HEG1_HUMAN
ID HEG1_HUMAN Reviewed; 1381 AA.
AC Q9ULI3; Q6NX66; Q8NC40; Q9BSV0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein HEG homolog 1;
DE Flags: Precursor;
GN Name=HEG1; Synonyms=KIAA1237;
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 GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-1381.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1117-1381.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 682-1381 (ISOFORM 2), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1140-1381 (ISOFORM 1), AND VARIANT LEU-980.
RC TISSUE=Kidney, and Ovary;
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-159 AND ASN-520.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [6]
RP GLYCOSYLATION AT THR-67, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 1356-1381 IN COMPLEX WITH KRIT1,
RP AND INTERACTION WITH KRIT1.
RX PubMed=23007647; DOI=10.1083/jcb.201205109;
RA Gingras A.R., Liu J.J., Ginsberg M.H.;
RT "Structural basis of the junctional anchorage of the cerebral cavernous
RT malformations complex.";
RL J. Cell Biol. 199:39-48(2012).
CC -!- FUNCTION: Receptor component of the CCM signaling pathway which is a
CC crucial regulator of heart and vessel formation and integrity. May act
CC through the stabilization of endothelial cell junctions. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CCM2 and KRIT1; KRIT1 markedly facilitates
CC interaction with CCM2. {ECO:0000269|PubMed:23007647}.
CC -!- INTERACTION:
CC Q9ULI3; O00522: KRIT1; NbExp=5; IntAct=EBI-12734419, EBI-1573121;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}. Cell junction
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ULI3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULI3-2; Sequence=VSP_025275, VSP_025276;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH67235.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11336.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC026342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB033063; BAA86551.2; -; mRNA.
DR EMBL; AK074987; BAC11336.1; ALT_INIT; mRNA.
DR EMBL; BC004539; AAH04539.2; -; mRNA.
DR EMBL; BC067235; AAH67235.1; ALT_INIT; mRNA.
DR CCDS; CCDS46898.1; -. [Q9ULI3-1]
DR RefSeq; NP_065784.1; NM_020733.1. [Q9ULI3-1]
DR PDB; 3U7D; X-ray; 2.49 A; B/D=1356-1381.
DR PDB; 4HDQ; X-ray; 1.95 A; C=1356-1381.
DR PDBsum; 3U7D; -.
DR PDBsum; 4HDQ; -.
DR AlphaFoldDB; Q9ULI3; -.
DR SMR; Q9ULI3; -.
DR BioGRID; 121560; 7.
DR CORUM; Q9ULI3; -.
DR IntAct; Q9ULI3; 3.
DR STRING; 9606.ENSP00000311502; -.
DR GlyConnect; 763; 18 N-Linked glycans (9 sites), 5 O-Linked glycans (4 sites).
DR GlyGen; Q9ULI3; 37 sites, 18 N-linked glycans (9 sites), 6 O-linked glycans (21 sites).
DR iPTMnet; Q9ULI3; -.
DR PhosphoSitePlus; Q9ULI3; -.
DR SwissPalm; Q9ULI3; -.
DR BioMuta; HEG1; -.
DR DMDM; 147645934; -.
DR EPD; Q9ULI3; -.
DR jPOST; Q9ULI3; -.
DR MassIVE; Q9ULI3; -.
DR MaxQB; Q9ULI3; -.
DR PaxDb; Q9ULI3; -.
DR PeptideAtlas; Q9ULI3; -.
DR PRIDE; Q9ULI3; -.
DR ProteomicsDB; 85037; -. [Q9ULI3-1]
DR ProteomicsDB; 85038; -. [Q9ULI3-2]
DR Antibodypedia; 2617; 20 antibodies from 9 providers.
DR DNASU; 57493; -.
DR Ensembl; ENST00000311127.9; ENSP00000311502.3; ENSG00000173706.14. [Q9ULI3-1]
DR GeneID; 57493; -.
DR KEGG; hsa:57493; -.
DR MANE-Select; ENST00000311127.9; ENSP00000311502.3; NM_020733.2; NP_065784.1.
DR UCSC; uc003ehs.4; human. [Q9ULI3-1]
DR CTD; 57493; -.
DR DisGeNET; 57493; -.
DR GeneCards; HEG1; -.
DR HGNC; HGNC:29227; HEG1.
DR HPA; ENSG00000173706; Low tissue specificity.
DR MIM; 614182; gene.
DR neXtProt; NX_Q9ULI3; -.
DR OpenTargets; ENSG00000173706; -.
DR PharmGKB; PA142671699; -.
DR VEuPathDB; HostDB:ENSG00000173706; -.
DR eggNOG; ENOG502QPW9; Eukaryota.
DR GeneTree; ENSGT00710000106813; -.
DR HOGENOM; CLU_006913_0_0_1; -.
DR InParanoid; Q9ULI3; -.
DR OMA; GMQKCVN; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; Q9ULI3; -.
DR TreeFam; TF335941; -.
DR PathwayCommons; Q9ULI3; -.
DR SignaLink; Q9ULI3; -.
DR BioGRID-ORCS; 57493; 12 hits in 1081 CRISPR screens.
DR ChiTaRS; HEG1; human.
DR GenomeRNAi; 57493; -.
DR Pharos; Q9ULI3; Tbio.
DR PRO; PR:Q9ULI3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9ULI3; protein.
DR Bgee; ENSG00000173706; Expressed in parietal pleura and 208 other tissues.
DR ExpressionAtlas; Q9ULI3; baseline and differential.
DR Genevisible; Q9ULI3; HS.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003209; P:cardiac atrium morphogenesis; IEA:Ensembl.
DR GO; GO:0055017; P:cardiac muscle tissue growth; IEA:Ensembl.
DR GO; GO:0007043; P:cell-cell junction assembly; IEA:InterPro.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0003017; P:lymph circulation; IEA:Ensembl.
DR GO; GO:0001945; P:lymph vessel development; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:1905709; P:negative regulation of membrane permeability; IDA:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:UniProtKB.
DR GO; GO:2000299; P:negative regulation of Rho-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0060039; P:pericardium development; IEA:Ensembl.
DR GO; GO:0090271; P:positive regulation of fibroblast growth factor production; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:1902414; P:protein localization to cell junction; IMP:UniProtKB.
DR GO; GO:0050878; P:regulation of body fluid levels; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR GO; GO:0048845; P:venous blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IEA:Ensembl.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR028720; HEG.
DR PANTHER; PTHR24037; PTHR24037; 2.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell junction; Cell membrane;
KW Developmental protein; Disulfide bond; EGF-like domain; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1381
FT /note="Protein HEG homolog 1"
FT /id="PRO_0000286981"
FT TOPO_DOM 30..1248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1249..1269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1270..1381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 985..1023
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1025..1063
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 24..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q7X6"
FT CARBOHYD 67
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:22171320"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 989..1000
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 994..1011
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1013..1022
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1029..1040
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1034..1049
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1051..1062
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 986..1012
FT /note="VNSCAVNPCLHNGECVADNTSRGYHCR -> GKTQSHKHMLTARPSPALRAT
FT WGSGFM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025275"
FT VAR_SEQ 1013..1381
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025276"
FT VARIANT 145
FT /note="Q -> R (in dbSNP:rs4404487)"
FT /id="VAR_048984"
FT VARIANT 305
FT /note="S -> P (in dbSNP:rs2981546)"
FT /id="VAR_059269"
FT VARIANT 602
FT /note="F -> S (in dbSNP:rs6790837)"
FT /id="VAR_032253"
FT VARIANT 980
FT /note="V -> L (in dbSNP:rs10804567)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032254"
FT VARIANT 1039
FT /note="M -> T (in dbSNP:rs6438869)"
FT /id="VAR_032255"
SQ SEQUENCE 1381 AA; 147461 MW; 2E8402AC5227F95C CRC64;
MASPRASRWP PPLLLLLLPL LLLPPAAPGT RDPPPSPARR ALSLAPLAGA GLELQLERRP
EREPPPTPPR ERRGPATPGP SYRAPEPGAA TQRGPSGRAP RGGSADAAWK HWPESNTEAH
VENITFYQNQ EDFSTVSSKE GVMVQTSGKS HAASDAPENL TLLAETADAR GRSGSSSRTN
FTILPVGYSL EIATALTSQS GNLASESLHL PSSSSEFDER IAAFQTKSGT ASEMGTERAM
GLSEEWTVHS QEATTSAWSP SFLPALEMGE LTTPSRKRNS SGPDLSWLHF YRTAASSPLL
DLSSSSESTE KLNNSTGLQS SSVSQTKTMH VATVFTDGGP RTLRSLTVSL GPVSKTEGFP
KDSRIATTSS SVLLSPSAVE SRRNSRVTGN PGDEEFIEPS TENEFGLTSL RWQNDSPTFG
EHQLASSSEV QNGSPMSQTE TVSRSVAPMR GGEITAHWLL TNSTTSADVT GSSASYPEGV
NASVLTQFSD STVQSGGSHT ALGDRSYSES SSTSSSESLN SSAPRGERSI AGISYGQVRG
TAIEQRTSSD HTDHTYLSST FTKGERALLS ITDNSSSSDI VESSTSYIKI SNSSHSEYSS
FFHAQTERSN ISSYDGEYAQ PSTESPVLHT SNLPSYTPTI NMPNTSVVLD TDAEFVSDSS
SSSSSSSSSS SSGPPLPLPS VSQSHHLFSS ILPSTRASVH LLKSTSDAST PWSSSPSPLP
VSLTTSTSAP LSVSQTTLPQ SSSTPVLPRA RETPVTSFQT STMTSFMTML HSSQTADLKS
QSTPHQEKVI TESKSPSLVS LPTESTKAVT TNSPLPPSLT ESSTEQTLPA TSTNLAQMSP
TFTTTILKTS QPLMTTPGTL SSTASLVTGP IAVQTTAGKQ LSLTHPEILV PQISTEGGIS
TERNRVIVDA TTGLIPLTSV PTSAKEMTTK LGVTAEYSPA SRSLGTSPSP QTTVVSTAED
LAPKSATFAV QSSTQSPTTV SSSASVNSCA VNPCLHNGEC VADNTSRGYH CRCPPSWQGD
DCSVDVNECL SNPCPSTAMC NNTQGSFICK CPVGYQLEKG ICNLVRTFVT EFKLKRTFLN
TTVEKHSDLQ EVENEITKTL NMCFSALPSY IRSTVHASRE SNAVVISLQT TFSLASNVTL
FDLADRMQKC VNSCKSSAEV CQLLGSQRRI FRAGSLCKRK SPECDKDTSI CTDLDGVALC
QCKSGYFQFN KMDHSCRACE DGYRLENETC MSCPFGLGGL NCGNPYQLIT VVIAAAGGGL
LLILGIALIV TCCRKNKNDI SKLIFKSGDF QMSPYAEYPK NPRSQEWGRE AIEMHENGST
KNLLQMTDVY YSPTSVRNPE LERNGLYPAY TGLPGSRHSC IFPGQYNPSF ISDESRRRDY
F
