IGSF8_HUMAN
ID IGSF8_HUMAN Reviewed; 613 AA.
AC Q969P0; Q8NG09; Q96DP4; Q9BTG9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Immunoglobulin superfamily member 8;
DE Short=IgSF8;
DE AltName: Full=CD81 partner 3;
DE AltName: Full=Glu-Trp-Ile EWI motif-containing protein 2;
DE Short=EWI-2;
DE AltName: Full=Keratinocytes-associated transmembrane protein 4;
DE Short=KCT-4;
DE AltName: Full=LIR-D1;
DE AltName: Full=Prostaglandin regulatory-like protein;
DE Short=PGRL;
DE AltName: CD_antigen=CD316;
DE Flags: Precursor;
GN Name=IGSF8; Synonyms=CD81P3, EWI2, KCT4;
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), FUNCTION, TISSUE SPECIFICITY,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH CD81 AND CD9.
RX PubMed=11504738; DOI=10.1074/jbc.m107338200;
RA Stipp C.S., Kolesnikova T.V., Hemler M.E.;
RT "EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein
RT subfamily.";
RL J. Biol. Chem. 276:40545-40554(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=12708969; DOI=10.1042/bj20030343;
RA Charrin S., Le Naour F., Labas V., Billard M., Le Caer J.-P., Emile J.-F.,
RA Petit M.-A., Boucheix C., Rubinstein E.;
RT "EWI-2 is a new component of the tetraspanin web in hepatocytes and
RT lymphoid cells.";
RL Biochem. J. 373:409-421(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=12752121; DOI=10.1046/j.1365-2133.2003.05244.x;
RA Bonkobara M., Das A., Takao J., Cruz P.D. Jr., Ariizumi K.;
RT "Identification of novel genes for secreted and membrane-anchored proteins
RT in human keratinocytes.";
RL Br. J. Dermatol. 148:654-664(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Zhang W., Li N., Wan T., Cao X.;
RT "Identification of novel membrane proteins.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 [7]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 28-40.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective labeling of
RT protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [8]
RP FUNCTION, INTERACTION WITH CD82, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP TISSUE SPECIFICITY.
RX PubMed=12750295;
RA Zhang X.A., Lane W.S., Charrin S., Rubinstein E., Liu L.;
RT "EWI2/PGRL associates with the metastasis suppressor KAI1/CD82 and inhibits
RT the migration of prostate cancer cells.";
RL Cancer Res. 63:2665-2674(2003).
RN [9]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
RP INTEGRIN ALPHA-3 BETA-1.
RX PubMed=14662754; DOI=10.1083/jcb.200309113;
RA Stipp C.S., Kolesnikova T.V., Hemler M.E.;
RT "EWI-2 regulates alpha3beta1 integrin-dependent cell functions on laminin-
RT 5.";
RL J. Cell Biol. 163:1167-1177(2003).
RN [10]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
RP INTEGRIN ALPHA-4 BETA-1.
RX PubMed=15070678; DOI=10.1182/blood-2003-07-2201;
RA Kolesnikova T.V., Stipp C.S., Rao R.M., Lane W.S., Luscinskas F.W.,
RA Hemler M.E.;
RT "EWI-2 modulates lymphocyte integrin alpha4beta1 functions.";
RL Blood 103:3013-3019(2004).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-327 AND ASN-463.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May play a key role in diverse functions ascribed to CD81 and
CC CD9 such as oocytes fertilization or hepatitis C virus function. May
CC regulate proliferation and differentiation of keratinocytes. May be a
CC negative regulator of cell motility: suppresses T-cell mobility
CC coordinately with CD81, associates with CD82 to suppress prostate
CC cancer cell migration, regulates epidermoid cell reaggregation and
CC motility on laminin-5 with CD9 and CD81 as key linkers. May also play a
CC role on integrin-dependent morphology and motility functions. May
CC participate in the regulation of neurite outgrowth and maintenance of
CC the neural network in the adult brain. {ECO:0000269|PubMed:11504738,
CC ECO:0000269|PubMed:12750295, ECO:0000269|PubMed:12752121,
CC ECO:0000269|PubMed:14662754, ECO:0000269|PubMed:15070678}.
CC -!- SUBUNIT: Interacts directly with CD82, CD81/tetraspanin-28 and
CC CD9/tetraspanin-29. Also interacts with integrin alpha-3/beta-1 and
CC integrin alpha-4/beta-1. {ECO:0000269|PubMed:11504738,
CC ECO:0000269|PubMed:12750295, ECO:0000269|PubMed:14662754,
CC ECO:0000269|PubMed:15070678}.
CC -!- INTERACTION:
CC Q969P0; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-8293590, EBI-11959885;
CC Q969P0; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-8293590, EBI-11749135;
CC Q969P0; P60372: KRTAP10-4; NbExp=3; IntAct=EBI-8293590, EBI-10178153;
CC Q969P0; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-8293590, EBI-10172290;
CC Q969P0; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-8293590, EBI-10171774;
CC Q969P0; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-8293590, EBI-10172052;
CC Q969P0; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-8293590, EBI-14065470;
CC Q969P0; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-8293590, EBI-11987425;
CC Q969P0; P22735: TGM1; NbExp=3; IntAct=EBI-8293590, EBI-2562368;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q969P0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969P0-2; Sequence=VSP_017429, VSP_017430;
CC Name=3;
CC IsoId=Q969P0-3; Sequence=VSP_017431;
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney, testis, liver and
CC placenta with moderate expression in all other tissues. Detected on a
CC majority of B-cells, T-cells, and natural killer cells but not on
CC monocytes, polynuclear cells and platelets.
CC {ECO:0000269|PubMed:11504738, ECO:0000269|PubMed:12708969,
CC ECO:0000269|PubMed:12750295}.
CC -!- DOMAIN: The Ig-like C2-type domains 3 and 4 are required for
CC interaction with CD81. {ECO:0000250}.
CC -!- DOMAIN: The short cytoplasmic domain is very basic, interacts with
CC membrane PIPs, and mediates plasma membrane localization.
CC {ECO:0000250}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/IGSF8ID45820ch1q23.html";
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DR EMBL; AF407274; AAL01052.1; -; mRNA.
DR EMBL; AY044845; AAK92220.1; -; mRNA.
DR EMBL; AY157579; AAO13163.1; -; mRNA.
DR EMBL; AF311906; AAM94901.1; -; mRNA.
DR EMBL; AK055843; BAB71027.1; -; mRNA.
DR EMBL; BC004108; AAH04108.2; -; mRNA.
DR EMBL; BC053881; AAH53881.1; -; mRNA.
DR CCDS; CCDS1195.1; -. [Q969P0-1]
DR RefSeq; NP_001193594.1; NM_001206665.2. [Q969P0-1]
DR RefSeq; NP_001307176.1; NM_001320247.1. [Q969P0-1]
DR RefSeq; NP_443100.1; NM_052868.5. [Q969P0-1]
DR RefSeq; XP_016858324.1; XM_017002835.1. [Q969P0-1]
DR RefSeq; XP_016858325.1; XM_017002836.1. [Q969P0-1]
DR RefSeq; XP_016858326.1; XM_017002837.1. [Q969P0-1]
DR AlphaFoldDB; Q969P0; -.
DR BioGRID; 125011; 225.
DR IntAct; Q969P0; 29.
DR MINT; Q969P0; -.
DR STRING; 9606.ENSP00000357065; -.
DR GlyConnect; 1394; 22 N-Linked glycans (2 sites).
DR GlyGen; Q969P0; 3 sites, 23 N-linked glycans (2 sites).
DR iPTMnet; Q969P0; -.
DR PhosphoSitePlus; Q969P0; -.
DR SwissPalm; Q969P0; -.
DR BioMuta; IGSF8; -.
DR DMDM; 74762642; -.
DR UCD-2DPAGE; Q969P0; -.
DR EPD; Q969P0; -.
DR jPOST; Q969P0; -.
DR MassIVE; Q969P0; -.
DR MaxQB; Q969P0; -.
DR PaxDb; Q969P0; -.
DR PeptideAtlas; Q969P0; -.
DR PRIDE; Q969P0; -.
DR ProteomicsDB; 75806; -. [Q969P0-1]
DR ProteomicsDB; 75807; -. [Q969P0-2]
DR ProteomicsDB; 75808; -. [Q969P0-3]
DR Antibodypedia; 2186; 264 antibodies from 29 providers.
DR DNASU; 93185; -.
DR Ensembl; ENST00000314485.12; ENSP00000316664.7; ENSG00000162729.14. [Q969P0-1]
DR Ensembl; ENST00000368086.5; ENSP00000357065.1; ENSG00000162729.14. [Q969P0-1]
DR Ensembl; ENST00000614243.4; ENSP00000477565.1; ENSG00000162729.14. [Q969P0-1]
DR GeneID; 93185; -.
DR KEGG; hsa:93185; -.
DR MANE-Select; ENST00000314485.12; ENSP00000316664.7; NM_052868.6; NP_443100.1.
DR UCSC; uc001fuz.4; human. [Q969P0-1]
DR CTD; 93185; -.
DR DisGeNET; 93185; -.
DR GeneCards; IGSF8; -.
DR HGNC; HGNC:17813; IGSF8.
DR HPA; ENSG00000162729; Tissue enhanced (brain).
DR MIM; 606644; gene.
DR neXtProt; NX_Q969P0; -.
DR OpenTargets; ENSG00000162729; -.
DR PharmGKB; PA29767; -.
DR VEuPathDB; HostDB:ENSG00000162729; -.
DR eggNOG; ENOG502QTUT; Eukaryota.
DR GeneTree; ENSGT00940000161314; -.
DR HOGENOM; CLU_005187_2_0_1; -.
DR InParanoid; Q969P0; -.
DR OMA; VQWLRWP; -.
DR OrthoDB; 409194at2759; -.
DR PhylomeDB; Q969P0; -.
DR TreeFam; TF332702; -.
DR PathwayCommons; Q969P0; -.
DR SignaLink; Q969P0; -.
DR BioGRID-ORCS; 93185; 8 hits in 1077 CRISPR screens.
DR ChiTaRS; IGSF8; human.
DR GeneWiki; IGSF8; -.
DR GenomeRNAi; 93185; -.
DR Pharos; Q969P0; Tbio.
DR PRO; PR:Q969P0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q969P0; protein.
DR Bgee; ENSG00000162729; Expressed in right hemisphere of cerebellum and 145 other tissues.
DR ExpressionAtlas; Q969P0; baseline and differential.
DR Genevisible; Q969P0; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048870; P:cell motility; NAS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
DR GO; GO:0007338; P:single fertilization; NAS:UniProtKB.
DR GO; GO:0007519; P:skeletal muscle tissue development; NAS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:19892738"
FT CHAIN 28..613
FT /note="Immunoglobulin superfamily member 8"
FT /id="PRO_0000226247"
FT TOPO_DOM 28..579
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 580..600
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 601..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..149
FT /note="Ig-like C2-type 1"
FT DOMAIN 162..286
FT /note="Ig-like C2-type 2"
FT DOMAIN 303..424
FT /note="Ig-like C2-type 3"
FT DOMAIN 431..560
FT /note="Ig-like C2-type 4"
FT REGION 155..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 274..276
FT /note="EWI motif"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT LIPID 604
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 605
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 49..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 186..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 326..406
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 462..544
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..241
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017429"
FT VAR_SEQ 242..315
FT /note="ELRLGKEGTDRYRMVVGGAQAGDAGTYHCTAAEWIQDPDGSWAQIAEKRAVL
FT AHVDVQTLSSQLAVTVGPGERR -> MRGRSWHWAAWRGQAHRSTHTWQCPLGDLCPRH
FT QLGGQLCRKWWESGQTWPWRLELPMLSDWLQGSFVWARKGP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017430"
FT VAR_SEQ 475..561
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_017431"
FT CONFLICT 303
FT /note="S -> R (in Ref. 4; AAM94901)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="A -> P (in Ref. 4; AAM94901)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 65034 MW; A7255D54D42EFB88 CRC64;
MGALRPTLLP PSLPLLLLLM LGMGCWAREV LVPEGPLYRV AGTAVSISCN VTGYEGPAQQ
NFEWFLYRPE APDTALGIVS TKDTQFSYAV FKSRVVAGEV QVQRLQGDAV VLKIARLQAQ
DAGIYECHTP STDTRYLGSY SGKVELRVLP DVLQVSAAPP GPRGRQAPTS PPRMTVHEGQ
ELALGCLART STQKHTHLAV SFGRSVPEAP VGRSTLQEVV GIRSDLAVEA GAPYAERLAA
GELRLGKEGT DRYRMVVGGA QAGDAGTYHC TAAEWIQDPD GSWAQIAEKR AVLAHVDVQT
LSSQLAVTVG PGERRIGPGE PLELLCNVSG ALPPAGRHAA YSVGWEMAPA GAPGPGRLVA
QLDTEGVGSL GPGYEGRHIA MEKVASRTYR LRLEAARPGD AGTYRCLAKA YVRGSGTRLR
EAASARSRPL PVHVREEGVV LEAVAWLAGG TVYRGETASL LCNISVRGGP PGLRLAASWW
VERPEDGELS SVPAQLVGGV GQDGVAELGV RPGGGPVSVE LVGPRSHRLR LHSLGPEDEG
VYHCAPSAWV QHADYSWYQA GSARSGPVTV YPYMHALDTL FVPLLVGTGV ALVTGATVLG
TITCCFMKRL RKR
