PO4F1_HUMAN
ID PO4F1_HUMAN Reviewed; 419 AA.
AC Q01851; Q14986; Q15318; Q5T227;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 4.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=POU domain, class 4, transcription factor 1 {ECO:0000312|HGNC:HGNC:9218};
DE AltName: Full=Brain-specific homeobox/POU domain protein 3A;
DE Short=Brain-3A;
DE Short=Brn-3A;
DE AltName: Full=Homeobox/POU domain protein RDC-1;
DE AltName: Full=Oct-T1;
GN Name=POU4F1 {ECO:0000312|HGNC:HGNC:9218};
GN Synonyms=BRN3A, RDC1 {ECO:0000303|PubMed:1357630};
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] (ISOFORM 2), AND DEVELOPMENTAL STAGE.
RC TISSUE=Placenta;
RX PubMed=1357630; DOI=10.1093/nar/20.18.4919;
RA Collum R.G., Fisher P.E., Datta M., Mellis S., Thiele C., Huebner K.,
RA Croce C.M., Israel M.A., Theil T., Moroy T., DePinho R.A., Alt F.W.;
RT "A novel POU homeodomain gene specifically expressed in cells of the
RT developing mammalian nervous system.";
RL Nucleic Acids Res. 20:4919-4925(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8234287; DOI=10.1073/pnas.90.21.10260;
RA Bhargava A.K., Li Z., Weissman S.M.;
RT "Differential expression of four members of the POU family of proteins in
RT activated and phorbol 12-myristate 13-acetate-treated Jurkat T cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10260-10264(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=7623109; DOI=10.1523/jneurosci.15-07-04762.1995;
RA Xiang M., Zhou L.-J., Macke J.P., Yoshioka T., Hendry S.H., Eddy R.L.,
RA Shows T.B., Nathans J.;
RT "The Brn-3 family of POU-domain factors: primary structure, binding
RT specificity, and expression in subsets of retinal ganglion cells and
RT somatosensory neurons.";
RL J. Neurosci. 15:4762-4785(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-163 DEL.
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-163 DEL.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=12934100; DOI=10.1038/sj.onc.1206635;
RA Calissano M., Latchman D.S.;
RT "Functional interaction between the small GTP-binding protein Rin and the
RT N-terminal of Brn-3a transcription factor.";
RL Oncogene 22:5408-5414(2003).
RN [7]
RP INVOLVEMENT IN ATITHS, VARIANT ATITHS ARG-306, AND CHARACTERIZATION OF
RP VARIANT ATITHS ARG-306.
RX PubMed=33783914; DOI=10.1002/humu.24201;
RA Webb B.D., Evans A., Naidich T.P., Bird L.M., Parikh S.,
RA Fernandez Garcia M., Henderson L.B., Millan F., Si Y., Brennand K.J.,
RA Hung P., Rucker J.C., Wheeler P.G., Schadt E.E.;
RT "Haploinsufficiency of POU4F1 causes an ataxia syndrome with hypotonia and
RT intention tremor.";
RL Hum. Mutat. 42:685-693(2021).
CC -!- FUNCTION: Multifunctional transcription factor with different regions
CC mediating its different effects. Acts by binding (via its C-terminal
CC domain) to sequences related to the consensus octamer motif 5'-
CC ATGCAAAT-3' in the regulatory regions of its target genes. Regulates
CC the expression of specific genes involved in differentiation and
CC survival within a subset of neuronal lineages. It has been shown that
CC activation of some of these genes requires its N-terminal domain, maybe
CC through a neuronal-specific cofactor. Ativates BCL2 expression and
CC protects neuronal cells from apoptosis (via the N-terminal domain).
CC Induces neuronal process outgrowth and the coordinate expression of
CC genes encoding synaptic proteins. Exerts its major developmental
CC effects in somatosensory neurons and in brainstem nuclei involved in
CC motor control. Stimulates the binding affinity of the nuclear estrogene
CC receptor ESR1 to DNA estrogen response element (ERE), and hence
CC modulates ESR1-induced transcriptional activity. May positively
CC regulate POU4F2 and POU4F3. Regulates dorsal root ganglion sensory
CC neuron specification and axonal projection into the spinal cord. Plays
CC a role in TNFSF11-mediated terminal osteoclast differentiation.
CC Negatively regulates its own expression interacting directly with a
CC highly conserved autoregulatory domain surrounding the transcription
CC initiation site. {ECO:0000250|UniProtKB:P17208}.
CC -!- FUNCTION: [Isoform 2]: Able to act as transcription factor, cannot
CC regulate the expression of the same subset of genes than isoform 1.
CC Does not have antiapoptotic effect on neuronal cells.
CC {ECO:0000250|UniProtKB:P17208}.
CC -!- SUBUNIT: Interacts (via N-terminus) with RIT2; the interaction controls
CC POU4F1 transactivation activity on some neuronal target genes. Isoform
CC 1 interacts with POU4F2; this interaction inhibits both POU4F1 DNA-
CC binding and transcriptional activities. Isoform 1 interacts (C-
CC terminus) with ESR1 (via DNA-binding domain); this interaction
CC decreases the estrogen receptor ESR1 transcriptional activity in a
CC DNA- and ligand 17-beta-estradiol-independent manner.
CC {ECO:0000250|UniProtKB:P17208}.
CC -!- INTERACTION:
CC Q01851; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-17480471, EBI-726739;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12934100}. Cytoplasm
CC {ECO:0000250|UniProtKB:P17208}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Brn-3A-Long {ECO:0000305};
CC IsoId=Q01851-1; Sequence=Displayed;
CC Name=2; Synonyms=Brn-3A-Short {ECO:0000305};
CC IsoId=Q01851-2; Sequence=VSP_058636;
CC -!- TISSUE SPECIFICITY: Expressed in the brain and the retina. Present in
CC the developing brain, spinal cord and eye. {ECO:0000269|PubMed:1357630,
CC ECO:0000269|PubMed:7623109}.
CC -!- DEVELOPMENTAL STAGE: Expression peaks early in embryogenesis (day 13.5)
CC and is undetectable 14 days after birth. {ECO:0000269|PubMed:1357630}.
CC -!- DOMAIN: The C-terminal domain is able to act as both DNA-binding domain
CC and a transcriptional activator. The N-terminal domain is also required
CC for transactivation activity on some target genes acting as a discrete
CC activation domain. Neurite outgrowth and expression of genes required
CC for synapse formation are primarily dependent on the C-terminal domain,
CC however the N-terminal domain is required for maximal induction.
CC {ECO:0000250|UniProtKB:P17208}.
CC -!- DISEASE: Ataxia, intention tremor, and hypotonia syndrome, childhood-
CC onset (ATITHS) [MIM:619352]: An autosomal dominant neurodevelopmental
CC disorder characterized by global developmental delay, mildly impaired
CC intellectual development with speech delay or learning disabilities,
CC delayed walking due to ataxia, intention tremor, and hypotonia apparent
CC from early childhood. Brain imaging shows cerebellar atrophy in some
CC patients. {ECO:0000269|PubMed:33783914}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-4
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA45907.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/POU4F1ID44173ch13q31.html";
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DR EMBL; L20433; AAA65605.1; -; mRNA.
DR EMBL; U10063; AAA57161.1; -; Genomic_DNA.
DR EMBL; U10062; AAA57161.1; JOINED; Genomic_DNA.
DR EMBL; AL445209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471093; EAW80585.1; -; Genomic_DNA.
DR EMBL; X64624; CAA45907.1; ALT_FRAME; mRNA.
DR CCDS; CCDS31996.1; -. [Q01851-1]
DR PIR; I59234; I59234.
DR PIR; S78452; S78452.
DR RefSeq; NP_006228.3; NM_006237.3. [Q01851-1]
DR AlphaFoldDB; Q01851; -.
DR SMR; Q01851; -.
DR BioGRID; 111453; 7.
DR IntAct; Q01851; 3.
DR MINT; Q01851; -.
DR STRING; 9606.ENSP00000366413; -.
DR iPTMnet; Q01851; -.
DR PhosphoSitePlus; Q01851; -.
DR BioMuta; POU4F1; -.
DR DMDM; 334302933; -.
DR MassIVE; Q01851; -.
DR PaxDb; Q01851; -.
DR PeptideAtlas; Q01851; -.
DR PRIDE; Q01851; -.
DR ProteomicsDB; 58010; -.
DR Antibodypedia; 24689; 156 antibodies from 31 providers.
DR DNASU; 5457; -.
DR Ensembl; ENST00000377208.7; ENSP00000366413.4; ENSG00000152192.8. [Q01851-1]
DR GeneID; 5457; -.
DR KEGG; hsa:5457; -.
DR MANE-Select; ENST00000377208.7; ENSP00000366413.4; NM_006237.4; NP_006228.3.
DR UCSC; uc001vkv.4; human. [Q01851-1]
DR CTD; 5457; -.
DR DisGeNET; 5457; -.
DR GeneCards; POU4F1; -.
DR HGNC; HGNC:9218; POU4F1.
DR HPA; ENSG00000152192; Group enriched (brain, retina).
DR MIM; 601632; gene.
DR MIM; 619352; phenotype.
DR neXtProt; NX_Q01851; -.
DR OpenTargets; ENSG00000152192; -.
DR PharmGKB; PA33542; -.
DR VEuPathDB; HostDB:ENSG00000152192; -.
DR eggNOG; KOG1168; Eukaryota.
DR GeneTree; ENSGT00940000162154; -.
DR HOGENOM; CLU_013065_0_0_1; -.
DR InParanoid; Q01851; -.
DR OMA; HPHMHSL; -.
DR OrthoDB; 929123at2759; -.
DR PhylomeDB; Q01851; -.
DR TreeFam; TF316413; -.
DR PathwayCommons; Q01851; -.
DR Reactome; R-HSA-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR SignaLink; Q01851; -.
DR SIGNOR; Q01851; -.
DR BioGRID-ORCS; 5457; 9 hits in 1103 CRISPR screens.
DR GeneWiki; POU4F1; -.
DR GenomeRNAi; 5457; -.
DR Pharos; Q01851; Tbio.
DR PRO; PR:Q01851; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q01851; protein.
DR Bgee; ENSG00000152192; Expressed in secondary oocyte and 38 other tissues.
DR Genevisible; Q01851; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:ParkinsonsUK-UCL.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:ARUK-UCL.
DR GO; GO:0051020; F:GTPase binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:BHF-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; TAS:BHF-UCL.
DR GO; GO:0021535; P:cell migration in hindbrain; IEA:Ensembl.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB.
DR GO; GO:0021953; P:central nervous system neuron differentiation; IEA:Ensembl.
DR GO; GO:0021986; P:habenula development; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; ISS:ARUK-UCL.
DR GO; GO:0060384; P:innervation; TAS:BHF-UCL.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0007498; P:mesoderm development; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:ARUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:ARUK-UCL.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0043069; P:negative regulation of programmed cell death; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0048665; P:neuron fate specification; ISS:BHF-UCL.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0048935; P:peripheral nervous system neuron development; ISS:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISS:UniProtKB.
DR GO; GO:0051355; P:proprioception involved in equilibrioception; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0050767; P:regulation of neurogenesis; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0048880; P:sensory system development; ISS:BHF-UCL.
DR GO; GO:0001967; P:suckling behavior; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; TAS:ProtInc.
DR GO; GO:0021559; P:trigeminal nerve development; ISS:BHF-UCL.
DR GO; GO:0003223; P:ventricular compact myocardium morphogenesis; IEA:Ensembl.
DR CDD; cd00086; homeodomain; 1.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013847; POU.
DR InterPro; IPR015584; POU4-TF1.
DR InterPro; IPR000327; POU_dom.
DR PANTHER; PTHR11636:SF42; PTHR11636:SF42; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR PRINTS; PR00028; POUDOMAIN.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00352; POU; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00035; POU_1; 1.
DR PROSITE; PS00465; POU_2; 1.
DR PROSITE; PS51179; POU_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Disease variant;
KW DNA-binding; Homeobox; Intellectual disability; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..419
FT /note="POU domain, class 4, transcription factor 1"
FT /id="PRO_0000100736"
FT DOMAIN 261..338
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 356..415
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 94..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 57..66
FT /note="POU-IV box"
FT VAR_SEQ 1..84
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_058636"
FT VARIANT 163
FT /note="Missing"
FT /id="VAR_046449"
FT VARIANT 306
FT /note="Q -> R (in ATITHS; decreased transcriptional
FT activity shown in a luciferase assay)"
FT /evidence="ECO:0000269|PubMed:33783914"
FT /id="VAR_085801"
FT CONFLICT 91..92
FT /note="TS -> H (in Ref. 1; CAA45907)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="A -> R (in Ref. 3; AAA57161)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="A -> AGAG (in Ref. 3; AAA57161)"
FT /evidence="ECO:0000305"
FT CONFLICT 146..147
FT /note="GP -> AA (in Ref. 1; CAA45907)"
FT /evidence="ECO:0000305"
FT CONFLICT 152..153
FT /note="GP -> PR (in Ref. 1; CAA45907)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="P -> PG (in Ref. 2; AAA65605, 3; AAA57161 and 1;
FT CAA45907)"
FT /evidence="ECO:0000305"
FT CONFLICT 170..171
FT /note="GP -> AA (in Ref. 1; CAA45907)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="G -> A (in Ref. 1; CAA45907)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="A -> S (in Ref. 2; AAA65605)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="Missing (in Ref. 1; CAA45907)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="A -> R (in Ref. 1; CAA45907)"
FT /evidence="ECO:0000305"
FT CONFLICT 272..274
FT /note="AER -> GS (in Ref. 1; CAA45907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 42697 MW; 6EDC2A2082F95F23 CRC64;
MMSMNSKQPH FAMHPTLPEH KYPSLHSSSE AIRRACLPTP PLQSNLFASL DETLLARAEA
LAAVDIAVSQ GKSHPFKPDA TYHTMNSVPC TSTSTVPLAH HHHHHHHHQA LEPGDLLDHI
SSPSLALMAG AGGAGAAAGG GGAHDGPGGG GGPGGGGGPG GGPGGGGGGG PGGGGGGPGG
GLLGGSAHPH PHMHSLGHLS HPAAAAAMNM PSGLPHPGLV AAAAHHGAAA AAAAAAAGQV
AAASAAAAVV GAAGLASICD SDTDPRELEA FAERFKQRRI KLGVTQADVG SALANLKIPG
VGSLSQSTIC RFESLTLSHN NMIALKPILQ AWLEEAEGAQ REKMNKPELF NGGEKKRKRT
SIAAPEKRSL EAYFAVQPRP SSEKIAAIAE KLDLKKNVVR VWFCNQRQKQ KRMKFSATY
