LHX4_HUMAN
ID LHX4_HUMAN Reviewed; 390 AA.
AC Q969G2; Q8NHE0; Q8NHM1; Q8TCJ1; Q8WWX2; Q969W2;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=LIM/homeobox protein Lhx4;
DE Short=LIM homeobox protein 4;
GN Name=LHX4;
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], AND CHROMOSOMAL TRANSLOCATION WITH IGHG1.
RX PubMed=12118377; DOI=10.1038/sj.onc.1205628;
RA Kawamata N., Sakajiri S., Sugimoto K.J., Isobe Y., Kobayashi H., Oshimi K.;
RT "A novel chromosomal translocation t(1;14)(q25;q32) in pre-B acute
RT lymphoblastic leukemia involves the LIM homeodomain protein gene, Lhx4.";
RL Oncogene 21:4983-4991(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu Y., Zhou Y., Wang J., Yuan J., Qiang B., Fan M.;
RT "Isolation and cloning of a novel cDNA encoding human LIM homeobox 4
RT protein.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Machinis K., Pantel J., Duquesnoy P., Netchine I., Sobrier M.-L.,
RA Dastot F., Amselem S.;
RT "Human LIM homeobox protein 4 (LHX4) gene.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 23-390.
RC TISSUE=Placenta;
RA Muraki T., Nakamura K., Sakai T.;
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-390, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF
RP 152-390, AND DISEASE.
RX PubMed=11567216; DOI=10.1086/323764;
RA Machinis K., Pantel J., Netchine I., Leger J., Camand O.J.A.,
RA Sobrier M.-L., Dastot-Le Moal F., Duquesnoy P., Abitbol M., Czernichow P.,
RA Amselem S.;
RT "Syndromic short stature in patients with a germline mutation in the LIM
RT homeobox LHX4.";
RL Am. J. Hum. Genet. 69:961-968(2001).
RN [8] {ECO:0007744|PDB:5HOD}
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 156-216 IN COMPLEX WITH DNA, AND
RP DNA-BINDING.
RX PubMed=28473536; DOI=10.1126/science.aaj2239;
RA Yin Y., Morgunova E., Jolma A., Kaasinen E., Sahu B., Khund-Sayeed S.,
RA Das P.K., Kivioja T., Dave K., Zhong F., Nitta K.R., Taipale M., Popov A.,
RA Ginno P.A., Domcke S., Yan J., Schubeler D., Vinson C., Taipale J.;
RT "Impact of cytosine methylation on DNA binding specificities of human
RT transcription factors.";
RL Science 356:0-0(2017).
RN [9]
RP VARIANT CPHD4 THR-389.
RX PubMed=17527005; DOI=10.1507/endocrj.k06-200;
RA Tajima T., Hattori T., Nakajima T., Okuhara K., Tsubaki J., Fujieda K.;
RT "A novel missense mutation (P366T) of the LHX4 gene causes severe combined
RT pituitary hormone deficiency with pituitary hypoplasia, ectopic posterior
RT lobe and a poorly developed sella turcica.";
RL Endocr. J. 54:637-641(2007).
RN [10]
RP VARIANTS CPHD4 CYS-84; ARG-190 AND PRO-210, AND CHARACTERIZATION OF
RP VARIANTS CPHD4 CYS-84; ARG-190 AND PRO-210.
RX PubMed=18073311; DOI=10.1210/jc.2007-1525;
RA Pfaeffle R.W., Hunter C.S., Savage J.J., Duran-Prado M., Mullen R.D.,
RA Neeb Z.P., Eiholzer U., Hesse V., Haddad N.G., Stobbe H.M., Blum W.F.,
RA Weigel J.F.W., Rhodes S.J.;
RT "Three novel missense mutations within the LHX4 gene are associated with
RT variable pituitary hormone deficiencies.";
RL J. Clin. Endocrinol. Metab. 93:1062-1071(2008).
CC -!- FUNCTION: May play a critical role in the development of respiratory
CC control mechanisms and in the normal growth and maturation of the lung.
CC Binds preferentially to methylated DNA (PubMed:28473536). {ECO:0000250,
CC ECO:0000269|PubMed:28473536}.
CC -!- INTERACTION:
CC Q969G2; P36404: ARL2; NbExp=3; IntAct=EBI-2865388, EBI-752365;
CC Q969G2; O15169: AXIN1; NbExp=3; IntAct=EBI-2865388, EBI-710484;
CC Q969G2; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-2865388, EBI-11524452;
CC Q969G2; Q8IYS8: BOD1L2; NbExp=3; IntAct=EBI-2865388, EBI-12118438;
CC Q969G2; Q00526: CDK3; NbExp=3; IntAct=EBI-2865388, EBI-1245761;
CC Q969G2; Q8N2Z9: CENPS; NbExp=3; IntAct=EBI-2865388, EBI-5529649;
CC Q969G2; Q9Y6H1: CHCHD2; NbExp=4; IntAct=EBI-2865388, EBI-2321769;
CC Q969G2; Q9BR76: CORO1B; NbExp=3; IntAct=EBI-2865388, EBI-351152;
CC Q969G2; Q5QP82: DCAF10; NbExp=3; IntAct=EBI-2865388, EBI-723230;
CC Q969G2; Q96LJ7: DHRS1; NbExp=3; IntAct=EBI-2865388, EBI-746300;
CC Q969G2; P59910: DNAJB13; NbExp=3; IntAct=EBI-2865388, EBI-11514233;
CC Q969G2; Q96HE7: ERO1A; NbExp=3; IntAct=EBI-2865388, EBI-2564539;
CC Q969G2; Q6P4F2: FDX2; NbExp=3; IntAct=EBI-2865388, EBI-10252800;
CC Q969G2; Q00444: HOXC5; NbExp=3; IntAct=EBI-2865388, EBI-11955357;
CC Q969G2; Q9C086: INO80B; NbExp=3; IntAct=EBI-2865388, EBI-715611;
CC Q969G2; P61371: ISL1; NbExp=3; IntAct=EBI-2865388, EBI-3906896;
CC Q969G2; Q96A47: ISL2; NbExp=4; IntAct=EBI-2865388, EBI-18560216;
CC Q969G2; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-2865388, EBI-6426443;
CC Q969G2; Q86U70-2: LDB1; NbExp=4; IntAct=EBI-2865388, EBI-11979761;
CC Q969G2; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-2865388, EBI-2341787;
CC Q969G2; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-2865388, EBI-726739;
CC Q969G2; Q9HD23-2: MRS2; NbExp=3; IntAct=EBI-2865388, EBI-13374520;
CC Q969G2; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-2865388, EBI-744402;
CC Q969G2; Q9Y5N6: ORC6; NbExp=8; IntAct=EBI-2865388, EBI-374840;
CC Q969G2; Q9NR21-1: PARP11; NbExp=3; IntAct=EBI-2865388, EBI-17644640;
CC Q969G2; P28069: POU1F1; NbExp=3; IntAct=EBI-2865388, EBI-8673859;
CC Q969G2; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-2865388, EBI-2798044;
CC Q969G2; P57086: SCAND1; NbExp=3; IntAct=EBI-2865388, EBI-745846;
CC Q969G2; O60880: SH2D1A; NbExp=7; IntAct=EBI-2865388, EBI-6983382;
CC Q969G2; Q9BV90: SNRNP25; NbExp=6; IntAct=EBI-2865388, EBI-9675976;
CC Q969G2; P09012: SNRPA; NbExp=3; IntAct=EBI-2865388, EBI-607085;
CC Q969G2; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-2865388, EBI-8451480;
CC Q969G2; Q7Z4G4: TRMT11; NbExp=3; IntAct=EBI-2865388, EBI-2515608;
CC Q969G2; Q7Z6J9: TSEN54; NbExp=3; IntAct=EBI-2865388, EBI-2559824;
CC Q969G2; Q5T7W7: TSTD2; NbExp=3; IntAct=EBI-2865388, EBI-8994397;
CC Q969G2; Q86UY0: TXNDC5; NbExp=3; IntAct=EBI-2865388, EBI-2825190;
CC Q969G2; O75604: USP2; NbExp=4; IntAct=EBI-2865388, EBI-743272;
CC Q969G2; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-2865388, EBI-712969;
CC Q969G2; P25490: YY1; NbExp=4; IntAct=EBI-2865388, EBI-765538;
CC Q969G2; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-2865388, EBI-2515601;
CC Q969G2; P36508: ZNF76; NbExp=3; IntAct=EBI-2865388, EBI-7254550;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
CC -!- DISEASE: Pituitary hormone deficiency, combined, 4 (CPHD4)
CC [MIM:262700]: Combined pituitary hormone deficiency is defined as the
CC impaired production of growth hormone and one or more of the other five
CC anterior pituitary hormones. CPHD4 is characterized by complete or
CC partial deficiencies of growth hormone, thyroid-stimulating hormone,
CC luteinizing hormone, follicle stimulating hormone and
CC adrenocorticotropic hormone. Clinical features include short stature,
CC cerebellar defects, and small sella turcica.
CC {ECO:0000269|PubMed:17527005, ECO:0000269|PubMed:18073311}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Note=A chromosomal aberration involving LHX4 may be a cause of
CC acute lymphoblastic leukemia. Translocation t(1;14)(q25;q32) with
CC IGHG1. {ECO:0000269|PubMed:11567216}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB62817.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY053457; AAL07260.1; -; mRNA.
DR EMBL; AF179849; AAK70923.1; -; mRNA.
DR EMBL; AF405430; AAM91896.1; -; Genomic_DNA.
DR EMBL; AF405425; AAM91896.1; JOINED; Genomic_DNA.
DR EMBL; AF405426; AAM91896.1; JOINED; Genomic_DNA.
DR EMBL; AF405427; AAM91896.1; JOINED; Genomic_DNA.
DR EMBL; AF405428; AAM91896.1; JOINED; Genomic_DNA.
DR EMBL; AF405429; AAM91896.1; JOINED; Genomic_DNA.
DR EMBL; AL139141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011759; AAH11759.1; -; mRNA.
DR EMBL; AB055703; BAB62817.1; ALT_INIT; mRNA.
DR EMBL; AB037683; BAC01272.1; -; mRNA.
DR EMBL; AF282899; AAK69169.1; -; mRNA.
DR EMBL; AH011598; AAM19349.1; -; Genomic_DNA.
DR CCDS; CCDS1338.1; -.
DR RefSeq; NP_203129.1; NM_033343.3.
DR PDB; 5HOD; X-ray; 2.68 A; A/D=156-216.
DR PDBsum; 5HOD; -.
DR AlphaFoldDB; Q969G2; -.
DR SMR; Q969G2; -.
DR BioGRID; 124635; 167.
DR DIP; DIP-29454N; -.
DR IntAct; Q969G2; 147.
DR MINT; Q969G2; -.
DR STRING; 9606.ENSP00000263726; -.
DR iPTMnet; Q969G2; -.
DR PhosphoSitePlus; Q969G2; -.
DR BioMuta; LHX4; -.
DR DMDM; 209572644; -.
DR MassIVE; Q969G2; -.
DR PaxDb; Q969G2; -.
DR PeptideAtlas; Q969G2; -.
DR PRIDE; Q969G2; -.
DR Antibodypedia; 20587; 385 antibodies from 28 providers.
DR DNASU; 89884; -.
DR Ensembl; ENST00000263726.4; ENSP00000263726.2; ENSG00000121454.6.
DR GeneID; 89884; -.
DR KEGG; hsa:89884; -.
DR MANE-Select; ENST00000263726.4; ENSP00000263726.2; NM_033343.4; NP_203129.1.
DR UCSC; uc001goe.3; human.
DR CTD; 89884; -.
DR DisGeNET; 89884; -.
DR GeneCards; LHX4; -.
DR HGNC; HGNC:21734; LHX4.
DR HPA; ENSG00000121454; Tissue enriched (retina).
DR MalaCards; LHX4; -.
DR MIM; 262700; phenotype.
DR MIM; 602146; gene.
DR neXtProt; NX_Q969G2; -.
DR OpenTargets; ENSG00000121454; -.
DR Orphanet; 95494; Combined pituitary hormone deficiencies, genetic forms.
DR Orphanet; 226307; Hypothyroidism due to deficient transcription factors involved in pituitary development or function.
DR Orphanet; 95496; Pituitary stalk interruption syndrome.
DR Orphanet; 85442; Short stature-pituitary and cerebellar defects-small sella turcica syndrome.
DR PharmGKB; PA134962876; -.
DR VEuPathDB; HostDB:ENSG00000121454; -.
DR eggNOG; KOG4577; Eukaryota.
DR GeneTree; ENSGT00940000157906; -.
DR HOGENOM; CLU_027802_5_0_1; -.
DR InParanoid; Q969G2; -.
DR OMA; GLDYTMD; -.
DR OrthoDB; 1174754at2759; -.
DR PhylomeDB; Q969G2; -.
DR TreeFam; TF315442; -.
DR PathwayCommons; Q969G2; -.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR SignaLink; Q969G2; -.
DR SIGNOR; Q969G2; -.
DR BioGRID-ORCS; 89884; 16 hits in 1095 CRISPR screens.
DR ChiTaRS; LHX4; human.
DR GeneWiki; LHX4; -.
DR GenomeRNAi; 89884; -.
DR Pharos; Q969G2; Tbio.
DR PRO; PR:Q969G2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q969G2; protein.
DR Bgee; ENSG00000121454; Expressed in buccal mucosa cell and 108 other tissues.
DR ExpressionAtlas; Q969G2; baseline and differential.
DR Genevisible; Q969G2; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0021526; P:medial motor column neuron differentiation; IEA:Ensembl.
DR GO; GO:0008045; P:motor neuron axon guidance; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0001890; P:placenta development; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00412; LIM; 2.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00132; LIM; 2.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosomal rearrangement; Disease variant; DNA-binding;
KW Dwarfism; Homeobox; LIM domain; Metal-binding; Nucleus; Proto-oncogene;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..390
FT /note="LIM/homeobox protein Lhx4"
FT /id="PRO_0000075787"
FT DOMAIN 28..87
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 88..150
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DNA_BIND 157..216
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 161..181
FT /note="Interaction with DNA"
FT /evidence="ECO:0000305|PubMed:28473536"
FT REGION 199..211
FT /note="Interaction with 5-mCpG DNA"
FT /evidence="ECO:0000305|PubMed:28473536"
FT REGION 230..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 84
FT /note="R -> C (in CPHD4; has impaired activity on CGA,
FT POU1F1 and TSHB promoters but exhibits normal DNA binding
FT to the CGA pituitary glycoprotein basal element (PGBE) and
FT interaction with the POU1F1 protein; dbSNP:rs121912642)"
FT /evidence="ECO:0000269|PubMed:18073311"
FT /id="VAR_058715"
FT VARIANT 190
FT /note="L -> R (in CPHD4; the mutant protein is inactive in
FT DNA binding and pituitary gene activation assays;
FT dbSNP:rs121912643)"
FT /evidence="ECO:0000269|PubMed:18073311"
FT /id="VAR_058716"
FT VARIANT 210
FT /note="A -> P (in CPHD4; the mutant protein is inactive in
FT DNA binding and pituitary gene activation assays;
FT dbSNP:rs121912641)"
FT /evidence="ECO:0000269|PubMed:18073311"
FT /id="VAR_058717"
FT VARIANT 328
FT /note="N -> S (in dbSNP:rs7536561)"
FT /id="VAR_046661"
FT VARIANT 389
FT /note="P -> T (in CPHD4; dbSNP:rs145433128)"
FT /evidence="ECO:0000269|PubMed:17527005"
FT /id="VAR_063241"
FT CONFLICT 335
FT /note="D -> G (in Ref. 1; AAL07260)"
FT /evidence="ECO:0000305"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:5HOD"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:5HOD"
FT HELIX 198..214
FT /evidence="ECO:0007829|PDB:5HOD"
SQ SEQUENCE 390 AA; 43124 MW; 6499F38E78B79FD1 CRC64;
MMQSATVPAE GAVKGLPEML GVPMQQIPQC AGCNQHILDK FILKVLDRHW HSSCLKCADC
QMQLADRCFS RAGSVYCKED FFKRFGTKCT ACQQGIPPTQ VVRKAQDFVY HLHCFACIIC
NRQLATGDEF YLMEDGRLVC KEDYETAKQN DDSEAGAKRP RTTITAKQLE TLKNAYKNSP
KPARHVREQL SSETGLDMRV VQVWFQNRRA KEKRLKKDAG RHRWGQFYKS VKRSRGSSKQ
EKESSAEDCG VSDSELSFRE DQILSELGHT NRIYGNVGDV TGGQLMNGSF SMDGTGQSYQ
DLRDGSPYGI PQSPSSISSL PSHAPLLNGL DYTVDSNLGI IAHAGQGVSQ TLRAMAGGPT
SDISTGSSVG YPDFPTSPGS WLDEMDHPPF
