AREL1_HUMAN
ID AREL1_HUMAN Reviewed; 823 AA.
AC O15033; B4E2C7; Q7LDY1; Q8IYY9;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Apoptosis-resistant E3 ubiquitin protein ligase 1 {ECO:0000305};
DE EC=2.3.2.26 {ECO:0000269|PubMed:23479728, ECO:0000269|PubMed:25752577};
DE AltName: Full=Apoptosis-resistant HECT-type E3 ubiquitin transferase 1 {ECO:0000303|PubMed:23479728};
GN Name=AREL1 {ECO:0000303|PubMed:23479728, ECO:0000312|HGNC:HGNC:20363};
GN Synonyms=KIAA0317 {ECO:0000303|PubMed:9205841};
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH SEPTIN4; HTRA2 AND
RP DIABLO, ACTIVE SITE, AUTOUBIQUITINATION, AND MUTAGENESIS OF CYS-790.
RX PubMed=23479728; DOI=10.1074/jbc.m112.436113;
RA Kim J.B., Kim S.Y., Kim B.M., Lee H., Kim I., Yun J., Jo Y., Oh T., Jo Y.,
RA Chae H.D., Shin D.Y.;
RT "Identification of a novel anti-apoptotic E3 ubiquitin ligase that
RT ubiquitinates antagonists of inhibitor of apoptosis proteins SMAC, HtrA2,
RT and ARTS.";
RL J. Biol. Chem. 288:12014-12021(2013).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=25752577; DOI=10.1016/j.molcel.2015.01.042;
RA Michel M.A., Elliott P.R., Swatek K.N., Simicek M., Pruneda J.N.,
RA Wagstaff J.L., Freund S.M., Komander D.;
RT "Assembly and specific recognition of K29- and K33-linked polyubiquitin.";
RL Mol. Cell 58:95-109(2015).
RN [8]
RP FUNCTION, INTERACTION WITH SOCS2, AND CHARACTERIZATION OF VARIANT LEU-779.
RX PubMed=31578312; DOI=10.1172/jci.insight.129110;
RA Lear T.B., McKelvey A.C., Evankovich J.W., Rajbhandari S., Coon T.A.,
RA Dunn S.R., Londino J.D., McVerry B.J., Zhang Y., Valenzi E., Burton C.L.,
RA Gordon R., Gingras S., Lockwood K.C., Jurczak M.J., Lafyatis R.,
RA Shlomchik M.J., Liu Y., Chen B.B.;
RT "KIAA0317 regulates pulmonary inflammation through SOCS2 degradation.";
RL JCI Insight 4:0-0(2019).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that catalyzes 'Lys-11'- or 'Lys-
CC 33'-linked polyubiquitin chains, with some preference for 'Lys-33'
CC linkages (PubMed:25752577). E3 ubiquitin-protein ligases accept
CC ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a
CC thioester and then directly transfers the ubiquitin to targeted
CC substrates (PubMed:23479728, PubMed:31578312). Ubiquitinates SEPTIN4,
CC DIABLO/SMAC and HTRA2 in vitro (PubMed:23479728). Modulates pulmonary
CC inflammation by targeting SOCS2 for ubiquitination and subsequent
CC degradation by the proteasome (PubMed:31578312).
CC {ECO:0000269|PubMed:23479728, ECO:0000269|PubMed:25752577,
CC ECO:0000269|PubMed:31578312}.
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=2.3.2.26; Evidence={ECO:0000269|PubMed:23479728,
CC ECO:0000269|PubMed:25752577};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:23479728, ECO:0000269|PubMed:25752577}.
CC -!- SUBUNIT: Interacts with SOCS2 (PubMed:31578312). Interacts (via HECT
CC domain) with HTRA2, DIABLO/SMAC and SEPTIN4; in the cytoplasm following
CC induction of apoptosis (PubMed:23479728). {ECO:0000269|PubMed:23479728,
CC ECO:0000269|PubMed:31578312}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15033-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15033-2; Sequence=VSP_013259;
CC -!- PTM: Autoubiquitinated in vitro in the presence of E2 enzyme
CC UBE2D1/UBCH5A. {ECO:0000269|PubMed:23479728}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20775.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB002315; BAA20775.2; ALT_INIT; mRNA.
DR EMBL; AK304217; BAG65089.1; -; mRNA.
DR EMBL; AC007956; AAF61276.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81186.1; -; Genomic_DNA.
DR EMBL; BC032944; AAH32944.1; -; mRNA.
DR CCDS; CCDS41971.1; -. [O15033-1]
DR RefSeq; NP_001034568.1; NM_001039479.1. [O15033-1]
DR RefSeq; XP_011535717.1; XM_011537415.2. [O15033-1]
DR PDB; 6JX5; X-ray; 2.40 A; A/B/C=436-823.
DR PDB; 6LOH; X-ray; 3.21 A; A/B/C=435-811.
DR PDBsum; 6JX5; -.
DR PDBsum; 6LOH; -.
DR AlphaFoldDB; O15033; -.
DR SMR; O15033; -.
DR BioGRID; 115203; 36.
DR IntAct; O15033; 8.
DR STRING; 9606.ENSP00000348714; -.
DR iPTMnet; O15033; -.
DR PhosphoSitePlus; O15033; -.
DR BioMuta; AREL1; -.
DR EPD; O15033; -.
DR jPOST; O15033; -.
DR MassIVE; O15033; -.
DR MaxQB; O15033; -.
DR PaxDb; O15033; -.
DR PeptideAtlas; O15033; -.
DR PRIDE; O15033; -.
DR ProteomicsDB; 48389; -. [O15033-1]
DR ProteomicsDB; 48390; -. [O15033-2]
DR Antibodypedia; 25651; 59 antibodies from 17 providers.
DR DNASU; 9870; -.
DR Ensembl; ENST00000356357.9; ENSP00000348714.4; ENSG00000119682.18. [O15033-1]
DR Ensembl; ENST00000681599.1; ENSP00000505623.1; ENSG00000119682.18. [O15033-1]
DR GeneID; 9870; -.
DR KEGG; hsa:9870; -.
DR MANE-Select; ENST00000356357.9; ENSP00000348714.4; NM_001039479.2; NP_001034568.1.
DR UCSC; uc001xqb.4; human. [O15033-1]
DR CTD; 9870; -.
DR DisGeNET; 9870; -.
DR GeneCards; AREL1; -.
DR HGNC; HGNC:20363; AREL1.
DR HPA; ENSG00000119682; Low tissue specificity.
DR MalaCards; AREL1; -.
DR MIM; 615380; gene.
DR neXtProt; NX_O15033; -.
DR OpenTargets; ENSG00000119682; -.
DR PharmGKB; PA134985474; -.
DR VEuPathDB; HostDB:ENSG00000119682; -.
DR eggNOG; KOG0939; Eukaryota.
DR GeneTree; ENSGT00940000156723; -.
DR InParanoid; O15033; -.
DR OMA; HLPPMHT; -.
DR OrthoDB; 266565at2759; -.
DR PhylomeDB; O15033; -.
DR TreeFam; TF323417; -.
DR BRENDA; 2.3.2.26; 2681.
DR PathwayCommons; O15033; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; O15033; -.
DR SIGNOR; O15033; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 9870; 23 hits in 1114 CRISPR screens.
DR ChiTaRS; AREL1; human.
DR GenomeRNAi; 9870; -.
DR Pharos; O15033; Tdark.
DR PRO; PR:O15033; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O15033; protein.
DR Bgee; ENSG00000119682; Expressed in cortical plate and 177 other tissues.
DR ExpressionAtlas; O15033; baseline and differential.
DR Genevisible; O15033; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:1990390; P:protein K33-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS50237; HECT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..823
FT /note="Apoptosis-resistant E3 ubiquitin protein ligase 1"
FT /id="PRO_0000120349"
FT REPEAT 52..158
FT /note="Filamin"
FT DOMAIN 483..823
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 315..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..789
FT /note="Interaction with SOCS2"
FT /evidence="ECO:0000269|PubMed:31578312"
FT ACT_SITE 790
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104,
FT ECO:0000269|PubMed:23479728"
FT VAR_SEQ 790..823
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013259"
FT VARIANT 779
FT /note="P -> L (loss of interaction with SOCS2;
FT dbSNP:rs371610162)"
FT /evidence="ECO:0000269|PubMed:31578312"
FT /id="VAR_083342"
FT MUTAGEN 790
FT /note="C->A: Failure to form ubiquitin thioester complex."
FT /evidence="ECO:0000269|PubMed:23479728"
FT CONFLICT 114
FT /note="T -> N (in Ref. 5; AAH32944)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="P -> H (in Ref. 5; AAH32944)"
FT /evidence="ECO:0000305"
FT HELIX 439..453
FT /evidence="ECO:0007829|PDB:6JX5"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:6JX5"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 471..478
FT /evidence="ECO:0007829|PDB:6JX5"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:6JX5"
FT STRAND 489..495
FT /evidence="ECO:0007829|PDB:6JX5"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:6LOH"
FT HELIX 504..519
FT /evidence="ECO:0007829|PDB:6JX5"
FT STRAND 524..531
FT /evidence="ECO:0007829|PDB:6JX5"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:6JX5"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 550..567
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 582..589
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 597..601
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 603..615
FT /evidence="ECO:0007829|PDB:6JX5"
FT TURN 619..621
FT /evidence="ECO:0007829|PDB:6JX5"
FT STRAND 624..630
FT /evidence="ECO:0007829|PDB:6JX5"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:6LOH"
FT STRAND 636..643
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 646..648
FT /evidence="ECO:0007829|PDB:6JX5"
FT TURN 653..655
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 656..668
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 670..672
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 673..686
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 689..692
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 697..705
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 712..718
FT /evidence="ECO:0007829|PDB:6JX5"
FT STRAND 720..723
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 726..730
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 732..742
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 745..756
FT /evidence="ECO:0007829|PDB:6JX5"
FT STRAND 757..760
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 765..768
FT /evidence="ECO:0007829|PDB:6JX5"
FT STRAND 774..782
FT /evidence="ECO:0007829|PDB:6JX5"
FT STRAND 786..788
FT /evidence="ECO:0007829|PDB:6LOH"
FT HELIX 789..791
FT /evidence="ECO:0007829|PDB:6JX5"
FT STRAND 794..798
FT /evidence="ECO:0007829|PDB:6JX5"
FT HELIX 802..812
FT /evidence="ECO:0007829|PDB:6JX5"
SQ SEQUENCE 823 AA; 94223 MW; 9E26273B529DB477 CRC64;
MFYVIGGITV SVVAFFFTIK FLFELAARVV SFLQNEDRER RGDRTIYDYV RGNYLDPRSC
KVSWDWKDPY EVGHSMAFRV HLFYKNGQPF PAHRPVGLRV HISHVELAVE IPVTQEVLQE
PNSNVVKVAF TVRKAGRYEI TVKLGGLNVA YSPYYKIFQP GMVVPSKTKI VCHFSTLVLT
CGQPHTLQIV PRDEYDNPTN NSMSLRDEHN YTLSIHELGP QEEESTGVSF EKSVTSNRQT
FQVFLRLTLH SRGCFHACIS YQNQPINNGE FDIIVLSEDE KNIVERNVST SGVSIYFEAY
LYNATNCSST PWHLPPMHMT SSQRRPSTAV DEEDEDSPSE CHTPEKVKKP KKVYCYVSPK
QFSVKEFYLK IIPWRLYTFR VCPGTKFSYL GPDPVHKLLT LVVDDGIQPP VELSCKERNI
LAATFIRSLH KNIGGSETFQ DKVNFFQREL RQVHMKRPHS KVTLKVSRHA LLESSLKATR
NFSISDWSKN FEVVFQDEEA LDWGGPRREW FELICKALFD TTNQLFTRFS DNNQALVHPN
PNRPAHLRLK MYEFAGRLVG KCLYESSLGG AYKQLVRARF TRSFLAQIIG LRMHYKYFET
DDPEFYKSKV CFILNNDMSE MELVFAEEKY NKSGQLDKVV ELMTGGAQTP VTNANKIFYL
NLLAQYRLAS QVKEEVEHFL KGLNELVPEN LLAIFDENEL ELLMCGTGDI SVSDFKAHAV
VVGGSWHFRE KVMRWFWTVV SSLTQEELAR LLQFTTGSSQ LPPGGFAALC PSFQIIAAPT
HSTLPTAHTC FNQLCLPTYD SYEEVHRMLQ LAISEGCEGF GML
