SAV1_HUMAN
ID SAV1_HUMAN Reviewed; 383 AA.
AC Q9H4B6; A8K4B8; D3DSB6; Q6IA58; Q9H949; Q9HAK9;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Protein salvador homolog 1;
DE AltName: Full=45 kDa WW domain protein;
DE Short=hWW45;
GN Name=SAV1; Synonyms=WW45;
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].
RX PubMed=11027580; DOI=10.1006/bbrc.2000.3582;
RA Valverde P.;
RT "Cloning, expression and mapping of hWW45, a novel WW-domain containing
RT gene.";
RL Biochem. Biophys. Res. Commun. 276:990-998(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetus, and Neuron;
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].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 INTERACTION WITH STK3/MST2.
RX PubMed=15688006; DOI=10.1038/sj.onc.1208445;
RA Chan E.H.Y., Nousiainen M., Chalamalasetty R.B., Schaefer A., Nigg E.A.,
RA Sillje H.H.W.;
RT "The Ste20-like kinase Mst2 activates the human large tumor suppressor
RT kinase Lats1.";
RL Oncogene 24:2076-2086(2005).
RN [7]
RP FUNCTION, HOMODIMERIZATION, INTERACTION WITH STK3/MST2 AND STK4/MST1, AND
RP PHOSPHORYLATION.
RX PubMed=16930133; DOI=10.1111/j.1742-4658.2006.05427.x;
RA Callus B.A., Verhagen A.M., Vaux D.L.;
RT "Association of mammalian sterile twenty kinases, Mst1 and Mst2, with
RT hSalvador via C-terminal coiled-coil domains, leads to its stabilization
RT and phosphorylation.";
RL FEBS J. 273:4264-4276(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STK4/MST1, AND TISSUE
RP SPECIFICITY.
RX PubMed=19212654;
RA Luo X., Li Z., Yan Q., Li X., Tao D., Wang J., Leng Y., Gardner K.,
RA Judge S.I., Li Q.Q., Hu J., Gong J.;
RT "The human WW45 protein enhances MST1-mediated apoptosis in vivo.";
RL Int. J. Mol. Med. 23:357-362(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP INTERACTION WITH WTIP AND AJUBA.
RX PubMed=20303269; DOI=10.1016/j.cub.2010.02.035;
RA Das Thakur M., Feng Y., Jagannathan R., Seppa M.J., Skeath J.B.,
RA Longmore G.D.;
RT "Ajuba LIM proteins are negative regulators of the Hippo signaling
RT pathway.";
RL Curr. Biol. 20:657-662(2010).
RN [12]
RP FUNCTION, AND INTERACTION WITH NEK2.
RX PubMed=21076410; DOI=10.1038/ncb2120;
RA Mardin B.R., Lange C., Baxter J.E., Hardy T., Scholz S.R., Fry A.M.,
RA Schiebel E.;
RT "Components of the Hippo pathway cooperate with Nek2 kinase to regulate
RT centrosome disjunction.";
RL Nat. Cell Biol. 12:1166-1176(2010).
RN [13]
RP FUNCTION, AND INTERACTION WITH ESR1.
RX PubMed=21104395; DOI=10.1007/s00109-010-0698-y;
RA Park Y., Park J., Lee Y., Lim W., Oh B.C., Shin C., Kim W., Lee Y.;
RT "Mammalian MST2 kinase and human Salvador activate and reduce estrogen
RT receptor alpha in the absence of ligand.";
RL J. Mol. Med. 89:181-191(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP 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 [15]
RP INTERACTION WITH STK3.
RX PubMed=28087714; DOI=10.1101/gad.284539.116;
RA Kwan J., Sczaniecka A., Arash E.H., Nguyen L., Chen C.C., Ratkovic S.,
RA Klezovitch O., Attisano L., McNeill H., Emili A., Vasioukhin V.;
RT "DLG5 connects cell polarity and Hippo signaling protein networks by
RT linking PAR-1 with MST1/2.";
RL Genes Dev. 30:2696-2709(2016).
RN [16]
RP VARIANT ASP-185.
RX PubMed=12202036; DOI=10.1016/s0092-8674(02)00824-3;
RA Tapon N., Harvey K.F., Bell D.W., Wahrer D.C.R., Schiripo T.A., Haber D.A.,
RA Hariharan I.K.;
RT "Salvador promotes both cell cycle exit and apoptosis in Drosophila and is
RT mutated in human cancer cell lines.";
RL Cell 110:467-478(2002).
CC -!- FUNCTION: Regulator of STK3/MST2 and STK4/MST1 in the Hippo signaling
CC pathway which plays a pivotal role in organ size control and tumor
CC suppression by restricting proliferation and promoting apoptosis. The
CC core of this pathway is composed of a kinase cascade wherein STK3/MST2
CC and STK4/MST1, in complex with its regulatory protein SAV1,
CC phosphorylates and activates LATS1/2 in complex with its regulatory
CC protein MOB1, which in turn phosphorylates and inactivates YAP1
CC oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits
CC its translocation into the nucleus to regulate cellular genes important
CC for cell proliferation, cell death, and cell migration. SAV1 is
CC required for STK3/MST2 and STK4/MST1 activation and promotes cell-cycle
CC exit and terminal differentiation in developing epithelial tissues.
CC Plays a role in centrosome disjunction by regulating the localization
CC of NEK2 to centrosomes, and its ability to phosphorylate CROCC and
CC CEP250. In conjunction with STK3/MST2, activates the transcriptional
CC activity of ESR1 through the modulation of its phosphorylation.
CC {ECO:0000269|PubMed:16930133, ECO:0000269|PubMed:19212654,
CC ECO:0000269|PubMed:21076410, ECO:0000269|PubMed:21104395}.
CC -!- SUBUNIT: Homodimer. Stabilized through interaction with STK3/MST2 or
CC STK4/MST1. Interacts (via SARAH domain) with isoform 1 of NEK2.
CC Interacts with ESR1 only in the presence of STK3/MST2. Interacts with
CC WTIP and AJUBA. {ECO:0000269|PubMed:15688006,
CC ECO:0000269|PubMed:16930133, ECO:0000269|PubMed:19212654,
CC ECO:0000269|PubMed:20303269, ECO:0000269|PubMed:21076410,
CC ECO:0000269|PubMed:21104395, ECO:0000269|PubMed:28087714}.
CC -!- INTERACTION:
CC Q9H4B6; O00165: HAX1; NbExp=7; IntAct=EBI-1017775, EBI-357001;
CC Q9H4B6; Q9H4B6: SAV1; NbExp=2; IntAct=EBI-1017775, EBI-1017775;
CC Q9H4B6; Q13188: STK3; NbExp=26; IntAct=EBI-1017775, EBI-992580;
CC Q9H4B6; Q13043: STK4; NbExp=19; IntAct=EBI-1017775, EBI-367376;
CC Q9H4B6; Q13043-1: STK4; NbExp=2; IntAct=EBI-1017775, EBI-15638366;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19212654}. Cytoplasm
CC {ECO:0000269|PubMed:19212654}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in adult tissues with
CC highest expression in the pancreas, aorta and interventricular septum
CC and lowest expression in skeletal muscle. Expression was higher in
CC fetal than in the adult heart. Expressed in various cell lines.
CC {ECO:0000269|PubMed:19212654}.
CC -!- PTM: Phosphorylated by STK3/MST2 and STK4/MST1. Phosphorylation is not
CC required for SAV1 stability and may increase the number of protein
CC binding sites on the scaffold molecule. {ECO:0000269|PubMed:16930133}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SAV1ID42206ch14q13.html";
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; AJ292969; CAC13972.1; -; mRNA.
DR EMBL; AK021500; BAB13835.1; -; mRNA.
DR EMBL; AK023071; BAB14390.1; -; mRNA.
DR EMBL; AK290883; BAF83572.1; -; mRNA.
DR EMBL; CR457297; CAG33578.1; -; mRNA.
DR EMBL; CH471078; EAW65702.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65704.1; -; Genomic_DNA.
DR EMBL; BC020537; AAH20537.1; -; mRNA.
DR CCDS; CCDS9701.1; -.
DR PIR; JC7507; JC7507.
DR RefSeq; NP_068590.1; NM_021818.3.
DR PDB; 6AO5; X-ray; 2.96 A; B=291-383.
DR PDBsum; 6AO5; -.
DR AlphaFoldDB; Q9H4B6; -.
DR SMR; Q9H4B6; -.
DR BioGRID; 121917; 167.
DR CORUM; Q9H4B6; -.
DR DIP; DIP-36127N; -.
DR IntAct; Q9H4B6; 98.
DR MINT; Q9H4B6; -.
DR STRING; 9606.ENSP00000324729; -.
DR iPTMnet; Q9H4B6; -.
DR PhosphoSitePlus; Q9H4B6; -.
DR BioMuta; SAV1; -.
DR DMDM; 32699681; -.
DR EPD; Q9H4B6; -.
DR jPOST; Q9H4B6; -.
DR MassIVE; Q9H4B6; -.
DR MaxQB; Q9H4B6; -.
DR PaxDb; Q9H4B6; -.
DR PeptideAtlas; Q9H4B6; -.
DR PRIDE; Q9H4B6; -.
DR ProteomicsDB; 80818; -.
DR Antibodypedia; 23683; 253 antibodies from 27 providers.
DR DNASU; 60485; -.
DR Ensembl; ENST00000324679.5; ENSP00000324729.4; ENSG00000151748.15.
DR GeneID; 60485; -.
DR KEGG; hsa:60485; -.
DR MANE-Select; ENST00000324679.5; ENSP00000324729.4; NM_021818.4; NP_068590.1.
DR UCSC; uc001wyh.3; human.
DR CTD; 60485; -.
DR DisGeNET; 60485; -.
DR GeneCards; SAV1; -.
DR HGNC; HGNC:17795; SAV1.
DR HPA; ENSG00000151748; Low tissue specificity.
DR MIM; 607203; gene.
DR neXtProt; NX_Q9H4B6; -.
DR OpenTargets; ENSG00000151748; -.
DR PharmGKB; PA134875018; -.
DR VEuPathDB; HostDB:ENSG00000151748; -.
DR eggNOG; KOG1891; Eukaryota.
DR GeneTree; ENSGT00940000156106; -.
DR HOGENOM; CLU_060422_0_0_1; -.
DR InParanoid; Q9H4B6; -.
DR OMA; AARYYYP; -.
DR OrthoDB; 284488at2759; -.
DR PhylomeDB; Q9H4B6; -.
DR TreeFam; TF317631; -.
DR PathwayCommons; Q9H4B6; -.
DR Reactome; R-HSA-2028269; Signaling by Hippo.
DR SignaLink; Q9H4B6; -.
DR SIGNOR; Q9H4B6; -.
DR BioGRID-ORCS; 60485; 16 hits in 1092 CRISPR screens.
DR ChiTaRS; SAV1; human.
DR GeneWiki; SAV1; -.
DR GenomeRNAi; 60485; -.
DR Pharos; Q9H4B6; Tbio.
DR PRO; PR:Q9H4B6; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9H4B6; protein.
DR Bgee; ENSG00000151748; Expressed in oocyte and 194 other tissues.
DR ExpressionAtlas; Q9H4B6; baseline and differential.
DR Genevisible; Q9H4B6; HS.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0031697; F:beta-1 adrenergic receptor binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0046332; F:SMAD binding; IBA:GO_Central.
DR GO; GO:0070699; F:type II activin receptor binding; IBA:GO_Central.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR GO; GO:0035329; P:hippo signaling; ISS:UniProtKB.
DR GO; GO:0060575; P:intestinal epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0097283; P:keratinocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0060487; P:lung epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:1902174; P:positive regulation of keratinocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IEA:Ensembl.
DR CDD; cd00201; WW; 2.
DR InterPro; IPR011524; SARAH_dom.
DR InterPro; IPR030030; Sav.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR47522; PTHR47522; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF51045; SSF51045; 2.
DR PROSITE; PS50951; SARAH; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..383
FT /note="Protein salvador homolog 1"
FT /id="PRO_0000076060"
FT DOMAIN 199..232
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 234..267
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 321..368
FT /note="SARAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00310"
FT COILED 344..373
FT /evidence="ECO:0000255"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEB2"
FT MOD_RES 210
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT VARIANT 185
FT /note="A -> D (in a colon cancer cell line)"
FT /evidence="ECO:0000269|PubMed:12202036"
FT /id="VAR_015880"
FT CONFLICT 5
FT /note="K -> Q (in Ref. 1; CAC13972)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="Q -> R (in Ref. 3; CAG33578)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="L -> F (in Ref. 2; BAB13835)"
FT /evidence="ECO:0000305"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:6AO5"
FT HELIX 306..313
FT /evidence="ECO:0007829|PDB:6AO5"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:6AO5"
FT HELIX 329..375
FT /evidence="ECO:0007829|PDB:6AO5"
SQ SEQUENCE 383 AA; 44634 MW; 4012C40A8601417A CRC64;
MLSRKKTKNE VSKPAEVQGK YVKKETSPLL RNLMPSFIRH GPTIPRRTDI CLPDSSPNAF
STSGDVVSRN QSFLRTPIQR TPHEIMRRES NRLSAPSYLA RSLADVPREY GSSQSFVTEV
SFAVENGDSG SRYYYSDNFF DGQRKRPLGD RAHEDYRYYE YNHDLFQRMP QNQGRHASGI
GRVAATSLGN LTNHGSEDLP LPPGWSVDWT MRGRKYYIDH NTNTTHWSHP LEREGLPPGW
ERVESSEFGT YYVDHTNKKA QYRHPCAPSV PRYDQPPPVT YQPQQTERNQ SLLVPANPYH
TAEIPDWLQV YARAPVKYDH ILKWELFQLA DLDTYQGMLK LLFMKELEQI VKMYEAYRQA
LLTELENRKQ RQQWYAQQHG KNF
