ID   TRAF7_HUMAN             Reviewed;         670 AA.
AC   Q6Q0C0; Q9H073;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=E3 ubiquitin-protein ligase TRAF7;
DE            EC=2.3.2.- {ECO:0000250|UniProtKB:Q922B6};
DE            EC=2.3.2.27 {ECO:0000269|PubMed:37086853};
DE   AltName: Full=RING finger and WD repeat-containing protein 1;
DE   AltName: Full=RING finger protein 119;
DE   AltName: Full=RING-type E3 ubiquitin transferase TRAF7 {ECO:0000305};
DE   AltName: Full=TNF receptor-associated factor 7;
GN   Name=TRAF7; Synonyms=RFWD1, RNF119;
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] {ECO:0000305, ECO:0000312|EMBL:AAS68363.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   ALTERNATIVE SPLICING, AND INTERACTION WITH MAP3K3.
RX   PubMed=15001576; DOI=10.1074/jbc.c400063200;
RA   Xu L.-G., Li L.-Y., Shu H.-B.;
RT   "TRAF7 potentiates MEKK3-induced AP1 and CHOP activation and induces
RT   apoptosis.";
RL   J. Biol. Chem. 279:17278-17282(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Uterus;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [3] {ECO:0000305}
RP   FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, HOMODIMERIZATION, AND
RP   INTERACTION WITH MAP3K3.
RX   PubMed=14743216; DOI=10.1038/ncb1086;
RA   Bouwmeester T., Bauch A., Ruffner H., Angrand P.-O., Bergamini G.,
RA   Croughton K., Cruciat C., Eberhard D., Gagneur J., Ghidelli S., Hopf C.,
RA   Huhse B., Mangano R., Michon A.-M., Schirle M., Schlegl J., Schwab M.,
RA   Stein M.A., Bauer A., Casari G., Drewes G., Gavin A.-C., Jackson D.B.,
RA   Joberty G., Neubauer G., Rick J., Kuster B., Superti-Furga G.;
RT   "A physical and functional map of the human TNF-alpha/NF-kappa B signal
RT   transduction pathway.";
RL   Nat. Cell Biol. 6:97-105(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-91, AND
RP   IDENTIFICATION BY 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   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21518757; DOI=10.1074/jbc.m110.215426;
RA   Zotti T., Uva A., Ferravante A., Vessichelli M., Scudiero I.,
RA   Ceccarelli M., Vito P., Stilo R.;
RT   "TRAF7 protein promotes Lys-29-linked polyubiquitination of IkappaB kinase
RT   (IKKgamma)/NF-kappaB essential modulator (NEMO) and p65/RelA protein and
RT   represses NF-kappaB activation.";
RL   J. Biol. Chem. 286:22924-22933(2011).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, 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   [7]
RP   FUNCTION, INVOLVEMENT IN CAFDADD, VARIANTS CAFDADD GLU-346; GLY-371;
RP   ALA-601 AND GLN-655, AND CHARACTERIZATION OF VARIANTS CAFDADD GLU-346;
RP   GLY-371; ALA-601 AND GLN-655.
RX   PubMed=29961569; DOI=10.1016/j.ajhg.2018.06.005;
RG   Undiagnosed Diseases Network;
RA   Tokita M.J., Chen C.A., Chitayat D., Macnamara E., Rosenfeld J.A.,
RA   Hanchard N., Lewis A.M., Brown C.W., Marom R., Shao Y., Novacic D.,
RA   Wolfe L., Wahl C., Tifft C.J., Toro C., Bernstein J.A., Hale C.L.,
RA   Silver J., Hudgins L., Ananth A., Hanson-Kahn A., Shuster S.,
RA   Magoulas P.L., Patel V.N., Zhu W., Chen S.M., Jiang Y., Liu P., Eng C.M.,
RA   Batkovskyte D., di Ronza A., Sardiello M., Lee B.H., Schaaf C.P., Yang Y.,
RA   Wang X.;
RT   "De novo missense variants in TRAF7 cause developmental delay, congenital
RT   anomalies, and dysmorphic features.";
RL   Am. J. Hum. Genet. 103:154-162(2018).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP   CYS-131.
RX   PubMed=37086853; DOI=10.1016/j.virs.2023.04.005;
RA   Huang J.P., Yang Y.X., Chen T., Wang D.D., Li J., Xu L.G.;
RT   "TRAF7 negatively regulates the RLR signaling pathway by facilitating the
RT   K48-linked ubiquitination of TBK1.";
RL   Virol. Sin. 38:419-428(2023).
CC   -!- FUNCTION: E3 ubiquitin and SUMO-protein ligase that plays a role in
CC       different biological processes such as innate immunity, inflammation or
CC       apoptosis (PubMed:15001576, PubMed:37086853). Potentiates MAP3K3-
CC       mediated activation of JUN/AP1 and DDIT3 transcriptional regulators
CC       (PubMed:14743216). Negatively regulates MYB transcriptional activity by
CC       sequestering it to the cytosol via SUMOylation (By similarity). Plays a
CC       role in the phosphorylation of MAPK1 and/or MAPK3, probably via its
CC       interaction with MAP3K3. Negatively regulates RLR-mediated innate
CC       immunity by promoting 'Lys-48'-linked ubiquitination of TBK1 through
CC       its RING domain to inhibit the cellular antiviral response
CC       (PubMed:37086853). Promotes 'Lys-29'-linked polyubiquitination of
CC       NEMO/IKBKG and RELA leading to targeting these two proteins to
CC       lysosomal degradative pathways, reducing the transcriptional activity
CC       of NF-kappa-B (PubMed:21518757). {ECO:0000250|UniProtKB:Q922B6,
CC       ECO:0000269|PubMed:14743216, ECO:0000269|PubMed:15001576,
CC       ECO:0000269|PubMed:21518757, ECO:0000269|PubMed:29961569,
CC       ECO:0000269|PubMed:37086853}.
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=2.3.2.27; Evidence={ECO:0000269|PubMed:37086853};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Homodimer. Interacts with MAP3K3 and promotes the kinase
CC       activity of this enzyme. {ECO:0000269|PubMed:14743216,
CC       ECO:0000269|PubMed:15001576}.
CC   -!- INTERACTION:
CC       Q6Q0C0; Q99759: MAP3K3; NbExp=3; IntAct=EBI-307556, EBI-307281;
CC       Q6Q0C0; Q9ERK0: Ripk4; Xeno; NbExp=2; IntAct=EBI-307556, EBI-6116422;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC       {ECO:0000269|PubMed:14743216}. Cytoplasm {ECO:0000269|PubMed:21518757,
CC       ECO:0000269|PubMed:37086853}. Nucleus {ECO:0000269|PubMed:37086853}.
CC       Note=Colocalizes with MAP3K3 to vesicle-like structures throughout the
CC       cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000269|PubMed:15001576};
CC         IsoId=Q6Q0C0-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:15001576};
CC         IsoId=Q6Q0C0-2; Sequence=VSP_051607;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed with high levels in skeletal
CC       muscle, heart, colon, spleen, kidney, liver and placenta.
CC       {ECO:0000269|PubMed:15001576}.
CC   -!- PTM: Phosphorylated by MAP3K3. {ECO:0000269|PubMed:14743216}.
CC   -!- PTM: Ubiquitinates itself upon phosphorylation.
CC   -!- DISEASE: Cardiac, facial, and digital anomalies with developmental
CC       delay (CAFDADD) [MIM:618164]: An autosomal dominant disorder
CC       characterized by delayed motor and speech development, developmental
CC       regression, congenital heart defects, limb and digital anomalies, and
CC       dysmorphic features. Cardiac features include pulmonary stenosis,
CC       patent ductus arteriosus, aortic coarctation, valvular defects,
CC       hypoplastic left heart, double outlet right ventricle, and conduction
CC       abnormalities. Dysmorphic facial features include multiple hair whorls
CC       or hairline abnormalities, ptosis, epicanthal folds, and low-set or
CC       dysplastic ears. {ECO:0000269|PubMed:29961569}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the WD repeat TRAF7 family. {ECO:0000305}.
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DR   EMBL; AY569455; AAS68363.1; -; mRNA.
DR   EMBL; AL136921; CAB66855.1; -; mRNA.
DR   CCDS; CCDS10461.1; -. [Q6Q0C0-1]
DR   RefSeq; NP_115647.2; NM_032271.2. [Q6Q0C0-1]
DR   AlphaFoldDB; Q6Q0C0; -.
DR   SMR; Q6Q0C0; -.
DR   BioGRID; 123964; 128.
DR   CORUM; Q6Q0C0; -.
DR   IntAct; Q6Q0C0; 48.
DR   MINT; Q6Q0C0; -.
DR   STRING; 9606.ENSP00000318944; -.
DR   iPTMnet; Q6Q0C0; -.
DR   PhosphoSitePlus; Q6Q0C0; -.
DR   BioMuta; TRAF7; -.
DR   DMDM; 54036486; -.
DR   EPD; Q6Q0C0; -.
DR   jPOST; Q6Q0C0; -.
DR   MassIVE; Q6Q0C0; -.
DR   MaxQB; Q6Q0C0; -.
DR   PaxDb; 9606-ENSP00000318944; -.
DR   PeptideAtlas; Q6Q0C0; -.
DR   ProteomicsDB; 67263; -. [Q6Q0C0-1]
DR   ProteomicsDB; 67264; -. [Q6Q0C0-2]
DR   Pumba; Q6Q0C0; -.
DR   Antibodypedia; 23591; 203 antibodies from 29 providers.
DR   DNASU; 84231; -.
DR   Ensembl; ENST00000326181.11; ENSP00000318944.6; ENSG00000131653.14. [Q6Q0C0-1]
DR   Ensembl; ENST00000704452.1; ENSP00000515903.1; ENSG00000131653.14. [Q6Q0C0-1]
DR   GeneID; 84231; -.
DR   KEGG; hsa:84231; -.
DR   MANE-Select; ENST00000326181.11; ENSP00000318944.6; NM_032271.3; NP_115647.2.
DR   UCSC; uc002cow.4; human. [Q6Q0C0-1]
DR   AGR; HGNC:20456; -.
DR   CTD; 84231; -.
DR   DisGeNET; 84231; -.
DR   GeneCards; TRAF7; -.
DR   HGNC; HGNC:20456; TRAF7.
DR   HPA; ENSG00000131653; Low tissue specificity.
DR   MalaCards; TRAF7; -.
DR   MIM; 606692; gene.
DR   MIM; 618164; phenotype.
DR   neXtProt; NX_Q6Q0C0; -.
DR   OpenTargets; ENSG00000131653; -.
DR   Orphanet; 2495; Meningioma.
DR   Orphanet; 592570; TRAF7-associated heart defect-digital anomalies-facial dysmorphism-motor and speech delay syndrome.
DR   PharmGKB; PA134917323; -.
DR   VEuPathDB; HostDB:ENSG00000131653; -.
DR   eggNOG; KOG0274; Eukaryota.
DR   eggNOG; KOG0297; Eukaryota.
DR   GeneTree; ENSGT00940000157022; -.
DR   HOGENOM; CLU_026971_0_0_1; -.
DR   InParanoid; Q6Q0C0; -.
DR   OMA; NHHILCG; -.
DR   OrthoDB; 1109965at2759; -.
DR   PhylomeDB; Q6Q0C0; -.
DR   TreeFam; TF328643; -.
DR   PathwayCommons; Q6Q0C0; -.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q6Q0C0; -.
DR   SIGNOR; Q6Q0C0; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 84231; 44 hits in 1197 CRISPR screens.
DR   GenomeRNAi; 84231; -.
DR   Pharos; Q6Q0C0; Tbio.
DR   PRO; PR:Q6Q0C0; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q6Q0C0; Protein.
DR   Bgee; ENSG00000131653; Expressed in stromal cell of endometrium and 163 other cell types or tissues.
DR   ExpressionAtlas; Q6Q0C0; baseline and differential.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProt.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IDA:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
DR   GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IMP:UniProtKB.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IDA:UniProt.
DR   GO; GO:0035519; P:protein K29-linked ubiquitination; IDA:UniProt.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR   GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR   CDD; cd16644; mRING-HC-C3HC3D_TRAF7; 1.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   InterPro; IPR001293; Znf_TRAF.
DR   PANTHER; PTHR19848:SF8; E3 UBIQUITIN-PROTEIN LIGASE TRAF7; 1.
DR   PANTHER; PTHR19848; WD40 REPEAT PROTEIN; 1.
DR   Pfam; PF00400; WD40; 5.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 2.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS50145; ZF_TRAF; 1.
DR   Genevisible; Q6Q0C0; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cytoplasm; Cytoplasmic vesicle;
KW   Disease variant; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation; Ubl conjugation pathway; WD repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..670
FT                   /note="E3 ubiquitin-protein ligase TRAF7"
FT                   /id="PRO_0000051296"
FT   REPEAT          394..433
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          437..474
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          477..513
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          515..554
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          557..594
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          597..638
FT                   /note="WD 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          641..669
FT                   /note="WD 7"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         131..165
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         222..276
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          49..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         61
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         88
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   VAR_SEQ         1..76
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11230166,
FT                   ECO:0000303|PubMed:15001576"
FT                   /id="VSP_051607"
FT   VARIANT         346
FT                   /note="K -> E (in CAFDADD; no significant effect on
FT                   phosphorylation of MAPK1 and/or MAPK3; dbSNP:rs1567252467)"
FT                   /evidence="ECO:0000269|PubMed:29961569"
FT                   /id="VAR_081685"
FT   VARIANT         371
FT                   /note="R -> G (in CAFDADD; decreased phosphorylation of
FT                   MAPK1 and/or MAPK3; dbSNP:rs1567252659)"
FT                   /evidence="ECO:0000269|PubMed:29961569"
FT                   /id="VAR_081686"
FT   VARIANT         601
FT                   /note="T -> A (in CAFDADD; decreased phosphorylation of
FT                   MAPK1 and/or MAPK3; dbSNP:rs1567254067)"
FT                   /evidence="ECO:0000269|PubMed:29961569"
FT                   /id="VAR_081687"
FT   VARIANT         655
FT                   /note="R -> Q (in CAFDADD; decreased phosphorylation of
FT                   MAPK1 and/or MAPK3; dbSNP:rs1331463984)"
FT                   /evidence="ECO:0000269|PubMed:29961569"
FT                   /id="VAR_081688"
FT   MUTAGEN         131
FT                   /note="C->S: Complete loss of IFN-beta promoter inhibition
FT                   after viral infection."
FT                   /evidence="ECO:0000269|PubMed:37086853"
SQ   SEQUENCE   670 AA;  74609 MW;  5624045D674849C6 CRC64;
     MSSGKSARYN RFSGGPSNLP TPDVTTGTRM ETTFGPAFSA VTTITKADGT STYKQHCRTP
     SSSSTLAYSP RDEEDSMPPI STPRRSDSAI SVRSLHSESS MSLRSTFSLP EEEEEPEPLV
     FAEQPSVKLC CQLCCSVFKD PVITTCGHTF CRRCALKSEK CPVDNVKLTV VVNNIAVAEQ
     IGELFIHCRH GCRVAGSGKP PIFEVDPRGC PFTIKLSARK DHEGSCDYRP VRCPNNPSCP
     PLLRMNLEAH LKECEHIKCP HSKYGCTFIG NQDTYETHLE TCRFEGLKEF LQQTDDRFHE
     MHVALAQKDQ EIAFLRSMLG KLSEKIDQLE KSLELKFDVL DENQSKLSED LMEFRRDASM
     LNDELSHINA RLNMGILGSY DPQQIFKCKG TFVGHQGPVW CLCVYSMGDL LFSGSSDKTI
     KVWDTCTTYK CQKTLEGHDG IVLALCIQGC KLYSGSADCT IIVWDIQNLQ KVNTIRAHDN
     PVCTLVSSHN VLFSGSLKAI KVWDIVGTEL KLKKELTGLN HWVRALVAAQ SYLYSGSYQT
     IKIWDIRTLD CIHVLQTSGG SVYSIAVTNH HIVCGTYENL IHVWDIESKE QVRTLTGHVG
     TVYALAVIST PDQTKVFSAS YDRSLRVWSM DNMICTQTLL RHQGSVTALA VSRGRLFSGA
     VDSTVKVWTC
//