OSTC_HUMAN
ID OSTC_HUMAN Reviewed; 149 AA.
AC Q9NRP0; A8MYS2; B2R5H1; D6RH22; Q9P075; Q9P1R4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Oligosaccharyltransferase complex subunit OSTC {ECO:0000305};
DE AltName: Full=Hydrophobic protein HSF-28;
GN Name=OSTC {ECO:0000312|HGNC:HGNC:24448}; ORFNames=DC2, HDCMD45P, HSPC307;
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 1).
RC TISSUE=Kidney;
RA Favier A.-L., Harsi C., Chrobozcek J.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Dendritic cell;
RA Zhao Z., Huang X., Li N., Zhu X., Cao X.;
RT "A novel gene from human dendritic cell.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Dendritic cell;
RA Peng Y., Li Y., Li N., Gu W., Han Z., Fu G., Chen Z.;
RT "Novel genes expressed in human dendritic cell.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15146197; DOI=10.1038/nbt971;
RA Brandenberger R., Wei H., Zhang S., Lei S., Murage J., Fisk G.J., Li Y.,
RA Xu C., Fang R., Guegler K., Rao M.S., Mandalam R., Lebkowski J.,
RA Stanton L.W.;
RT "Transcriptome characterization elucidates signaling networks that control
RT human ES cell growth and differentiation.";
RL Nat. Biotechnol. 22:707-716(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mesangial cell;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Urinary bladder;
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 [10]
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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PSEN1 AND NCSTN.
RX PubMed=21768116; DOI=10.1074/jbc.m111.249748;
RA Wilson C.M., Magnaudeix A., Yardin C., Terro F.;
RT "DC2 and keratinocyte-associated protein 2 (KCP2), subunits of the
RT oligosaccharyltransferase complex, are regulators of the gamma-secretase-
RT directed processing of amyloid precursor protein (APP).";
RL J. Biol. Chem. 286:31080-31091(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13] {ECO:0007744|PDB:6S7O}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), IDENTIFICATION AS
RP COMPONENT OF THE STT3A-CONTAINING OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX,
RP FUNCTION, AND PATHWAY.
RX PubMed=31831667; DOI=10.1126/science.aaz3505;
RA Ramirez A.S., Kowal J., Locher K.P.;
RT "Cryo-electron microscopy structures of human oligosaccharyltransferase
RT complexes OST-A and OST-B.";
RL Science 366:1372-1375(2019).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-9.
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: Specific component of the STT3A-containing form of the
CC oligosaccharyl transferase (OST) complex that catalyzes the initial
CC transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from
CC the lipid carrier dolichol-pyrophosphate to an asparagine residue
CC within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains,
CC the first step in protein N-glycosylation (PubMed:31831667). N-
CC glycosylation occurs cotranslationally and the complex associates with
CC the Sec61 complex at the channel-forming translocon complex that
CC mediates protein translocation across the endoplasmic reticulum (ER).
CC All subunits are required for a maximal enzyme activity. May be
CC involved in N-glycosylation of APP (amyloid-beta precursor protein).
CC Can modulate gamma-secretase cleavage of APP by enhancing
CC endoprotelysis of PSEN1. {ECO:0000269|PubMed:21768116,
CC ECO:0000269|PubMed:31831667}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:31831667}.
CC -!- SUBUNIT: Specific component of the STT3A-containing form of the
CC oligosaccharyltransferase (OST) complex (PubMed:31831667). OST exists
CC in two different complex forms which contain common core subunits RPN1,
CC RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic
CC subunits, and form-specific accessory subunits (PubMed:21768116,
CC PubMed:31831667). STT3A complex assembly occurs through the formation
CC of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2
CC contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well
CC as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and
CC OST48. The STT3A complex can form stable complexes with the Sec61
CC complex or with both the Sec61 and TRAP complexes (By similarity).
CC Interacts with PSEN1 and NCSTN; indicative for an association with the
CC gamma-secretase complex (PubMed:21768116).
CC {ECO:0000250|UniProtKB:P86218, ECO:0000269|PubMed:21768116,
CC ECO:0000269|PubMed:31831667}.
CC -!- INTERACTION:
CC Q9NRP0; Q92838: EDA; NbExp=3; IntAct=EBI-1044658, EBI-529425;
CC Q9NRP0; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-1044658, EBI-11988865;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:21768116}. Membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRP0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRP0-2; Sequence=VSP_047376;
CC -!- SIMILARITY: Belongs to the OSTC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28985.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAF65186.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CN430159; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF343342; AAK69656.1; -; mRNA.
DR EMBL; AF068297; AAF65186.1; ALT_INIT; mRNA.
DR EMBL; AF161425; AAF28985.1; ALT_INIT; mRNA.
DR EMBL; AF201937; AAF86873.1; -; mRNA.
DR EMBL; CN430159; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK312185; BAG35118.1; -; mRNA.
DR EMBL; AC107071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX06233.1; -; Genomic_DNA.
DR EMBL; BC016321; AAH16321.1; -; mRNA.
DR EMBL; BC054857; AAH54857.1; -; mRNA.
DR CCDS; CCDS3681.1; -. [Q9NRP0-1]
DR CCDS; CCDS58921.1; -. [Q9NRP0-2]
DR RefSeq; NP_001254746.1; NM_001267817.1.
DR RefSeq; NP_001254747.1; NM_001267818.1. [Q9NRP0-2]
DR RefSeq; NP_067050.1; NM_021227.3. [Q9NRP0-1]
DR PDB; 6S7O; EM; 3.50 A; H=1-149.
DR PDBsum; 6S7O; -.
DR AlphaFoldDB; Q9NRP0; -.
DR SMR; Q9NRP0; -.
DR BioGRID; 121833; 59.
DR ComplexPortal; CPX-5621; Oligosaccharyltransferase complex A.
DR IntAct; Q9NRP0; 26.
DR MINT; Q9NRP0; -.
DR STRING; 9606.ENSP00000426167; -.
DR TCDB; 9.B.142.3.17; the integral membrane glycosyltransferase family 39 (gt39) family.
DR iPTMnet; Q9NRP0; -.
DR PhosphoSitePlus; Q9NRP0; -.
DR SwissPalm; Q9NRP0; -.
DR BioMuta; OSTC; -.
DR DMDM; 74734324; -.
DR EPD; Q9NRP0; -.
DR jPOST; Q9NRP0; -.
DR MassIVE; Q9NRP0; -.
DR MaxQB; Q9NRP0; -.
DR PaxDb; Q9NRP0; -.
DR PeptideAtlas; Q9NRP0; -.
DR PRIDE; Q9NRP0; -.
DR ProteomicsDB; 14790; -.
DR ProteomicsDB; 82398; -. [Q9NRP0-1]
DR TopDownProteomics; Q9NRP0-1; -. [Q9NRP0-1]
DR Antibodypedia; 26281; 91 antibodies from 20 providers.
DR DNASU; 58505; -.
DR Ensembl; ENST00000361564.9; ENSP00000354676.4; ENSG00000198856.13. [Q9NRP0-1]
DR Ensembl; ENST00000512478.2; ENSP00000426167.2; ENSG00000198856.13. [Q9NRP0-2]
DR GeneID; 58505; -.
DR KEGG; hsa:58505; -.
DR MANE-Select; ENST00000361564.9; ENSP00000354676.4; NM_021227.4; NP_067050.1.
DR UCSC; uc003hzb.3; human. [Q9NRP0-1]
DR CTD; 58505; -.
DR DisGeNET; 58505; -.
DR GeneCards; OSTC; -.
DR HGNC; HGNC:24448; OSTC.
DR HPA; ENSG00000198856; Low tissue specificity.
DR MIM; 619023; gene.
DR neXtProt; NX_Q9NRP0; -.
DR OpenTargets; ENSG00000198856; -.
DR PharmGKB; PA164724280; -.
DR VEuPathDB; HostDB:ENSG00000198856; -.
DR eggNOG; KOG3356; Eukaryota.
DR GeneTree; ENSGT00390000001376; -.
DR HOGENOM; CLU_109136_1_0_1; -.
DR InParanoid; Q9NRP0; -.
DR OMA; WIFMRMK; -.
DR OrthoDB; 1575260at2759; -.
DR PhylomeDB; Q9NRP0; -.
DR TreeFam; TF323315; -.
DR BRENDA; 2.4.99.18; 2681.
DR PathwayCommons; Q9NRP0; -.
DR SignaLink; Q9NRP0; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 58505; 433 hits in 1050 CRISPR screens.
DR ChiTaRS; OSTC; human.
DR GenomeRNAi; 58505; -.
DR Pharos; Q9NRP0; Tbio.
DR PRO; PR:Q9NRP0; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9NRP0; protein.
DR Bgee; ENSG00000198856; Expressed in stromal cell of endometrium and 180 other tissues.
DR ExpressionAtlas; Q9NRP0; baseline and differential.
DR Genevisible; Q9NRP0; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:HGNC.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:ComplexPortal.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IC:HGNC-UCL.
DR InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR InterPro; IPR042416; OSTC.
DR PANTHER; PTHR13160; PTHR13160; 1.
DR Pfam; PF04756; OST3_OST6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..149
FT /note="Oligosaccharyltransferase complex subunit OSTC"
FT /id="PRO_0000320602"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..83
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..149
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT VAR_SEQ 145..149
FT /note="GYLMG -> RSLALLPRLECSGVISAHYKLCLPGAI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15146197"
FT /id="VSP_047376"
FT VARIANT 9
FT /note="F -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_039231"
FT CONFLICT 119
FT /note="L -> P (in Ref. 2; AAF65186)"
FT /evidence="ECO:0000305"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 84..107
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 114..142
FT /evidence="ECO:0007829|PDB:6S7O"
SQ SEQUENCE 149 AA; 16829 MW; E59289BB927442B4 CRC64;
METLYRVPFL VLECPNLKLK KPPWLHMPSA MTVYALVVVS YFLITGGIIY DVIVEPPSVG
SMTDEHGHQR PVAFLAYRVN GQYIMEGLAS SFLFTMGGLG FIILDRSNAP NIPKLNRFLL
LFIGFVCVLL SFFMARVFMR MKLPGYLMG
