BNC2_HUMAN
ID BNC2_HUMAN Reviewed; 1099 AA.
AC Q6ZN30; B1APG9; Q6T3A3; Q8NAR2; Q9H6J0; Q9NXV0;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Zinc finger protein basonuclin-2;
GN Name=BNC2 {ECO:0000312|HGNC:HGNC:30988};
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] {ECO:0000305, ECO:0000312|EMBL:BAD18545.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon {ECO:0000312|EMBL:BAA90908.1},
RC Kidney epithelium {ECO:0000312|EMBL:BAB15269.1},
RC Teratocarcinoma {ECO:0000312|EMBL:BAC03837.1}, and
RC Tongue {ECO:0000312|EMBL:BAD18545.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAR99389.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 73-1099 (ISOFORM 1), SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=15081112; DOI=10.1016/j.ygeno.2003.11.009;
RA Romano R.-A., Li H., Tummala R., Maul R., Sinha S.;
RT "Identification of Basonuclin2, a DNA-binding zinc-finger protein expressed
RT in germ tissues and skin keratinocytes.";
RL Genomics 83:821-833(2004).
RN [4] {ECO:0000305}
RP PROBABLE FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14988505; DOI=10.1073/pnas.0400268101;
RA Vanhoutteghem A., Djian P.;
RT "Basonuclin 2: an extremely conserved homolog of the zinc finger protein
RT basonuclin.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3468-3473(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-277; LYS-396; LYS-416; LYS-421;
RP LYS-641; LYS-894 AND LYS-919, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [7]
RP INVOLVEMENT IN LUTO, VARIANTS LUTO ILE-158; GLN-346; 853-ARG--ASP-1099 DEL
RP AND ARG-888, FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=31051115; DOI=10.1016/j.ajhg.2019.03.023;
RA Kolvenbach C.M., Dworschak G.C., Frese S., Japp A.S., Schuster P.,
RA Wenzlitschke N., Yilmaz O., Lopes F.M., Pryalukhin A., Schierbaum L.,
RA van der Zanden L.F.M., Kause F., Schneider R., Taranta-Janusz K.,
RA Szczepanska M., Pawlaczyk K., Newman W.G., Beaman G.M., Stuart H.M.,
RA Cervellione R.M., Feitz W.F.J., van Rooij I.A.L.M., Schreuder M.F.,
RA Steffens M., Weber S., Merz W.M., Feldkoetter M., Hoppe B., Thiele H.,
RA Altmueller J., Berg C., Kristiansen G., Ludwig M., Reutter H., Woolf A.S.,
RA Hildebrandt F., Grote P., Zaniew M., Odermatt B., Hilger A.C.;
RT "Rare variants in BNC2 are implicated in autosomal-dominant congenital
RT lower urinary-tract obstruction.";
RL Am. J. Hum. Genet. 104:994-1006(2019).
CC -!- FUNCTION: Probable transcription factor specific for skin
CC keratinocytes. May play a role in the differentiation of spermatozoa
CC and oocytes (PubMed:14988505). May also play an important role in early
CC urinary-tract development (PubMed:31051115).
CC {ECO:0000269|PubMed:14988505, ECO:0000269|PubMed:31051115}.
CC -!- INTERACTION:
CC Q6ZN30; P25800: LMO1; NbExp=3; IntAct=EBI-6115618, EBI-8639312;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15081112}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15081112};
CC IsoId=Q6ZN30-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q6ZN30-2; Sequence=VSP_051873, VSP_051874;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, uterus and small
CC intestine, and weakly expressed in colon and prostate. Also expressed
CC in skin, primary keratinocytes, immortalized keratinocytes, and HeLa
CC and HEK293 cells. Not detected in blood, thymus, spleen or Hep-G2
CC cells. {ECO:0000269|PubMed:14988505, ECO:0000269|PubMed:15081112}.
CC -!- DEVELOPMENTAL STAGE: In a 7-week embryo, expressed in the urogenital
CC sinus, the precursor of the bladder, and its outflow tract. The most
CC prominent expression is in the primitive urothelium, and there is
CC weaker expression in the surrounding mesenchyme. Expression also
CC detected in the urothelium of the adult male urethra.
CC {ECO:0000269|PubMed:31051115}.
CC -!- DISEASE: Lower urinary tract obstruction, congenital (LUTO)
CC [MIM:618612]: A disorder characterized by urinary bladder outflow
CC obstruction, which can represent an anatomical blockage or a functional
CC obstruction. The most common anatomical causes are posterior urethral
CC valves at the level of the prostatic urethra, a lesion unique to males.
CC Less common are anterior urethral valves, also called urethral atresia,
CC that can occur in either sex. LUTO is an autosomal dominant disease
CC with variable expression. {ECO:0000269|PubMed:31051115}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR99389.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA90908.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15269.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC03837.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK000050; BAA90908.1; ALT_INIT; mRNA.
DR EMBL; AK025882; BAB15269.1; ALT_INIT; mRNA.
DR EMBL; AK092247; BAC03837.1; ALT_INIT; mRNA.
DR EMBL; AK131398; BAD18545.1; -; mRNA.
DR EMBL; AL449983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY438376; AAR99389.1; ALT_INIT; mRNA.
DR CCDS; CCDS6482.2; -. [Q6ZN30-1]
DR RefSeq; NP_060107.3; NM_017637.5. [Q6ZN30-1]
DR AlphaFoldDB; Q6ZN30; -.
DR BioGRID; 120155; 8.
DR IntAct; Q6ZN30; 4.
DR STRING; 9606.ENSP00000370047; -.
DR iPTMnet; Q6ZN30; -.
DR PhosphoSitePlus; Q6ZN30; -.
DR BioMuta; BNC2; -.
DR DMDM; 74762393; -.
DR EPD; Q6ZN30; -.
DR MassIVE; Q6ZN30; -.
DR MaxQB; Q6ZN30; -.
DR PaxDb; Q6ZN30; -.
DR PeptideAtlas; Q6ZN30; -.
DR PRIDE; Q6ZN30; -.
DR ProteomicsDB; 67969; -. [Q6ZN30-1]
DR ProteomicsDB; 67970; -. [Q6ZN30-2]
DR Antibodypedia; 10169; 83 antibodies from 19 providers.
DR DNASU; 54796; -.
DR Ensembl; ENST00000380672.9; ENSP00000370047.3; ENSG00000173068.18. [Q6ZN30-1]
DR Ensembl; ENST00000484726.5; ENSP00000431516.1; ENSG00000173068.18. [Q6ZN30-2]
DR GeneID; 54796; -.
DR KEGG; hsa:54796; -.
DR MANE-Select; ENST00000380672.9; ENSP00000370047.3; NM_017637.6; NP_060107.3.
DR UCSC; uc003zml.4; human. [Q6ZN30-1]
DR CTD; 54796; -.
DR DisGeNET; 54796; -.
DR GeneCards; BNC2; -.
DR HGNC; HGNC:30988; BNC2.
DR HPA; ENSG00000173068; Tissue enhanced (endometrium, ovary, smooth muscle).
DR MalaCards; BNC2; -.
DR MIM; 608669; gene.
DR MIM; 618612; phenotype.
DR neXtProt; NX_Q6ZN30; -.
DR OpenTargets; ENSG00000173068; -.
DR Orphanet; 93110; Posterior urethral valve.
DR PharmGKB; PA134953132; -.
DR VEuPathDB; HostDB:ENSG00000173068; -.
DR eggNOG; ENOG502QR8N; Eukaryota.
DR GeneTree; ENSGT00390000005844; -.
DR InParanoid; Q6ZN30; -.
DR OMA; KMDTPAI; -.
DR OrthoDB; 96985at2759; -.
DR PhylomeDB; Q6ZN30; -.
DR TreeFam; TF350399; -.
DR PathwayCommons; Q6ZN30; -.
DR SignaLink; Q6ZN30; -.
DR BioGRID-ORCS; 54796; 19 hits in 1095 CRISPR screens.
DR ChiTaRS; BNC2; human.
DR GeneWiki; BNC2; -.
DR GenomeRNAi; 54796; -.
DR Pharos; Q6ZN30; Tbio.
DR PRO; PR:Q6ZN30; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q6ZN30; protein.
DR Bgee; ENSG00000173068; Expressed in germinal epithelium of ovary and 162 other tissues.
DR ExpressionAtlas; Q6ZN30; baseline and differential.
DR Genevisible; Q6ZN30; HS.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000182; F:rDNA binding; IEA:Ensembl.
DR GO; GO:0003416; P:endochondral bone growth; IEA:Ensembl.
DR GO; GO:0060485; P:mesenchyme development; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0043586; P:tongue development; IEA:Ensembl.
DR InterPro; IPR040436; Disconnected-like.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15021; PTHR15021; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1099
FT /note="Zinc finger protein basonuclin-2"
FT /id="PRO_0000046934"
FT ZN_FING 441..464
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 833..856
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1035..1058
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1063..1090
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 45..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..663
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 396
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 416
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 421
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 641
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 894
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 919
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 881..903
FT /note="HSANINLHRKLLTKELDDMGLDS -> YWEKSNEQNGLLVSWGETLSSLK
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_051873"
FT VAR_SEQ 904..1099
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_051874"
FT VARIANT 158
FT /note="T -> I (in LUTO; unknown pathological significance;
FT dbSNP:rs144242525)"
FT /evidence="ECO:0000269|PubMed:31051115"
FT /id="VAR_083492"
FT VARIANT 346
FT /note="E -> Q (in LUTO; unknown pathological significance;
FT dbSNP:rs945575406)"
FT /evidence="ECO:0000269|PubMed:31051115"
FT /id="VAR_083493"
FT VARIANT 550
FT /note="L -> V (in dbSNP:rs4961490)"
FT /id="VAR_052707"
FT VARIANT 782
FT /note="T -> A (in dbSNP:rs3739714)"
FT /id="VAR_033543"
FT VARIANT 853..1099
FT /note="Missing (in LUTO; dbSNP:rs1350162888)"
FT /evidence="ECO:0000269|PubMed:31051115"
FT /id="VAR_083494"
FT VARIANT 888
FT /note="H -> R (in LUTO; dbSNP:rs1563774686)"
FT /evidence="ECO:0000269|PubMed:31051115"
FT /id="VAR_083495"
FT CONFLICT 560
FT /note="F -> L (in Ref. 1; BAC03837)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="K -> T (in Ref. 1; BAC03837)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="G -> E (in Ref. 1; BAB15269)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1099 AA; 122330 MW; B1601EACD158D3D3 CRC64;
MAHLGPTPPP HSLNYKSEDR LSEQDWPAYF KVPCCGVDTS QIESEEAEVD VRERETQRDR
EPKRARDLTL RDSCTDNSMQ FGTRTTTAEP GFMGTWQNAD TNLLFRMSQQ AIRCTLVNCT
CECFQPGKIN LRTCDQCKHG WVAHALDKLS TQHLYHPTQV EIVQSNVVFD ISSLMLYGTQ
AVPVRLKILL DRLFSVLKQE EVLHILHGLG WTLRDYVRGY ILQDAAGKVL DRWAIMSREE
EIITLQQFLR FGETKSIVEL MAIQEKEGQA VAVPSSKTDS DIRTFIESNN RTRSPSLLAH
LENSNPSSIH HFENIPNSLA FLLPFQYINP VSAPLLGLPP NGLLLEQPGL RLREPSLSTQ
NEYNESSESE VSPTPYKNDQ TPNRNALTSI TNVEPKTEPA CVSPIQNSAP VSDLTKTEHP
KSSFRIHRMR RMGSASRKGR VFCNACGKTF YDKGTLKIHY NAVHLKIKHR CTIEGCNMVF
SSLRSRNRHS ANPNPRLHMP MLRNNRDKDL IRATSGAATP VIASTKSNLA LTSPGRPPMG
FTTPPLDPVL QNPLPSQLVF SGLKTVQPVP PFYRSLLTPG EMVSPPTSLP TSPIIPTSGT
IEQHPPPPSE PVVPAVMMAT HEPSADLAPK KKPRKSSMPV KIEKEIIDTA DEFDDEDDDP
NDGGAVVNDM SHDNHCHSQE EMSPGMSVKD FSKHNRTRCI SRTEIRRADS MTSEDQEPER
DYENESESSE PKLGEESMEG DEHIHSEVSE KVLMNSERPD ENHSEPSHQD VIKVKEEFTD
PTYDMFYMSQ YGLYNGGGAS MAALHESFTS SLNYGSPQKF SPEGDLCSSP DPKICYVCKK
SFKSSYSVKL HYRNVHLKEM HVCTVAGCNA AFPSRRSRDR HSANINLHRK LLTKELDDMG
LDSSQPSLSK DLRDEFLVKI YGAQHPMGLD VREDASSPAG TEDSHLNGYG RGMAEDYMVL
DLSTTSSLQS SSSIHSSRES DAGSDEGILL DDIDGASDSG ESAHKAEAPA LPGSLGAEVS
GSLMFSSLSG SNGGIMCNIC HKMYSNKGTL RVHYKTVHLR EMHKCKVPGC NMMFSSVRSR
NRHSQNPNLH KNIPFTSVD
