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   27-MAR-2024, entry version 174.
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="https://atlasgeneticsoncology.org/gene/45820/IGSF8";
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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; 233.
DR   IntAct; Q969P0; 30.
DR   MINT; Q969P0; -.
DR   STRING; 9606.ENSP00000357065; -.
DR   GlyConnect; 1394; 22 N-Linked glycans (2 sites).
DR   GlyCosmos; Q969P0; 3 sites, 23 glycans.
DR   GlyGen; Q969P0; 4 sites, 23 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q969P0; -.
DR   PhosphoSitePlus; Q969P0; -.
DR   SwissPalm; Q969P0; -.
DR   BioMuta; IGSF8; -.
DR   DMDM; 74762642; -.
DR   EPD; Q969P0; -.
DR   jPOST; Q969P0; -.
DR   MassIVE; Q969P0; -.
DR   MaxQB; Q969P0; -.
DR   PaxDb; 9606-ENSP00000357065; -.
DR   PeptideAtlas; Q969P0; -.
DR   ProteomicsDB; 75806; -. [Q969P0-1]
DR   ProteomicsDB; 75807; -. [Q969P0-2]
DR   ProteomicsDB; 75808; -. [Q969P0-3]
DR   Pumba; Q969P0; -.
DR   Antibodypedia; 2186; 290 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   AGR; HGNC:17813; -.
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; 4170975at2759; -.
DR   PhylomeDB; Q969P0; -.
DR   TreeFam; TF332702; -.
DR   PathwayCommons; Q969P0; -.
DR   SignaLink; Q969P0; -.
DR   BioGRID-ORCS; 93185; 9 hits in 1157 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 146 other cell types or tissues.
DR   ExpressionAtlas; Q969P0; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0016020; C:membrane; IDA: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; Immunoglobulins; 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   PANTHER; PTHR12207:SF22; IMMUNOGLOBULIN SUPERFAMILY MEMBER 8; 1.
DR   PANTHER; PTHR12207; V-SET AND TRANSMEMBRANE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 4.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   UCD-2DPAGE; Q969P0; -.
DR   Genevisible; Q969P0; HS.
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
//