EMAL2_HUMAN
ID EMAL2_HUMAN Reviewed; 649 AA.
AC O95834; B7Z3I2; B7Z3Q9; K7ERL7; Q59EN8; Q8N5A2; Q9UG50;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Echinoderm microtubule-associated protein-like 2;
DE Short=EMAP-2;
DE Short=HuEMAP-2;
GN Name=EML2; Synonyms=EMAP2, EMAPL2;
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), AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=10521658; DOI=10.1016/s0378-1119(99)00335-2;
RA Lepley D.M., Palange J.M., Suprenant K.A.;
RT "Sequence and expression patterns of a human EMAP-related protein-2
RT (HuEMAP-2).";
RL Gene 237:343-349(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 33-850 (ISOFORM 3).
RC TISSUE=Substantia nigra, and Thalamus;
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 MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-427 (ISOFORM 1).
RC TISSUE=Liver;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 76-649 (ISOFORM 1), AND VARIANT
RP ASP-235.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, INTERACTION WITH TUBULIN, AND SUBCELLULAR LOCATION.
RX PubMed=11694528; DOI=10.1074/jbc.m106628200;
RA Eichenmuller B., Everley P., Palange J., Lepley D., Suprenant K.A.;
RT "The human EMAP-like protein-70 (ELP70) is a microtubule destabilizer that
RT localizes to the mitotic apparatus.";
RL J. Biol. Chem. 277:1301-1309(2002).
RN [8]
RP INTERACTION WITH TUBULIN.
RX PubMed=24706829; DOI=10.1073/pnas.1322892111;
RA Richards M.W., Law E.W., Rennalls L.P., Busacca S., O'Regan L., Fry A.M.,
RA Fennell D.A., Bayliss R.;
RT "Crystal structure of EML1 reveals the basis for Hsp90 dependence of
RT oncogenic EML4-ALK by disruption of an atypical beta-propeller domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:5195-5200(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 11-60 OF ISOFORM 2, SUBUNIT
RP (ISOFORM 2), INTERACTION WITH EML3, AND COILED COIL (ISOFORM 2).
RX PubMed=25740311; DOI=10.1042/bj20150039;
RA Richards M.W., O'Regan L., Roth D., Montgomery J.M., Straube A., Fry A.M.,
RA Bayliss R.;
RT "Microtubule association of EML proteins and the EML4-ALK variant 3
RT oncoprotein require an N-terminal trimerization domain.";
RL Biochem. J. 467:529-536(2015).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-484.
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: Tubulin binding protein that inhibits microtubule nucleation
CC and growth, resulting in shorter microtubules.
CC {ECO:0000269|PubMed:11694528}.
CC -!- SUBUNIT: [Isoform 2]: Homotrimer; self-association is mediated by the
CC N-terminal coiled coil. {ECO:0000269|PubMed:25740311}.
CC -!- SUBUNIT: Interacts with GRID2 and may also interact with GRID1 (By
CC similarity). Interacts with EML3 (PubMed:25740311). Binds unpolymerized
CC tubulins via its WD repeat region (PubMed:11694528, PubMed:24706829).
CC {ECO:0000250|UniProtKB:Q6P6T4, ECO:0000269|PubMed:11694528,
CC ECO:0000269|PubMed:24706829, ECO:0000269|PubMed:25740311}.
CC -!- INTERACTION:
CC O95834; Q8NHP7: EXD1; NbExp=3; IntAct=EBI-1054588, EBI-10192266;
CC O95834; Q04864: REL; NbExp=3; IntAct=EBI-1054588, EBI-307352;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11694528}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:11694528}. Note=Colocalizes with the microtubule
CC cytoskeleton. Colocalizes with the mitotic spindle.
CC {ECO:0000269|PubMed:11694528}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95834-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95834-2; Sequence=VSP_042541;
CC Name=3;
CC IsoId=O95834-3; Sequence=VSP_047538;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10521658}.
CC -!- DOMAIN: Contains a tandem atypical propeller in EMLs (TAPE) domain. The
CC N-terminal beta-propeller is formed by canonical WD repeats; in
CC contrast, the second beta-propeller contains one blade that is formed
CC by discontinuous parts of the polypeptide chain (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat EMAP family. {ECO:0000305}.
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DR EMBL; AF103939; AAD19904.1; -; mRNA.
DR EMBL; AL096717; CAB46373.2; -; mRNA.
DR EMBL; AK295905; BAH12218.1; -; mRNA.
DR EMBL; AK296258; BAH12295.1; -; mRNA.
DR EMBL; AC006132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC098776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032630; AAH32630.1; -; mRNA.
DR EMBL; AB209773; BAD93010.1; -; mRNA.
DR CCDS; CCDS12670.1; -. [O95834-1]
DR CCDS; CCDS54280.1; -. [O95834-2]
DR CCDS; CCDS59399.1; -. [O95834-3]
DR RefSeq; NP_001180197.1; NM_001193268.1. [O95834-3]
DR RefSeq; NP_001180198.1; NM_001193269.1. [O95834-2]
DR RefSeq; NP_036287.1; NM_012155.2. [O95834-1]
DR PDB; 4CGB; X-ray; 2.15 A; A/B/C/D/E/F=-.
DR PDBsum; 4CGB; -.
DR AlphaFoldDB; O95834; -.
DR SMR; O95834; -.
DR BioGRID; 117290; 33.
DR IntAct; O95834; 7.
DR STRING; 9606.ENSP00000468312; -.
DR GlyGen; O95834; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95834; -.
DR MetOSite; O95834; -.
DR PhosphoSitePlus; O95834; -.
DR BioMuta; EML2; -.
DR EPD; O95834; -.
DR jPOST; O95834; -.
DR MassIVE; O95834; -.
DR MaxQB; O95834; -.
DR PaxDb; O95834; -.
DR PeptideAtlas; O95834; -.
DR PRIDE; O95834; -.
DR ProteomicsDB; 51079; -. [O95834-1]
DR ProteomicsDB; 51080; -. [O95834-2]
DR Antibodypedia; 2407; 163 antibodies from 25 providers.
DR DNASU; 24139; -.
DR Ensembl; ENST00000245925.8; ENSP00000245925.3; ENSG00000125746.18. [O95834-1]
DR Ensembl; ENST00000536630.5; ENSP00000442365.1; ENSG00000125746.18. [O95834-2]
DR Ensembl; ENST00000587152.6; ENSP00000468312.1; ENSG00000125746.18. [O95834-3]
DR GeneID; 24139; -.
DR KEGG; hsa:24139; -.
DR MANE-Select; ENST00000245925.8; ENSP00000245925.3; NM_012155.4; NP_036287.1.
DR UCSC; uc002pcn.4; human. [O95834-1]
DR CTD; 24139; -.
DR DisGeNET; 24139; -.
DR GeneCards; EML2; -.
DR HGNC; HGNC:18035; EML2.
DR HPA; ENSG00000125746; Low tissue specificity.
DR MIM; 617494; gene.
DR neXtProt; NX_O95834; -.
DR OpenTargets; ENSG00000125746; -.
DR PharmGKB; PA27768; -.
DR VEuPathDB; HostDB:ENSG00000125746; -.
DR eggNOG; KOG2106; Eukaryota.
DR GeneTree; ENSGT00940000153887; -.
DR HOGENOM; CLU_011754_2_0_1; -.
DR InParanoid; O95834; -.
DR OMA; IEDPGRC; -.
DR OrthoDB; 271572at2759; -.
DR PhylomeDB; O95834; -.
DR TreeFam; TF317832; -.
DR PathwayCommons; O95834; -.
DR SignaLink; O95834; -.
DR BioGRID-ORCS; 24139; 14 hits in 1073 CRISPR screens.
DR ChiTaRS; EML2; human.
DR GenomeRNAi; 24139; -.
DR Pharos; O95834; Tbio.
DR PRO; PR:O95834; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O95834; protein.
DR Bgee; ENSG00000125746; Expressed in C1 segment of cervical spinal cord and 194 other tissues.
DR ExpressionAtlas; O95834; baseline and differential.
DR Genevisible; O95834; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:UniProtKB.
DR GO; GO:0010968; P:regulation of microtubule nucleation; IDA:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR033016; EML2.
DR InterPro; IPR005108; HELP.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13720:SF50; PTHR13720:SF50; 1.
DR Pfam; PF03451; HELP; 1.
DR Pfam; PF00400; WD40; 6.
DR SMART; SM00320; WD40; 11.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..649
FT /note="Echinoderm microtubule-associated protein-like 2"
FT /id="PRO_0000050962"
FT REPEAT 56..93
FT /note="WD 1"
FT REPEAT 97..144
FT /note="WD 2"
FT REPEAT 151..192
FT /note="WD 3"
FT REPEAT 195..234
FT /note="WD 4"
FT REPEAT 241..280
FT /note="WD 5"
FT REPEAT 285..323
FT /note="WD 6"
FT REPEAT 369..406
FT /note="WD 7"
FT REPEAT 410..447
FT /note="WD 8"
FT REPEAT 452..489
FT /note="WD 9"
FT REPEAT 495..535
FT /note="WD 10"
FT REPEAT 564..602
FT /note="WD 11"
FT REPEAT 609..648
FT /note="WD 12"
FT REGION 10..649
FT /note="Tandem atypical propeller in EMLs"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..6
FT /note="MSSFGA -> MSLDDNLSGTSGMEVDDRVSALEQRLQLQEDELAVLKAALAD
FT ALRRLRACEEQGAALRARGTPKGRAPPRLGTTASVCQLLKGLPTRTPLNGSGPPRRVGG
FT YATSPSSPKKEATSGRSSVRRYLSPERLASVRREDPRSRTTSSSSNCSAKKE (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042541"
FT VAR_SEQ 1..6
FT /note="MSSFGA -> MLERRALLWQREAGPGWGDRARAGTGGAGGGCGGAMAERGPA
FT FCGLYDTSSLLRYCNDDNLSGTSGMEVDDRVSALEQRLQLQEDELAVLKAALADALRRL
FT RACEEQGAALRARGTPKGRAPPRLGTTASVCQLLKGLPTRTPLNGSGPPRRVGGYATSP
FT SSPKKEATSGRSSVRRYLSPERLASVRREDPRSRTTSSSSNCSAKKE (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047538"
FT VARIANT 33
FT /note="M -> V (in dbSNP:rs12151009)"
FT /id="VAR_031723"
FT VARIANT 187
FT /note="L -> F (in dbSNP:rs7252175)"
FT /id="VAR_031724"
FT VARIANT 235
FT /note="E -> D (in dbSNP:rs1545040)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_024697"
FT VARIANT 357
FT /note="R -> H (in dbSNP:rs3816045)"
FT /id="VAR_022026"
FT VARIANT 484
FT /note="V -> L (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1270442107)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035879"
FT CONFLICT 294
FT /note="D -> G (in Ref. 3; CAB46373)"
FT /evidence="ECO:0000305"
FT CONFLICT 419..427
FT /note="DPARSAGFH -> MAAAGHGDP (in Ref. 3; AAH32630)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="S -> F (in Ref. 3; CAB46373)"
FT /evidence="ECO:0000305"
FT HELIX 15..55
FT /evidence="ECO:0007829|PDB:4CGB"
FT COILED O95834-2:13..58
FT /evidence="ECO:0000269|PubMed:25740311"
FT COILED O95834-3:73..114
FT /evidence="ECO:0000255"
SQ SEQUENCE 649 AA; 70679 MW; F356D3D974D208C9 CRC64;
MSSFGAGKTK EVIFSVEDGS VKMFLRGRPV PMMIPDELAP TYSLDTRSEL PSCRLKLEWV
YGYRGRDCRA NLYLLPTGEI VYFVASVAVL YSVEEQRQRH YLGHNDDIKC LAIHPDMVTI
ATGQVAGTTK EGKPLPPHVR IWDSVSLSTL HVLGLGVFDR AVCCVGFSKS NGGNLLCAVD
ESNDHMLSVW DWAKETKVVD VKCSNEAVLV ATFHPTDPTV LITCGKSHIY FWTLEGGSLS
KRQGLFEKHE KPKYVLCVTF LEGGDVVTGD SGGNLYVWGK GGNRITQAVL GAHDGGVFGL
CALRDGTLVS GGGRDRRVVL WGSDYSKLQE VEVPEDFGPV RTVAEGHGDT LYVGTTRNSI
LQGSVHTGFS LLVQGHVEEL WGLATHPSRA QFVTCGQDKL VHLWSSDSHQ PLWSRIIEDP
ARSAGFHPSG SVLAVGTVTG RWLLLDTETH DLVAIHTDGN EQISVVSFSP DGAYLAVGSH
DNLVYVYTVD QGGRKVSRLG KCSGHSSFIT HLDWAQDSSC FVTNSGDYEI LYWDPATCKQ
ITSADAVRNM EWATATCVLG FGVFGIWSEG ADGTDINAVA RSHDGKLLAS ADDFGKVHLF
SYPCCQPRAL SHKYGGHSSH VTNVAFLWDD SMALTTGGKD TSVLQWRVV
