly with AJUBA (via ITS LIM domains); CC the interaction results in the HDAC-dependent corepression of a subset CC of GFI1 target genes and, occurs independently of the SNAG domain. CC Interacts with SPI1; the interaction inhibits SPI1 transcriptional CC activity targeted at macrophage-specific genes, repressing macrophage CC differentiation of myeloid progenitor cells and promoting granulocyte CC commitment (By similarity). Interacts with RUNX1T1; the interaction CC represses HDAC-mediated transcriptional activity. Interacts with RELA; CC the interaction occurs on liposaccharide (LPS) stimulation and controls CC RELA DNA binding activity and regulates endotoxin-mediated TOLL-like CC receptor inflammatory response. Interacts (via the C-terminal zinc CC fingers) with ZBTB17; the interaction results in the recruitment of CC GFI1 to the CDKN1A/p21 and CDKN1B promoters and repression of CC transcription. {ECO:0000250, ECO:0000250|UniProtKB:P70338, CC ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:12874834, CC ECO:0000269|PubMed:16287849, ECO:0000269|PubMed:17197705, CC ECO:0000269|PubMed:17646546, ECO:0000269|PubMed:18805794, CC ECO:0000269|PubMed:19164764, ECO:0000269|PubMed:20190815, CC ECO:0000269|PubMed:20547752}. CC -!- INTERACTION: CC Q99684; Q13111: CHAF1A; NbExp=4; IntAct=EBI-949368, EBI-1020839; CC Q99684; Q96KQ7: EHMT2; NbExp=2; IntAct=EBI-949368, EBI-744366; CC Q99684; Q13547: HDAC1; NbExp=4; IntAct=EBI-949368, EBI-301834; CC Q99684; Q9NQX1: PRDM5; NbExp=2; IntAct=EBI-949368, EBI-4292031; CC Q99684; Q04206: RELA; NbExp=2; IntAct=EBI-949368, EBI-73886; CC Q99684; Q91XC0: Ajuba; Xeno; NbExp=4; IntAct=EBI-949368, EBI-1565930; CC Q99684; P17433: Spi1; Xeno; NbExp=2; IntAct=EBI-949368, EBI-607588; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11060035, CC ECO:0000269|PubMed:12874834, ECO:0000269|PubMed:18805794, CC ECO:0000269|PubMed:20547752, ECO:0000269|PubMed:8754800}. CC Note=Colocalizes with PIAS3 and RUNX1T1 in nuclear dots. CC -!- INDUCTION: Down-regulated by TGFB1. {ECO:0000269|PubMed:20190815, CC ECO:0000269|PubMed:20547752}. CC -!- DOMAIN: Zinc fingers 3, 4 and 5 are required for DNA-binding and for CC interaction with SPI1. {ECO:0000269|PubMed:17197705}. CC -!- DOMAIN: The SNAG domain of GFIs is required for nuclear location and CC for interaction with some corepressors. {ECO:0000250}. CC -!- PTM: Ubiquitinated. Ubiquitination and degradation by the proteasome is CC inhibited by the ubiquitin ligase, ARIH2. CC {ECO:0000269|PubMed:17646546}. CC -!- DISEASE: Neutropenia, severe congenital 2, autosomal dominant (SCN2) CC [MIM:613107]: A disorder of hematopoiesis characterized by maturation CC arrest of granulopoiesis at the level of promyelocytes with peripheral CC blood absolute neutrophil counts below 0.5 x 10(9)/l and early onset of CC severe bacterial infections. {ECO:0000269|PubMed:12778173}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Dominant nonimmune chronic idiopathic neutropenia of adults CC (NI-CINA) [MIM:607847]: Relatively mild form of neutropenia diagnosed CC in adults, but predisposing to leukemia in a subset of patients. CC {ECO:0000269|PubMed:12778173}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- WEB RESOURCE: Name=GFI1base; Note=GFI1 mutation db; CC URL="http://structure.bmc.lu.se/idbase/GFI1base/"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40706/GFI1"; 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; U67369; AAB37272.1; -; mRNA. DR EMBL; BC032751; AAH32751.1; -; mRNA. DR EMBL; BC074866; AAH74866.1; -; mRNA. DR EMBL; BC074867; AAH74867.1; -; mRNA. DR CCDS; CCDS30773.1; -. DR RefSeq; NP_001120687.1; NM_001127215.1. DR RefSeq; NP_001120688.1; NM_001127216.1. DR RefSeq; NP_005254.2; NM_005263.3. DR RefSeq; XP_005270806.1; XM_005270749.3. DR RefSeq; XP_011539547.1; XM_011541245.2. DR RefSeq; XP_011539548.1; XM_011541246.2. DR AlphaFoldDB; Q99684; -. DR SMR; Q99684; -. DR BioGRID; 108940; 22. DR CORUM; Q99684; -. DR DIP; DIP-38452N; -. DR IntAct; Q99684; 17. DR STRING; 9606.ENSP00000294702; -. DR iPTMnet; Q99684; -. DR PhosphoSitePlus; Q99684; -. DR BioMuta; GFI1; -. DR DMDM; 33860154; -. DR EPD; Q99684; -. DR jPOST; Q99684; -. DR MassIVE; Q99684; -. DR PaxDb; 9606-ENSP00000359357; -. DR PeptideAtlas; Q99684; -. DR ProteomicsDB; 78396; -. DR Antibodypedia; 4402; 345 antibodies from 33 providers. DR DNASU; 2672; -. DR Ensembl; ENST00000294702.6; ENSP00000294702.5; ENSG00000162676.13. DR Ensembl; ENST00000370332.5; ENSP00000359357.1; ENSG00000162676.13. DR Ensembl; ENST00000427103.6; ENSP00000399719.1; ENSG00000162676.13. DR GeneID; 2672; -. DR KEGG; hsa:2672; -. DR MANE-Select; ENST00000294702.6; ENSP00000294702.5; NM_005263.5; NP_005254.2. DR UCSC; uc001dou.5; human. DR AGR; HGNC:4237; -. DR CTD; 2672; -. DR DisGeNET; 2672; -. DR GeneCards; GFI1; -. DR HGNC; HGNC:4237; GFI1. DR HPA; ENSG00000162676; Group enriched (bone marrow, lymphoid tissue). DR MalaCards; GFI1; -. DR MIM; 600871; gene. DR MIM; 607847; phenotype. DR MIM; 613107; phenotype. DR neXtProt; NX_Q99684; -. DR OpenTargets; ENSG00000162676; -. DR Orphanet; 486; Autosomal dominant severe congenital neutropenia. DR PharmGKB; PA24344; -. DR VEuPathDB; HostDB:ENSG00000162676; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000156166; -. DR HOGENOM; CLU_002678_94_9_1; -. DR InParanoid; Q99684; -. DR OMA; HSYRPCA; -. DR OrthoDB; 5341097at2759; -. DR PhylomeDB; Q99684; -. DR TreeFam; TF350784; -. DR PathwayCommons; Q99684; -. DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis. DR SignaLink; Q99684; -. DR SIGNOR; Q99684; -. DR BioGRID-ORCS; 2672; 43 hits in 1176 CRISPR screens. DR GeneWiki; GFI1; -. DR GenomeRNAi; 2672; -. DR Pharos; Q99684; Tbio. DR PRO; PR:Q99684; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q99684; Protein. DR Bgee; ENSG00000162676; Expressed in granulocyte and 109 other cell types or tissues. DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB. DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB. DR GO; GO:0010956; P:negative regulation of calcidiol 1-monooxygenase activity; IDA:BHF-UCL. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:UniProtKB. DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0010957; P:negative regulation of vitamin D biosynthetic process; IC:BHF-UCL. DR GO; GO:0070105; P:positive regulation of interleukin-6-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 6. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR23226; ZINC FINGER AND SCAN DOMAIN-CONTAINING; 1. DR PANTHER; PTHR23226:SF405; ZINC FINGER PROTEIN 135-LIKE; 1. DR Pfam; PF00096; zf-C2H2; 6. DR SMART; SM00355; ZnF_C2H2; 6. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6. DR Genevisible; Q99684; HS. PE 1: Evidence at protein level; KW Disease variant; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..422 FT /note="Zinc finger protein Gfi-1" FT /id="PRO_0000047193" FT ZN_FING 255..278 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 284..306 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 312..334 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 340..362 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 368..390 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 396..419 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..109 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1..20 FT /note="SNAG domain" FT /evidence="ECO:0000250" FT REGION 140..257 FT /note="Required for interaction with RELA" FT /evidence="ECO:0000269|PubMed:20547752" FT MOD_RES 20 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q07120" FT MOD_RES 56 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q07120" FT VARIANT 36 FT /note="S -> N (in dbSNP:rs34631763)" FT /id="VAR_052722" FT VARIANT 382 FT /note="N -> S (in SCN2; zero neutrophil count. marked FT monocytosis and reduced T- and B-lymphocyte number leading FT to recurrent infectious complications. Abolishes FT recognition of DNA binding site of zinc finger. Diminished FT repression activity and elevated ELA2 expression. No effect FT on repression of CDKN1A/p21 transcription; FT dbSNP:rs28936381)" FT /evidence="ECO:0000269|PubMed:12778173, FT ECO:0000269|PubMed:20190815" FT /id="VAR_016212" FT VARIANT 403 FT /note="K -> R (in NI-CINA; Neutropenic and elevated FT monocytosis but no history of infectious complications. No FT effect on DNA binding but diminished GFI1 repression FT activity; dbSNP:rs28936382)" FT /evidence="ECO:0000269|PubMed:12778173" FT /id="VAR_016213" FT MUTAGEN 2 FT /note="P->A: Abrogates transcriptional repression." FT /evidence="ECO:0000269|PubMed:17197705" FT CONFLICT 73..77 FT /note="DSCEG -> RQLRS (in Ref. 1; AAB37272)" FT /evidence="ECO:0000305" FT CONFLICT 184..186 FT /note="SCS -> NCI (in Ref. 1; AAB37272)" FT /evidence="ECO:0000305" FT CONFLICT 213 FT /note="R -> K (in Ref. 1; AAB37272)" FT /evidence="ECO:0000305" FT CONFLICT 228 FT /note="G -> R (in Ref. 1; AAB37272)" FT /evidence="ECO:0000305" FT CONFLICT 232 FT /note="D -> N (in Ref. 1; AAB37272)" FT /evidence="ECO:0000305" FT CONFLICT 367 FT /note="P -> L (in Ref. 1; AAB37272)" FT /evidence="ECO:0000305" SQ SEQUENCE 422 AA; 45297 MW; 740A466F72C5FC72 CRC64; MPRSFLVKSK KAHSYHQPRS PGPDYSLRLE NVPAPSRADS TSNAGGAKAE PRDRLSPESQ LTEAPDRASA SPDSCEGSVC ERSSEFEDFW RPPSPSASPA SEKSMCPSLD EAQPFPLPFK PYSWSGLAGS DLRHLVQSYR PCGALERGAG LGLFCEPAPE PGHPAALYGP KRAAGGAGAG APGSCSAGAG ATAGPGLGLY GDFGSAAAGL YERPTAAAGL LYPERGHGLH ADKGAGVKVE SELLCTRLLL GGGSYKCIKC SKVFSTPHGL EVHVRRSHSG TRPFACEMCG KTFGHAVSLE QHKAVHSQER SFDCKICGKS FKRSSTLSTH LLIHSDTRPY PCQYCGKRFH QKSDMKKHTF IHTGEKPHKC QVCGKAFSQS SNLITHSRKH TGFKPFGCDL CGKGFQRKVD LRRHRETQHG LK //