ID TRI34_HUMAN Reviewed; 488 AA. AC Q9BYJ4; D3DQS7; Q9C016; Q9HCR0; Q9HCR1; Q9HCR2; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 2. DT 24-JAN-2024, entry version 175. DE RecName: Full=E3 ubiquitin-protein ligase TRIM34; DE EC=2.3.2.27 {ECO:0000305|PubMed:35065966}; DE AltName: Full=Interferon-responsive finger protein 1; DE AltName: Full=RING finger protein 21; GN Name=TRIM34; Synonyms=IFP1, RNF21; 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), ALTERNATIVE SPLICING, RP INDUCTION, AND TISSUE SPECIFICITY. RX PubMed=11013086; DOI=10.1006/geno.2000.6318; RA Orimo A., Tominaga N., Yoshimura K., Yamauchi Y., Nomura M., Sato M., RA Nogi Y., Suzuki M., Suzuki H., Ikeda K., Inoue S., Muramatsu M.; RT "Molecular cloning of ring finger protein 21 (RNF21)/interferon-responsive RT finger protein (ifp1), which possesses two RING-B box-coiled coil domains RT in tandem."; RL Genomics 69:143-149(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140; RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L., RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S., RA Pelicci P.G., Ballabio A.; RT "The tripartite motif family identifies cell compartments."; RL EMBO J. 20:2140-2151(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Thyroid; 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 [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] OF 79-488 (ISOFORM 1). RC TISSUE=Lymph node; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP FUNCTION, INTERACTION WITH TRIM5, INTERACTION WITH HIV-1 CAPSID PROTEIN RP (MICROBIAL INFECTION), SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=17156811; DOI=10.1016/j.virol.2006.10.035; RA Li X., Gold B., O'hUigin C., Diaz-Griffero F., Song B., Si Z., Li Y., RA Yuan W., Stremlau M., Mische C., Javanbakht H., Scally M., Winkler C., RA Dean M., Sodroski J.; RT "Unique features of TRIM5alpha among closely related human TRIM family RT members."; RL Virology 360:419-433(2007). RN [7] RP INTERACTION WITH TRIM5, AND MUTAGENESIS OF ARG-121. RX PubMed=21680743; DOI=10.1074/jbc.m111.260406; RA Li X., Yeung D.F., Fiegen A.M., Sodroski J.; RT "Determinants of the higher order association of the restriction factor RT TRIM5alpha and other tripartite motif (TRIM) proteins."; RL J. Biol. Chem. 286:27959-27970(2011). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=31487507; DOI=10.1016/j.yexcr.2019.111594; RA Sun D., An X., Ji B.; RT "TRIM34 facilitates the formation of multinucleated giant cells by RT enhancing cell fusion and phagocytosis in epithelial cells."; RL Exp. Cell Res. 384:111594-111594(2019). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=32282853; DOI=10.1371/journal.ppat.1008507; RA Ohainle M., Kim K., Komurlu Keceli S., Felton A., Campbell E., Luban J., RA Emerman M.; RT "TRIM34 restricts HIV-1 and SIV capsids in a TRIM5alpha-dependent manner."; RL PLoS Pathog. 16:e1008507-e1008507(2020). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=31956709; DOI=10.1016/j.heliyon.2019.e03115; RA An X., Ji B., Sun D.; RT "TRIM34 localizes to the mitochondria and mediates apoptosis through the RT mitochondrial pathway in HEK293T cells."; RL Heliyon 6:e03115-e03115(2020). RN [11] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=35065966; DOI=10.1016/j.jbc.2022.101611; RA Wang X., Xiong J., Zhou D., Zhang S., Wang L., Tian Q., Li C., Liu J., RA Wu Y., Li J., Wang J.; RT "TRIM34 modulates influenza virus-activated programmed cell death by RT targeting Z-DNA-binding protein 1 for K63-linked polyubiquitination."; RL J. Biol. Chem. 298:101611-101611(2022). RN [12] RP STRUCTURE BY NMR OF 8-79. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the RING-finger domain from human tripartite motif RT protein 34."; RL Submitted (SEP-2007) to the PDB data bank. CC -!- FUNCTION: Functions as antiviral protein and contributes to the defense CC against retroviral infections (PubMed:17156811, PubMed:32282853). Acts CC as a capsid-specific restriction factor with the help of TRIM5 and CC prevents infection from non-host-adapted retroviruses CC (PubMed:32282853). During influenza A virus infection, promotes CC programmed cell death by targeting ZBP1 for 'Lys-63'-linked CC polyubiquitination (PubMed:35065966). In turn, promotes ZBP1 CC recruitment of RIPK3 to mediate virus-induced programmed necrosis CC (PubMed:35065966). Negatively regulates the function of mitochondria by CC enhancing mitochondrial depolarization leading to cytochrome c release CC and mitochondria-dependent apoptosis (PubMed:31956709). Promotes also CC the formation of multinucleated giant cells by means of cell fusion and CC phagocytosis in epithelial cells (PubMed:31487507). CC {ECO:0000269|PubMed:17156811, ECO:0000269|PubMed:31487507, CC ECO:0000269|PubMed:31956709, ECO:0000269|PubMed:32282853, CC ECO:0000269|PubMed:35065966}. 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:0000305|PubMed:35065966}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Homotrimer. Interacts (via B-box and SPRY domain) with TRIM5 CC (PubMed:21680743, PubMed:17156811). {ECO:0000269|PubMed:17156811, CC ECO:0000269|PubMed:21680743}. CC -!- SUBUNIT: (Microbial infection) Interacts (via the B30.2/SPRY domain) CC with HIV-1 capsid complexes (PubMed:17156811). CC {ECO:0000269|PubMed:17156811}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17156811, CC ECO:0000269|PubMed:31487507, ECO:0000269|PubMed:32282853}. CC Mitochondrion {ECO:0000269|PubMed:31956709}. Note=Localizes in CC cytoplasmic bodies together with TRIM5 and incoming HIV-1 capsids CC during infection. {ECO:0000269|PubMed:32282853}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Medium; CC IsoId=Q9BYJ4-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=Q9BYJ4-2; Sequence=VSP_011921, VSP_011922; CC -!- TISSUE SPECIFICITY: [Isoform 1]: Is the most abundant form. It is CC highly expressed in the placenta, spleen, colon and peripheral blood CC leukocytes. {ECO:0000269|PubMed:11013086}. CC -!- INDUCTION: [Isoform 1]: Up-regulated by interferons. CC {ECO:0000269|PubMed:11013086}. CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG53517.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB17050.1; Type=Miscellaneous discrepancy; Note=The in vivo relevance of this transcript of the TRIM6 (AC Q9C030) and TRIM34 genes creating a chimeric protein of 842 residues is uncertain.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB039902; BAB17049.1; -; mRNA. DR EMBL; AB039903; BAB17050.1; ALT_SEQ; mRNA. DR EMBL; AB039904; BAB17051.1; -; mRNA. DR EMBL; AF220143; AAG53516.1; -; mRNA. DR EMBL; AF220144; AAG53517.1; ALT_INIT; mRNA. DR EMBL; AK027876; BAB55424.1; -; mRNA. DR EMBL; CH471064; EAW68778.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68780.1; -; Genomic_DNA. DR EMBL; AL583914; CAC29498.1; -; mRNA. DR CCDS; CCDS31391.1; -. [Q9BYJ4-1] DR RefSeq; NP_001003827.1; NM_001003827.1. [Q9BYJ4-1] DR RefSeq; NP_067629.2; NM_021616.5. [Q9BYJ4-1] DR RefSeq; NP_569074.2; NM_130390.2. DR PDB; 2EGP; NMR; -; A=8-79. DR PDBsum; 2EGP; -. DR AlphaFoldDB; Q9BYJ4; -. DR SMR; Q9BYJ4; -. DR BioGRID; 119809; 22. DR IntAct; Q9BYJ4; 6. DR STRING; 9606.ENSP00000346916; -. DR iPTMnet; Q9BYJ4; -. DR PhosphoSitePlus; Q9BYJ4; -. DR BioMuta; TRIM34; -. DR DMDM; 55976584; -. DR EPD; Q9BYJ4; -. DR jPOST; Q9BYJ4; -. DR MassIVE; Q9BYJ4; -. DR MaxQB; Q9BYJ4; -. DR PaxDb; 9606-ENSP00000346916; -. DR PeptideAtlas; Q9BYJ4; -. DR ProteomicsDB; 79657; -. [Q9BYJ4-1] DR ProteomicsDB; 79658; -. [Q9BYJ4-2] DR Antibodypedia; 57793; 153 antibodies from 20 providers. DR DNASU; 53840; -. DR Ensembl; ENST00000429814.3; ENSP00000402595.2; ENSG00000258659.7. [Q9BYJ4-1] DR Ensembl; ENST00000514226.5; ENSP00000422947.1; ENSG00000258659.7. [Q9BYJ4-1] DR GeneID; 53840; -. DR KEGG; hsa:53840; -. DR MANE-Select; ENST00000429814.3; ENSP00000402595.2; NM_021616.6; NP_067629.2. DR UCSC; uc001mbh.4; human. [Q9BYJ4-1] DR AGR; HGNC:10063; -. DR CTD; 53840; -. DR DisGeNET; 53840; -. DR GeneCards; TRIM34; -. DR HGNC; HGNC:10063; TRIM34. DR HPA; ENSG00000258659; Low tissue specificity. DR MIM; 605684; gene. DR neXtProt; NX_Q9BYJ4; -. DR OpenTargets; ENSG00000258659; -. DR PharmGKB; PA35533; -. DR VEuPathDB; HostDB:ENSG00000258659; -. DR eggNOG; KOG2177; Eukaryota. DR GeneTree; ENSGT00940000162320; -. DR HOGENOM; CLU_013137_0_3_1; -. DR InParanoid; Q9BYJ4; -. DR OMA; CHICEFI; -. DR OrthoDB; 3453019at2759; -. DR PhylomeDB; Q9BYJ4; -. DR PathwayCommons; Q9BYJ4; -. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR SignaLink; Q9BYJ4; -. DR SIGNOR; Q9BYJ4; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 53840; 10 hits in 1114 CRISPR screens. DR EvolutionaryTrace; Q9BYJ4; -. DR GenomeRNAi; 53840; -. DR Pharos; Q9BYJ4; Tbio. DR PRO; PR:Q9BYJ4; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9BYJ4; Protein. DR Bgee; ENSG00000258659; Expressed in monocyte and 102 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central. DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central. 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:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR GO; GO:0045087; P:innate immune response; IBA:GO_Central. DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IBA:GO_Central. DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central. DR GO; GO:0032880; P:regulation of protein localization; IBA:GO_Central. DR GO; GO:0046596; P:regulation of viral entry into host cell; IBA:GO_Central. DR CDD; cd19761; Bbox2_TRIM5-like; 1. DR CDD; cd16591; RING-HC_TRIM5-like_C-IV; 1. DR CDD; cd15825; SPRY_PRY_TRIM34; 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; IPR003877; SPRY_dom. DR InterPro; IPR035826; TRIM34_PRY/SPRY. 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:SF647; TRIPARTITE MOTIF-CONTAINING PROTEIN 34; 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; 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; Q9BYJ4; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Antiviral defense; Coiled coil; KW Cytoplasm; Metal-binding; Mitochondrion; Reference proteome; Repeat; KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..488 FT /note="E3 ubiquitin-protein ligase TRIM34" FT /id="PRO_0000056248" FT DOMAIN 283..488 FT /note="B30.2/SPRY" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548" FT ZN_FING 15..60 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT ZN_FING 92..134 FT /note="B box-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT COILED 131..239 FT /evidence="ECO:0000255" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 119 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 125 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT VAR_SEQ 259..270 FT /note="SEIWRLKKPKMV -> CVWVATSGACEL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11013086" FT /id="VSP_011921" FT VAR_SEQ 271..488 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11013086" FT /id="VSP_011922" FT VARIANT 276 FT /note="T -> S (in dbSNP:rs6578670)" FT /id="VAR_019825" FT VARIANT 282 FT /note="D -> H (in dbSNP:rs3740997)" FT /id="VAR_019826" FT VARIANT 404 FT /note="N -> K (in dbSNP:rs16933844)" FT /id="VAR_052141" FT MUTAGEN 121 FT /note="R->E: Reduced association with TRIM5." FT /evidence="ECO:0000269|PubMed:21680743" FT CONFLICT 349 FT /note="H -> Y (in Ref. 5)" FT /evidence="ECO:0000305" FT TURN 16..19 FT /evidence="ECO:0007829|PDB:2EGP" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:2EGP" FT HELIX 36..39 FT /evidence="ECO:0007829|PDB:2EGP" FT STRAND 47..49 FT /evidence="ECO:0007829|PDB:2EGP" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:2EGP" FT HELIX 67..69 FT /evidence="ECO:0007829|PDB:2EGP" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:2EGP" SQ SEQUENCE 488 AA; 56864 MW; F2D60A16576187A0 CRC64; MASKILLNVQ EEVTCPICLE LLTEPLSLDC GHSLCRACIT VSNKEAVTSM GGKSSCPVCG ISYSFEHLQA NQHLANIVER LKEVKLSPDN GKKRDLCDHH GEKLLLFCKE DRKVICWLCE RSQEHRGHHT VLTEEVFKEC QEKLQAVLKR LKKEEEEAEK LEADIREEKT SWKYQVQTER QRIQTEFDQL RSILNNEEQR ELQRLEEEEK KTLDKFAEAE DELVQQKQLV RELISDVECR SQWSTMELLQ DMSGIMKWSE IWRLKKPKMV SKKLKTVFHA PDLSRMLQMF RELTAVRCYW VDVTLNSVNL NLNLVLSEDQ RQVISVPIWP FQCYNYGVLG SQYFSSGKHY WEVDVSKKTA WILGVYCRTY SRHMKYVVRR CANRQNLYTK YRPLFGYWVI GLQNKCKYGV FEESLSSDPE VLTLSMAVPP CRVGVFLDYE AGIVSFFNVT SHGSLIYKFS KCCFSQPVYP YFNPWNCPAP MTLCPPSS //