TMTC4_HUMAN
ID TMTC4_HUMAN Reviewed; 741 AA.
AC Q5T4D3; A6NLI7; B7Z666; Q5T4D4; Q5T4D5; Q5T4D6; Q8WV63; Q96SU8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein O-mannosyl-transferase TMTC4 {ECO:0000305};
DE EC=2.4.1.109 {ECO:0000269|PubMed:28973932};
DE AltName: Full=Transmembrane and TPR repeat-containing protein 4 {ECO:0000312|HGNC:HGNC:25904};
GN Name=TMTC4 {ECO:0000312|HGNC:HGNC:25904};
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] (ISOFORMS 3 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 222-741 (ISOFORM 1).
RC TISSUE=Brain, and 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Endometrial adenocarcinoma;
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 GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 196-741 (ISOFORM 2).
RC TISSUE=Skin;
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 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 [6]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-655.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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.
CC {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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5T4D3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T4D3-2; Sequence=VSP_023622, VSP_023623;
CC Name=3;
CC IsoId=Q5T4D3-3; Sequence=VSP_038261;
CC Name=4;
CC IsoId=Q5T4D3-4; Sequence=VSP_054873;
CC -!- SIMILARITY: Belongs to the TMTC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH18707.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AK056409; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB55179.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK056409; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK027530; BAB55179.1; ALT_INIT; mRNA.
DR EMBL; AK299859; BAH13152.1; -; mRNA.
DR EMBL; BX647956; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL359085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018707; AAH18707.1; ALT_INIT; mRNA.
DR CCDS; CCDS41904.1; -. [Q5T4D3-1]
DR CCDS; CCDS66575.1; -. [Q5T4D3-4]
DR CCDS; CCDS9497.2; -. [Q5T4D3-3]
DR RefSeq; NP_001073137.1; NM_001079669.2. [Q5T4D3-1]
DR RefSeq; NP_001273382.1; NM_001286453.1. [Q5T4D3-4]
DR RefSeq; NP_116202.2; NM_032813.3. [Q5T4D3-3]
DR RefSeq; XP_016876285.1; XM_017020796.1.
DR AlphaFoldDB; Q5T4D3; -.
DR SMR; Q5T4D3; -.
DR BioGRID; 124339; 53.
DR IntAct; Q5T4D3; 20.
DR STRING; 9606.ENSP00000343871; -.
DR GlyGen; Q5T4D3; 1 site.
DR iPTMnet; Q5T4D3; -.
DR PhosphoSitePlus; Q5T4D3; -.
DR BioMuta; TMTC4; -.
DR DMDM; 134035049; -.
DR EPD; Q5T4D3; -.
DR jPOST; Q5T4D3; -.
DR MassIVE; Q5T4D3; -.
DR MaxQB; Q5T4D3; -.
DR PaxDb; Q5T4D3; -.
DR PeptideAtlas; Q5T4D3; -.
DR PRIDE; Q5T4D3; -.
DR ProteomicsDB; 64449; -. [Q5T4D3-1]
DR ProteomicsDB; 64450; -. [Q5T4D3-2]
DR ProteomicsDB; 64451; -. [Q5T4D3-3]
DR ProteomicsDB; 6752; -.
DR Antibodypedia; 11042; 124 antibodies from 17 providers.
DR DNASU; 84899; -.
DR Ensembl; ENST00000328767.9; ENSP00000365409.2; ENSG00000125247.16. [Q5T4D3-4]
DR Ensembl; ENST00000342624.10; ENSP00000343871.5; ENSG00000125247.16. [Q5T4D3-3]
DR Ensembl; ENST00000376234.7; ENSP00000365408.3; ENSG00000125247.16. [Q5T4D3-1]
DR GeneID; 84899; -.
DR KEGG; hsa:84899; -.
DR MANE-Select; ENST00000342624.10; ENSP00000343871.5; NM_032813.5; NP_116202.2. [Q5T4D3-3]
DR UCSC; uc001vot.5; human. [Q5T4D3-1]
DR CTD; 84899; -.
DR DisGeNET; 84899; -.
DR GeneCards; TMTC4; -.
DR HGNC; HGNC:25904; TMTC4.
DR HPA; ENSG00000125247; Tissue enhanced (brain).
DR MIM; 618203; gene.
DR neXtProt; NX_Q5T4D3; -.
DR OpenTargets; ENSG00000125247; -.
DR PharmGKB; PA142670721; -.
DR VEuPathDB; HostDB:ENSG00000125247; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000158521; -.
DR HOGENOM; CLU_011615_2_0_1; -.
DR InParanoid; Q5T4D3; -.
DR OMA; KAWANIL; -.
DR OrthoDB; 1320023at2759; -.
DR PhylomeDB; Q5T4D3; -.
DR TreeFam; TF328339; -.
DR PathwayCommons; Q5T4D3; -.
DR SignaLink; Q5T4D3; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 84899; 12 hits in 1076 CRISPR screens.
DR ChiTaRS; TMTC4; human.
DR GeneWiki; TMTC4; -.
DR GenomeRNAi; 84899; -.
DR Pharos; Q5T4D3; Tdark.
DR PRO; PR:Q5T4D3; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q5T4D3; protein.
DR Bgee; ENSG00000125247; Expressed in oviduct epithelium and 181 other tissues.
DR ExpressionAtlas; Q5T4D3; baseline and differential.
DR Genevisible; Q5T4D3; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051117; F:ATPase binding; IPI:MGI.
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:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR GO; GO:1905584; P:outer hair cell apoptotic process; IEA:Ensembl.
DR GO; GO:0032470; P:positive regulation of endoplasmic reticulum calcium ion concentration; IEA:Ensembl.
DR GO; GO:0035269; P:protein O-linked mannosylation; IMP:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR Gene3D; 1.25.40.10; -; 3.
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; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 7.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Reference proteome;
KW Repeat; TPR repeat; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..741
FT /note="Protein O-mannosyl-transferase TMTC4"
FT /id="PRO_0000280295"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 448..481
FT /note="TPR 1"
FT REPEAT 482..515
FT /note="TPR 2"
FT REPEAT 517..549
FT /note="TPR 3"
FT REPEAT 550..583
FT /note="TPR 4"
FT REPEAT 584..617
FT /note="TPR 5"
FT REPEAT 619..651
FT /note="TPR 6"
FT REPEAT 652..685
FT /note="TPR 7"
FT REPEAT 686..719
FT /note="TPR 8"
FT VAR_SEQ 1
FT /note="M -> MIPNQHNAGAGSHQPAVFRM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038261"
FT VAR_SEQ 55..165
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054873"
FT VAR_SEQ 594..612
FT /note="YADLNRHVDALNAWRNATV -> VSAGCPVPVEGKMGYFSYL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023622"
FT VAR_SEQ 613..741
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023623"
FT VARIANT 286
FT /note="V -> M (in dbSNP:rs3809371)"
FT /id="VAR_031117"
FT VARIANT 419
FT /note="V -> I (in dbSNP:rs946837)"
FT /id="VAR_031118"
FT VARIANT 655
FT /note="M -> V (in a breast cancer sample; somatic mutation;
FT dbSNP:rs144940475)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036455"
FT CONFLICT 441
FT /note="L -> P (in Ref. 1; BAB55179)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="Y -> N (in Ref. 1; BAB55179)"
FT /evidence="ECO:0000305"
FT CONFLICT 667
FT /note="K -> E (in Ref. 1; BAB55179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 741 AA; 82991 MW; 42BB8FE4A7D86C98 CRC64;
MAVLDTDLDH ILPSSVLPPF WAKLVVGSVA IVCFARSYDG DFVFDDSEAI VNNKDLQAET
PLGDLWHHDF WGSRLSSNTS HKSYRPLTVL TFRINYYLSG GFHPVGFHVV NILLHSGISV
LMVDVFSVLF GGLQYTSKGR RLHLAPRASL LAALLFAVHP VHTECVAGVV GRADLLCALF
FLLSFLGYCK AFRESNKEGA HSSTFWVLLS IFLGAVAMLC KEQGITVLGL NAVFDILVIG
KFNVLEIVQK VLHKDKSLEN LGMLRNGGLL FRMTLLTSGG AGMLYVRWRI MGTGPPAFTE
VDNPASFADS MLVRAVNYNY YYSLNAWLLL CPWWLCFDWS MGCIPLIKSI SDWRVIALAA
LWFCLIGLIC QALCSEDGHK RRILTLGLGF LVIPFLPASN LFFRVGFVVA ERVLYLPSVG
YCVLLTFGFG ALSKHTKKKK LIAAVVLGIL FINTLRCVLR SGEWRSEEQL FRSALSVCPL
NAKVHYNIGK NLADKGNQTA AIRYYREAVR LNPKYVHAMN NLGNILKERN ELQEAEELLS
LAVQIQPDFA AAWMNLGIVQ NSLKRFEAAE QSYRTAIKHR RKYPDCYYNL GRLYADLNRH
VDALNAWRNA TVLKPEHSLA WNNMIILLDN TGNLAQAEAV GREALELIPN DHSLMFSLAN
VLGKSQKYKE SEALFLKAIK ANPNAASYHG NLAVLYHRWG HLDLAKKHYE ISLQLDPTAS
GTKENYGLLR RKLELMQKKA V
