TTLL4_HUMAN
ID TTLL4_HUMAN Reviewed; 1199 AA.
AC Q14679; A8K6V5; Q8WW29;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Tubulin monoglutamylase TTLL4 {ECO:0000250|UniProtKB:Q80UG8};
DE EC=6.3.2.- {ECO:0000250|UniProtKB:Q80UG8};
DE AltName: Full=Protein monoglutamylase TTLL4 {ECO:0000250|UniProtKB:Q80UG8};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 4;
GN Name=TTLL4 {ECO:0000312|HGNC:HGNC:28976}; Synonyms=KIAA0173;
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], AND VARIANT GLN-34.
RC TISSUE=Bone marrow;
RX PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V. The
RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-17; SER-518;
RP GLY-524 AND SER-852.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP DOMAIN, AND MUTAGENESIS OF 978-LYS--LYS-981.
RX PubMed=25959773; DOI=10.1016/j.cell.2015.04.003;
RA Garnham C.P., Vemu A., Wilson-Kubalek E.M., Yu I., Szyk A., Lander G.C.,
RA Milligan R.A., Roll-Mecak A.;
RT "Multivalent microtubule recognition by tubulin tyrosine ligase-like family
RT glutamylases.";
RL Cell 161:1112-1123(2015).
CC -!- FUNCTION: Monoglutamylase which modifies both tubulin and non-tubulin
CC proteins, adding a single glutamate on the gamma-carboxyl group of
CC specific glutamate residues of target proteins. Involved in the side-
CC chain initiation step of the polyglutamylation reaction but not in the
CC elongation step. Preferentially modifies beta-tail tubulin over the
CC alpha-tubulin. Monoglutamylates nucleosome assembly proteins NAP1L1 and
CC NAP1L4. Monoglutamylates nucleotidyltransferase CGAS, leading to
CC inhibition of CGAS catalytic activity, thereby preventing antiviral
CC defense function. Involved in KLF4 glutamylation which impedes its
CC ubiquitination, thereby leading to somatic cell reprogramming,
CC pluripotency maintenance and embryogenesis.
CC {ECO:0000250|UniProtKB:Q80UG8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-
CC glutamyl-L-glutamyl-[protein] + H(+) + phosphate;
CC Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q80UG8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145;
CC Evidence={ECO:0000250|UniProtKB:Q80UG8};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q80UG8}. Cell
CC projection, cilium {ECO:0000250|UniProtKB:Q80UG8}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q80UG8}.
CC Note=Located in cilia. In some cells, also found in basal bodies.
CC {ECO:0000250|UniProtKB:Q80UG8}.
CC -!- DOMAIN: The flexible c-MTBD (cationic microtubule binding domain)
CC region mediates binding to microtubules. It is positively charged and
CC becomes ordered when bound to microtubules: it interacts with a
CC negatively charged patch on tubulin. The presence of positive charges
CC in the c-MTBD region is essential for proper binding.
CC {ECO:0000250|UniProtKB:Q6ZT98, ECO:0000269|PubMed:25959773}.
CC -!- DOMAIN: Arg-727 is the main determinant for regioselectivity, which
CC segregates between initiases and elongases in all tubulin--tyrosine
CC ligase family. A glutamine residue at this position is found in
CC elongases TTLL6, TTLL9, TTLL11, TTLL13, TTLL10 and favors glutamate-
CC chain elongation, whereas an arginine residue is found in initiases
CC TTLL2, TTLL4, TTLL5, TTLL3, TTLL8 and favors initiation.
CC {ECO:0000250|UniProtKB:A4Q9E8}.
CC -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11490.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D79995; BAA11490.2; ALT_INIT; mRNA.
DR EMBL; AK291770; BAF84459.1; -; mRNA.
DR EMBL; CH471063; EAW70651.1; -; Genomic_DNA.
DR EMBL; BC021707; AAH21707.1; -; mRNA.
DR CCDS; CCDS2422.1; -.
DR RefSeq; NP_055455.3; NM_014640.4.
DR PDB; 5T6X; X-ray; 1.69 A; C=295-304.
DR PDBsum; 5T6X; -.
DR AlphaFoldDB; Q14679; -.
DR SMR; Q14679; -.
DR BioGRID; 115012; 22.
DR IntAct; Q14679; 8.
DR STRING; 9606.ENSP00000375951; -.
DR iPTMnet; Q14679; -.
DR PhosphoSitePlus; Q14679; -.
DR BioMuta; TTLL4; -.
DR DMDM; 143811470; -.
DR EPD; Q14679; -.
DR jPOST; Q14679; -.
DR MassIVE; Q14679; -.
DR MaxQB; Q14679; -.
DR PaxDb; Q14679; -.
DR PeptideAtlas; Q14679; -.
DR PRIDE; Q14679; -.
DR ProteomicsDB; 60114; -.
DR Antibodypedia; 34286; 130 antibodies from 24 providers.
DR DNASU; 9654; -.
DR Ensembl; ENST00000258398.8; ENSP00000258398.4; ENSG00000135912.11.
DR Ensembl; ENST00000392102.6; ENSP00000375951.1; ENSG00000135912.11.
DR GeneID; 9654; -.
DR KEGG; hsa:9654; -.
DR MANE-Select; ENST00000392102.6; ENSP00000375951.1; NM_014640.5; NP_055455.3.
DR UCSC; uc002viy.4; human.
DR CTD; 9654; -.
DR DisGeNET; 9654; -.
DR GeneCards; TTLL4; -.
DR HGNC; HGNC:28976; TTLL4.
DR HPA; ENSG00000135912; Low tissue specificity.
DR MIM; 618738; gene.
DR neXtProt; NX_Q14679; -.
DR OpenTargets; ENSG00000135912; -.
DR PharmGKB; PA134935712; -.
DR VEuPathDB; HostDB:ENSG00000135912; -.
DR eggNOG; KOG2156; Eukaryota.
DR GeneTree; ENSGT00940000157916; -.
DR InParanoid; Q14679; -.
DR OMA; FRTIREH; -.
DR OrthoDB; 219807at2759; -.
DR PhylomeDB; Q14679; -.
DR TreeFam; TF313087; -.
DR PathwayCommons; Q14679; -.
DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR SignaLink; Q14679; -.
DR BioGRID-ORCS; 9654; 9 hits in 1079 CRISPR screens.
DR ChiTaRS; TTLL4; human.
DR GenomeRNAi; 9654; -.
DR Pharos; Q14679; Tbio.
DR PRO; PR:Q14679; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q14679; protein.
DR Bgee; ENSG00000135912; Expressed in left testis and 150 other tissues.
DR ExpressionAtlas; Q14679; baseline and differential.
DR Genevisible; Q14679; HS.
DR GO; GO:0097731; C:9+0 non-motile cilium; IEA:Ensembl.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070739; F:protein-glutamic acid ligase activity; ISS:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR GO; GO:0070740; F:tubulin-glutamic acid ligase activity; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0018200; P:peptidyl-glutamic acid modification; ISS:UniProtKB.
DR GO; GO:0018095; P:protein polyglutamylation; ISS:UniProtKB.
DR GO; GO:0120222; P:regulation of blastocyst development; IEA:Ensembl.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR027748; TTLL-4.
DR PANTHER; PTHR12241:SF145; PTHR12241:SF145; 1.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Ligase; Magnesium; Metal-binding; Microtubule;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..1199
FT /note="Tubulin monoglutamylase TTLL4"
FT /id="PRO_0000212442"
FT DOMAIN 604..947
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..812
FT /note="L-glutamate"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT REGION 918..1029
FT /note="c-MTBD region"
FT /evidence="ECO:0000269|PubMed:25959773"
FT REGION 1130..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 727..728
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 727
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_part="L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:29973"
FT /ligand_part_note="L-glutamate acceptor residue in protein
FT target"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 749..752
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 762..764
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 788
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 809..810
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 833
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 893
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 906
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 906
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 908
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 924
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT SITE 727
FT /note="Essential for specifying initiation versus
FT elongation step of the polyglutamylase activity"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VARIANT 17
FT /note="N -> S (in dbSNP:rs11542786)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031464"
FT VARIANT 34
FT /note="E -> Q (in dbSNP:rs3731877)"
FT /evidence="ECO:0000269|PubMed:8724849"
FT /id="VAR_031465"
FT VARIANT 364
FT /note="L -> P (in dbSNP:rs3731875)"
FT /id="VAR_031466"
FT VARIANT 418
FT /note="R -> H (in dbSNP:rs2114664)"
FT /id="VAR_013140"
FT VARIANT 518
FT /note="G -> S (in dbSNP:rs17851914)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031467"
FT VARIANT 524
FT /note="S -> G (in dbSNP:rs17851915)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031468"
FT VARIANT 852
FT /note="A -> S (in dbSNP:rs17856640)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031469"
FT VARIANT 1138
FT /note="T -> I (in dbSNP:rs9989776)"
FT /id="VAR_057315"
FT MUTAGEN 978..981
FT /note="KMKK->EMEE: Decreased binding to microtubules and
FT polyglutamylase activity."
FT /evidence="ECO:0000269|PubMed:25959773"
SQ SEQUENCE 1199 AA; 133378 MW; 9B95597237588956 CRC64;
MASAGTQHYS IGLRQKNSFK QSGPSGTVPA TPPEKPSEGR VWPQAHQQVK PIWKLEKKQV
ETLSAGLGPG LLGVPPQPAY FFCPSTLCSS GTTAVIAGHS SSCYLHSLPD LFNSTLLYRR
SSYRQKPYQQ LESFCLRSSP SEKSPFSLPQ KSLPVSLTAN KATSSMVFSM AQPMASSSTE
PYLCLAAAGE NPSGKSLASA ISGKIPSPLS SSYKPMLNNN SFMWPNSTPV PLLQTTQGLK
PVSPPKIQPV SWHHSGGTGD CAPQPVDHKV PKSIGTVPAD ASAHIALSTA SSHDTSTTSV
ASSWYNRNNL AMRAEPLSCA LDDSSDSQDP TKEIRFTEAV RKLTARGFEK MPRQGCQLEQ
SSFLNPSFQW NVLNRSRRWK PPAVNQQFPQ EDAGSVRRVL PGASDTLGLD NTVFCTKRIS
IHLLASHASG LNHNPACESV IDSSAFGEGK APGPPFPQTL GIANVATRLS SIQLGQSEKE
RPEEARELDS SDRDISSATD LQPDQAETED TEEELVDGLE DCCSRDENEE EEGDSECSSL
SAVSPSESVA MISRSCMEIL TKPLSNHEKV VRPALIYSLF PNVPPTIYFG TRDERVEKLP
WEQRKLLRWK MSTVTPNIVK QTIGRSHFKI SKRNDDWLGC WGHHMKSPSF RSIREHQKLN
HFPGSFQIGR KDRLWRNLSR MQSRFGKKEF SFFPQSFILP QDAKLLRKAW ESSSRQKWIV
KPPASARGIG IQVIHKWSQL PKRRPLLVQR YLHKPYLISG SKFDLRIYVY VTSYDPLRIY
LFSDGLVRFA SCKYSPSMKS LGNKFMHLTN YSVNKKNAEY QANADEMACQ GHKWALKALW
NYLSQKGVNS DAIWEKIKDV VVKTIISSEP YVTSLLKMYV RRPYSCHELF GFDIMLDENL
KPWVLEVNIS PSLHSSSPLD ISIKGQMIRD LLNLAGFVLP NAEDIISSPS SCSSSTTSLP
TSPGDKCRMA PEHVTAQKMK KAYYLTQKIP DQDFYASVLD VLTPDDVRIL VEMEDEFSRR
GQFERIFPSH ISSRYLRFFE QPRYFNILTT QWEQKYHGNK LKGVDLLRSW CYKGFHMGVV
SDSAPVWSLP TSLLTISKDD VILNAFSKSE TSKLGKQSSC EVSLLLSEDG TTPKSKKTQA
GLSPYPQKPS SSKDSEDTSK EPSLSTQTLP VIKCSGQTSR LSASSTFQSI SDSLLAVSP
