D19L2_HUMAN
ID D19L2_HUMAN Reviewed; 758 AA.
AC Q6NUT2; A4FVC1; B4E191; Q3ZCX2; Q6UWG8; Q96LZ9;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable C-mannosyltransferase DPY19L2;
DE EC=2.4.1.- {ECO:0000250|UniProtKB:P34413};
DE AltName: Full=Dpy-19-like protein 2;
DE AltName: Full=Protein dpy-19 homolog 2;
GN Name=DPY19L2 {ECO:0000312|HGNC:HGNC:19414};
GN ORFNames=UNQ3127/PRO10284 {ECO:0000303|PubMed:12975309};
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), AND VARIANTS VAL-37;
RP VAL-41 AND ALA-51.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Testis;
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=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-37 AND
RP VAL-41 AND ALA-51.
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 [5]
RP GENE DUPLICATION, AND TISSUE SPECIFICITY.
RX PubMed=16526957; DOI=10.1186/1471-2164-7-45;
RA Carson A.R., Cheung J., Scherer S.W.;
RT "Duplication and relocation of the functional DPY19L2 gene within low copy
RT repeats.";
RL BMC Genomics 7:45-45(2006).
RN [6]
RP INVOLVEMENT IN SPGF9, AND FUNCTION.
RX PubMed=21397063; DOI=10.1016/j.ajhg.2011.01.018;
RA Koscinski I., Elinati E., Fossard C., Redin C., Muller J.,
RA Velez de la Calle J., Schmitt F., Ben Khelifa M., Ray P., Kilani Z.,
RA Barratt C.L., Viville S.;
RT "DPY19L2 deletion as a major cause of globozoospermia.";
RL Am. J. Hum. Genet. 88:344-350(2011).
RN [7]
RP INVOLVEMENT IN SPGF9, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=21397064; DOI=10.1016/j.ajhg.2011.02.007;
RA Harbuz R., Zouari R., Pierre V., Ben Khelifa M., Kharouf M., Coutton C.,
RA Merdassi G., Abada F., Escoffier J., Nikas Y., Vialard F., Koscinski I.,
RA Triki C., Sermondade N., Schweitzer T., Zhioua A., Zhioua F., Latrous H.,
RA Halouani L., Ouafi M., Makni M., Jouk P.S., Sele B., Hennebicq S.,
RA Satre V., Viville S., Arnoult C., Lunardi J., Ray P.F.;
RT "A recurrent deletion of DPY19L2 causes infertility in man by blocking
RT sperm head elongation and acrosome formation.";
RL Am. J. Hum. Genet. 88:351-361(2011).
CC -!- FUNCTION: Probable C-mannosyltransferase that mediates C-mannosylation
CC of tryptophan residues on target proteins.
CC {ECO:0000250|UniProtKB:P34413}.
CC -!- FUNCTION: Required during spermatogenesis for sperm head elongation and
CC acrosome formation (PubMed:21397063, PubMed:21397064). Also plays a
CC role in acrosome attachment to the nuclear envelope (By similarity).
CC {ECO:0000250|UniProtKB:P0CW70, ECO:0000269|PubMed:21397063,
CC ECO:0000269|PubMed:21397064}.
CC -!- SUBUNIT: Interacts with FAM209. {ECO:0000250|UniProtKB:P0CW70}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000250|UniProtKB:P0CW70}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Colocalizes with DPY19L2 at the inner nuclear
CC membrane. {ECO:0000250|UniProtKB:P0CW70}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NUT2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NUT2-2; Sequence=VSP_056136;
CC -!- TISSUE SPECIFICITY: Widely expressed with high expression in testis.
CC Not detectable in ejaculated sperm (at protein level).
CC {ECO:0000269|PubMed:16526957, ECO:0000269|PubMed:21397064}.
CC -!- DISEASE: Spermatogenic failure 9 (SPGF9) [MIM:613958]: An infertility
CC disorder caused by spermatogenesis defects. The most prominent feature
CC is the malformation of the acrosome, which can be totally absent in
CC most severe cases. Additional features are an abnormal nuclear shape
CC and abnormal arrangement of the mitochondria of the spermatozoon.
CC {ECO:0000269|PubMed:21397063, ECO:0000269|PubMed:21397064}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. Deletions in DPY19L2 are probably the major cause of SPGF9.
CC -!- MISCELLANEOUS: It has been suggested that DPY19L2P1 is an inactive
CC pseudogene from which DPY19L2 has evolved by duplication. However,
CC expressed transcript sequences derived from the DPY19L2P1 locus are
CC known to exist.
CC -!- SIMILARITY: Belongs to the dpy-19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI25216.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI25217.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY358792; AAQ89152.1; -; mRNA.
DR EMBL; AK057511; BAB71515.1; -; mRNA.
DR EMBL; AK303727; BAG64703.1; -; mRNA.
DR EMBL; AC027667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031225; AAH31225.1; -; mRNA.
DR EMBL; BC068442; AAH68442.1; -; mRNA.
DR EMBL; BC125215; AAI25216.2; ALT_INIT; mRNA.
DR EMBL; BC125216; AAI25217.2; ALT_INIT; mRNA.
DR CCDS; CCDS31851.1; -. [Q6NUT2-1]
DR RefSeq; NP_776173.3; NM_173812.4. [Q6NUT2-1]
DR AlphaFoldDB; Q6NUT2; -.
DR BioGRID; 129556; 4.
DR IntAct; Q6NUT2; 5.
DR STRING; 9606.ENSP00000315988; -.
DR iPTMnet; Q6NUT2; -.
DR PhosphoSitePlus; Q6NUT2; -.
DR BioMuta; DPY19L2; -.
DR DMDM; 162416266; -.
DR EPD; Q6NUT2; -.
DR jPOST; Q6NUT2; -.
DR MassIVE; Q6NUT2; -.
DR MaxQB; Q6NUT2; -.
DR PaxDb; Q6NUT2; -.
DR PeptideAtlas; Q6NUT2; -.
DR PRIDE; Q6NUT2; -.
DR ProteomicsDB; 5737; -.
DR ProteomicsDB; 66711; -. [Q6NUT2-1]
DR Antibodypedia; 53106; 127 antibodies from 19 providers.
DR DNASU; 283417; -.
DR Ensembl; ENST00000324472.9; ENSP00000315988.4; ENSG00000177990.12. [Q6NUT2-1]
DR GeneID; 283417; -.
DR KEGG; hsa:283417; -.
DR MANE-Select; ENST00000324472.9; ENSP00000315988.4; NM_173812.5; NP_776173.3.
DR UCSC; uc001srp.2; human. [Q6NUT2-1]
DR CTD; 283417; -.
DR DisGeNET; 283417; -.
DR GeneCards; DPY19L2; -.
DR HGNC; HGNC:19414; DPY19L2.
DR HPA; ENSG00000177990; Tissue enhanced (testis).
DR MalaCards; DPY19L2; -.
DR MIM; 613893; gene.
DR MIM; 613958; phenotype.
DR neXtProt; NX_Q6NUT2; -.
DR OpenTargets; ENSG00000177990; -.
DR Orphanet; 171709; Male infertility due to globozoospermia.
DR PharmGKB; PA142671949; -.
DR VEuPathDB; HostDB:ENSG00000177990; -.
DR eggNOG; KOG4587; Eukaryota.
DR GeneTree; ENSGT00530000063023; -.
DR HOGENOM; CLU_014404_0_1_1; -.
DR InParanoid; Q6NUT2; -.
DR OMA; WLIQGCA; -.
DR OrthoDB; 1115173at2759; -.
DR PhylomeDB; Q6NUT2; -.
DR TreeFam; TF313376; -.
DR PathwayCommons; Q6NUT2; -.
DR SignaLink; Q6NUT2; -.
DR BioGRID-ORCS; 283417; 265 hits in 1029 CRISPR screens.
DR ChiTaRS; DPY19L2; human.
DR GenomeRNAi; 283417; -.
DR Pharos; Q6NUT2; Tbio.
DR PRO; PR:Q6NUT2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6NUT2; protein.
DR Bgee; ENSG00000177990; Expressed in apex of heart and 126 other tissues.
DR ExpressionAtlas; Q6NUT2; baseline and differential.
DR Genevisible; Q6NUT2; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0018406; P:protein C-linked glycosylation via 2'-alpha-mannosyl-L-tryptophan; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IMP:UniProtKB.
DR InterPro; IPR018732; Dpy-19/Dpy-19-like.
DR InterPro; IPR030042; DPY19L2.
DR PANTHER; PTHR31488; PTHR31488; 1.
DR PANTHER; PTHR31488:SF6; PTHR31488:SF6; 1.
DR Pfam; PF10034; Dpy19; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation;
KW Glycosyltransferase; Membrane; Nucleus; Reference proteome;
KW Spermatogenesis; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..758
FT /note="Probable C-mannosyltransferase DPY19L2"
FT /id="PRO_0000311879"
FT TOPO_DOM 1..107
FT /note="Nuclear"
FT /evidence="ECO:0000250|UniProtKB:P0CW70"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..194
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..241
FT /note="Nuclear"
FT /evidence="ECO:0000305"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..296
FT /note="Nuclear"
FT /evidence="ECO:0000305"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..343
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..371
FT /note="Nuclear"
FT /evidence="ECO:0000305"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..422
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..488
FT /note="Nuclear"
FT /evidence="ECO:0000305"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..533
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..758
FT /note="Nuclear"
FT /evidence="ECO:0000250|UniProtKB:P0CW70"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..553
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056136"
FT VARIANT 37
FT /note="M -> V (in dbSNP:rs10878075)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_037333"
FT VARIANT 41
FT /note="A -> V (in dbSNP:rs10878074)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_037334"
FT VARIANT 51
FT /note="S -> A (in dbSNP:rs10878073)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_037335"
FT VARIANT 757
FT /note="V -> I (in dbSNP:rs12314553)"
FT /id="VAR_062214"
FT CONFLICT 152
FT /note="L -> P (in Ref. 4; AAH68442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 758 AA; 87374 MW; 1A5538AF7001EB35 CRC64;
MRKQGVSSKR LQSSGRSQSK GRRGASLARE PEVEEEMEKS ALGGGKLPRG SWRSSPGRIQ
SLKERKGLEL EVVAKTFLLG PFQFVRNSLA QLREKVQELQ ARRFSSRTTL GIAVFVAILH
WLHLVTLFEN DRHFSHLSSL EREMTFRTEM GLYYSYFKTI IEAPSFLEGL WMIMNDRLTE
YPLIINAIKR FHLYPEVIIA SWYCTFMGIM NLFGLETKTC WNVTRIEPLN EVQSCEGLGD
PACFYVGVIF ILNGLMMGLF FMYGAYLSGT QLGGLITVLC FFFNHGEATR VMWTPPLRES
FSYPFLVLQM CILTLILRTS SNDRRPFIAL CLSNVAFMLP WQFAQFILFT QIASLFPMYV
VGYIEPSKFQ KIIYMNMISV TLSFILMFGN SMYLSSYYSS SLLMTWAIIL KRNEIQKLGV
SKLNFWLIQG SAWWCGTIIL KFLTSKILGV SDHIRLSDLI AARILRYTDF DTLIYTCAPE
FDFMEKATPL RYTKTLLLPV VMVITCFIFK KTVRDISYVL ATNIYLRKQL LEHSELAFHT
LQLLVFTALA ILIMRLKMFL TPHMCVMASL ICSRQLFGWL FRRVRFEKVI FGILTVMSIQ
GYANLRNQWS IIGEFNNLPQ EELLQWIKYS TTSDAVFAGA MPTMASIKLS TLHPIVNHPH
YEDADLRART KIVYSTYSRK SAKEVRDKLL ELHVNYYVLE EAWCVVRTKP GCSMLEIWDV
EDPSNAANPP LCSVLLEDAR PYFTTVFQNS VYRVLKVN
