HECD1_MOUSE
ID HECD1_MOUSE Reviewed; 2618 AA.
AC Q69ZR2;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=E3 ubiquitin-protein ligase HECTD1;
DE EC=2.3.2.26 {ECO:0000269|PubMed:22431752};
DE AltName: Full=HECT domain-containing protein 1;
DE AltName: Full=HECT-type E3 ubiquitin transferase HECTD1;
DE AltName: Full=Protein open mind;
GN Name=Hectd1; Synonyms=Kiaa1131, Opm;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1045-2618.
RC TISSUE=Thymus;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17442300; DOI=10.1016/j.ydbio.2007.03.018;
RA Zohn I.E., Anderson K.V., Niswander L.;
RT "The Hectd1 ubiquitin ligase is required for development of the head
RT mesenchyme and neural tube closure.";
RL Dev. Biol. 306:208-221(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-1389 AND SER-1572,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE, ACTIVE SITE,
RP AND MUTAGENESIS OF CYS-2587.
RX PubMed=22431752; DOI=10.1083/jcb.201105101;
RA Sarkar A.A., Zohn I.E.;
RT "Hectd1 regulates intracellular localization and secretion of Hsp90 to
RT control cellular behavior of the cranial mesenchyme.";
RL J. Cell Biol. 196:789-800(2012).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=33711283; DOI=10.1016/j.stem.2021.02.008;
RA Lv K., Gong C., Antony C., Han X., Ren J.G., Donaghy R., Cheng Y.,
RA Pellegrino S., Warren A.J., Paralkar V.R., Tong W.;
RT "HectD1 controls hematopoietic stem cell regeneration by coordinating
RT ribosome assembly and protein synthesis.";
RL Cell Stem Cell 28:1275-1290(2021).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates
CC (PubMed:22431752, PubMed:33711283). Mediates 'Lys-63'-linked
CC polyubiquitination of HSP90AA1 which leads to its intracellular
CC localization and reduced secretion (PubMed:22431752). Negatively
CC regulating HSP90AA1 secretion in cranial mesenchyme cells impairs their
CC emigration and is consequently essential for the correct development of
CC the cranial neural folds and neural tube closure (PubMed:17442300,
CC PubMed:22431752). Catalyzes ubiquitination and degradation of ZNF622,
CC an assembly factor for the ribosomal 60S subunit, in hematopoietic
CC cells, thereby promoting hematopoietic stem cell renewal
CC (PubMed:33711283). {ECO:0000269|PubMed:17442300,
CC ECO:0000269|PubMed:22431752, ECO:0000269|PubMed:33711283}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000269|PubMed:22431752};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:22431752}.
CC -!- SUBUNIT: Interacts with IGSF1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9ULT8}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed throughout early
CC development of the embryo. {ECO:0000269|PubMed:17442300}.
CC -!- DISRUPTION PHENOTYPE: Perinatal lethality, exencephaly, impaired neural
CC fold elevation, abnormal head mesenchyme morphology and defects in eye
CC and cranial vault morphology (PubMed:17442300, PubMed:22431752).
CC Cranial mesenchyme (CM) cells are larger, have an abnormal shape and an
CC abnormal emigration (PubMed:22431752). It is likely that the increased
CC motility of CM cells results in the exencephaly phenotype
CC (PubMed:22431752). Mice with a conditional deletion in hematopoietic
CC cells show reduced hematopoietic stem cell frequency and protein
CC translational rate upon proliferative stress, causing defects in
CC transplantation ability and ex vivo maintenance (PubMed:33711283).
CC {ECO:0000269|PubMed:17442300, ECO:0000269|PubMed:22431752,
CC ECO:0000269|PubMed:33711283}.
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily. {ECO:0000305}.
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DR EMBL; AC159644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC157213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK173106; BAD32384.1; -; mRNA.
DR AlphaFoldDB; Q69ZR2; -.
DR BMRB; Q69ZR2; -.
DR SMR; Q69ZR2; -.
DR STRING; 10090.ENSMUSP00000136449; -.
DR iPTMnet; Q69ZR2; -.
DR PhosphoSitePlus; Q69ZR2; -.
DR SwissPalm; Q69ZR2; -.
DR EPD; Q69ZR2; -.
DR jPOST; Q69ZR2; -.
DR MaxQB; Q69ZR2; -.
DR PaxDb; Q69ZR2; -.
DR PeptideAtlas; Q69ZR2; -.
DR PRIDE; Q69ZR2; -.
DR ProteomicsDB; 269579; -.
DR Antibodypedia; 5457; 121 antibodies from 25 providers.
DR Ensembl; ENSMUST00000179265; ENSMUSP00000136449; ENSMUSG00000035247.
DR MGI; MGI:2384768; Hectd1.
DR VEuPathDB; HostDB:ENSMUSG00000035247; -.
DR eggNOG; KOG4276; Eukaryota.
DR GeneTree; ENSGT00940000156572; -.
DR InParanoid; Q69ZR2; -.
DR PhylomeDB; Q69ZR2; -.
DR TreeFam; TF323674; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR ChiTaRS; Hectd1; mouse.
DR PRO; PR:Q69ZR2; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q69ZR2; protein.
DR Bgee; ENSMUSG00000035247; Expressed in rostral migratory stream and 245 other tissues.
DR ExpressionAtlas; Q69ZR2; baseline and differential.
DR Genevisible; Q69ZR2; MM.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0035904; P:aorta development; IMP:MGI.
DR GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
DR GO; GO:0003170; P:heart valve development; IMP:MGI.
DR GO; GO:0001779; P:natural killer cell differentiation; IMP:MGI.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; IMP:MGI.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0060708; P:spongiotrophoblast differentiation; IMP:MGI.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IMP:MGI.
DR GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR041200; FKBP3_BTHB.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR InterPro; IPR010606; Mib_Herc2.
DR InterPro; IPR037252; Mib_Herc2_sf.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR45670; PTHR45670; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF18410; BTHB; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF06701; MIB_HERC2; 1.
DR Pfam; PF07738; Sad1_UNC; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF159034; SSF159034; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS51416; MIB_HERC2; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Phosphoprotein; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..2618
FT /note="E3 ubiquitin-protein ligase HECTD1"
FT /id="PRO_0000396127"
FT REPEAT 396..425
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 427..456
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 460..492
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 580..613
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT DOMAIN 1271..1343
FT /note="MIB/HERC2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT DOMAIN 2156..2618
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 247..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1597..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1679..1761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1782..1806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2034..2108
FT /note="K-box"
FT /evidence="ECO:0000250"
FT REGION 2302..2323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1438..1462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1705
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1706..1726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2587
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104,
FT ECO:0000269|PubMed:22431752"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULT8"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULT8"
FT MOD_RES 1572
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1777
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULT8"
FT MOD_RES 2323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULT8"
FT MUTAGEN 2587
FT /note="C->G: Loss of activity. No effect on binding to
FT HSP90AA1."
FT /evidence="ECO:0000269|PubMed:22431752"
FT CONFLICT 1070
FT /note="F -> S (in Ref. 2; BAD32384)"
FT /evidence="ECO:0000305"
FT CONFLICT 2472..2474
FT /note="Missing (in Ref. 2; BAD32384)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2618 AA; 290086 MW; 8A06C9F973B11AFA CRC64;
MADVDPDTLL EWLQMGQGDE RDMQLIALEQ LCMLLLMSDN VDRCFETCPP RTFLPALCKI
FLDESAPDNV LEVTARAITY YLDVSAECTR RIVGVDGAIK ALCNRLVVVE LNNRTSRDLA
EQCVKVLELI CTRESGAVFE AGGLNCVLTF IRDSGHLVHK DTLHSAMAVV SRLCGKMEPQ
DSSLEICVES LSSLLKHEDH QVSDGALRCF ASLADRFTRR GVDPAPLAKH GLTEELLSRM
AAAGGTVSGP SSACKPGRST TGAPSAAADS KLSNQVSTIV SLLSTLCRGS PLVTHDLLRS
ELPDSIESAL QGDERCVLDT MRLVDLLLVL LFEGRKALPK SSAGSTGRIP GLRRLDSSGE
RSHRQLIDCI RSKDTDALID AIDTGAAFEV NFMDDVGQTL LNWASAFGTQ EMVEFLCERG
ADVNRGQRSS SLHYAACFGR PQVAKTLLRH GANPDLRDED GKTPLDKARE RGHSEVVAIL
QSPGDWMCPV NKGDDKKKKD TNKDEEECNE PRGDPEMAPL YLKRLLPVFA QTFQHTMLPS
IRKASLALIR KMIHFCSEAL LKEVCDSDVG HNLPTTLVEI TATVLDQEDD DDGHLLALQI
IRDLVDKGGD IFLDQLARLG VISKVSALAG PSSDDENEEE SKPEKEDEPQ EDAKELQQGK
PYHWRDWSII RGRDCLYIWS DAAALELSNG SNGWFRFILD GKLATMYSSG SPEGGSDSSE
SRSEFLEKLQ RARGQVKPST SSQPILSAPG PTKLTVGNWS LTCLKEGEIA IHNSDGQQAT
ILKEDLPGFV FESNRGTKHS FTAETSLGSE FVTGWTGKRG RKLKSKLEKT KQKVRTMARD
LYDDHFKAVE SMPRGVVVTL RNIATQLESS WELHTNRQCI EGENTWRDLM KTALENLIVL
LKDENTISPY EMCSSGLVQA LLTVLNNVSI FRATKQKQNE VLVERINVFK TAFSESEDDE
SYSRPAVALI RKLIAVLESI ERLPLHLYDT PGSTYNLQIL TRRLRFRLER APGETSLIDR
TGRMLKMEPL ATVESLEQYL LKMVAKQWYD FDRSSFVFVR KLREGQNFIF RHQHDFDENG
IIYWIGTNAK TAYEWVNPAA YGLVVVTSSE GRNLPYGRLE DILSRDNSAL NCHSNDDKNA
WFAIDLGVWV IPSAYTLRHA RGYGRSALRN WVFQVSKDGQ NWTSLYTHVD DCSLNEPGST
ATWPLDPAKD EKQGWRHVRL KQMGKNASGQ THYLSLSGFE LYGTVNGVCE DQLGKAAKEA
EANLRRQRRL VRSQVLKYMV PGARVIRGLD WKWRDQDGSP QGEGTVTGEL HNGWIDVTWD
AGGSNSYRMG AEGKFDLKLA PGYDPDTVAS PKPVSSTVSG TTQSWSSLVK NNCPDKTSAA
AGSSSRKGSS SSVCSVASSS DISLASTKTE RRSEIVMEHS IVSGADVHEP IVVLSSAENV
PQTEVGSSSS ASTSTLTAET GSENAERKLG PDSSVRAPGE SSAISMGIVS VSSPDVSSVS
ELTNKEAASQ RPLSSSASNR LSVSSLLAAG APMSSSASVP NLSSRETSSL ESFVRRVANI
ARTNATNNMN LSRSSSDNNT NTLGRNVMST ATSPLMGAQS FPNLTTPGTT STVTMSTSSV
TSSSNVATAT TVLSVGQSLS NTLTTSLTST SSESDTGQEA EYSLYDFLDS CRASTLLAEL
DDDEDLPEPD EEDDENEDDN QEDQEYEEVM ILRRPSLQRR AGSRSDVTHH VVTSQLPQVP
SGAGSRPVGE QEEEEYETKG GRRRAWDDDY VLKRQFSALV PAFDPRPGRT NVQQTTDLEI
PPPGTPHSEL LEEVECTPSP RLALTLKVTG LGTTREVELP LTNFRSTIFY YVQKLLQLSC
NGNVKSDKLR RIWEPTYTIM YREMKDSDKE KENGKMGCWS IEHVEQYLGT DELPKNDLIT
YLQKNADAAF LRHWKLTGTN KSIRKNRNCS QLIAAYKDFC EHGTKSGLNQ GAISSLQSSD
ILNLTKEQPQ AKAGNGQSPC GVEDVLQLLR ILYIVASDPY SRISQEDGDE QPQFTFPPDE
FTSKKITTKI LQQIEEPLAL ASGALPDWCE QLTSKCPFLI PFETRQLYFT CTAFGASRAI
VWLQNRREAT VERTRTTSSV RRDDPGEFRV GRLKHERVKV PRGESLMEWA ENVMQIHADR
KSVLEVEFLG EEGTGLGPTL EFYALVAAEF QRTDLGTWLC DDNFPDDESR HVDLGGGLKP
PGYYVQRSCG LFTAPFPQDS DELERITKLF HFLGIFLAKC IQDNRLVDLP ISKPFFKLMC
MGDIKSNMSK LIYESRGDRD LHCTESQSEA STEEGHDSLS VGSFEEDSKS EFILDPPKPK
PPAWFNGILT WEDFELVNPH RARFLKEIKD LAIKRRQILG NKSLSEDEKN TKLQELVLRN
PSGSGPPLSI EDLGLNFQFC PSSRIYGFTA VDLKPSGEDE MITMDNAEEY VDLMFDFCMH
TGIQKQMEAF RGNVDGFNKV FPMEKLSSFS HEEVQMILCG NQSPSWAAED IINYTEPKLG
YTRDSPGFLR FVRVLCGMSS DERKAFLQFT TGCSTLPPGG LANLHPRLTV VRKVDATDAS
YPSVNTCVHY LKLPEYSSEE IMRERLLAAT MEKGFHLN
