NRDC_HUMAN
ID NRDC_HUMAN Reviewed; 1151 AA.
AC O43847; A6NI41; O15241; O15242; Q5VUL0; Q96HB2; Q9NU57;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Nardilysin;
DE EC=3.4.24.61;
DE AltName: Full=N-arginine dibasic convertase;
DE Short=NRD convertase;
DE Short=NRD-C;
DE AltName: Full=Nardilysin convertase {ECO:0000312|HGNC:HGNC:7995};
DE Flags: Precursor;
GN Name=NRDC {ECO:0000312|HGNC:HGNC:7995}; Synonyms=NRD1;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RX PubMed=9581555; DOI=10.1042/bj3270773;
RA Hospital V., Prat A., Joulie C., Cherif D., Day R., Cohen P.;
RT "Human and rat testis express two mRNA species encoding variants of NRD
RT convertase, a metalloendopeptidase of the insulinase family.";
RL Biochem. J. 327:773-779(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLU-154 DEL.
RC TISSUE=Heart;
RX PubMed=9479496; DOI=10.1006/geno.1997.5078;
RA Fumagalli P., Accarino M., Egeo A., Scartezzini P., Rappazzo G.,
RA Pizzuti A., Avvantaggiato V., Simeone A., Arrigo G., Zuffardi O.,
RA Ottolenghi S., Taramelli R.;
RT "Human NRD convertase: a highly conserved metalloendopeptidase expressed at
RT specific sites during development and in adult tissues.";
RL Genomics 47:238-245(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [GENOMIC DNA] OF 1-107.
RX PubMed=11042131; DOI=10.1042/bj3510755;
RA Winter A.G., Pierotti A.R.;
RT "Gene expression of the dibasic-pair cleaving enzyme NRD convertase (N-
RT arginine dibasic convertase) is differentially regulated in the GH3
RT pituitary and Mat-Lu prostate cell lines.";
RL Biochem. J. 351:755-764(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-94 AND SER-96, AND
RP IDENTIFICATION BY 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Cleaves peptide substrates on the N-terminus of arginine
CC residues in dibasic pairs.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of polypeptides, preferably at -Xaa-|-Arg-Lys-, and
CC less commonly at -Arg-|-Arg-Xaa-, in which Xaa is not Arg or Lys.;
CC EC=3.4.24.61;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- INTERACTION:
CC O43847; P04637: TP53; NbExp=6; IntAct=EBI-2371631, EBI-366083;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=NRD1;
CC IsoId=O43847-1; Sequence=Displayed;
CC Name=2; Synonyms=NRD2;
CC IsoId=O43847-2; Sequence=VSP_007114;
CC -!- TISSUE SPECIFICITY: Primarily in adult heart, skeletal muscle, and
CC testis and at much lower levels in other tissues.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39597.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X93207; CAA63694.1; -; mRNA.
DR EMBL; X93209; CAA63698.1; -; mRNA.
DR EMBL; U64898; AAC39597.1; ALT_FRAME; mRNA.
DR EMBL; AL050343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06809.1; -; Genomic_DNA.
DR EMBL; BC008775; AAH08775.1; -; mRNA.
DR EMBL; AJ000350; CAA04025.1; -; Genomic_DNA.
DR CCDS; CCDS41335.1; -. [O43847-1]
DR CCDS; CCDS559.1; -. [O43847-2]
DR RefSeq; NP_001095132.1; NM_001101662.1. [O43847-1]
DR RefSeq; NP_001229290.1; NM_001242361.1.
DR RefSeq; NP_002516.2; NM_002525.2. [O43847-2]
DR AlphaFoldDB; O43847; -.
DR SMR; O43847; -.
DR BioGRID; 110954; 122.
DR IntAct; O43847; 46.
DR MINT; O43847; -.
DR STRING; 9606.ENSP00000346890; -.
DR MEROPS; M16.005; -.
DR MEROPS; M16.983; -.
DR MEROPS; M16.987; -.
DR iPTMnet; O43847; -.
DR MetOSite; O43847; -.
DR PhosphoSitePlus; O43847; -.
DR BioMuta; NRDC; -.
DR EPD; O43847; -.
DR jPOST; O43847; -.
DR MassIVE; O43847; -.
DR MaxQB; O43847; -.
DR PaxDb; O43847; -.
DR PeptideAtlas; O43847; -.
DR PRIDE; O43847; -.
DR ProteomicsDB; 49200; -. [O43847-1]
DR ProteomicsDB; 49201; -. [O43847-2]
DR Antibodypedia; 19043; 160 antibodies from 25 providers.
DR DNASU; 4898; -.
DR Ensembl; ENST00000352171.12; ENSP00000262679.8; ENSG00000078618.23. [O43847-1]
DR Ensembl; ENST00000354831.11; ENSP00000346890.7; ENSG00000078618.23. [O43847-2]
DR GeneID; 4898; -.
DR KEGG; hsa:4898; -.
DR MANE-Select; ENST00000352171.12; ENSP00000262679.8; NM_001101662.2; NP_001095132.1.
DR UCSC; uc001ctd.5; human. [O43847-1]
DR CTD; 4898; -.
DR DisGeNET; 4898; -.
DR GeneCards; NRDC; -.
DR HGNC; HGNC:7995; NRDC.
DR HPA; ENSG00000078618; Tissue enhanced (skeletal).
DR MIM; 602651; gene.
DR neXtProt; NX_O43847; -.
DR OpenTargets; ENSG00000078618; -.
DR PharmGKB; PA31774; -.
DR VEuPathDB; HostDB:ENSG00000078618; -.
DR eggNOG; KOG0959; Eukaryota.
DR GeneTree; ENSGT00940000155026; -.
DR InParanoid; O43847; -.
DR OMA; INQVMEH; -.
DR OrthoDB; 1008844at2759; -.
DR PhylomeDB; O43847; -.
DR BRENDA; 3.4.24.61; 2681.
DR PathwayCommons; O43847; -.
DR SignaLink; O43847; -.
DR BioGRID-ORCS; 4898; 112 hits in 1072 CRISPR screens.
DR ChiTaRS; NRDC; human.
DR GeneWiki; NRD1; -.
DR GenomeRNAi; 4898; -.
DR Pharos; O43847; Tbio.
DR PRO; PR:O43847; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O43847; protein.
DR Bgee; ENSG00000078618; Expressed in gluteal muscle and 207 other tissues.
DR ExpressionAtlas; O43847; baseline and differential.
DR Genevisible; O43847; HS.
DR GO; GO:0009986; C:cell surface; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0048408; F:epidermal growth factor binding; TAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; NAS:UniProtKB.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:BHF-UCL.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0052548; P:regulation of endopeptidase activity; IDA:BHF-UCL.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR032632; Peptidase_M16_M.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; SSF63411; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Metal-binding; Metalloprotease;
KW Phosphoprotein; Protease; Reference proteome; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1151
FT /note="Nardilysin"
FT /id="PRO_0000026755"
FT REGION 53..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..196
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 236
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 210
FT /note="Q -> QQLQSLFLLWSKLTDRLWFKSTYSKMSSTLLVETRNLYGVVGAESRS
FT APVQHLAGWQAEEQQGETDTVL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9581555"
FT /id="VSP_007114"
FT VARIANT 154
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:9479496"
FT /id="VAR_080827"
FT VARIANT 832
FT /note="Y -> S (in dbSNP:rs34957144)"
FT /id="VAR_057058"
FT CONFLICT 23..24
FT /note="EL -> DV (in Ref. 1; CAA63698/CAA63694)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="Q -> L (in Ref. 1; CAA63698/CAA63694)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="A -> G (in Ref. 2; AAC39597)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="V -> A (in Ref. 1; CAA63698/CAA63694)"
FT /evidence="ECO:0000305"
FT CONFLICT 1087
FT /note="V -> A (in Ref. 2; AAC39597)"
FT /evidence="ECO:0000305"
FT CONFLICT 1100
FT /note="T -> S (in Ref. 1; CAA63698/CAA63694)"
FT /evidence="ECO:0000305"
FT CONFLICT 1126
FT /note="D -> S (in Ref. 2; AAC39597)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1151 AA; 131701 MW; CD03BF258AF65122 CRC64;
MLRRVTVAAV CATRRKLCEA GRELAALWGI ETRGRCEDSA AARPFPILAM PGRNKAKSTC
SCPDLQPNGQ DLGENSRVAR LGADESEEEG RRGSLSNAGD PEIVKSPSDP KQYRYIKLQN
GLQALLISDL SNMEGKTGNT TDDEEEEEVE EEEEDDDEDS GAEIEDDDEE GFDDEDEFDD
EHDDDLDTED NELEELEERA EARKKTTEKQ SAAALCVGVG SFADPDDLPG LAHFLEHMVF
MGSLKYPDEN GFDAFLKKHG GSDNASTDCE RTVFQFDVQR KYFKEALDRW AQFFIHPLMI
RDAIDREVEA VDSEYQLARP SDANRKEMLF GSLARPGHPM GKFFWGNAET LKHEPRKNNI
DTHARLREFW MRYYSSHYMT LVVQSKETLD TLEKWVTEIF SQIPNNGLPR PNFGHLTDPF
DTPAFNKLYR VVPIRKIHAL TITWALPPQQ QHYRVKPLHY ISWLVGHEGK GSILSFLRKK
CWALALFGGN GETGFEQNST YSVFSISITL TDEGYEHFYE VAYTVFQYLK MLQKLGPEKR
IFEEIRKIED NEFHYQEQTD PVEYVENMCE NMQLYPLQDI LTGDQLLFEY KPEVIGEALN
QLVPQKANLV LLSGANEGKC DLKEKWFGTQ YSIEDIENSW AELWNSNFEL NPDLHLPAEN
KYIATDFTLK AFDCPETEYP VKIVNTPQGC LWYKKDNKFK IPKAYIRFHL ISPLIQKSAA
NVVLFDIFVN ILTHNLAEPA YEADVAQLEY KLVAGEHGLI IRVKGFNHKL PLLFQLIIDY
LAEFNSTPAV FTMITEQLKK TYFNILIKPE TLAKDVRLLI LEYARWSMID KYQALMDGLS
LESLLSFVKE FKSQLFVEGL VQGNVTSTES MDFLKYVVDK LNFKPLEQEM PVQFQVVELP
SGHHLCKVKA LNKGDANSEV TVYYQSGTRS LREYTLMELL VMHMEEPCFD FLRTKQTLGY
HVYPTCRNTS GILGFSVTVG TQATKYNSEV VDKKIEEFLS SFEEKIENLT EEAFNTQVTA
LIKLKECEDT HLGEEVDRNW NEVVTQQYLF DRLAHEIEAL KSFSKSDLVN WFKAHRGPGS
KMLSVHVVGY GKYELEEDGT PSSEDSNSSC EVMQLTYLPT SPLLADCIIP ITDIRAFTTT
LNLLPYHKIV K
