ZBED4_HUMAN
ID ZBED4_HUMAN Reviewed; 1171 AA.
AC O75132; B2RZH1; Q1ECU0; Q9UGG8;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Zinc finger BED domain-containing protein 4;
GN Name=ZBED4; Synonyms=KIAA0637;
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 [LARGE SCALE MRNA], AND VARIANT VAL-420.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-420.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-420.
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 [5]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=17209048; DOI=10.1074/jbc.m607180200;
RA Yamashita D., Komori H., Higuchi Y., Yamaguchi T., Osumi T., Hirose F.;
RT "Human DNA replication-related element binding factor (hDREF) self-
RT association via hATC domain is necessary for its nuclear accumulation and
RT DNA binding.";
RL J. Biol. Chem. 282:7563-7575(2007).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19369242; DOI=10.1167/iovs.08-2751;
RA Saghizadeh M., Akhmedov N.B., Yamashita C.K., Gribanova Y., Theendakara V.,
RA Mendoza E., Nelson S.F., Ljubimov A.V., Farber D.B.;
RT "ZBED4, a BED-type zinc-finger protein in the cones of the human retina.";
RL Invest. Ophthalmol. Vis. Sci. 50:3580-3588(2009).
RN [7]
RP INTERACTION WITH MYH9 AND SAFB, AND SUBCELLULAR LOCATION.
RX PubMed=22693546; DOI=10.1371/journal.pone.0035317;
RA Mokhonov V.V., Theendakara V.P., Gribanova Y.E., Ahmedli N.B., Farber D.B.;
RT "Sequence-specific binding of recombinant Zbed4 to DNA: insights into Zbed4
RT participation in gene transcription and its association with other
RT proteins.";
RL PLoS ONE 7:e35317-e35317(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-43 AND LYS-489, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
CC -!- FUNCTION: Transcriptional regulator that binds to poly-guanine tracts
CC in gene promoters and activates transcription (By similarity). Able to
CC bind single- and double-stranded DNA and RNA (By similarity).
CC {ECO:0000250|UniProtKB:Q80WQ9}.
CC -!- SUBUNIT: Homodimer; via C-terminus (PubMed:17209048). Interacts with
CC MYH9 (PubMed:22693546). Interacts with SAFB/SAFB1 (PubMed:22693546).
CC {ECO:0000269|PubMed:17209048, ECO:0000269|PubMed:22693546}.
CC -!- INTERACTION:
CC O75132; P50222: MEOX2; NbExp=3; IntAct=EBI-2860059, EBI-748397;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17209048,
CC ECO:0000269|PubMed:19369242, ECO:0000269|PubMed:22693546}. Cytoplasm
CC {ECO:0000269|PubMed:17209048, ECO:0000269|PubMed:22693546}.
CC Photoreceptor inner segment {ECO:0000269|PubMed:19369242}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, heart, lung, and weakly
CC expressed in brain, liver, muscle, placenta and small intestine
CC (PubMed:19369242). Expressed in the retina, found in the cone
CC photoreceptors, Mueller cells, cone pedicles and in the innermost
CC retinal layer (PubMed:19369242). {ECO:0000269|PubMed:19369242}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31612.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB014537; BAA31612.2; ALT_INIT; mRNA.
DR EMBL; CR456387; CAG30273.1; -; mRNA.
DR EMBL; AL117328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117670; AAI17671.1; -; mRNA.
DR EMBL; BC167155; AAI67155.1; -; mRNA.
DR CCDS; CCDS33677.1; -.
DR PIR; T00380; T00380.
DR RefSeq; NP_055653.2; NM_014838.2.
DR AlphaFoldDB; O75132; -.
DR SMR; O75132; -.
DR BioGRID; 115219; 22.
DR IntAct; O75132; 16.
DR MINT; O75132; -.
DR STRING; 9606.ENSP00000216268; -.
DR iPTMnet; O75132; -.
DR PhosphoSitePlus; O75132; -.
DR BioMuta; ZBED4; -.
DR EPD; O75132; -.
DR jPOST; O75132; -.
DR MassIVE; O75132; -.
DR MaxQB; O75132; -.
DR PaxDb; O75132; -.
DR PeptideAtlas; O75132; -.
DR PRIDE; O75132; -.
DR ProteomicsDB; 49794; -.
DR Antibodypedia; 59180; 12 antibodies from 7 providers.
DR DNASU; 9889; -.
DR Ensembl; ENST00000216268.6; ENSP00000216268.4; ENSG00000100426.7.
DR GeneID; 9889; -.
DR KEGG; hsa:9889; -.
DR MANE-Select; ENST00000216268.6; ENSP00000216268.4; NM_014838.3; NP_055653.2.
DR UCSC; uc003bix.3; human.
DR CTD; 9889; -.
DR DisGeNET; 9889; -.
DR GeneCards; ZBED4; -.
DR HGNC; HGNC:20721; ZBED4.
DR HPA; ENSG00000100426; Low tissue specificity.
DR MIM; 612552; gene.
DR neXtProt; NX_O75132; -.
DR OpenTargets; ENSG00000100426; -.
DR PharmGKB; PA134948378; -.
DR VEuPathDB; HostDB:ENSG00000100426; -.
DR eggNOG; KOG1121; Eukaryota.
DR GeneTree; ENSGT00940000161365; -.
DR HOGENOM; CLU_006260_0_0_1; -.
DR InParanoid; O75132; -.
DR OMA; HMWRAHK; -.
DR OrthoDB; 223749at2759; -.
DR PhylomeDB; O75132; -.
DR TreeFam; TF322818; -.
DR PathwayCommons; O75132; -.
DR SignaLink; O75132; -.
DR BioGRID-ORCS; 9889; 16 hits in 1101 CRISPR screens.
DR ChiTaRS; ZBED4; human.
DR GenomeRNAi; 9889; -.
DR Pharos; O75132; Tdark.
DR PRO; PR:O75132; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O75132; protein.
DR Bgee; ENSG00000100426; Expressed in ganglionic eminence and 131 other tissues.
DR Genevisible; O75132; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:ARUK-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISS:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR InterPro; IPR008906; HATC_C_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR003656; Znf_BED.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR Pfam; PF02892; zf-BED; 4.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50808; ZF_BED; 4.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1171
FT /note="Zinc finger BED domain-containing protein 4"
FT /id="PRO_0000066563"
FT ZN_FING 115..172
FT /note="BED-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT ZN_FING 285..342
FT /note="BED-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT ZN_FING 456..512
FT /note="BED-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT ZN_FING 558..615
FT /note="BED-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT REGION 25..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1171
FT /note="Required for homodimerization and nuclear
FT accumulation"
FT /evidence="ECO:0000269|PubMed:17209048"
FT COMPBIAS 35..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 477
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 480
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 500
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 505
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 579
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 582
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 603
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 608
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 43
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 489
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 420
FT /note="I -> V (in dbSNP:rs910799)"
FT /evidence="ECO:0000269|PubMed:15461802,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9734811"
FT /id="VAR_027809"
FT CONFLICT 584
FT /note="R -> Q (in Ref. 4; AAI17671)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1171 AA; 130322 MW; 485746484E87B389 CRC64;
MENNLKTCPK EDGDFVSDKI KFKIEEEDDD GIPPDSLERM DFKSEQEDMK QTDSGGERAG
LGGTGCSCKP PGKYLSAESE DDYGALFSQY SSTLYDVAME AVTQSLLSSR NMSSRKKSPA
WKHFFISPRD STKAICMYCV KEFSRGKNEK DLSTSCLMRH VRRAHPTVLI QENGSVSAVS
SFPSPSLLLP PQPADAGDLS TILSPIKLVQ KVASKIPSPD RITEESVSVV SSEEISSDMS
VSEKCGREEA LVGSSPHLPA LHYDEPAENL AEKSLPLPKS TSGSRRRSAV WKHFYLSPLD
NSKAVCIHCM NEFSRGKNGK DLGTSCLIRH MWRAHRAIVL QENGGTGIPP LYSTPPTLLP
SLLPPEGELS SVSSSPVKPV RESPSASSSP DRLTEDLQSH LNPGDGLMED VAAFSSSDDI
GEASASSPEK QQADGLSPRL FESGAIFQQN KKVMKRLKSE VWHHFSLAPM DSLKAECRYC
GCAISRGKKG DVGTSCLMRH LYRRHPEVVG SQKGFLGASL ANSPYATLAS AESSSSKLTD
LPTVVTKNNQ VMFPVNSKKT SKLWNHFSIC SADSTKVVCL HCGRTISRGK KPTNLGTSCL
LRHLQRFHSN VLKTEVSETA RPSSPDTRVP RGTELSGASS FDDTNEKFYD SHPVAKKITS
LIAEMIALDL QPYSFVDNVG FNRLLEYLKP QYSLPAPSYF SRTAIPGMYD NVKQIIMSHL
KEAESGVIHF TSGIWMSNQT REYLTLTAHW VSFESPARPR CDDHHCSALL DVSQVDCDYS
GNSIQKQLEC WWEAWVTSTG LQVGITVTDN ASIGKTLNEG EHSSVQCFSH TVNLIVSEAI
KSQRMVQNLL SLARKICERV HRSPKAKEKL AELQREYALP QHHLIQDVPS KWSTSFHMLE
RLIEQKRAIN EMSVECNFRE LISCDQWEVM QSVCRALKPF EAASREMSTQ MSTLSQVIPM
VHILNRKVEM LFEETMGIDT MLRSLKEAMV SRLSATLHDP RYVFATLLDP RYKASLFTEE
EAEQYKQDLI RELELMNSTS EDVAASHRCD AGSPSKDSAA EENLWSLVAK VKKKDPREKL
PEAMVLAYLE EEVLEHSCDP LTYWNLKKAS WPGLSALAVR FLGCPPSIVP SEKLFNTPTE
NGSLGQSRLM MEHFEKLIFL KVNLPLIYFQ Y
