ID   SCG3_HUMAN              Reviewed;         468 AA.
AC   Q8WXD2; A8K2B0; B3KQP6; B4DK99; F5H3R8; Q96C83; Q96GE8; Q9Y6G7;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 3.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Secretogranin-3;
DE   AltName: Full=Secretogranin III;
DE            Short=SgIII;
DE   Flags: Precursor;
GN   Name=SCG3; ORFNames=UNQ2502/PRO5990;
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] (ISOFORM 1).
RC   TISSUE=Pituitary;
RA   Song H., Peng Y., Huang Q., Dai M., Mao Y., Zhang Q., Mao M., Fu G.,
RA   Luo M., Chen J., Hu R.;
RT   "Human secretogranin III mRNA, complete cds.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=12098761;
RA   Rong Y.P., Liu F., Zeng L.C., Ma W.J., Wei D.Z., Han Z.G.;
RT   "Cloning and characterization of a novel human secretory protein:
RT   secretogranin III.";
RL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:411-417(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Retinoblastoma, and Thalamus;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-167.
RC   TISSUE=Brain, and Lung;
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   [8]
RP   POLYMORPHISM.
RX   PubMed=17200173; DOI=10.1210/jc.2006-1808;
RA   Tanabe A., Yanagiya T., Iida A., Saito S., Sekine A., Takahashi A.,
RA   Nakamura T., Tsunoda T., Kamohara S., Nakata Y., Kotani K., Komatsu R.,
RA   Itoh N., Mineo I., Wada J., Funahashi T., Miyazaki S., Tokunaga K.,
RA   Hamaguchi K., Shimada T., Tanaka K., Yamada K., Hanafusa T., Oikawa S.,
RA   Yoshimatsu H., Sakata T., Matsuzawa Y., Kamatani N., Nakamura Y., Hotta K.;
RT   "Functional single-nucleotide polymorphisms in the secretogranin III (SCG3)
RT   gene that form secretory granules with appetite-related neuropeptides are
RT   associated with obesity.";
RL   J. Clin. Endocrinol. Metab. 92:1145-1154(2007).
RN   [9]
RP   INTERACTION WITH SCG2, AND FUNCTION.
RX   PubMed=19357184; DOI=10.1677/joe-08-0531;
RA   Hotta K., Hosaka M., Tanabe A., Takeuchi T.;
RT   "Secretogranin II binds to secretogranin III and forms secretory granules
RT   with orexin, neuropeptide Y, and POMC.";
RL   J. Endocrinol. 202:111-121(2009).
RN   [10]
RP   GLYCOSYLATION AT THR-216; THR-231 AND SER-359, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=23234360; DOI=10.1021/pr300963h;
RA   Halim A., Ruetschi U., Larson G., Nilsson J.;
RT   "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT   of human cerebrospinal fluid glycoproteins.";
RL   J. Proteome Res. 12:573-584(2013).
RN   [11]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-37.
RX   PubMed=25326458; DOI=10.1074/mcp.m114.043703;
RA   Noborn F., Gomez Toledo A., Sihlbom C., Lengqvist J., Fries E., Kjellen L.,
RA   Nilsson J., Larson G.;
RT   "Identification of chondroitin sulfate linkage region glycopeptides reveals
RT   prohormones as a novel class of proteoglycans.";
RL   Mol. Cell. Proteomics 14:41-49(2015).
RN   [12]
RP   FUNCTION.
RX   PubMed=29154827; DOI=10.1016/j.bbrc.2017.11.080;
RA   Tang F., Pacheco M.T.F., Chen P., Liang D., Li W.;
RT   "Secretogranin III promotes angiogenesis through MEK/ERK signaling
RT   pathway.";
RL   Biochem. Biophys. Res. Commun. 495:781-786(2018).
CC   -!- FUNCTION: Member of the granin protein family that regulates the
CC       biogenesis of secretory granules (PubMed:19357184). Acts as a sorting
CC       receptor for intragranular proteins including chromogranin A/CHGA (By
CC       similarity). May also play a role in angiogenesis. Promotes endothelial
CC       proliferation, migration and tube formation through MEK/ERK signaling
CC       pathway (PubMed:29154827). {ECO:0000250|UniProtKB:P47868,
CC       ECO:0000269|PubMed:19357184, ECO:0000269|PubMed:29154827}.
CC   -!- SUBUNIT: Interacts with CHGA (PubMed:19357184) (By similarity).
CC       Interacts with secretogranin II/SCG2 (PubMed:19357184). Interacts (via
CC       C-terminus) with CPE (By similarity). {ECO:0000250|UniProtKB:P47867,
CC       ECO:0000269|PubMed:19357184}.
CC   -!- INTERACTION:
CC       Q8WXD2; O00560: SDCBP; NbExp=3; IntAct=EBI-12162999, EBI-727004;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC       {ECO:0000250|UniProtKB:P47868}. Cytoplasmic vesicle, secretory vesicle
CC       membrane {ECO:0000250|UniProtKB:P47868}; Peripheral membrane protein
CC       {ECO:0000250}. Secreted {ECO:0000269|PubMed:12098761,
CC       ECO:0000269|PubMed:25326458}. Note=Associated with the secretory
CC       granule membrane through direct binding to cholesterol-enriched lipid
CC       rafts. {ECO:0000250|UniProtKB:P47868}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8WXD2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8WXD2-2; Sequence=VSP_042876;
CC   -!- TISSUE SPECIFICITY: Detected in urine (at protein level)
CC       (PubMed:25326458). Expressed in brain, heart, kidney, liver and
CC       skeletal muscle. {ECO:0000269|PubMed:12098761,
CC       ECO:0000269|PubMed:25326458}.
CC   -!- PTM: O-glycosylated. {ECO:0000269|PubMed:23234360,
CC       ECO:0000269|PubMed:25326458}.
CC   -!- POLYMORPHISM: Polymorphisms in the 5'-flanking region and in intron 1
CC       may have an effect on transcriptional activity and be associated with
CC       an increase in subcutaneous, but not visceral, fat area. Hence, may
CC       influence the risk of obesity.
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DR   EMBL; AF078851; AAD44483.1; -; mRNA.
DR   EMBL; AF453583; AAL67431.1; -; mRNA.
DR   EMBL; AY359093; AAQ89451.1; -; mRNA.
DR   EMBL; AK075314; BAG52108.1; -; mRNA.
DR   EMBL; AK290175; BAF82864.1; -; mRNA.
DR   EMBL; AK296466; BAG59111.1; -; mRNA.
DR   EMBL; AC020892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471082; EAW77426.1; -; Genomic_DNA.
DR   EMBL; BC009511; AAH09511.2; -; mRNA.
DR   EMBL; BC014539; AAH14539.1; -; mRNA.
DR   CCDS; CCDS10142.1; -. [Q8WXD2-1]
DR   CCDS; CCDS53947.1; -. [Q8WXD2-2]
DR   RefSeq; NP_001158729.1; NM_001165257.1. [Q8WXD2-2]
DR   RefSeq; NP_037375.2; NM_013243.3. [Q8WXD2-1]
DR   AlphaFoldDB; Q8WXD2; -.
DR   BioGRID; 118874; 10.
DR   DIP; DIP-29451N; -.
DR   IntAct; Q8WXD2; 10.
DR   STRING; 9606.ENSP00000220478; -.
DR   GlyConnect; 732; 13 N-Linked glycans (1 site), 1 O-Linked glycan (3 sites).
DR   GlyCosmos; Q8WXD2; 5 sites, 16 glycans.
DR   GlyGen; Q8WXD2; 8 sites, 14 N-linked glycans (2 sites), 3 O-linked glycans (5 sites).
DR   iPTMnet; Q8WXD2; -.
DR   PhosphoSitePlus; Q8WXD2; -.
DR   BioMuta; SCG3; -.
DR   DMDM; 46397796; -.
DR   EPD; Q8WXD2; -.
DR   jPOST; Q8WXD2; -.
DR   MassIVE; Q8WXD2; -.
DR   PaxDb; 9606-ENSP00000220478; -.
DR   PeptideAtlas; Q8WXD2; -.
DR   ProteomicsDB; 75012; -. [Q8WXD2-1]
DR   ProteomicsDB; 75013; -. [Q8WXD2-2]
DR   Antibodypedia; 1520; 314 antibodies from 31 providers.
DR   DNASU; 29106; -.
DR   Ensembl; ENST00000220478.8; ENSP00000220478.3; ENSG00000104112.9. [Q8WXD2-1]
DR   Ensembl; ENST00000542355.6; ENSP00000445205.2; ENSG00000104112.9. [Q8WXD2-2]
DR   GeneID; 29106; -.
DR   KEGG; hsa:29106; -.
DR   MANE-Select; ENST00000220478.8; ENSP00000220478.3; NM_013243.4; NP_037375.2.
DR   UCSC; uc002abh.4; human. [Q8WXD2-1]
DR   AGR; HGNC:13707; -.
DR   CTD; 29106; -.
DR   DisGeNET; 29106; -.
DR   GeneCards; SCG3; -.
DR   HGNC; HGNC:13707; SCG3.
DR   HPA; ENSG00000104112; Tissue enhanced (brain, pituitary gland, retina).
DR   MIM; 611796; gene.
DR   neXtProt; NX_Q8WXD2; -.
DR   OpenTargets; ENSG00000104112; -.
DR   PharmGKB; PA34988; -.
DR   VEuPathDB; HostDB:ENSG00000104112; -.
DR   eggNOG; ENOG502QUJH; Eukaryota.
DR   GeneTree; ENSGT00390000005488; -.
DR   HOGENOM; CLU_031198_1_0_1; -.
DR   InParanoid; Q8WXD2; -.
DR   OMA; TDKAIHN; -.
DR   OrthoDB; 5353945at2759; -.
DR   PhylomeDB; Q8WXD2; -.
DR   TreeFam; TF331266; -.
DR   PathwayCommons; Q8WXD2; -.
DR   Reactome; R-HSA-114608; Platelet degranulation.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   SignaLink; Q8WXD2; -.
DR   BioGRID-ORCS; 29106; 14 hits in 1153 CRISPR screens.
DR   ChiTaRS; SCG3; human.
DR   GeneWiki; SCG3; -.
DR   GenomeRNAi; 29106; -.
DR   Pharos; Q8WXD2; Tbio.
DR   PRO; PR:Q8WXD2; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q8WXD2; Protein.
DR   Bgee; ENSG00000104112; Expressed in islet of Langerhans and 119 other cell types or tissues.
DR   ExpressionAtlas; Q8WXD2; baseline and differential.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0030667; C:secretory granule membrane; IBA:GO_Central.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0033366; P:protein localization to secretory granule; IBA:GO_Central.
DR   InterPro; IPR026197; SCG3.
DR   PANTHER; PTHR17388; SECRETOGRANIN III; 1.
DR   PANTHER; PTHR17388:SF2; SECRETOGRANIN-3; 1.
DR   Pfam; PF15467; SGIII; 1.
DR   Genevisible; Q8WXD2; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cleavage on pair of basic residues;
KW   Cytoplasmic vesicle; Glycoprotein; Membrane; Phosphoprotein; Proteoglycan;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..468
FT                   /note="Secretogranin-3"
FT                   /id="PRO_0000005461"
FT   REGION          23..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..406
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47867"
FT   MOD_RES         362
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47867"
FT   CARBOHYD        37
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000269|PubMed:25326458"
FT   CARBOHYD        216
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:23234360"
FT   CARBOHYD        231
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:23234360"
FT   CARBOHYD        359
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:23234360"
FT   VAR_SEQ         1..232
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_042876"
FT   VARIANT         125
FT                   /note="S -> N (in dbSNP:rs2305710)"
FT                   /id="VAR_013827"
FT   VARIANT         167
FT                   /note="V -> A (in dbSNP:rs17851186)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_067273"
FT   VARIANT         233
FT                   /note="M -> V (in dbSNP:rs35664837)"
FT                   /id="VAR_034484"
FT   CONFLICT        79
FT                   /note="K -> R (in Ref. 1; AAD44483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        150
FT                   /note="D -> G (in Ref. 4; BAG52108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        272..274
FT                   /note="EEL -> RDF (in Ref. 1; AAD44483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        421
FT                   /note="K -> R (in Ref. 4; BAG59111)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   468 AA;  53005 MW;  5E6BBDDFFF3B8D82 CRC64;
     MGFLGTGTWI LVLVLPIQAF PKPGGSQDKS LHNRELSAER PLNEQIAEAE EDKIKKTYPP
     ENKPGQSNYS FVDNLNLLKA ITEKEKIEKE RQSIRSSPLD NKLNVEDVDS TKNRKLIDDY
     DSTKSGLDHK FQDDPDGLHQ LDGTPLTAED IVHKIAARIY EENDRAVFDK IVSKLLNLGL
     ITESQAHTLE DEVAEVLQKL ISKEANNYEE DPNKPTSWTE NQAGKIPEKV TPMAAIQDGL
     AKGENDETVS NTLTLTNGLE RRTKTYSEDN FEELQYFPNF YALLKSIDSE KEAKEKETLI
     TIMKTLIDFV KMMVKYGTIS PEEGVSYLEN LDEMIALQTK NKLEKNATDN ISKLFPAPSE
     KSHEETDSTK EEAAKMEKEY GSLKDSTKDD NSNPGGKTDE PKGKTEAYLE AIRKNIEWLK
     KHDKKGNKED YDLSKMRDFI NKQADAYVEK GILDKEEAEA IKRIYSSL
//