GNL3L_HUMAN
ID GNL3L_HUMAN Reviewed; 582 AA.
AC Q9NVN8;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Guanine nucleotide-binding protein-like 3-like protein;
GN Name=GNL3L;
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].
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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 FUNCTION.
RX PubMed=16251348; DOI=10.1091/mbc.e05-09-0848;
RA Du X., Rao M.R.K.S., Chen X.Q., Wu W., Mahalingam S., Balasundaram D.;
RT "The homologous putative GTPases Grn1p from fission yeast and the human
RT GNL3L are required for growth and play a role in processing of nucleolar
RT pre-rRNA.";
RL Mol. Biol. Cell 17:460-474(2006).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 9-LYS-LYS-10;
RP 19-LYS-LYS-20; 34-LYS-LYS-35; 145-ARG--PRO-147 AND 309-PRO-GLY-310.
RX PubMed=17034816; DOI=10.1016/j.jmb.2006.09.007;
RA Rao M.R.K.S., Kumari G., Balasundaram D., Sankaranarayanan R.,
RA Mahalingam S.;
RT "A novel lysine-rich domain and GTP binding motifs regulate the nucleolar
RT retention of human guanine nucleotide binding protein, GNL3L.";
RL J. Mol. Biol. 364:637-654(2006).
RN [6]
RP FUNCTION, INTERACTION WITH TERF1, AND DEVELOPMENTAL STAGE.
RX PubMed=19487455; DOI=10.1083/jcb.200812121;
RA Zhu Q., Meng L., Hsu J.K., Lin T., Teishima J., Tsai R.Y.;
RT "GNL3L stabilizes the TRF1 complex and promotes mitotic transition.";
RL J. Cell Biol. 185:827-839(2009).
RN [7]
RP FUNCTION, AND INTERACTION WITH MDM2 AND TP53.
RX PubMed=21132010; DOI=10.1038/onc.2010.550;
RA Meng L., Hsu J.K., Tsai R.Y.;
RT "GNL3L depletion destabilizes MDM2 and induces p53-dependent G2/M arrest.";
RL Oncogene 30:1716-1726(2011).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-477, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
CC -!- FUNCTION: Stabilizes TERF1 telomeric association by preventing TERF1
CC recruitment by PML. Stabilizes TERF1 protein by preventing its
CC ubiquitination and hence proteasomal degradation. Does so by
CC interfering with TERF1-binding to FBXO4 E3 ubiquitin-protein ligase.
CC Required for cell proliferation. By stabilizing TRF1 protein during
CC mitosis, promotes metaphase-to-anaphase transition. Stabilizes MDM2
CC protein by preventing its ubiquitination, and hence proteasomal
CC degradation. By acting on MDM2, may affect TP53 activity. Required for
CC normal processing of ribosomal pre-rRNA. Binds GTP.
CC {ECO:0000269|PubMed:16251348, ECO:0000269|PubMed:17034816,
CC ECO:0000269|PubMed:19487455, ECO:0000269|PubMed:21132010}.
CC -!- SUBUNIT: Interacts with MDM2; this interaction, which occurs in the
CC nucleoplasm, stabilizes MDM2. Indirectly interacts with TP53, via MDM2-
CC binding. Interacts with TERF1; this interaction probably occurs in the
CC nucleoplasm and is increased during mitosis, when the nucleolus is
CC disassembled. This binding may promote TERF1 homodimerization.
CC Interacts with TERT. {ECO:0000269|PubMed:19487455,
CC ECO:0000269|PubMed:21132010}.
CC -!- INTERACTION:
CC Q9NVN8; P13196: ALAS1; NbExp=3; IntAct=EBI-746682, EBI-3905054;
CC Q9NVN8; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-746682, EBI-10303987;
CC Q9NVN8; P63167: DYNLL1; NbExp=3; IntAct=EBI-746682, EBI-349105;
CC Q9NVN8; Q08379: GOLGA2; NbExp=3; IntAct=EBI-746682, EBI-618309;
CC Q9NVN8; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-746682, EBI-2549423;
CC Q9NVN8; O75031: HSF2BP; NbExp=3; IntAct=EBI-746682, EBI-7116203;
CC Q9NVN8; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-746682, EBI-2556193;
CC Q9NVN8; O95751: LDOC1; NbExp=5; IntAct=EBI-746682, EBI-740738;
CC Q9NVN8; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-746682, EBI-741037;
CC Q9NVN8; Q00987: MDM2; NbExp=8; IntAct=EBI-746682, EBI-389668;
CC Q9NVN8; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-746682, EBI-11522433;
CC Q9NVN8; P31321: PRKAR1B; NbExp=3; IntAct=EBI-746682, EBI-2805516;
CC Q9NVN8; Q9HAT0: ROPN1; NbExp=7; IntAct=EBI-746682, EBI-1378139;
CC Q9NVN8; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-746682, EBI-2130429;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:17034816}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during mitosis and down-regulated in
CC the G1 phase. {ECO:0000269|PubMed:19487455}.
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs described
CC by a G4-G1-G3 pattern.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; AK001475; BAA91712.1; -; mRNA.
DR EMBL; AL391139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011720; AAH11720.1; -; mRNA.
DR CCDS; CCDS14360.1; -.
DR RefSeq; NP_001171748.1; NM_001184819.1.
DR RefSeq; NP_061940.1; NM_019067.5.
DR AlphaFoldDB; Q9NVN8; -.
DR SMR; Q9NVN8; -.
DR BioGRID; 120037; 139.
DR IntAct; Q9NVN8; 44.
DR MINT; Q9NVN8; -.
DR STRING; 9606.ENSP00000338573; -.
DR GlyGen; Q9NVN8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NVN8; -.
DR MetOSite; Q9NVN8; -.
DR PhosphoSitePlus; Q9NVN8; -.
DR BioMuta; GNL3L; -.
DR DMDM; 74752999; -.
DR EPD; Q9NVN8; -.
DR jPOST; Q9NVN8; -.
DR MassIVE; Q9NVN8; -.
DR MaxQB; Q9NVN8; -.
DR PaxDb; Q9NVN8; -.
DR PeptideAtlas; Q9NVN8; -.
DR PRIDE; Q9NVN8; -.
DR ProteomicsDB; 82836; -.
DR Antibodypedia; 43618; 211 antibodies from 23 providers.
DR DNASU; 54552; -.
DR Ensembl; ENST00000336470.8; ENSP00000338573.4; ENSG00000130119.17.
DR Ensembl; ENST00000360845.3; ENSP00000354091.2; ENSG00000130119.17.
DR Ensembl; ENST00000674225.1; ENSP00000501441.1; ENSG00000130119.17.
DR Ensembl; ENST00000674311.1; ENSP00000501452.1; ENSG00000130119.17.
DR Ensembl; ENST00000674498.1; ENSP00000501411.1; ENSG00000130119.17.
DR GeneID; 54552; -.
DR KEGG; hsa:54552; -.
DR MANE-Select; ENST00000360845.3; ENSP00000354091.2; NM_001184819.2; NP_001171748.1.
DR UCSC; uc004dth.3; human.
DR CTD; 54552; -.
DR DisGeNET; 54552; -.
DR GeneCards; GNL3L; -.
DR HGNC; HGNC:25553; GNL3L.
DR HPA; ENSG00000130119; Low tissue specificity.
DR MIM; 300873; gene.
DR neXtProt; NX_Q9NVN8; -.
DR OpenTargets; ENSG00000130119; -.
DR PharmGKB; PA134922876; -.
DR VEuPathDB; HostDB:ENSG00000130119; -.
DR eggNOG; KOG2484; Eukaryota.
DR GeneTree; ENSGT00940000155877; -.
DR HOGENOM; CLU_011106_5_4_1; -.
DR InParanoid; Q9NVN8; -.
DR OMA; NWIKYFR; -.
DR OrthoDB; 1210675at2759; -.
DR PhylomeDB; Q9NVN8; -.
DR TreeFam; TF313085; -.
DR PathwayCommons; Q9NVN8; -.
DR SignaLink; Q9NVN8; -.
DR BioGRID-ORCS; 54552; 324 hits in 718 CRISPR screens.
DR ChiTaRS; GNL3L; human.
DR GenomeRNAi; 54552; -.
DR Pharos; Q9NVN8; Tbio.
DR PRO; PR:Q9NVN8; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9NVN8; protein.
DR Bgee; ENSG00000130119; Expressed in nipple and 192 other tissues.
DR ExpressionAtlas; Q9NVN8; baseline and differential.
DR Genevisible; Q9NVN8; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IDA:BHF-UCL.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:BHF-UCL.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; IMP:BHF-UCL.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:BHF-UCL.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
DR GO; GO:1904816; P:positive regulation of protein localization to chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IMP:BHF-UCL.
DR GO; GO:0031647; P:regulation of protein stability; IDA:BHF-UCL.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; GTP-binding; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; Ubl conjugation.
FT CHAIN 1..582
FT /note="Guanine nucleotide-binding protein-like 3-like
FT protein"
FT /id="PRO_0000284381"
FT DOMAIN 125..310
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 9..35
FT /note="Required for nucleolar localization"
FT COILED 58..88
FT /evidence="ECO:0000255"
FT BINDING 173..176
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 259..266
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 303..306
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT CROSSLNK 477
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VARIANT 320
FT /note="R -> H (in dbSNP:rs2298284)"
FT /id="VAR_049495"
FT MUTAGEN 9..10
FT /note="KK->AA: Loss of nucleolar localization; when
FT associated with 34-A-A-35. Loss of nuclear location; when
FT associated with 19-A-A-20."
FT /evidence="ECO:0000269|PubMed:17034816"
FT MUTAGEN 19..20
FT /note="KK->AA: Loss of nuclear location; when associated
FT with 9-A-A-10. Loss of nuclear location; when associated
FT with 34-A-A-35."
FT /evidence="ECO:0000269|PubMed:17034816"
FT MUTAGEN 34..35
FT /note="KK->AA: Loss of nucleolar localization; when
FT associated with 9-A-A-10. Loss of nuclear location; when
FT associated with 19-A-A-20."
FT /evidence="ECO:0000269|PubMed:17034816"
FT MUTAGEN 145..147
FT /note="RDP->AAA: Loss of GTP binding. Loss of nucleolar
FT localization. No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:17034816"
FT MUTAGEN 309..310
FT /note="PG->AA: Loss of nucleolar localization. No effect on
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:17034816"
SQ SEQUENCE 582 AA; 65573 MW; B65EE072424F54BC CRC64;
MMKLRHKNKK PGEGSKGHKK ISWPYPQPAK QNGKKATSKV PSAPHFVHPN DHANREAELK
KKWVEEMREK QQAAREQERQ KRRTIESYCQ DVLRRQEEFE HKEEVLQELN MFPQLDDEAT
RKAYYKEFRK VVEYSDVILE VLDARDPLGC RCFQMEEAVL RAQGNKKLVL VLNKIDLVPK
EVVEKWLDYL RNELPTVAFK ASTQHQVKNL NRCSVPVDQA SESLLKSKAC FGAENLMRVL
GNYCRLGEVR THIRVGVVGL PNVGKSSLIN SLKRSRACSV GAVPGITKFM QEVYLDKFIR
LLDAPGIVPG PNSEVGTILR NCVHVQKLAD PVTPVETILQ RCNLEEISNY YGVSGFQTTE
HFLTAVAHRL GKKKKGGLYS QEQAAKAVLA DWVSGKISFY IPPPATHTLP THLSAEIVKE
MTEVFDIEDT EQANEDTMEC LATGESDELL GDTDPLEMEI KLLHSPMTKI ADAIENKTTV
YKIGDLTGYC TNPNRHQMGW AKRNVDHRPK SNSMVDVCSV DRRSVLQRIM ETDPLQQGQA
LASALKNKKK MQKRADKIAS KLSDSMMSAL DLSGNADDGV GD
