TRI62_HUMAN
ID TRI62_HUMAN Reviewed; 475 AA.
AC Q9BVG3; B3KVH5; B4DTE4; D3DPR1; Q9NVG0;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM62 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:23402750, ECO:0000269|PubMed:26488816};
DE AltName: Full=Tripartite motif-containing protein 62 {ECO:0000303|PubMed:23402750};
GN Name=TRIM62 {ECO:0000303|PubMed:23402750, ECO:0000312|HGNC:HGNC:25574};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Synovium;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION,
RP POLYUBIQUITINATION, AND INTERACTION WITH UBE2D2.
RX PubMed=23402750; DOI=10.1016/j.bbrc.2013.02.012;
RA Huang F., Xiao H., Sun B.L., Yang R.G.;
RT "Characterization of TRIM62 as a RING finger E3 ubiquitin ligase and its
RT subcellular localization.";
RL Biochem. Biophys. Res. Commun. 432:208-213(2013).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 11-CYS--CYS-14.
RX PubMed=26488816; DOI=10.1016/j.immuni.2015.10.005;
RA Cao Z., Conway K.L., Heath R.J., Rush J.S., Leshchiner E.S.,
RA Ramirez-Ortiz Z.G., Nedelsky N.B., Huang H., Ng A., Gardet A., Cheng S.C.,
RA Shamji A.F., Rioux J.D., Wijmenga C., Netea M.G., Means T.K., Daly M.J.,
RA Xavier R.J.;
RT "Ubiquitin ligase TRIM62 regulates CARD9-mediated anti-fungal immunity and
RT intestinal inflammation.";
RL Immunity 43:715-726(2015).
CC -!- FUNCTION: E3 ubiquitin ligase that plays a role in antifungal immunity
CC by mediating 'Lys-27'-linked ubiquitination of CARD9 downstream of C-
CC type lectin receptors; leading to CARD9 activation, followed by
CC activation of NF-kappa-B and MAP kinase p38 pathways (PubMed:26488816).
CC E3 ubiquitin ligase activity is dependent on E2 ubiquitin-conjugating
CC enzyme UBE2D2 (PubMed:23402750). {ECO:0000269|PubMed:23402750,
CC ECO:0000269|PubMed:26488816}.
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:23402750,
CC ECO:0000269|PubMed:26488816};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:23402750, ECO:0000269|PubMed:26488816}.
CC -!- SUBUNIT: Interacts with the ubiquitin-conjugating enzyme, UBE2D2.
CC {ECO:0000269|PubMed:23402750}.
CC -!- INTERACTION:
CC Q9BVG3; Q96JC9: EAF1; NbExp=3; IntAct=EBI-6929619, EBI-769261;
CC Q9BVG3; O95208-2: EPN2; NbExp=3; IntAct=EBI-6929619, EBI-12135243;
CC Q9BVG3; Q9NQT4: EXOSC5; NbExp=3; IntAct=EBI-6929619, EBI-371876;
CC Q9BVG3; Q9NVQ4-2: FAIM; NbExp=3; IntAct=EBI-6929619, EBI-12039347;
CC Q9BVG3; P35754: GLRX; NbExp=5; IntAct=EBI-6929619, EBI-3905236;
CC Q9BVG3; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-6929619, EBI-2557469;
CC Q9BVG3; Q8TDD2: SP7; NbExp=5; IntAct=EBI-6929619, EBI-10713842;
CC Q9BVG3; Q9P0N9: TBC1D7; NbExp=3; IntAct=EBI-6929619, EBI-3258000;
CC Q9BVG3; Q9BVG3: TRIM62; NbExp=5; IntAct=EBI-6929619, EBI-6929619;
CC Q9BVG3; P51668: UBE2D1; NbExp=3; IntAct=EBI-6929619, EBI-743540;
CC Q9BVG3; P61077: UBE2D3; NbExp=3; IntAct=EBI-6929619, EBI-348268;
CC Q9BVG3; Q9Y2X8: UBE2D4; NbExp=3; IntAct=EBI-6929619, EBI-745527;
CC Q9BVG3; Q969T4: UBE2E3; NbExp=3; IntAct=EBI-6929619, EBI-348496;
CC Q9BVG3; O14933: UBE2L6; NbExp=3; IntAct=EBI-6929619, EBI-2129974;
CC Q9BVG3; O94888: UBXN7; NbExp=3; IntAct=EBI-6929619, EBI-1993627;
CC Q9BVG3; Q68CQ4: UTP25; NbExp=3; IntAct=EBI-6929619, EBI-747711;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23402750,
CC ECO:0000269|PubMed:26488816}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BVG3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BVG3-2; Sequence=VSP_055441, VSP_055442;
CC -!- DOMAIN: The RING finger is required for ubiquitin ligase activity.
CC {ECO:0000269|PubMed:23402750}.
CC -!- PTM: Polyubiquitinated, autoubiquitinated in the presence of UBE2D2.
CC {ECO:0000269|PubMed:23402750}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AK001621; BAA91792.1; -; mRNA.
DR EMBL; AK122896; BAG53787.1; -; mRNA.
DR EMBL; AK300177; BAG61956.1; -; mRNA.
DR EMBL; AL662907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07466.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07467.1; -; Genomic_DNA.
DR EMBL; BC001222; AAH01222.1; -; mRNA.
DR EMBL; BC007999; AAH07999.1; -; mRNA.
DR EMBL; BC011689; AAH11689.1; -; mRNA.
DR EMBL; BC012152; AAH12152.1; -; mRNA.
DR CCDS; CCDS376.1; -. [Q9BVG3-1]
DR CCDS; CCDS81297.1; -. [Q9BVG3-2]
DR RefSeq; NP_001317412.1; NM_001330483.1. [Q9BVG3-2]
DR RefSeq; NP_060677.2; NM_018207.2. [Q9BVG3-1]
DR AlphaFoldDB; Q9BVG3; -.
DR SMR; Q9BVG3; -.
DR BioGRID; 120518; 31.
DR IntAct; Q9BVG3; 25.
DR MINT; Q9BVG3; -.
DR STRING; 9606.ENSP00000291416; -.
DR iPTMnet; Q9BVG3; -.
DR PhosphoSitePlus; Q9BVG3; -.
DR BioMuta; TRIM62; -.
DR DMDM; 74752380; -.
DR EPD; Q9BVG3; -.
DR MassIVE; Q9BVG3; -.
DR PaxDb; Q9BVG3; -.
DR PeptideAtlas; Q9BVG3; -.
DR PRIDE; Q9BVG3; -.
DR ProteomicsDB; 5103; -.
DR ProteomicsDB; 79199; -. [Q9BVG3-1]
DR Antibodypedia; 17083; 174 antibodies from 24 providers.
DR DNASU; 55223; -.
DR Ensembl; ENST00000291416.10; ENSP00000291416.5; ENSG00000116525.14. [Q9BVG3-1]
DR Ensembl; ENST00000543586.1; ENSP00000441173.1; ENSG00000116525.14. [Q9BVG3-2]
DR GeneID; 55223; -.
DR KEGG; hsa:55223; -.
DR MANE-Select; ENST00000291416.10; ENSP00000291416.5; NM_018207.3; NP_060677.2.
DR UCSC; uc001bxb.4; human. [Q9BVG3-1]
DR CTD; 55223; -.
DR DisGeNET; 55223; -.
DR GeneCards; TRIM62; -.
DR HGNC; HGNC:25574; TRIM62.
DR HPA; ENSG00000116525; Tissue enhanced (brain).
DR neXtProt; NX_Q9BVG3; -.
DR OpenTargets; ENSG00000116525; -.
DR PharmGKB; PA134890243; -.
DR VEuPathDB; HostDB:ENSG00000116525; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000158433; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q9BVG3; -.
DR OMA; TAHHRLI; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q9BVG3; -.
DR TreeFam; TF342569; -.
DR BRENDA; 2.3.2.27; 2681.
DR PathwayCommons; Q9BVG3; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q9BVG3; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 55223; 16 hits in 1116 CRISPR screens.
DR ChiTaRS; TRIM62; human.
DR GenomeRNAi; 55223; -.
DR Pharos; Q9BVG3; Tbio.
DR PRO; PR:Q9BVG3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BVG3; protein.
DR Bgee; ENSG00000116525; Expressed in oocyte and 184 other tissues.
DR Genevisible; Q9BVG3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:ARUK-UCL.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB.
DR GO; GO:1905036; P:positive regulation of antifungal innate immune response; IDA:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0044314; P:protein K27-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0046596; P:regulation of viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0019076; P:viral release from host cell; IMP:UniProtKB.
DR CDD; cd13744; SPRY_PRY_TRIM62; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 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; IPR035830; PRY/SPRY_TRIM62.
DR InterPro; IPR003877; SPRY_dom.
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 Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 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.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Immunity; Innate immunity;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..475
FT /note="E3 ubiquitin-protein ligase TRIM62"
FT /id="PRO_0000249574"
FT DOMAIN 277..475
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 11..54
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 88..128
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 127..241
FT /evidence="ECO:0000255"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 1..15
FT /note="MACSLKDELLCSICL -> MPEKTAVDQPWTQAL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055441"
FT VAR_SEQ 16..136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055442"
FT MUTAGEN 11..14
FT /note="CSIC->ASIA: Abolished E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:26488816"
FT CONFLICT 102
FT /note="F -> L (in Ref. 1; BAA91792)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="R -> L (in Ref. 1; BAA91792)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 54268 MW; DC15CA9B795DFBB0 CRC64;
MACSLKDELL CSICLSIYQD PVSLGCEHYF CRRCITEHWV RQEAQGARDC PECRRTFAEP
ALAPSLKLAN IVERYSSFPL DAILNARRAA RPCQAHDKVK LFCLTDRALL CFFCDEPALH
EQHQVTGIDD AFDELQRELK DQLQALQDSE REHTEALQLL KRQLAETKSS TKSLRTTIGE
AFERLHRLLR ERQKAMLEEL EADTARTLTD IEQKVQRYSQ QLRKVQEGAQ ILQERLAETD
RHTFLAGVAS LSERLKGKIH ETNLTYEDFP TSKYTGPLQY TIWKSLFQDI HPVPAALTLD
PGTAHQRLIL SDDCTIVAYG NLHPQPLQDS PKRFDVEVSV LGSEAFSSGV HYWEVVVAEK
TQWVIGLAHE AASRKGSIQI QPSRGFYCIV MHDGNQYSAC TEPWTRLNVR DKLDKVGVFL
DYDQGLLIFY NADDMSWLYT FREKFPGKLC SYFSPGQSHA NGKNVQPLRI NTVRI
