GPN3_HUMAN
ID GPN3_HUMAN Reviewed; 284 AA.
AC Q9UHW5; B2RC54; D4YWV1; F5H759; Q53FS3; Q6UVZ6; Q7Z3D3; Q8NEI2; Q96HK9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=GPN-loop GTPase 3 {ECO:0000303|Ref.2};
DE AltName: Full=ATP-binding domain 1 family member C;
GN Name=GPN3 {ECO:0000303|Ref.2, ECO:0000312|HGNC:HGNC:30186};
GN Synonyms=ATPBD1C; ORFNames=AD-009, UNQ1876/PRO4319;
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).
RX PubMed=16533400; DOI=10.1186/1471-2164-7-48;
RA Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P.,
RA Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.;
RT "NovelFam3000 -- uncharacterized human protein domains conserved across
RT model organisms.";
RL BMC Genomics 7:48-48(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver, and Ovary;
RA Charrier-Savournin F., Roussi S., Alonso B., Chaumont V., Locard-Paulet M.,
RA Bellanger L., Pellequer J.L., Godon C., Armengaud J.;
RT "GPN-loop GTPases: a new GTPase family regulated by dimerization.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Retina;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-52 AND
RP ALA-244.
RC TISSUE=Bone marrow, 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 [10]
RP BINDING TO RNA POYMERASE II.
RX PubMed=20864038; DOI=10.1016/j.molcel.2010.08.023;
RA Boulon S., Pradet-Balade B., Verheggen C., Molle D., Boireau S.,
RA Georgieva M., Azzag K., Robert M.C., Ahmad Y., Neel H., Lamond A.I.,
RA Bertrand E.;
RT "HSP90 and its R2TP/Prefoldin-like cochaperone are involved in the
RT cytoplasmic assembly of RNA polymerase II.";
RL Mol. Cell 39:912-924(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP FUNCTION, BINDING TO RNA POYMERASE II, AND INTERACTION WITH GPN1; RPB1;
RP RPB4 AND RPB7.
RX PubMed=21768307; DOI=10.1128/mcb.05442-11;
RA Carre C., Shiekhattar R.;
RT "Human GTPases associate with RNA polymerase II to mediate its nuclear
RT import.";
RL Mol. Cell. Biol. 31:3953-3962(2011).
CC -!- FUNCTION: Small GTPase required for proper localization of RNA
CC polymerase II (RNAPII). May act at an RNAP assembly step prior to
CC nuclear import. {ECO:0000269|PubMed:21768307}.
CC -!- SUBUNIT: Heterodimer with GPN1 (PubMed:21768307). Binds to RNA
CC polymerase II (RNAPII) (PubMed:20864038, PubMed:21768307). Interacts
CC directly with subunits RPB4 and RPB7 and the CTD of RPB1
CC (PubMed:21768307). {ECO:0000269|PubMed:20864038,
CC ECO:0000269|PubMed:21768307}.
CC -!- INTERACTION:
CC Q9UHW5; Q9HCN4: GPN1; NbExp=3; IntAct=EBI-395491, EBI-745137;
CC Q9UHW5; Q9BX10: GTPBP2; NbExp=3; IntAct=EBI-395491, EBI-6115579;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UHW5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHW5-2; Sequence=VSP_028125;
CC Name=3;
CC IsoId=Q9UHW5-3; Sequence=VSP_047327;
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD97937.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY364262; AAQ76821.1; -; mRNA.
DR EMBL; AM992619; CAQ52399.1; -; mRNA.
DR EMBL; AM992620; CAQ52400.1; -; mRNA.
DR EMBL; AF117229; AAF17210.1; -; mRNA.
DR EMBL; AY359078; AAQ89437.1; -; mRNA.
DR EMBL; BX537973; CAD97937.1; ALT_INIT; mRNA.
DR EMBL; AK314946; BAG37451.1; -; mRNA.
DR EMBL; AK223209; BAD96929.1; -; mRNA.
DR EMBL; AC002350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008416; AAH08416.1; -; mRNA.
DR EMBL; BC031024; AAH31024.1; -; mRNA.
DR CCDS; CCDS53830.1; -. [Q9UHW5-2]
DR CCDS; CCDS53831.1; -. [Q9UHW5-3]
DR CCDS; CCDS9147.1; -. [Q9UHW5-1]
DR RefSeq; NP_001157844.1; NM_001164372.1. [Q9UHW5-3]
DR RefSeq; NP_001157845.1; NM_001164373.1. [Q9UHW5-2]
DR RefSeq; NP_057385.3; NM_016301.3. [Q9UHW5-1]
DR AlphaFoldDB; Q9UHW5; -.
DR SMR; Q9UHW5; -.
DR BioGRID; 119359; 109.
DR IntAct; Q9UHW5; 67.
DR MINT; Q9UHW5; -.
DR STRING; 9606.ENSP00000442770; -.
DR GlyGen; Q9UHW5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UHW5; -.
DR PhosphoSitePlus; Q9UHW5; -.
DR BioMuta; GPN3; -.
DR DMDM; 158564000; -.
DR EPD; Q9UHW5; -.
DR jPOST; Q9UHW5; -.
DR MassIVE; Q9UHW5; -.
DR MaxQB; Q9UHW5; -.
DR PaxDb; Q9UHW5; -.
DR PeptideAtlas; Q9UHW5; -.
DR PRIDE; Q9UHW5; -.
DR ProteomicsDB; 27390; -.
DR ProteomicsDB; 84420; -. [Q9UHW5-1]
DR ProteomicsDB; 84421; -. [Q9UHW5-2]
DR Antibodypedia; 31008; 63 antibodies from 16 providers.
DR DNASU; 51184; -.
DR Ensembl; ENST00000228827.8; ENSP00000228827.3; ENSG00000111231.9. [Q9UHW5-1]
DR Ensembl; ENST00000537466.6; ENSP00000443068.2; ENSG00000111231.9. [Q9UHW5-2]
DR Ensembl; ENST00000543199.5; ENSP00000442770.1; ENSG00000111231.9. [Q9UHW5-3]
DR GeneID; 51184; -.
DR KEGG; hsa:51184; -.
DR MANE-Select; ENST00000228827.8; ENSP00000228827.3; NM_016301.4; NP_057385.3.
DR UCSC; uc001tqr.4; human. [Q9UHW5-1]
DR CTD; 51184; -.
DR DisGeNET; 51184; -.
DR GeneCards; GPN3; -.
DR HGNC; HGNC:30186; GPN3.
DR HPA; ENSG00000111231; Low tissue specificity.
DR neXtProt; NX_Q9UHW5; -.
DR OpenTargets; ENSG00000111231; -.
DR PharmGKB; PA162390164; -.
DR VEuPathDB; HostDB:ENSG00000111231; -.
DR eggNOG; KOG1534; Eukaryota.
DR GeneTree; ENSGT00950000183172; -.
DR HOGENOM; CLU_037460_0_0_1; -.
DR InParanoid; Q9UHW5; -.
DR OMA; CFEYLLQ; -.
DR OrthoDB; 964931at2759; -.
DR PhylomeDB; Q9UHW5; -.
DR TreeFam; TF105810; -.
DR PathwayCommons; Q9UHW5; -.
DR SignaLink; Q9UHW5; -.
DR BioGRID-ORCS; 51184; 695 hits in 1058 CRISPR screens.
DR ChiTaRS; GPN3; human.
DR GenomeRNAi; 51184; -.
DR Pharos; Q9UHW5; Tbio.
DR PRO; PR:Q9UHW5; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9UHW5; protein.
DR Bgee; ENSG00000111231; Expressed in skeletal muscle tissue of biceps brachii and 198 other tissues.
DR ExpressionAtlas; Q9UHW5; baseline and differential.
DR Genevisible; Q9UHW5; HS.
DR GO; GO:0032991; C:protein-containing complex; IDA:LIFEdb.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004130; Gpn.
DR InterPro; IPR030228; Gpn3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21231; PTHR21231; 1.
DR PANTHER; PTHR21231:SF7; PTHR21231:SF7; 1.
DR Pfam; PF03029; ATP_bind_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTP-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..284
FT /note="GPN-loop GTPase 3"
FT /id="PRO_0000304790"
FT MOTIF 72..74
FT /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 13..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT BINDING 174..177
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT SITE 74
FT /note="Stabilizes the phosphate intermediate; shared with
FT dimeric partner"
FT /evidence="ECO:0000250|UniProtKB:Q9UYR9"
FT VAR_SEQ 1..16
FT /note="MPRYAQLVMGPAGSGK -> MLPKTRGAFHFSIPDPQHICKSRGSPYRSNVC
FT TQTTDRSTWRKDAELYLLSVITQ (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047327"
FT VAR_SEQ 15
FT /note="G -> GKVRICGDKER (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028125"
FT VARIANT 52
FT /note="A -> V (in dbSNP:rs17856906)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035107"
FT VARIANT 244
FT /note="V -> A (in dbSNP:rs17850320)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035108"
FT CONFLICT 6..7
FT /note="QL -> HC (in Ref. 1; AAQ76821 and 3; AAF17210)"
FT /evidence="ECO:0000305"
FT CONFLICT 13..16
FT /note="GSGK -> HAKR (in Ref. 1; AAQ76821 and 3; AAF17210)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="Q -> H (in Ref. 4; AAQ89437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 32761 MW; 8E604ECB5C1DE3B5 CRC64;
MPRYAQLVMG PAGSGKSTYC ATMVQHCEAL NRSVQVVNLD PAAEHFNYSV MADIRELIEV
DDVMEDDSLR FGPNGGLVFC MEYFANNFDW LENCLGHVED DYILFDCPGQ IELYTHLPVM
KQLVQQLEQW EFRVCGVFLV DSQFMVESFK FISGILAALS AMISLEIPQV NIMTKMDLLS
KKAKKEIEKF LDPDMYSLLE DSTSDLRSKK FKKLTKAICG LIDDYSMVRF LPYDQSDEES
MNIVLQHIDF AIQYGEDLEF KEPKEREDES SSMFDEYFQE CQDE
