TMTC3_HUMAN
ID TMTC3_HUMAN Reviewed; 915 AA.
AC Q6ZXV5; Q5CZ86; Q5H9T6; Q68DQ6; Q68DX0; Q7Z332; Q8NC50;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein O-mannosyl-transferase TMTC3 {ECO:0000305};
DE EC=2.4.1.109 {ECO:0000269|PubMed:28973932};
DE AltName: Full=Protein SMILE {ECO:0000303|PubMed:17974005};
DE AltName: Full=Transmembrane and TPR repeat-containing protein 3 {ECO:0000312|HGNC:HGNC:26899};
GN Name=TMTC3 {ECO:0000312|HGNC:HGNC:26899};
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 2).
RC TISSUE=Tooth;
RA Bleicher F., Heidet E., Carrouel F., Couble M.L., Magloire H.;
RT "SMILE, a new gene expressed by human odontoblasts.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala, Endometrial tumor, Uterine endothelium, and Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 52-876 (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-503, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21603654; DOI=10.1371/journal.pone.0019321;
RA Racape M., Duong Van Huyen J.P., Danger R., Giral M., Bleicher F.,
RA Foucher Y., Pallier A., Pilet P., Tafelmeyer P., Ashton-Chess J.,
RA Dugast E., Pettre S., Charreau B., Soulillou J.P., Brouard S.;
RT "The involvement of SMILE/TMTC3 in endoplasmic reticulum stress response.";
RL PLoS ONE 6:E19321-E19321(2011).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=28973932; DOI=10.1073/pnas.1708319114;
RA Larsen I.S.B., Narimatsu Y., Joshi H.J., Siukstaite L., Harrison O.J.,
RA Brasch J., Goodman K.M., Hansen L., Shapiro L., Honig B., Vakhrushev S.Y.,
RA Clausen H., Halim A.;
RT "Discovery of an O-mannosylation pathway selectively serving cadherins and
RT protocadherins.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:11163-11168(2017).
RN [8]
RP INVOLVEMENT IN LIS8, AND VARIANTS LIS8 ASP-67 AND GLU-384.
RX PubMed=27773428; DOI=10.1016/j.ajhg.2016.09.007;
RA Jerber J., Zaki M.S., Al-Aama J.Y., Rosti R.O., Ben-Omran T., Dikoglu E.,
RA Silhavy J.L., Caglar C., Musaev D., Albrecht B., Campbell K.P., Willer T.,
RA Almuriekhi M., Caglayan A.O., Vajsar J., Bilguevar K., Ogur G.,
RA Abou Jamra R., Guenel M., Gleeson J.G.;
RT "Biallelic mutations in TMTC3, encoding a transmembrane and TPR-containing
RT protein, lead to cobblestone lissencephaly.";
RL Am. J. Hum. Genet. 99:1181-1189(2016).
CC -!- FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine
CC or threonine residues. The 4 members of the TMTC family are O-mannosyl-
CC transferases dedicated primarily to the cadherin superfamily, each
CC member seems to have a distinct role in decorating the cadherin domains
CC with O-linked mannose glycans at specific regions. Also acts as O-
CC mannosyl-transferase on other proteins such as PDIA3 (PubMed:28973932).
CC Involved in the positive regulation of proteasomal protein degradation
CC in the endoplasmic reticulum (ER), and the control of ER stress
CC response. {ECO:0000269|PubMed:21603654, ECO:0000269|PubMed:28973932}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137321; EC=2.4.1.109;
CC Evidence={ECO:0000269|PubMed:28973932};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17378;
CC Evidence={ECO:0000269|PubMed:28973932};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137323; EC=2.4.1.109;
CC Evidence={ECO:0000269|PubMed:28973932};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53397;
CC Evidence={ECO:0000269|PubMed:28973932};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:28973932}.
CC -!- INTERACTION:
CC Q6ZXV5; O75553: DAB1; NbExp=3; IntAct=EBI-10188441, EBI-7875264;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:21603654}. Note=In odontoblast cultures, it
CC colocalizes with PDIA3 in the endoplasmic reticulum.
CC {ECO:0000269|PubMed:21603654}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZXV5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZXV5-2; Sequence=VSP_023619;
CC -!- DISEASE: Lissencephaly 8 (LIS8) [MIM:617255]: A form of lissencephaly,
CC a disorder of cortical development characterized by agyria or
CC pachygyria and disorganization of the clear neuronal lamination of
CC normal six-layered cortex. LIS8 patients manifest delayed psychomotor
CC development, intellectual disability with poor or absent speech, early-
CC onset refractory seizures, hypotonia, cortical gyral abnormalities, and
CC hypoplasia of the corpus callosum, brainstem and cerebellum. LIS8
CC inheritance is autosomal recessive. {ECO:0000269|PubMed:27773428}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the TMTC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11325.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ697717; CAG26973.1; -; mRNA.
DR EMBL; BX538169; CAD98046.1; -; mRNA.
DR EMBL; CR749244; CAH18100.1; -; mRNA.
DR EMBL; CR749309; CAH18164.1; -; mRNA.
DR EMBL; CR933632; CAI45938.1; -; mRNA.
DR EMBL; CR936640; CAI56780.1; -; mRNA.
DR EMBL; BC117175; AAI17176.1; -; mRNA.
DR EMBL; BC117177; AAI17178.1; -; mRNA.
DR EMBL; AK074973; BAC11325.1; ALT_INIT; mRNA.
DR CCDS; CCDS9032.1; -. [Q6ZXV5-2]
DR RefSeq; NP_861448.2; NM_181783.3. [Q6ZXV5-2]
DR AlphaFoldDB; Q6ZXV5; -.
DR SMR; Q6ZXV5; -.
DR BioGRID; 127757; 115.
DR IntAct; Q6ZXV5; 18.
DR MINT; Q6ZXV5; -.
DR STRING; 9606.ENSP00000266712; -.
DR TCDB; 8.A.95.1.1; the transmembrane and tpr repeat-containing protein 3 (tmtc3) family.
DR GlyGen; Q6ZXV5; 5 sites, 4 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q6ZXV5; -.
DR PhosphoSitePlus; Q6ZXV5; -.
DR SwissPalm; Q6ZXV5; -.
DR BioMuta; TMTC3; -.
DR DMDM; 134035047; -.
DR EPD; Q6ZXV5; -.
DR jPOST; Q6ZXV5; -.
DR MassIVE; Q6ZXV5; -.
DR MaxQB; Q6ZXV5; -.
DR PaxDb; Q6ZXV5; -.
DR PeptideAtlas; Q6ZXV5; -.
DR PRIDE; Q6ZXV5; -.
DR ProteomicsDB; 68498; -. [Q6ZXV5-1]
DR ProteomicsDB; 68499; -. [Q6ZXV5-2]
DR Antibodypedia; 52318; 28 antibodies from 12 providers.
DR DNASU; 160418; -.
DR Ensembl; ENST00000266712.11; ENSP00000266712.6; ENSG00000139324.12. [Q6ZXV5-2]
DR GeneID; 160418; -.
DR KEGG; hsa:160418; -.
DR MANE-Select; ENST00000266712.11; ENSP00000266712.6; NM_181783.4; NP_861448.2. [Q6ZXV5-2]
DR UCSC; uc001tau.3; human. [Q6ZXV5-1]
DR CTD; 160418; -.
DR DisGeNET; 160418; -.
DR GeneCards; TMTC3; -.
DR HGNC; HGNC:26899; TMTC3.
DR HPA; ENSG00000139324; Low tissue specificity.
DR MalaCards; TMTC3; -.
DR MIM; 617218; gene.
DR MIM; 617255; phenotype.
DR neXtProt; NX_Q6ZXV5; -.
DR OpenTargets; ENSG00000139324; -.
DR Orphanet; 98892; Periventricular nodular heterotopia.
DR PharmGKB; PA142670720; -.
DR VEuPathDB; HostDB:ENSG00000139324; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000157538; -.
DR HOGENOM; CLU_011615_1_0_1; -.
DR InParanoid; Q6ZXV5; -.
DR OMA; SDYVQAY; -.
DR PhylomeDB; Q6ZXV5; -.
DR TreeFam; TF328339; -.
DR PathwayCommons; Q6ZXV5; -.
DR SignaLink; Q6ZXV5; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 160418; 20 hits in 1080 CRISPR screens.
DR ChiTaRS; TMTC3; human.
DR GenomeRNAi; 160418; -.
DR Pharos; Q6ZXV5; Tdark.
DR PRO; PR:Q6ZXV5; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6ZXV5; protein.
DR Bgee; ENSG00000139324; Expressed in endothelial cell and 190 other tissues.
DR ExpressionAtlas; Q6ZXV5; baseline and differential.
DR Genevisible; Q6ZXV5; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000030; F:mannosyltransferase activity; IMP:UniProtKB.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:0035269; P:protein O-linked mannosylation; IMP:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR013618; TMTC_DUF1736.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF08409; DUF1736; 1.
DR Pfam; PF13174; TPR_6; 1.
DR Pfam; PF13181; TPR_8; 5.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 9.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Endoplasmic reticulum; Glycoprotein;
KW Lissencephaly; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..915
FT /note="Protein O-mannosyl-transferase TMTC3"
FT /id="PRO_0000280293"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 412..445
FT /note="TPR 1"
FT REPEAT 446..479
FT /note="TPR 2"
FT REPEAT 481..513
FT /note="TPR 3"
FT REPEAT 528..562
FT /note="TPR 4"
FT REPEAT 563..596
FT /note="TPR 5"
FT REPEAT 597..631
FT /note="TPR 6"
FT REPEAT 669..702
FT /note="TPR 7"
FT REPEAT 704..736
FT /note="TPR 8"
FT REPEAT 737..771
FT /note="TPR 9"
FT REPEAT 773..805
FT /note="TPR 10"
FT REGION 848..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 503
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 618
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.1"
FT /id="VSP_023619"
FT VARIANT 67
FT /note="H -> D (in LIS8)"
FT /evidence="ECO:0000269|PubMed:27773428"
FT /id="VAR_077900"
FT VARIANT 384
FT /note="G -> E (in LIS8)"
FT /evidence="ECO:0000269|PubMed:27773428"
FT /id="VAR_077901"
FT CONFLICT 120
FT /note="S -> R (in Ref. 2; CAH18164)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="S -> P (in Ref. 3; BAC11325)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="Y -> C (in Ref. 3; BAC11325)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="V -> G (in Ref. 2; CAD98046)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="T -> A (in Ref. 2; CAH18100)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="I -> V (in Ref. 2; CAI45938)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="A -> V (in Ref. 2; CAD98046)"
FT /evidence="ECO:0000305"
FT CONFLICT 864
FT /note="D -> N (in Ref. 2; CAD98046)"
FT /evidence="ECO:0000305"
FT CONFLICT 883
FT /note="T -> A (in Ref. 2; CAD98046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 915 AA; 104009 MW; 2B6787CE1B7CB83C CRC64;
MANINLKEIT LIVGVVTACY WNSLFCGFVF DDVSAILDNK DLHPSTPLKT LFQNDFWGTP
MSEERSHKSY RPLTVLTFRL NYLLSELKPM SYHLLNMIFH AVVSVIFLKV CKLFLDNKSS
VIASLLFAVH PIHTEAVTGV VGRAELLSSI FFLAAFLSYT RSKGPDNSII WTPIALTVFL
VAVATLCKEQ GITVVGICCV YEVFIAQGYT LPLLCTTAGQ FLRGKGSIPF SMLQTLVKLI
VLMFSTLLLV VIRVQVIQSQ LPVFTRFDNP AAVSPTPTRQ LTFNYLLPVN AWLLLNPSEL
CCDWTMGTIP LIESLLDIRN LATFTFFCFL GMLGVFSIRY SGDSSKTVLM ALCLMALPFI
PASNLFFPVG FVVAERVLYV PSMGFCILVA HGWQKISTKS VFKKLSWICL SMVILTHSLK
TFHRNWDWES EYTLFMSALK VNKNNAKLWN NVGHALENEK NFERALKYFL QATHVQPDDI
GAHMNVGRTY KNLNRTKEAE ESYMMAKSLM PQIIPGKKYA ARIAPNHLNV YINLANLIRA
NESRLEEADQ LYRQAISMRP DFKQAYISRG ELLLKMNKPL KAKEAYLKAL ELDRNNADLW
YNLAIVHIEL KEPNEALKKN FNRALELNPK HKLALFNSAI VMQESGEVKL RPEARKRLLS
YINEEPLDAN GYFNLGMLAM DDKKDNEAEI WMKKAIKLQA DFRSALFNLA LLYSQTAKEL
KALPILEELL RYYPDHIKGL ILKGDILMNQ KKDILGAKKC FERILEMDPS NVQGKHNLCV
VYFEEKDLLK AERCLLETLA LAPHEEYIQR HLNIVRDKIS SSSFIEPIFP TSKISSVEGK
KIPTESVKEI RGESRQTQIV KTSDNKSQSK SNKQLGKNGD EETPHKTTKD IKEIEKKRVA
ALKRLEEIER ILNGE
