ID   TRI35_HUMAN             Reviewed;         493 AA.
AC   Q9UPQ4; Q86XQ0; Q8WVA4;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   24-JAN-2024, entry version 181.
DE   RecName: Full=E3 ubiquitin-protein ligase TRIM35 {ECO:0000303|PubMed:32562145};
DE            EC=2.3.2.27;
DE   AltName: Full=Hemopoietic lineage switch protein 5;
GN   Name=TRIM35; Synonyms=HLS5, KIAA1098;
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=Liver;
RX   PubMed=14662771; DOI=10.1074/jbc.m306751200;
RA   Lalonde J.-P., Lim R., Ingley E., Tilbrook P.A., Thompson M.J.,
RA   McCulloch R., Beaumont J.G., Wicking C., Eyre H.J., Sutherland G.R.,
RA   Howe K., Solomon E., Williams J.H., Klinken S.P.;
RT   "HLS5, a novel RBCC (ring finger, B box, coiled-coil) family member
RT   isolated from a hemopoietic lineage switch, is a candidate tumor
RT   suppressor.";
RL   J. Biol. Chem. 279:8181-8189(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA   Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:197-205(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-4 AND SER-8, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [6]
RP   FUNCTION, INTERACTION WITH PKM, AND SUBCELLULAR LOCATION.
RX   PubMed=25263439; DOI=10.1038/onc.2014.325;
RA   Chen Z., Wang Z., Guo W., Zhang Z., Zhao F., Zhao Y., Jia D., Ding J.,
RA   Wang H., Yao M., He X.;
RT   "TRIM35 Interacts with pyruvate kinase isoform M2 to suppress the Warburg
RT   effect and tumorigenicity in hepatocellular carcinoma.";
RL   Oncogene 34:3946-3956(2015).
RN   [7]
RP   FUNCTION, INDUCTION BY TLR5 AND TLR7, AND INTERACTION WITH IRF7.
RX   PubMed=25907537; DOI=10.1016/j.febslet.2015.04.019;
RA   Wang Y., Yan S., Yang B., Wang Y., Zhou H., Lian Q., Sun B.;
RT   "TRIM35 negatively regulates TLR7- and TLR9-mediated type I interferon
RT   production by targeting IRF7.";
RL   FEBS Lett. 589:1322-1330(2015).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH TRAF3.
RX   PubMed=32562145; DOI=10.1007/s13238-020-00734-6;
RA   Sun N., Jiang L., Ye M., Wang Y., Wang G., Wan X., Zhao Y., Wen X.,
RA   Liang L., Ma S., Liu L., Bu Z., Chen H., Li C.;
RT   "TRIM35 mediates protection against influenza infection by activating TRAF3
RT   and degrading viral PB2.";
RL   Protein Cell 11:894-914(2020).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that participates in multiple
CC       biological processes including cell death, glucose metabolism, and in
CC       particular, the innate immune response. Mediates 'Lys-63'-linked
CC       polyubiquitination of TRAF3 thereby promoting type I interferon
CC       production via RIG-I signaling pathway (PubMed:32562145). Can also
CC       catalyze 'Lys-48'-linked polyubiquitination and proteasomal degradation
CC       of viral proteins such as influenza virus PB2 (PubMed:32562145). Acts
CC       as a negative feedback regulator of TLR7- and TLR9-triggered signaling.
CC       Mechanistically, promotes the 'Lys-48'-linked ubiquitination of IRF7
CC       and induces its degradation via a proteasome-dependent pathway
CC       (PubMed:25907537). Reduces FGFR1-dependent tyrosine phosphorylation of
CC       PKM, inhibiting PKM-dependent lactate production, glucose metabolism,
CC       and cell growth (PubMed:25263439). {ECO:0000269|PubMed:25263439,
CC       ECO:0000269|PubMed:25907537, ECO:0000269|PubMed:32562145}.
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;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with PKM isoform M2, but not isoform M1; this
CC       interaction may compete with that between PKM and FGFR1, and hence
CC       reduces FGFR1-dependent tyrosine phosphorylation of PKM
CC       (PubMed:25263439). Interacts with IRF7; this interaction promotes IRF7
CC       proteasomal degradation (PubMed:25907537). Interacts with TRAF3; this
CC       interaction promotes TRAF3 activation (PubMed:32562145).
CC       {ECO:0000269|PubMed:25263439, ECO:0000269|PubMed:25907537,
CC       ECO:0000269|PubMed:32562145}.
CC   -!- INTERACTION:
CC       Q9UPQ4-2; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-17716262, EBI-10827839;
CC       Q9UPQ4-2; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-17716262, EBI-11524452;
CC       Q9UPQ4-2; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-17716262, EBI-12011224;
CC       Q9UPQ4-2; P27658: COL8A1; NbExp=3; IntAct=EBI-17716262, EBI-747133;
CC       Q9UPQ4-2; Q86UW9: DTX2; NbExp=3; IntAct=EBI-17716262, EBI-740376;
CC       Q9UPQ4-2; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-17716262, EBI-744099;
CC       Q9UPQ4-2; P22607: FGFR3; NbExp=3; IntAct=EBI-17716262, EBI-348399;
CC       Q9UPQ4-2; Q53EP0-3: FNDC3B; NbExp=3; IntAct=EBI-17716262, EBI-10242151;
CC       Q9UPQ4-2; Q14749: GNMT; NbExp=3; IntAct=EBI-17716262, EBI-744239;
CC       Q9UPQ4-2; Q14957: GRIN2C; NbExp=3; IntAct=EBI-17716262, EBI-8285963;
CC       Q9UPQ4-2; P28799: GRN; NbExp=3; IntAct=EBI-17716262, EBI-747754;
CC       Q9UPQ4-2; I6L957: HNRNPA2B1; NbExp=3; IntAct=EBI-17716262, EBI-1642515;
CC       Q9UPQ4-2; P42858: HTT; NbExp=9; IntAct=EBI-17716262, EBI-466029;
CC       Q9UPQ4-2; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-17716262, EBI-11955401;
CC       Q9UPQ4-2; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-17716262, EBI-2556193;
CC       Q9UPQ4-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-17716262, EBI-10975473;
CC       Q9UPQ4-2; P06239-3: LCK; NbExp=3; IntAct=EBI-17716262, EBI-13287659;
CC       Q9UPQ4-2; P25800: LMO1; NbExp=3; IntAct=EBI-17716262, EBI-8639312;
CC       Q9UPQ4-2; Q16656-4: NRF1; NbExp=3; IntAct=EBI-17716262, EBI-11742836;
CC       Q9UPQ4-2; Q9BYG5: PARD6B; NbExp=3; IntAct=EBI-17716262, EBI-295391;
CC       Q9UPQ4-2; O14737: PDCD5; NbExp=3; IntAct=EBI-17716262, EBI-712290;
CC       Q9UPQ4-2; Q9UPV7: PHF24; NbExp=3; IntAct=EBI-17716262, EBI-17717171;
CC       Q9UPQ4-2; P67775: PPP2CA; NbExp=3; IntAct=EBI-17716262, EBI-712311;
CC       Q9UPQ4-2; O43741: PRKAB2; NbExp=3; IntAct=EBI-17716262, EBI-1053424;
CC       Q9UPQ4-2; O60260-5: PRKN; NbExp=3; IntAct=EBI-17716262, EBI-21251460;
CC       Q9UPQ4-2; P86480: PRR20D; NbExp=3; IntAct=EBI-17716262, EBI-12754095;
CC       Q9UPQ4-2; P47897: QARS1; NbExp=4; IntAct=EBI-17716262, EBI-347462;
CC       Q9UPQ4-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-17716262, EBI-396669;
CC       Q9UPQ4-2; Q92529: SHC3; NbExp=3; IntAct=EBI-17716262, EBI-79084;
CC       Q9UPQ4-2; Q12824-2: SMARCB1; NbExp=3; IntAct=EBI-17716262, EBI-358436;
CC       Q9UPQ4-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-17716262, EBI-5235340;
CC       Q9UPQ4-2; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-17716262, EBI-11955057;
CC       Q9UPQ4-2; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-17716262, EBI-8451480;
CC       Q9UPQ4-2; Q9UDY6-2: TRIM10; NbExp=3; IntAct=EBI-17716262, EBI-11981577;
CC       Q9UPQ4-2; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-17716262, EBI-3918381;
CC       Q9UPQ4-2; P61086: UBE2K; NbExp=6; IntAct=EBI-17716262, EBI-473850;
CC       Q9UPQ4-2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-17716262, EBI-741480;
CC       Q9UPQ4-2; O76024: WFS1; NbExp=3; IntAct=EBI-17716262, EBI-720609;
CC       Q9UPQ4-2; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-17716262, EBI-11741890;
CC       Q9UPQ4-2; Q9Y649; NbExp=3; IntAct=EBI-17716262, EBI-25900580;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25263439}. Nucleus
CC       {ECO:0000250}. Note=Found predominantly in cytoplasm with a granular
CC       distribution. Found in punctuate nuclear bodies (By similarity).
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UPQ4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UPQ4-2; Sequence=VSP_012061;
CC   -!- INDUCTION: By TLR7 and TLR9 stimulation. {ECO:0000269|PubMed:25907537}.
CC   -!- DOMAIN: The RING finger domain and the coiled-coil region are required
CC       for the apoptosis-inducing activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA83050.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF492463; AAO85480.1; -; mRNA.
DR   EMBL; AB029021; BAA83050.1; ALT_INIT; mRNA.
DR   EMBL; BC018337; AAH18337.1; -; mRNA.
DR   EMBL; BC069226; AAH69226.1; -; mRNA.
DR   CCDS; CCDS6056.2; -. [Q9UPQ4-1]
DR   RefSeq; NP_741983.2; NM_171982.4. [Q9UPQ4-1]
DR   AlphaFoldDB; Q9UPQ4; -.
DR   SMR; Q9UPQ4; -.
DR   BioGRID; 116716; 105.
DR   IntAct; Q9UPQ4; 68.
DR   STRING; 9606.ENSP00000301924; -.
DR   GlyGen; Q9UPQ4; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UPQ4; -.
DR   PhosphoSitePlus; Q9UPQ4; -.
DR   BioMuta; TRIM35; -.
DR   DMDM; 56404980; -.
DR   EPD; Q9UPQ4; -.
DR   jPOST; Q9UPQ4; -.
DR   MassIVE; Q9UPQ4; -.
DR   MaxQB; Q9UPQ4; -.
DR   PaxDb; 9606-ENSP00000301924; -.
DR   PeptideAtlas; Q9UPQ4; -.
DR   ProteomicsDB; 85414; -. [Q9UPQ4-1]
DR   ProteomicsDB; 85415; -. [Q9UPQ4-2]
DR   Antibodypedia; 10095; 325 antibodies from 33 providers.
DR   DNASU; 23087; -.
DR   Ensembl; ENST00000305364.9; ENSP00000301924.4; ENSG00000104228.13. [Q9UPQ4-1]
DR   GeneID; 23087; -.
DR   KEGG; hsa:23087; -.
DR   MANE-Select; ENST00000305364.9; ENSP00000301924.4; NM_171982.5; NP_741983.2.
DR   UCSC; uc003xfl.2; human. [Q9UPQ4-1]
DR   AGR; HGNC:16285; -.
DR   CTD; 23087; -.
DR   DisGeNET; 23087; -.
DR   GeneCards; TRIM35; -.
DR   HGNC; HGNC:16285; TRIM35.
DR   HPA; ENSG00000104228; Low tissue specificity.
DR   MIM; 617007; gene.
DR   neXtProt; NX_Q9UPQ4; -.
DR   OpenTargets; ENSG00000104228; -.
DR   PharmGKB; PA38115; -.
DR   VEuPathDB; HostDB:ENSG00000104228; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000160868; -.
DR   HOGENOM; CLU_013137_0_3_1; -.
DR   InParanoid; Q9UPQ4; -.
DR   OMA; CYDPFRE; -.
DR   OrthoDB; 5479648at2759; -.
DR   PhylomeDB; Q9UPQ4; -.
DR   TreeFam; TF334286; -.
DR   PathwayCommons; Q9UPQ4; -.
DR   Reactome; R-HSA-877300; Interferon gamma signaling.
DR   SignaLink; Q9UPQ4; -.
DR   SIGNOR; Q9UPQ4; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 23087; 21 hits in 1204 CRISPR screens.
DR   ChiTaRS; TRIM35; human.
DR   GenomeRNAi; 23087; -.
DR   Pharos; Q9UPQ4; Tbio.
DR   PRO; PR:Q9UPQ4; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q9UPQ4; Protein.
DR   Bgee; ENSG00000104228; Expressed in calcaneal tendon and 148 other cell types or tissues.
DR   ExpressionAtlas; Q9UPQ4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0044790; P:suppression of viral release by host; IDA:UniProtKB.
DR   CDD; cd16599; RING-HC_TRIM35_C-IV; 1.
DR   CDD; cd12893; SPRY_PRY_TRIM35; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR003879; Butyrophylin_SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR   PANTHER; PTHR24103:SF665; E3 UBIQUITIN-PROTEIN LIGASE TRIM35; 1.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   Genevisible; Q9UPQ4; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Apoptosis; Coiled coil; Cytoplasm;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..493
FT                   /note="E3 ubiquitin-protein ligase TRIM35"
FT                   /id="PRO_0000056250"
FT   DOMAIN          284..487
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         21..61
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         96..137
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   COILED          210..251
FT                   /evidence="ECO:0000255"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   VAR_SEQ         146..206
FT                   /note="AKCRNMEHALREKAKAFWAMRRSYEAIAKHNQVEAAWLEGRIRQEFDKLREF
FT                   LRVEEQAIL -> VRSLIAEERRNFLPTHQWIVTKTRLQTSSPNLQSRRQGQVQEHGAC
FT                   TAGEGQGLLGHAALL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012061"
SQ   SEQUENCE   493 AA;  56540 MW;  BFB7E5BFD3AD7E2D CRC64;
     MERSPDVSPG PSRSFKEELL CAVCYDPFRD AVTLRCGHNF CRGCVSRCWE VQVSPTCPVC
     KDRASPADLR TNHTLNNLVE KLLREEAEGA RWTSYRFSRV CRLHRGQLSL FCLEDKELLC
     CSCQADPRHQ GHRVQPVKDT AHDFRAKCRN MEHALREKAK AFWAMRRSYE AIAKHNQVEA
     AWLEGRIRQE FDKLREFLRV EEQAILDAMA EETRQKQLLA DEKMKQLTEE TEVLAHEIER
     LQMEMKEDDV SFLMKHKSRK RRLFCTMEPE PVQPGMLIDV CKYLGSLQYR VWKKMLASVE
     SVPFSFDPNT AAGWLSVSDD LTSVTNHGYR VQVENPERFS SAPCLLGSRV FSQGSHAWEV
     ALGGLQSWRV GVVRVRQDSG AEGHSHSCYH DTRSGFWYVC RTQGVEGDHC VTSDPATSPL
     VLAIPRRLRV ELECEEGELS FYDAERHCHL YTFHARFGEV RPYFYLGGAR GAGPPEPLRI
     CPLHISVKEE LDG
//