SNAI1_MOUSE
ID SNAI1_MOUSE Reviewed; 264 AA.
AC Q02085;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Zinc finger protein SNAI1;
DE AltName: Full=Protein snail homolog 1;
DE Short=Protein sna;
GN Name=Snai1; Synonyms=Sna;
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].
RC TISSUE=Embryo;
RX PubMed=1295727; DOI=10.1242/dev.116.4.1033;
RA Smith D.E., del Amo F.F., Gridley T.;
RT "Isolation of Sna, a mouse gene homologous to the Drosophila genes snail
RT and escargot: its expression pattern suggests multiple roles during
RT postimplantation development.";
RL Development 116:1033-1039(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1483390; DOI=10.1242/dev.116.1.227;
RA Nieto A.M., Bennett M.F., Sargent M.G., Wilkinson D.G.;
RT "Cloning and developmental expression of Sna, a murine homologue of the
RT Drosophila snail gene.";
RL Development 116:227-237(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Lung;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RC STRAIN=129/Sv;
RX PubMed=9271672; DOI=10.1007/s003359900537;
RA Jiang R., Copeland N.G., Gilbert D.J., Jenkins N.A., Gridley T.;
RT "Genomic organization and chromosomal localization of the mouse snail (Sna)
RT gene.";
RL Mamm. Genome 8:686-688(1997).
RN [5]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=10655586; DOI=10.1038/35000025;
RA Cano A., Perez-Moreno M.A., Rodrigo I., Locascio A., Blanco M.J.,
RA del Barrio M.G., Portillo F., Nieto M.A.;
RT "The transcription factor snail controls epithelial-mesenchymal transitions
RT by repressing E-cadherin expression.";
RL Nat. Cell Biol. 2:76-83(2000).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11689706; DOI=10.1128/mcb.21.23.8184-8188.2001;
RA Carver E.A., Jiang R., Lan Y., Oram K.F., Gridley T.;
RT "The mouse snail gene encodes a key regulator of the epithelial-mesenchymal
RT transition.";
RL Mol. Cell. Biol. 21:8184-8188(2001).
RN [7]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=12832491; DOI=10.1128/mcb.23.14.5078-5089.2003;
RA Dominguez D., Montserrat-Sentis B., Virgos-Soler A., Guaita S., Grueso J.,
RA Porta M., Puig I., Baulida J., Franci C., Garcia de Herreros A.;
RT "Phosphorylation regulates the subcellular location and activity of the
RT snail transcriptional repressor.";
RL Mol. Cell. Biol. 23:5078-5089(2003).
RN [8]
RP INTERACTION WITH LIMD1; WTIP AND AJUBA.
RX PubMed=18331720; DOI=10.1016/j.devcel.2008.01.005;
RA Langer E.M., Feng Y., Zhaoyuan H., Rauscher F.J. III, Kroll K.L.,
RA Longmore G.D.;
RT "Ajuba LIM proteins are snail/slug corepressors required for neural crest
RT development in Xenopus.";
RL Dev. Cell 14:424-436(2008).
RN [9]
RP INTERACTION WITH KPNA2.
RX PubMed=19386897; DOI=10.1242/jcs.041749;
RA Mingot J.M., Vega S., Maestro B., Sanz J.M., Nieto M.A.;
RT "Characterization of Snail nuclear import pathways as representatives of
RT C2H2 zinc finger transcription factors.";
RL J. Cell Sci. 122:1452-1460(2009).
RN [10]
RP UBIQUITINATION BY FBXL14.
RX PubMed=19955572; DOI=10.1074/jbc.m109.065995;
RA Vinas-Castells R., Beltran M., Valls G., Gomez I., Garcia J.M.,
RA Montserrat-Sentis B., Baulida J., Bonilla F., de Herreros A.G., Diaz V.M.;
RT "The hypoxia-controlled FBXL14 ubiquitin ligase targets SNAIL1 for
RT proteasome degradation.";
RL J. Biol. Chem. 285:3794-3805(2010).
RN [11]
RP INTERACTION WITH CSNK2A1.
RX PubMed=19923321; DOI=10.1091/mbc.e09-06-0504;
RA MacPherson M.R., Molina P., Souchelnytskyi S., Wernstedt C.,
RA Martin-Perez J., Portillo F., Cano A.;
RT "Phosphorylation of serine 11 and serine 92 as new positive regulators of
RT human Snail1 function: potential involvement of casein kinase-2 and the
RT cAMP-activated kinase protein kinase A.";
RL Mol. Biol. Cell 21:244-253(2010).
RN [12]
RP INTERACTION WITH PARP1.
RX PubMed=21577210; DOI=10.1038/onc.2011.153;
RA Rodriguez M.I., Gonzalez-Flores A., Dantzer F., Collard J.,
RA de Herreros A.G., Oliver F.J.;
RT "Poly(ADP-ribose)-dependent regulation of Snail1 protein stability.";
RL Oncogene 30:4365-4372(2011).
RN [13]
RP FUNCTION.
RX PubMed=24239292; DOI=10.1016/j.molcel.2013.10.015;
RA Millanes-Romero A., Herranz N., Perrera V., Iturbide A.,
RA Loubat-Casanovas J., Gil J., Jenuwein T., Garcia de Herreros A., Peiro S.;
RT "Regulation of heterochromatin transcription by Snail1/LOXL2 during
RT epithelial-to-mesenchymal transition.";
RL Mol. Cell 52:746-757(2013).
CC -!- FUNCTION: Involved in induction of the epithelial to mesenchymal
CC transition (EMT), formation and maintenance of embryonic mesoderm,
CC growth arrest, survival and cell migration. Binds to 3 E-boxes of the
CC E-cadherin gene promoter and to the promoters of CLDN7 and KRT8 and, in
CC association with histone demethylase KDM1A which it recruits to the
CC promoters, causes a decrease in dimethylated H3K4 levels and represses
CC transcription. Involved in induction of the epithelial to mesenchymal
CC transition (EMT), formation and maintenance of embryonic mesoderm,
CC growth arrest, survival and cell migration. Binds to 3 E-boxes of the
CC E-cadherin/CDH1 gene promoter and to the promoters of CLDN7 and KRT8
CC and, in association with histone demethylase KDM1A which it recruits to
CC the promoters, causes a decrease in dimethylated H3K4 levels and
CC represses transcription. The N-terminal SNAG domain competes with
CC histone H3 for the same binding site on the histone demethylase complex
CC formed by KDM1A and RCOR1, and thereby inhibits demethylation of
CC histone H3 at 'Lys-4' (in vitro) (By similarity). During EMT, involved
CC with LOXL2 in negatively regulating pericentromeric heterochromatin
CC transcription (PubMed:24239292). SNAI1 recruits LOXL2 to
CC pericentromeric regions to oxidize histone H3 and repress transcription
CC which leads to release of heterochromatin component CBX5/HP1A, enabling
CC chromatin reorganization and acquisition of mesenchymal traits
CC (PubMed:24239292). Associates with EGR1 and SP1 to mediate 12-O-
CC tetradecanoylphorbol-13-acetate (TPA)-induced up-regulation of CDKN2B,
CC possibly by binding to the CDKN2B promoter region 5'-TCACA-3'. In
CC addition, may also activate the CDKN2B promoter by itself.
CC {ECO:0000250|UniProtKB:O95863, ECO:0000269|PubMed:10655586,
CC ECO:0000269|PubMed:11689706, ECO:0000269|PubMed:24239292}.
CC -!- SUBUNIT: Interacts with LOXL2 and LOXL3 (By similarity). Interacts with
CC FBXL14 and GSK3B. Interacts with BTRC; interaction occurs when it is
CC phosphorylated on the destruction motif. Interacts (via SNAG domain)
CC with LIMD1 (via LIM domains), WTIP (via LIM domains) and AJUBA (via LIM
CC domains). Interacts (via N-terminal region) with CSNK2A1. Interacts
CC with EGR1 upon TPA induction. Interacts (via N-terminal region) with
CC LATS2; the interaction is dependent on LATS2 kinase activity but
CC independent of SNAI1 Thr-203 phosphorylation. Interacts (via zinc
CC fingers) with KPNB1 and TNPO1; the interactions mediate nuclear import.
CC Interacts (via zinc fingers) with KPNA1; the interaction disrupts the
CC transport complex with KPNB1 and prevents nuclear import increasing
CC SNAI1 degradation in the cytoplasm. Interacts (via zinc fingers) with
CC KPNA2; the interaction, in combination with KPNB1, mediates nuclear
CC import. Interacts with KPNA4; this interaction mediates nuclear import.
CC May interact (via zinc fingers) with IPO7. Interacts (via zinc fingers)
CC with PARP1; the interaction requires SNAI1 to be poly-ADP-ribosylated
CC and non-phosphorylated (active) by GSK3B. Interacts (via SNAG domain)
CC with KDM1A; the interaction is necessary for the down-regulation of
CC dimethylated H3K4 mark and promoter activity of E-cadherin/CDH1, CDN7
CC and KRT8. Interacts with TP53/p53 and (via zinc fingers) with NOTCH1
CC (via intracellular domain); the interactions induce SNAI1 degradation
CC via MDM2-mediated ubiquitination and inhibit SNAI1-induced cell
CC invasion. Interacts with MDM2; the interaction promotes SNAI1
CC ubiquitination. Interacts (via zinc fingers) with CSNK1E. Interacts
CC with PAK1. {ECO:0000250|UniProtKB:O95863, ECO:0000269|PubMed:18331720,
CC ECO:0000269|PubMed:19386897, ECO:0000269|PubMed:19923321,
CC ECO:0000269|PubMed:21577210}.
CC -!- INTERACTION:
CC Q02085; P09874: PARP1; Xeno; NbExp=3; IntAct=EBI-6049807, EBI-355676;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12832491}. Cytoplasm
CC {ECO:0000269|PubMed:12832491}. Note=Once phosphorylated (probably on
CC Ser-107, Ser-111, Ser-115 and Ser-119) it is exported from the nucleus
CC to the cytoplasm where subsequent phosphorylation of the destruction
CC motif and ubiquitination involving BTRC occurs.
CC {ECO:0000250|UniProtKB:O95863}.
CC -!- TISSUE SPECIFICITY: While expression is completely absent from non-
CC invasive cell lines, it is high in invasive and metastatic cell types.
CC -!- DEVELOPMENTAL STAGE: Postimplantation. Expression is observed in
CC undifferentiated mesoderm and in tissues undergoing EMTs, namely the
CC precursors of the neural crest cells and the primitive streak.
CC {ECO:0000269|PubMed:10655586}.
CC -!- PTM: Phosphorylated by GSK3B. Once phosphorylated, it becomes a target
CC for BTRC ubiquitination. Phosphorylation by CSNK1E, probably at Ser-
CC 104, provides the priming site for the subsequent phosphorylation by
CC GSK3B, probably at Ser-100 and Ser-96. Phosphorylation by PAK1 may
CC modulate its transcriptional activity by promoting increased
CC accumulation in the nucleus. Phosphorylation at Ser-11 and Ser-104
CC positively regulates its function in induction of EMT and/or cell
CC survival, respectively. Phosphorylation by LATS2, upon mitotic stress,
CC oncogenic stress or Hippo pathway activation, occurs in the nucleus and
CC promotes nuclear retention and stabilization of total cellular protein
CC level. {ECO:0000250|UniProtKB:O95863}.
CC -!- PTM: Ubiquitinated on Lys-98, Lys-137 and Lys-146 by FBXL14 and BTRC
CC leading to degradation. BTRC-triggered ubiquitination requires previous
CC GSK3B-mediated SNAI1 phosphorylation. Ubiquitination induced upon
CC interaction with NOTCH1 or p53 is mediated by MDM2 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: O-GlcNAcylation at Ser-112 is enhanced in hyperglycaemic
CC conditions, it opposes phosphorylation by GSK3B, and stabilizes the
CC protein. {ECO:0000250}.
CC -!- PTM: ADP-ribosylation by PARP1 increases protein half-life and may be
CC involved in TGFB-induced SNAI1 up-regulation. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryos die early in gestation, exhibiting
CC defects in gastrulation and mesoderm formation. Recessive lethal
CC mutation. {ECO:0000269|PubMed:11689706}.
CC -!- SIMILARITY: Belongs to the snail C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; M95604; AAA03481.1; -; mRNA.
DR EMBL; X67253; CAA47675.1; -; mRNA.
DR EMBL; BC034857; AAH34857.1; -; mRNA.
DR EMBL; U95961; AAB58054.1; -; Genomic_DNA.
DR CCDS; CCDS17102.1; -.
DR PIR; A49149; A49149.
DR RefSeq; NP_035557.1; NM_011427.3.
DR AlphaFoldDB; Q02085; -.
DR SMR; Q02085; -.
DR BioGRID; 203361; 32.
DR IntAct; Q02085; 2.
DR STRING; 10090.ENSMUSP00000050581; -.
DR GlyGen; Q02085; 1 site.
DR iPTMnet; Q02085; -.
DR PhosphoSitePlus; Q02085; -.
DR jPOST; Q02085; -.
DR PaxDb; Q02085; -.
DR PRIDE; Q02085; -.
DR ProteomicsDB; 261285; -.
DR Antibodypedia; 3135; 916 antibodies from 46 providers.
DR DNASU; 20613; -.
DR Ensembl; ENSMUST00000052631; ENSMUSP00000050581; ENSMUSG00000042821.
DR GeneID; 20613; -.
DR KEGG; mmu:20613; -.
DR UCSC; uc008nzy.1; mouse.
DR CTD; 6615; -.
DR MGI; MGI:98330; Snai1.
DR VEuPathDB; HostDB:ENSMUSG00000042821; -.
DR eggNOG; KOG2462; Eukaryota.
DR GeneTree; ENSGT00940000154681; -.
DR HOGENOM; CLU_002678_42_3_1; -.
DR InParanoid; Q02085; -.
DR OMA; GWASFRP; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q02085; -.
DR TreeFam; TF315515; -.
DR BioGRID-ORCS; 20613; 10 hits in 78 CRISPR screens.
DR ChiTaRS; Snai1; mouse.
DR PRO; PR:Q02085; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q02085; protein.
DR Bgee; ENSMUSG00000042821; Expressed in lamina propria of urethra and 192 other tissues.
DR ExpressionAtlas; Q02085; baseline and differential.
DR Genevisible; Q02085; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0070888; F:E-box binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0060536; P:cartilage morphogenesis; IGI:MGI.
DR GO; GO:0010631; P:epithelial cell migration; IGI:MGI.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:UniProtKB.
DR GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; IGI:BHF-UCL.
DR GO; GO:0031069; P:hair follicle morphogenesis; IDA:MGI.
DR GO; GO:0070828; P:heterochromatin organization; IMP:UniProtKB.
DR GO; GO:0060972; P:left/right pattern formation; IMP:MGI.
DR GO; GO:0007498; P:mesoderm development; IMP:MGI.
DR GO; GO:0001707; P:mesoderm formation; IMP:UniProtKB.
DR GO; GO:0060806; P:negative regulation of cell differentiation involved in embryonic placenta development; IDA:MGI.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; ISO:MGI.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010957; P:negative regulation of vitamin D biosynthetic process; ISO:MGI.
DR GO; GO:0061314; P:Notch signaling involved in heart development; IGI:BHF-UCL.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; IGI:MGI.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IDA:MGI.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Cytoplasm; Developmental protein; DNA-binding;
KW Glycoprotein; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..264
FT /note="Zinc finger protein SNAI1"
FT /id="PRO_0000047030"
FT ZN_FING 156..176
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 180..202
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 210..230
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 236..259
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..20
FT /note="SNAG domain"
FT /evidence="ECO:0000305"
FT REGION 2..7
FT /note="Required and sufficient for interaction with KDM1A"
FT /evidence="ECO:0000250|UniProtKB:O95863"
FT REGION 10..40
FT /note="LATS2 binding"
FT /evidence="ECO:0000250"
FT REGION 85..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..151
FT /note="Required for FBXL14-triggered degradation"
FT /evidence="ECO:0000250"
FT REGION 151..264
FT /note="Required for nuclear localization and interaction
FT with KPNB1, NOTCH1 and PARP1"
FT /evidence="ECO:0000250"
FT MOTIF 95..100
FT /note="Destruction motif"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95863"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95863"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95863"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95863"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95863"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95863"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95863"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95863"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95863"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95863"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95863"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95863"
FT CARBOHYD 112
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CROSSLNK 98
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O95863"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O95863"
FT CROSSLNK 146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O95863"
FT CONFLICT 219
FT /note="D -> V (in Ref. 2; CAA47675)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 29190 MW; 52E2061224A18DEB CRC64;
MPRSFLVRKP SDPRRKPNYS ELQDACVEFT FQQPYDQAHL LAAIPPPEVL NPAASLPTLI
WDSLLVPQVR PVAWATLPLR ESPKAVELTS LSDEDSGKSS QPPSPPSPAP SSFSSTSASS
LEAEAFIAFP GLGQLPKQLA RLSVAKDPQS RKIFNCKYCN KEYLSLGALK MHIRSHTLPC
VCTTCGKAFS RPWLLQGHVR THTGEKPFSC SHCNRAFADR SNLRAHLQTH SDVKRYQCQA
CARTFSRMSL LHKHQESGCS GGPR
