SEN34_HUMAN
ID SEN34_HUMAN Reviewed; 310 AA.
AC Q9BSV6; A6NNB1; B0V3J1; Q9BVT1; Q9H6H5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=tRNA-splicing endonuclease subunit Sen34;
DE EC=4.6.1.16;
DE AltName: Full=Leukocyte receptor cluster member 5;
DE AltName: Full=tRNA-intron endonuclease Sen34;
DE Short=HsSen34;
GN Name=TSEN34; Synonyms=LENG5, SEN34;
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], FUNCTION, SUBCELLULAR LOCATION, AND COMPONENT
RP OF A COMPLEX WITH SEN2; SEN15; SEN54 AND CLP1.
RX PubMed=15109492; DOI=10.1016/s0092-8674(04)00342-3;
RA Paushkin S.V., Patel M., Furia B.S., Peltz S.W., Trotta C.R.;
RT "Identification of a human endonuclease complex reveals a link between tRNA
RT splicing and pre-mRNA 3' end formation.";
RL Cell 117:311-321(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-112.
RC TISSUE=Kidney epithelium;
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=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
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].
RC TISSUE=Brain, and 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 [6]
RP IDENTIFICATION IN THE LRC.
RX PubMed=10941842; DOI=10.1007/s002510000187;
RA Wende H., Volz A., Ziegler A.;
RT "Extensive gene duplications and a large inversion characterize the human
RT leukocyte receptor cluster.";
RL Immunogenetics 51:703-713(2000).
RN [7]
RP ERRATUM OF PUBMED:10941842.
RA Wende H., Volz A., Ziegler A.;
RL Immunogenetics 52:3-4(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP VARIANT PCH2C TRP-58.
RX PubMed=18711368; DOI=10.1038/ng.204;
RA Budde B.S., Namavar Y., Barth P.G., Poll-The B.T., Nuernberg G., Becker C.,
RA van Ruissen F., Weterman M.A.J., Fluiter K., te Beek E.T., Aronica E.,
RA van der Knaap M.S., Hoehne W., Toliat M.R., Crow Y.J., Steinling M.,
RA Voit T., Roelenso F., Brussel W., Brockmann K., Kyllerman M.,
RA Boltshauser E., Hammersen G., Willemsen M., Basel-Vanagaite L.,
RA Kraegeloh-Mann I., de Vries L.S., Sztriha L., Muntoni F., Ferrie C.D.,
RA Battini R., Hennekam R.C.M., Grillo E., Beemer F.A., Stoets L.M.E.,
RA Wollnik B., Nuernberg P., Baas F.;
RT "tRNA splicing endonuclease mutations cause pontocerebellar hypoplasia.";
RL Nat. Genet. 40:1113-1118(2008).
CC -!- FUNCTION: Constitutes one of the two catalytic subunit of the tRNA-
CC splicing endonuclease complex, a complex responsible for identification
CC and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at
CC the 5'- and 3'-splice sites to release the intron. The products are an
CC intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and
CC 5'-OH termini. There are no conserved sequences at the splice sites,
CC but the intron is invariably located at the same site in the gene,
CC placing the splice sites an invariant distance from the constant
CC structural features of the tRNA body. It probably carries the active
CC site for 3'-splice site cleavage. The tRNA splicing endonuclease is
CC also involved in mRNA processing via its association with pre-mRNA 3'-
CC end processing factors, establishing a link between pre-tRNA splicing
CC and pre-mRNA 3'-end formation, suggesting that the endonuclease
CC subunits function in multiple RNA-processing events.
CC {ECO:0000269|PubMed:15109492}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-
CC half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with
CC a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.; EC=4.6.1.16;
CC -!- SUBUNIT: tRNA splicing endonuclease is a heterotetramer composed of
CC TSEN2, TSEN15, TSEN34/LENG5 and TSEN54. tRNA splicing endonuclease
CC complex also contains proteins of the pre-mRNA 3'-end processing
CC machinery such as CLP1, CPSF1, CPSF4 and CSTF2.
CC {ECO:0000269|PubMed:10941842}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15109492}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:15109492}. Note=May be transiently
CC localized in the nucleolus.
CC -!- DISEASE: Pontocerebellar hypoplasia 2C (PCH2C) [MIM:612390]: A disorder
CC characterized by an abnormally small cerebellum and brainstem, and
CC progressive microcephaly from birth combined with extrapyramidal
CC dyskinesia. Severe chorea occurs and epilepsy is frequent. There are no
CC signs of spinal cord anterior horn cells degeneration.
CC {ECO:0000269|PubMed:18711368}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Belongs to the leukocyte receptor cluster (LRC) present
CC on 19q13.4.
CC -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15284.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK025929; BAB15284.1; ALT_SEQ; mRNA.
DR EMBL; CU457734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU151838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72203.1; -; Genomic_DNA.
DR EMBL; BC004530; AAH04530.1; -; mRNA.
DR EMBL; BC020805; AAH20805.1; -; mRNA.
DR CCDS; CCDS42609.1; -.
DR RefSeq; NP_001070914.1; NM_001077446.3.
DR RefSeq; NP_001269261.1; NM_001282332.1.
DR RefSeq; NP_076980.2; NM_024075.4.
DR RefSeq; XP_011525596.1; XM_011527294.2.
DR RefSeq; XP_011525597.1; XM_011527295.1.
DR PDB; 6Z9U; X-ray; 2.10 A; A/C=208-310.
DR PDBsum; 6Z9U; -.
DR AlphaFoldDB; Q9BSV6; -.
DR SMR; Q9BSV6; -.
DR BioGRID; 122505; 31.
DR CORUM; Q9BSV6; -.
DR IntAct; Q9BSV6; 7.
DR STRING; 9606.ENSP00000397402; -.
DR GlyGen; Q9BSV6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BSV6; -.
DR PhosphoSitePlus; Q9BSV6; -.
DR BioMuta; TSEN34; -.
DR DMDM; 50401668; -.
DR EPD; Q9BSV6; -.
DR jPOST; Q9BSV6; -.
DR MassIVE; Q9BSV6; -.
DR MaxQB; Q9BSV6; -.
DR PaxDb; Q9BSV6; -.
DR PeptideAtlas; Q9BSV6; -.
DR PRIDE; Q9BSV6; -.
DR ProteomicsDB; 78929; -.
DR Antibodypedia; 32835; 38 antibodies from 12 providers.
DR DNASU; 79042; -.
DR Ensembl; ENST00000302937.8; ENSP00000305524.4; ENSG00000170892.13.
DR Ensembl; ENST00000396383.5; ENSP00000379667.1; ENSG00000170892.13.
DR Ensembl; ENST00000396388.3; ENSP00000379671.2; ENSG00000170892.13.
DR Ensembl; ENST00000429671.7; ENSP00000397402.4; ENSG00000170892.13.
DR Ensembl; ENST00000455798.6; ENSP00000400743.2; ENSG00000170892.13.
DR Ensembl; ENST00000611560.4; ENSP00000480422.1; ENSG00000274796.4.
DR Ensembl; ENST00000611798.4; ENSP00000480899.1; ENSG00000278605.4.
DR Ensembl; ENST00000612236.4; ENSP00000480503.1; ENSG00000274129.4.
DR Ensembl; ENST00000612393.4; ENSP00000478622.1; ENSG00000278622.4.
DR Ensembl; ENST00000613310.4; ENSP00000477766.1; ENSG00000274078.4.
DR Ensembl; ENST00000613712.4; ENSP00000484865.1; ENSG00000273896.4.
DR Ensembl; ENST00000613888.4; ENSP00000481068.1; ENSG00000278712.4.
DR Ensembl; ENST00000614948.4; ENSP00000478156.1; ENSG00000278622.4.
DR Ensembl; ENST00000614984.1; ENSP00000483266.1; ENSG00000278712.4.
DR Ensembl; ENST00000615000.4; ENSP00000479654.1; ENSG00000278605.4.
DR Ensembl; ENST00000615079.1; ENSP00000484694.1; ENSG00000278605.4.
DR Ensembl; ENST00000615900.1; ENSP00000484964.1; ENSG00000274078.4.
DR Ensembl; ENST00000615975.4; ENSP00000484225.1; ENSG00000278622.4.
DR Ensembl; ENST00000616063.4; ENSP00000480964.1; ENSG00000274129.4.
DR Ensembl; ENST00000616209.1; ENSP00000481374.1; ENSG00000274672.4.
DR Ensembl; ENST00000617149.1; ENSP00000481639.1; ENSG00000273896.4.
DR Ensembl; ENST00000617902.4; ENSP00000484465.1; ENSG00000275165.4.
DR Ensembl; ENST00000618135.4; ENSP00000479576.1; ENSG00000274129.4.
DR Ensembl; ENST00000619994.1; ENSP00000482084.1; ENSG00000275165.4.
DR Ensembl; ENST00000622524.4; ENSP00000483436.1; ENSG00000274672.4.
DR Ensembl; ENST00000622538.1; ENSP00000482527.1; ENSG00000274796.4.
DR GeneID; 79042; -.
DR KEGG; hsa:79042; -.
DR MANE-Select; ENST00000396388.3; ENSP00000379671.2; NM_001077446.4; NP_001070914.1.
DR UCSC; uc032icq.1; human.
DR CTD; 79042; -.
DR DisGeNET; 79042; -.
DR GeneCards; TSEN34; -.
DR HGNC; HGNC:15506; TSEN34.
DR HPA; ENSG00000170892; Low tissue specificity.
DR MalaCards; TSEN34; -.
DR MIM; 608754; gene.
DR MIM; 612390; phenotype.
DR neXtProt; NX_Q9BSV6; -.
DR OpenTargets; ENSG00000170892; -.
DR Orphanet; 2524; Pontocerebellar hypoplasia type 2.
DR PharmGKB; PA134871088; -.
DR VEuPathDB; HostDB:ENSG00000170892; -.
DR eggNOG; KOG4133; Eukaryota.
DR GeneTree; ENSGT00390000003912; -.
DR HOGENOM; CLU_049366_2_1_1; -.
DR InParanoid; Q9BSV6; -.
DR OMA; FIAYPGD; -.
DR PhylomeDB; Q9BSV6; -.
DR TreeFam; TF314631; -.
DR BioCyc; MetaCyc:HS10201-MON; -.
DR BRENDA; 4.6.1.16; 2681.
DR PathwayCommons; Q9BSV6; -.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR SignaLink; Q9BSV6; -.
DR BioGRID-ORCS; 79042; 413 hits in 1082 CRISPR screens.
DR GeneWiki; TSEN34; -.
DR GenomeRNAi; 79042; -.
DR Pharos; Q9BSV6; Tdark.
DR PRO; PR:Q9BSV6; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BSV6; protein.
DR Bgee; ENSG00000170892; Expressed in blood and 99 other tissues.
DR ExpressionAtlas; Q9BSV6; baseline and differential.
DR Genevisible; Q9BSV6; HS.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000214; C:tRNA-intron endonuclease complex; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0000213; F:tRNA-intron endonuclease activity; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000379; P:tRNA-type intron splice site recognition and cleavage; IBA:GO_Central.
DR Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR InterPro; IPR036167; tRNA_intron_Endo_cat-like_sf.
DR InterPro; IPR006677; tRNA_intron_Endonuc_cat-like.
DR InterPro; IPR006676; tRNA_splic.
DR InterPro; IPR016690; tRNA_splic_SEN34.
DR Pfam; PF01974; tRNA_int_endo; 1.
DR PIRSF; PIRSF017250; tRNA_splic_SEN34; 1.
DR SUPFAM; SSF53032; SSF53032; 1.
DR TIGRFAMs; TIGR00324; endA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Lyase; mRNA processing; Neurodegeneration;
KW Nucleus; Pontocerebellar hypoplasia; Reference proteome; tRNA processing.
FT CHAIN 1..310
FT /note="tRNA-splicing endonuclease subunit Sen34"
FT /id="PRO_0000109463"
FT REGION 119..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT /evidence="ECO:0000250"
FT ACT_SITE 255
FT /evidence="ECO:0000250"
FT ACT_SITE 286
FT /evidence="ECO:0000250"
FT VARIANT 58
FT /note="R -> W (in PCH2C; dbSNP:rs113994150)"
FT /evidence="ECO:0000269|PubMed:18711368"
FT /id="VAR_054811"
FT VARIANT 112
FT /note="L -> V (in dbSNP:rs17849378)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_061149"
FT HELIX 217..229
FT /evidence="ECO:0007829|PDB:6Z9U"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:6Z9U"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:6Z9U"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:6Z9U"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:6Z9U"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:6Z9U"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:6Z9U"
FT HELIX 275..279
FT /evidence="ECO:0007829|PDB:6Z9U"
FT STRAND 284..293
FT /evidence="ECO:0007829|PDB:6Z9U"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:6Z9U"
SQ SEQUENCE 310 AA; 33652 MW; 1C1522D030148EC3 CRC64;
MLVVEVANGR SLVWGAEAVQ ALRERLGVGG RTVGALPRGP RQNSRLGLPL LLMPEEARLL
AEIGAVTLVS APRPDSRHHS LALTSFKRQQ EESFQEQSAL AAEARETRRQ ELLEKITEGQ
AAKKQKLEQA SGASSSQEAG SSQAAKEDET SDGQASGEQE EAGPSSSQAG PSNGVAPLPR
SALLVQLATA RPRPVKARPL DWRVQSKDWP HAGRPAHELR YSIYRDLWER GFFLSAAGKF
GGDFLVYPGD PLRFHAHYIA QCWAPEDTIP LQDLVAAGRL GTSVRKTLLL CSPQPDGKVV
YTSLQWASLQ
