TNF13_HUMAN
ID TNF13_HUMAN Reviewed; 250 AA.
AC O75888; A8MYD5; B4DVT2; Q541E1; Q5U0G8; Q96HV6; Q9P1M8; Q9P1M9;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Tumor necrosis factor ligand superfamily member 13;
DE AltName: Full=A proliferation-inducing ligand;
DE Short=APRIL;
DE AltName: Full=TNF- and APOL-related leukocyte expressed ligand 2;
DE Short=TALL-2;
DE AltName: Full=TNF-related death ligand 1;
DE Short=TRDL-1;
DE AltName: CD_antigen=CD256;
DE Flags: Precursor;
GN Name=TNFSF13; Synonyms=APRIL, TALL2, ZTNF2; ORFNames=UNQ383/PRO715;
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].
RC TISSUE=Uterus;
RX PubMed=9743536; DOI=10.1084/jem.188.6.1185;
RA Hahne M., Kataoka T., Schroeter M., Hofmann K., Irmler M., Bodmer J.-L.,
RA Schneider P., Bornand T., Holler N., French L.E., Sordat B., Rimoldi D.,
RA Tschopp J.;
RT "APRIL, a new ligand of the tumor necrosis factor family, stimulates tumor
RT cell growth.";
RL J. Exp. Med. 188:1185-1190(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10331498; DOI=10.1002/jlb.65.5.680;
RA Shu H.-B., Hu W.-H., Johnson H.;
RT "TALL-1 is a novel member of the TNF family that is down-regulated by
RT mitogens.";
RL J. Leukoc. Biol. 65:680-683(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Farrah T., Grant F., Haldeman B., Whitmore T., Gross J., O'Hara P.;
RT "Homo sapiens tumor necrosis factor homolog.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA).
RX PubMed=10706119;
RA Kelly K.A., Manos E.J., Jensen G.T., Nadauld L., Jones D.A.;
RT "APRIL/TRDL-1, a tumor necrosis factor-like ligand, stimulates cell
RT death.";
RL Cancer Res. 60:1021-1027(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RX PubMed=12411489; DOI=10.1093/emboj/cdf565;
RA Pradet-Balade B., Medema J.P., Lopez-Fraga M., Lozano J.C.,
RA Kolfschoten G.M., Picard A., Martinez-A C., Garcia-Sanz J.A., Hahne M.;
RT "An endogenous hybrid mRNA encodes TWE-PRIL, a functional cell surface
RT TWEAK-APRIL fusion protein.";
RL EMBO J. 21:5711-5720(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kawasaki A., Tsuchiya N., Kusaoi M., Murakami T., Fukazawa T., Matsuta K.,
RA Hashimoto H., Tokunaga K.;
RT "Polymorphisms of human APRIL gene.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Spleen;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT ARG-67.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA), AND VARIANT SER-96.
RC TISSUE=Ovary;
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 [12]
RP FUNCTION.
RX PubMed=10973284; DOI=10.1038/79802;
RA Yu G., Boone T., Delaney J., Hawkins N., Kelley M.J., Ramakrishnan M.,
RA McCabe S., Qiu W.R., Kornuc M., Xia X.-Z., Guo J., Stolina M., Boyle W.J.,
RA Sarosi I., Hsu H., Senaldi G., Theill L.E.;
RT "APRIL and TALL-I and receptors BCMA and TACI: system for regulating
RT humoral immunity.";
RL Nat. Immunol. 1:252-256(2000).
RN [13]
RP PROTEOLYTIC PROCESSING BY FURIN, MUTAGENESIS OF 101-ARG--ARG-104, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11571266; DOI=10.1093/embo-reports/kve198;
RA Lopez-Fraga M., Fernandez R., Albar J.P., Hahne M.;
RT "Biologically active APRIL is secreted following intracellular processing
RT in the Golgi apparatus by furin convertase.";
RL EMBO Rep. 2:945-951(2001).
CC -!- FUNCTION: Cytokine that binds to TNFRSF13B/TACI and to TNFRSF17/BCMA.
CC Plays a role in the regulation of tumor cell growth. May be involved in
CC monocyte/macrophage-mediated immunological processes.
CC {ECO:0000269|PubMed:10973284}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000305}.
CC -!- INTERACTION:
CC O75888-3; P05067: APP; NbExp=3; IntAct=EBI-12856452, EBI-77613;
CC O75888-3; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-12856452, EBI-744081;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11571266}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=Alpha;
CC IsoId=O75888-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=O75888-2; Sequence=VSP_006450;
CC Name=Gamma;
CC IsoId=O75888-3; Sequence=VSP_006451;
CC Name=4;
CC IsoId=O75888-4; Sequence=VSP_043154;
CC Name=TWE-PRIL; Synonyms=TNFSF12-TNFSF13;
CC IsoId=O43508-2; Sequence=External;
CC Name=5;
CC IsoId=O75888-5; Sequence=VSP_046725, VSP_046726;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in transformed cell lines,
CC cancers of colon, thyroid, lymphoid tissues and specifically expressed
CC in monocytes and macrophages.
CC -!- INDUCTION: Down-regulated by phorbol myristate acetate/ionomycin
CC treatment.
CC -!- PTM: The precursor is cleaved by furin. {ECO:0000269|PubMed:11571266}.
CC -!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
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DR EMBL; AF046888; AAC61312.1; -; mRNA.
DR EMBL; AF136294; AAD29422.1; -; mRNA.
DR EMBL; AF184972; AAF01321.1; -; mRNA.
DR EMBL; AF114011; AAF59828.1; -; mRNA.
DR EMBL; AF114012; AAF59829.1; -; mRNA.
DR EMBL; AF114013; AAF59830.1; -; mRNA.
DR EMBL; AY358880; AAQ89239.1; -; mRNA.
DR EMBL; AY081050; AAL90442.1; -; mRNA.
DR EMBL; AB222992; BAE16556.1; -; Genomic_DNA.
DR EMBL; AK301221; BAG62794.1; -; mRNA.
DR EMBL; BT019561; AAV38368.1; -; mRNA.
DR EMBL; BT019562; AAV38369.1; -; mRNA.
DR EMBL; AC016876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008042; AAH08042.1; -; mRNA.
DR CCDS; CCDS11111.1; -. [O75888-1]
DR CCDS; CCDS11112.1; -. [O75888-2]
DR CCDS; CCDS42256.1; -. [O75888-3]
DR CCDS; CCDS56018.1; -. [O75888-4]
DR CCDS; CCDS56019.1; -. [O75888-5]
DR RefSeq; NP_001185552.1; NM_001198623.1. [O75888-4]
DR RefSeq; NP_001185553.1; NM_001198624.1. [O75888-5]
DR RefSeq; NP_003799.1; NM_003808.3. [O75888-1]
DR RefSeq; NP_742084.1; NM_172087.2. [O75888-2]
DR RefSeq; NP_742085.1; NM_172088.2. [O75888-3]
DR PDB; 4ZCH; X-ray; 2.43 A; A/B=115-250.
DR PDBsum; 4ZCH; -.
DR AlphaFoldDB; O75888; -.
DR SMR; O75888; -.
DR BioGRID; 114278; 32.
DR DIP; DIP-6232N; -.
DR IntAct; O75888; 6.
DR MINT; O75888; -.
DR STRING; 9606.ENSP00000343505; -.
DR ChEMBL; CHEMBL3713436; -.
DR GlyConnect; 2946; 10 N-Linked glycans (1 site).
DR GlyGen; O75888; 1 site, 12 N-linked glycans (1 site).
DR iPTMnet; O75888; -.
DR PhosphoSitePlus; O75888; -.
DR BioMuta; TNFSF13; -.
DR jPOST; O75888; -.
DR MassIVE; O75888; -.
DR MaxQB; O75888; -.
DR PaxDb; O75888; -.
DR PeptideAtlas; O75888; -.
DR PRIDE; O75888; -.
DR Antibodypedia; 1191; 750 antibodies from 45 providers.
DR DNASU; 8741; -.
DR Ensembl; ENST00000338784.9; ENSP00000343505.4; ENSG00000161955.17. [O75888-1]
DR Ensembl; ENST00000349228.8; ENSP00000314455.6; ENSG00000161955.17. [O75888-2]
DR Ensembl; ENST00000396542.5; ENSP00000379792.1; ENSG00000161955.17. [O75888-5]
DR Ensembl; ENST00000396545.4; ENSP00000379794.4; ENSG00000161955.17. [O75888-3]
DR Ensembl; ENST00000625791.2; ENSP00000486052.1; ENSG00000161955.17. [O75888-4]
DR GeneID; 8741; -.
DR KEGG; hsa:8741; -.
DR MANE-Select; ENST00000338784.9; ENSP00000343505.4; NM_003808.4; NP_003799.1.
DR UCSC; uc002ghj.3; human. [O75888-1]
DR CTD; 8741; -.
DR DisGeNET; 8741; -.
DR GeneCards; TNFSF13; -.
DR HGNC; HGNC:11928; TNFSF13.
DR HPA; ENSG00000161955; Tissue enhanced (salivary).
DR MIM; 604472; gene.
DR neXtProt; NX_O75888; -.
DR OpenTargets; ENSG00000161955; -.
DR PharmGKB; PA36621; -.
DR VEuPathDB; HostDB:ENSG00000161955; -.
DR eggNOG; ENOG502SAX4; Eukaryota.
DR GeneTree; ENSGT00940000161488; -.
DR HOGENOM; CLU_1234667_0_0_1; -.
DR InParanoid; O75888; -.
DR OMA; DYTLVEW; -.
DR OrthoDB; 1232325at2759; -.
DR PhylomeDB; O75888; -.
DR TreeFam; TF332331; -.
DR PathwayCommons; O75888; -.
DR Reactome; R-HSA-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
DR SignaLink; O75888; -.
DR SIGNOR; O75888; -.
DR BioGRID-ORCS; 8741; 12 hits in 1068 CRISPR screens.
DR GeneWiki; TNFSF13; -.
DR GenomeRNAi; 8741; -.
DR Pharos; O75888; Tbio.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O75888; protein.
DR Bgee; ENSG00000161955; Expressed in monocyte and 98 other tissues.
DR ExpressionAtlas; O75888; baseline and differential.
DR Genevisible; O75888; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0048018; F:receptor ligand activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0048298; P:positive regulation of isotype switching to IgA isotypes; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd00184; TNF; 1.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR021184; TNF_CS.
DR InterPro; IPR006052; TNF_dom.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00229; TNF; 1.
DR SMART; SM00207; TNF; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS00251; TNF_1; 1.
DR PROSITE; PS50049; TNF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cleavage on pair of basic residues;
KW Cytokine; Disulfide bond; Glycoprotein; Immunity; Reference proteome;
KW Secreted.
FT PROPEP 1..104
FT /id="PRO_0000034524"
FT CHAIN 105..250
FT /note="Tumor necrosis factor ligand superfamily member 13"
FT /id="PRO_0000034525"
FT REGION 61..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 104..105
FT /note="Cleavage; by furin"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 196..211
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..17
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_046725"
FT VAR_SEQ 86..113
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043154"
FT VAR_SEQ 87..114
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_046726"
FT VAR_SEQ 113..129
FT /note="KQHSVLHLVPINATSKD -> N (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:10706119"
FT /id="VSP_006450"
FT VAR_SEQ 247..249
FT /note="Missing (in isoform Gamma)"
FT /evidence="ECO:0000303|PubMed:10706119,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_006451"
FT VARIANT 67
FT /note="G -> R (in dbSNP:rs11552708)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_052586"
FT VARIANT 96
FT /note="N -> S (in dbSNP:rs3803800)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_052587"
FT MUTAGEN 101..104
FT /note="RKRR->AKRA: Abolishes proteolytic processing."
FT /evidence="ECO:0000269|PubMed:11571266"
FT STRAND 117..126
FT /evidence="ECO:0007829|PDB:4ZCH"
FT STRAND 132..150
FT /evidence="ECO:0007829|PDB:4ZCH"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:4ZCH"
FT STRAND 161..171
FT /evidence="ECO:0007829|PDB:4ZCH"
FT STRAND 175..185
FT /evidence="ECO:0007829|PDB:4ZCH"
FT STRAND 190..199
FT /evidence="ECO:0007829|PDB:4ZCH"
FT STRAND 209..219
FT /evidence="ECO:0007829|PDB:4ZCH"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:4ZCH"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:4ZCH"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:4ZCH"
SQ SEQUENCE 250 AA; 27433 MW; AE1A6B9457F6E298 CRC64;
MPASSPFLLA PKGPPGNMGG PVREPALSVA LWLSWGAALG AVACAMALLT QQTELQSLRR
EVSRLQGTGG PSQNGEGYPW QSLPEQSSDA LEAWENGERS RKRRAVLTQK QKKQHSVLHL
VPINATSKDD SDVTEVMWQP ALRRGRGLQA QGYGVRIQDA GVYLLYSQVL FQDVTFTMGQ
VVSREGQGRQ ETLFRCIRSM PSHPDRAYNS CYSAGVFHLH QGDILSVIIP RARAKLNLSP
HGTFLGFVKL
